ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures

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	Protein Summary
	AS Summary
	Protein Functional Features
	Gene Isoform Structures and Expression Levels
	Protein Structures
	pLDDT Score Distribution
	Ramachandran Plot of Protein Structures
	Potential Active Site Information
	Protein Structure and Feature Comparision
	Protein-Protein Interaction
	Related Drugs
	Related Diseases
	Clinically Important Variants

Protein:FGFR2

Protein Summary

Gene summary

Gene name: FGFR2
ASpdb.0 ID: 2263
	Gene
Gene symbol	FGFR2
Gene ID	2263
Gene name	fibroblast growth factor receptor 2
Synonyms	BBDS\|BEK\|BFR-1\|CD332\|CEK3\|CFD1\|ECT1\|JWS\|K-SAM\|KGFR\|TK14\|TK25
Cytomap	10q26.13
Type of gene	protein-coding
Description	fibroblast growth factor receptor 2BEK fibroblast growth factor receptorbacteria-expressed kinasekeratinocyte growth factor receptorprotein tyrosine kinase, receptor like 14
Modification date	20240416
UniProtAcc	P21802

Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez

Partner	Gene	GO ID	GO term	PubMed ID
Gene	FGFR2	GO:0005007	fibroblast growth factor receptor activity	8663044\|15629145
Gene	FGFR2	GO:0005634	nucleus	16597614\|17471512
Gene	FGFR2	GO:0005737	cytoplasm	16597614\|17471512
Gene	FGFR2	GO:0005886	plasma membrane	15629145\|16844695
Gene	FGFR2	GO:0005938	cell cortex	17471512
Gene	FGFR2	GO:0008284	positive regulation of cell population proliferation	8663044
Gene	FGFR2	GO:0008543	fibroblast growth factor receptor signaling pathway	8663044\|15629145
Gene	FGFR2	GO:0009986	cell surface	16597614
Gene	FGFR2	GO:0017134	fibroblast growth factor binding	8663044
Gene	FGFR2	GO:0018108	peptidyl-tyrosine phosphorylation	15629145\|16844695
Gene	FGFR2	GO:0046777	protein autophosphorylation	15629145
Gene	FGFR2	GO:0062023	collagen-containing extracellular matrix	17959718

AS Summary

Information of the canonical protein with experimentally identified structure from PDB (2023).

UniProt Acc	File name	PDB ID	Method	Resolution	Chain	Start	End
P21802-1	P21802-1_5eg3_A.pdb	5EG3	X-ray	2.61	A	466	774

ASpdb's canonical and alternatively spliced isoform information.

accession_id	gene_name	canonical_id	alternative_id	canonical_length	alternative_length	canonical_start	canonical_end	type	originalSEQ	variationSEQ	alternative_start	alternative_end
P21802	FGFR2	P21802-1	P21802-14	821	254	250	254	Substitution	ERSPH	GSQGL	250	254
P21802	FGFR2	P21802-1	P21802-14	821	254	255	821	Deletion	none	none	254	254
P21802	FGFR2	P21802-1	P21802-15	821	705	314	429	Deletion	none	none	313	313
P21802	FGFR2	P21802-1	P21802-16	821	822	313	313	Substitution	K	KVTK	313	316
P21802	FGFR2	P21802-1	P21802-16	821	822	428	429	Deletion	none	none	430	430
P21802	FGFR2	P21802-1	P21802-17	821	769	314	330	Substitution	AAGVNTTDKEIEVLYIR	HSGINSSNAEVLALF	314	328
P21802	FGFR2	P21802-1	P21802-17	821	769	334	335	Substitution	FE	EA	332	333
P21802	FGFR2	P21802-1	P21802-17	821	769	341	353	Substitution	TCLAGNSIGISFH	ICKVSNYIGQANQ	339	351
P21802	FGFR2	P21802-1	P21802-17	821	769	361	361	Substitution	P	PKQQ	359	362
P21802	FGFR2	P21802-1	P21802-17	821	769	768	821	Substitution	EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	I	769	769
P21802	FGFR2	P21802-1	P21802-18	821	820	314	330	Substitution	AAGVNTTDKEIEVLYIR	HSGINSSNAEVLALF	314	328
P21802	FGFR2	P21802-1	P21802-18	821	820	334	335	Substitution	FE	EA	332	333
P21802	FGFR2	P21802-1	P21802-18	821	820	341	353	Substitution	TCLAGNSIGISFH	ICKVSNYIGQANQ	339	351
P21802	FGFR2	P21802-1	P21802-18	821	820	361	361	Substitution	P	PKQQ	359	362
P21802	FGFR2	P21802-1	P21802-18	821	820	428	429	Deletion	none	none	428	428
P21802	FGFR2	P21802-1	P21802-19	821	366	314	330	Substitution	AAGVNTTDKEIEVLYIR	HSGINSSNAEVLALF	314	328
P21802	FGFR2	P21802-1	P21802-19	821	366	334	335	Substitution	FE	EA	332	333
P21802	FGFR2	P21802-1	P21802-19	821	366	341	353	Substitution	TCLAGNSIGISFH	ICKVSNYIGQANQ	339	351
P21802	FGFR2	P21802-1	P21802-19	821	366	361	361	Substitution	P	PKQQ	359	362
P21802	FGFR2	P21802-1	P21802-19	821	366	362	365	Substitution	APGR	GRRC	363	366
P21802	FGFR2	P21802-1	P21802-19	821	366	366	821	Deletion	none	none	366	366
P21802	FGFR2	P21802-1	P21802-2	821	768	768	821	Substitution	EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	I	768	768
P21802	FGFR2	P21802-1	P21802-20	821	704	37	152	Substitution	EPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKR	G	37	37
P21802	FGFR2	P21802-1	P21802-20	821	704	429	430	Deletion	none	none	313	313
P21802	FGFR2	P21802-1	P21802-21	821	707	37	125	Deletion	none	none	36	36
P21802	FGFR2	P21802-1	P21802-21	821	707	769	821	Substitution	YLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	EKKVSGAVDCHKPPCNPSHLPCVLAVDQ	680	707
P21802	FGFR2	P21802-1	P21802-22	821	680	37	125	Deletion	none	none	36	36
P21802	FGFR2	P21802-1	P21802-22	821	680	314	330	Substitution	AAGVNTTDKEIEVLYIR	HSGINSSNAEVLALF	225	239
P21802	FGFR2	P21802-1	P21802-22	821	680	334	335	Substitution	FE	EA	243	244
P21802	FGFR2	P21802-1	P21802-22	821	680	341	353	Substitution	TCLAGNSIGISFH	ICKVSNYIGQANQ	250	262
P21802	FGFR2	P21802-1	P21802-22	821	680	361	361	Substitution	P	PKQQ	270	273
P21802	FGFR2	P21802-1	P21802-22	821	680	768	821	Substitution	EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	I	680	680
P21802	FGFR2	P21802-1	P21802-23	821	709	250	361	Deletion	none	none	249	249
P21802	FGFR2	P21802-1	P21802-3	821	822	314	330	Substitution	AAGVNTTDKEIEVLYIR	HSGINSSNAEVLALF	314	328
P21802	FGFR2	P21802-1	P21802-3	821	822	334	335	Substitution	FE	EA	332	333
P21802	FGFR2	P21802-1	P21802-3	821	822	341	353	Substitution	TCLAGNSIGISFH	ICKVSNYIGQANQ	339	351
P21802	FGFR2	P21802-1	P21802-3	821	822	361	361	Substitution	P	PKQQ	359	362
P21802	FGFR2	P21802-1	P21802-4	821	682	37	125	Deletion	none	none	36	36
P21802	FGFR2	P21802-1	P21802-4	821	682	314	330	Substitution	AAGVNTTDKEIEVLYIR	HSGINSSNAEVLALF	225	239
P21802	FGFR2	P21802-1	P21802-4	821	682	334	335	Substitution	FE	EA	243	244
P21802	FGFR2	P21802-1	P21802-4	821	682	341	353	Substitution	TCLAGNSIGISFH	ICKVSNYIGQANQ	250	262
P21802	FGFR2	P21802-1	P21802-4	821	682	361	361	Substitution	P	PKQQ	270	273
P21802	FGFR2	P21802-1	P21802-4	821	682	428	429	Deletion	none	none	339	339
P21802	FGFR2	P21802-1	P21802-4	821	682	761	821	Substitution	LTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	PPNPSLMSIFRK	671	682
P21802	FGFR2	P21802-1	P21802-5	821	819	428	429	Deletion	none	none	427	427
P21802	FGFR2	P21802-1	P21802-6	821	785	428	429	Deletion	none	none	427	427
P21802	FGFR2	P21802-1	P21802-6	821	785	778	821	Substitution	QYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	PYSPCYPDPR	776	785
P21802	FGFR2	P21802-1	P21802-8	821	766	428	429	Deletion	none	none	427	427
P21802	FGFR2	P21802-1	P21802-8	821	766	768	821	Substitution	EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	I	766	766

Multiple sequence alignment of our canonical and alternatively spliced FGFR2

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of FGFR2

UniProt-id	ENSG	ENST	ENSP
P21802-1	ENSG00000066468.24	ENST00000358487.10	ENSP00000351276.6
P21802-14	ENSG00000066468.24	ENST00000359354.6	ENSP00000352309.2
P21802-15	ENSG00000066468.24	ENST00000369060.8	ENSP00000358056.4
P21802-17	ENSG00000066468.24	ENST00000369056.5	ENSP00000358052.1
P21802-20	ENSG00000066468.24	ENST00000356226.8	ENSP00000348559.4
P21802-20	ENSG00000066468.24	ENST00000682550.1	ENSP00000507633.1
P21802-21	ENSG00000066468.24	ENST00000357555.9	ENSP00000350166.5
P21802-22	ENSG00000066468.24	ENST00000360144.7	ENSP00000353262.3
P21802-23	ENSG00000066468.24	ENST00000369061.8	ENSP00000358057.4
P21802-3	ENSG00000066468.24	ENST00000457416.7	ENSP00000410294.2
P21802-5	ENSG00000066468.24	ENST00000346997.6	ENSP00000263451.5
P21802-5	ENSG00000066468.24	ENST00000351936.11	ENSP00000309878.10
P21802-5	ENSG00000066468.24	ENST00000683211.1	ENSP00000508257.1

UniProt-id	NM ID	NP ID
P21802-1	NM_000141.4	NP_000132.3
P21802-15	NM_001144917.1	NP_001138389.1
P21802-17	NM_001144913.1	NP_001138385.1
P21802-20	NM_001144918.1	NP_001138390.1
P21802-21	NM_001144915.1	NP_001138387.1
P21802-22	NM_001144919.1	NP_001138391.1
P21802-23	NM_001144914.1	NP_001138386.1
P21802-3	NM_022970.3	NP_075259.4
P21802-5	NM_001320658.1	NP_001307587.1

Amino acid sequences of our canonical and alternatively spliced FGFR2

accession_id	Protein sequence
P21802-1	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVL PAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTR LSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKM IGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAAR NVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGH RMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLP
P21802-14	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP
P21802-15	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEF PRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEY ASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDY YKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQ
P21802-16	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKVTKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWL TVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVSAESSSSMNSNTPLVRITT RLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMK MIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAA RNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEG HRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCL
P21802-17	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEADAGEYICKVSNYIGQANQSAWLTVLPK QQAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITT RLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMK MIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAA RNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEG
P21802-18	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEADAGEYICKVSNYIGQANQSAWLTVLPK QQAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVSAESSSSMNSNTPLVRITTRL SSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMI GKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARN VLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHR MDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQ
P21802-19	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEADAGEYICKVSNYIGQANQSAWLTVLPK
P21802-2	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVL PAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTR LSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKM IGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAAR NVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGH
P21802-20	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEGAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIG GYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVE KNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGV FLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFP RDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYA SKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYY KKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQR
P21802-21	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRC PAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTV VGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTV LPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITT RLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMK MIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAA RNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEG
P21802-22	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRC PAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTV VGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEADAGEYICKVSNYIGQANQSAWLTVLP KQQAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRIT TRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMM KMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLA ARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKE
P21802-23	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVAPGREKEITASPDYLEIAIYC IGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDP KWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYV IVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDIN NIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHA
P21802-3	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEADAGEYICKVSNYIGQANQSAWLTVLPK QQAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITT RLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMK MIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAA RNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEG HRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCL
P21802-4	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRC PAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTV VGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEADAGEYICKVSNYIGQANQSAWLTVLP KQQAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVSAESSSSMNSNTPLVRITTR LSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKM IGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAAR NVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGH
P21802-5	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVL PAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVSAESSSSMNSNTPLVRITTRLS STADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIG KHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNV LVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRM DKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQY
P21802-6	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVL PAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVSAESSSSMNSNTPLVRITTRLS STADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIG KHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNV LVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRM
P21802-8	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGE YLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCP AGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVV GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVL PAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVSAESSSSMNSNTPLVRITTRLS STADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIG KHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNV LVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRM

Protein Functional Features

Main function of this protein. (from UniProt)

FGFR2 (go to UniProt):P21802

Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at
download page
* Minus value of BPloci means that the break pointn is located before the CDS.

- Retained protein feature among the 13 regional features.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=250;End=254
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=255;End=821
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=314;End=429
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=313;End=313
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=314;End=330
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=334;End=335
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=341;End=353
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=361;End=361
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=314;End=330
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=334;End=335
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=341;End=353
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=361;End=361
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=314;End=330
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=334;End=335
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=341;End=353
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=361;End=361
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=362;End=365
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=366;End=821
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=37;End=152
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=37;End=125
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=37;End=125
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=314;End=330
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=334;End=335
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=341;End=353
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=361;End=361
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=250;End=361
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=314;End=330
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=334;End=335
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=341;End=353
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=361;End=361
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=37;End=125
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=314;End=330
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=334;End=335
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=341;End=353
P21802	Topological domain	22	377	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=361;End=361
P21802	Transmembrane	378	398	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=255;End=821
P21802	Transmembrane	378	398	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=314;End=429
P21802	Transmembrane	378	398	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=366;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=255;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=314;End=429
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=428;End=429
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=768;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=428;End=429
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=366;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=768;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=429;End=430
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=769;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=768;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=428;End=429
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=761;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=428;End=429
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=428;End=429
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=778;End=821
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=428;End=429
P21802	Topological domain	399	821	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=768;End=821
P21802	Domain	25	125	Note=Ig-like C2-type 1	Type=Substitution;Start=37;End=152
P21802	Domain	25	125	Note=Ig-like C2-type 1	Type=Deletion;Start=37;End=125
P21802	Domain	25	125	Note=Ig-like C2-type 1	Type=Deletion;Start=37;End=125
P21802	Domain	25	125	Note=Ig-like C2-type 1	Type=Deletion;Start=37;End=125
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Deletion;Start=255;End=821
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Deletion;Start=314;End=429
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=313;End=313
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=314;End=330
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=334;End=335
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=341;End=353
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=314;End=330
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=334;End=335
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=341;End=353
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=314;End=330
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=334;End=335
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=341;End=353
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=314;End=330
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=334;End=335
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=341;End=353
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Deletion;Start=250;End=361
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=314;End=330
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=334;End=335
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=341;End=353
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=314;End=330
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=334;End=335
P21802	Domain	256	358	Note=Ig-like C2-type 3	Type=Substitution;Start=341;End=353
P21802	Domain	481	770	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Deletion;Start=255;End=821
P21802	Domain	481	770	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Substitution;Start=768;End=821
P21802	Domain	481	770	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Deletion;Start=366;End=821
P21802	Domain	481	770	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Substitution;Start=768;End=821
P21802	Domain	481	770	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Substitution;Start=769;End=821
P21802	Domain	481	770	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Substitution;Start=768;End=821
P21802	Domain	481	770	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Substitution;Start=761;End=821
P21802	Domain	481	770	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Substitution;Start=768;End=821
P21802	Region	131	151	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=37;End=152

Gene Isoform Structures and Expression Levels for FGFR2

Gene structures of our canonical and alternative spliced genes of FGFR2
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

Expression levels of gene isoforms across GTEx.

Expression levels of gene isoforms across TCGA.

Protein Structures

PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.

3D view using mol* of P21802-1

3D view using mol* of P21802-14

3D view using mol* of P21802-15

3D view using mol* of P21802-16

3D view using mol* of P21802-17

3D view using mol* of P21802-18

3D view using mol* of P21802-19

3D view using mol* of P21802-2

3D view using mol* of P21802-20

3D view using mol* of P21802-21

3D view using mol* of P21802-22

3D view using mol* of P21802-23

3D view using mol* of P21802-3

3D view using mol* of P21802-4

3D view using mol* of P21802-5

3D view using mol* of P21802-6

3D view using mol* of P21802-8

pLDDT Score Distribution

pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.

pLDDT distribution across the protein length of P21802-1

pLDDT distribution across the protein length of P21802-14

pLDDT distribution across the protein length of P21802-15

pLDDT distribution across the protein length of P21802-16

pLDDT distribution across the protein length of P21802-17

pLDDT distribution across the protein length of P21802-18

pLDDT distribution across the protein length of P21802-19

pLDDT distribution across the protein length of P21802-2

pLDDT distribution across the protein length of P21802-20

pLDDT distribution across the protein length of P21802-21

pLDDT distribution across the protein length of P21802-22

pLDDT distribution across the protein length of P21802-23

pLDDT distribution across the protein length of P21802-3

pLDDT distribution across the protein length of P21802-4

pLDDT distribution across the protein length of P21802-5

pLDDT distribution across the protein length of P21802-6

pLDDT distribution across the protein length of P21802-8

Ramachandran Plot of Protein Structures

Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.

Ramachandran plot of P21802-1

Ramachandran plot of P21802-16

Ramachandran plot of P21802-18

Ramachandran plot of P21802-19

Ramachandran plot of P21802-2

Ramachandran plot of P21802-21

Ramachandran plot of P21802-3

Ramachandran plot of P21802-4

Ramachandran plot of P21802-5

Ramachandran plot of P21802-6

Ramachandran plot of P21802-8

Potential Active Site Information

The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.

UniProt-id	Site score	Size	D score	Volume	Exposure	Enclosure	Contact	Phobic	Philic	Balance	Don/Acc	Residues
P21802-1	1.087	268	1.084	904.834	0.438	0.829	1.057	1.078	1.083	0.996	0.68	204,487,488,490,491,492,493,494,495,515,517,518,51 9,526,527,530,531,534,538,548,564,565,566,567,568, 570,571,625,626,630,631,633,643,644,645,646,647,64 9,657,658,659,660,661,663,664,665,666,670,680
P21802-14	0.991	173	1.001	575.211	0.635	0.684	0.932	0.308	1.071	0.287	0.653	34,35,36,37,38,39,40,41,42,43,44,71,73,74,75,76,78 ,104,105,106,108,115,116,117,118,119,164,166,167,1 68,169,170,173,174,175,176,178,217,226,247,249,250 ,251,252
P21802-15	1.047	221	1.064	777.238	0.528	0.764	0.962	0.995	1.026	0.969	0.66	371,372,374,375,376,377,378,379,399,401,402,403,40 8,410,411,414,415,418,422,432,448,449,450,451,454, 455,509,510,514,515,517,527,528,529,530,531,533,53 7,539,542,543,544,546,547,548,549,550
P21802-16	1.029	242	1.029	828.002	0.586	0.741	0.944	0.77	1.09	0.706	0.598	287,289,314,316,346,348,353,488,489,491,492,493,49 4,495,496,516,518,519,520,521,523,524,525,528,531, 532,535,539,549,565,566,567,568,571,572,625,627,63 1,632,634,644,645,646,647,648,660,662,663,664,665, 666,667
P21802-17	1.028	551	1.062	1959.559	0.601	0.708	0.883	0.697	0.93	0.75	0.785	189,190,191,197,198,199,200,201,203,204,206,207,20 8,209,210,211,212,213,444,445,446,447,448,487,488, 489,490,491,492,493,494,495,496,516,518,519,520,52 1,523,524,525,526,527,528,530,531,532,533,534,535, 538,539,549,565,566,567,568,569,570,571,572,575,57 6,579,580,592,594,626,627,631,632,634,644,645,646, 647,648,650,651,654,655,656,658,659,660,661,662,66 3,664,665,666,667,668,669,670,671,675,676,679,681, 710,714
P21802-18	1.041	188	0.982	727.846	0.522	0.76	1.01	0.276	1.27	0.218	0.621	199,200,201,203,204,205,206,207,208,209,219,220,57 0,572,573,576,577,579,581,582,585,586,587,588,589, 591,592,593,594,629,630,667,668,700,701,702,704,70 5
P21802-19	0.928	246	0.958	602.994	0.65	0.585	0.774	0.225	1.02	0.22	0.467	132,133,135,136,138,139,140,141,142,143,144,145,14 6,147,148,150,151,152,155,157,158,161,176,178,180, 181,182,183,184,185,186,188,189,190,191,197,198,19 9,200,209,211,212,213,214,215,216
P21802-2	1.041	122	0.99	321.734	0.485	0.76	0.982	0.434	1.246	0.348	0.643	625,647,649,653,654,655,656,657,658,659,665,666,67 0,674,675,676,678,679,680,713
P21802-20	1.052	837	1.079	2685.69	0.487	0.751	0.963	0.804	0.956	0.841	0.736	55,56,57,58,84,85,86,88,89,90,91,92,93,104,105,106 ,107,108,135,136,137,138,168,169,232,233,326,327,3 28,329,330,370,373,374,375,376,377,378,398,400,401 ,402,409,410,412,413,414,415,416,417,419,420,421,4 23,424,431,447,448,449,450,451,453,454,456,457,460 ,461,463,469,470,471,472,475,477,503,504,505,508,5 09,511,513,514,516,526,527,528,529,530,532,533,536 ,537,538,539,540,541,542,543,544,545,546,547,548,5 49,550,551,552,558,559,561,563,577,581,583,584,585 ,586,587,588,589,590,591,592,593,596,603,605,606
P21802-21	1.043	366	1.06	988.526	0.486	0.758	0.954	0.666	1.029	0.648	0.711	134,135,161,396,398,399,400,401,402,403,404,405,40 6,426,428,429,430,437,438,441,442,445,449,459,475, 476,477,478,479,481,482,534,536,537,541,542,544,55 4,555,556,557,558,560,561,562,564,565,566,567,568, 569,570,571,572,573,574,575,576,577,581,589,590,59 1,592
P21802-22	1.004	279	1.017	803.649	0.56	0.704	0.932	0.812	1.058	0.767	0.903	353,354,355,356,357,359,400,402,403,404,405,406,40 7,429,430,431,432,434,436,438,439,441,442,443,444, 445,446,448,449,452,453,532,534,537,543,555,556,55 8,559,561,562,564,565,566,567,568,569,570,571,572, 573,574,575,590,592
P21802-23	1.017	419	1.035	1250.235	0.547	0.723	0.946	0.782	1.041	0.751	0.822	329,331,333,335,375,376,378,379,380,381,382,383,40 3,405,406,407,414,415,417,418,419,420,421,422,424, 425,426,427,428,429,436,452,453,454,455,458,459,50 8,509,510,513,514,518,519,521,531,532,533,534,535, 537,538,540,541,542,543,544,545,546,547,548,549,55 0,551,553,554,558,562,563,564,566,567,568,576
P21802-3	1.046	368	1.073	1211.133	0.548	0.742	0.954	0.836	0.957	0.873	1.066	441,442,443,444,445,446,488,489,491,492,493,494,49 5,496,516,518,519,520,527,528,530,531,532,533,534, 535,537,538,539,541,542,549,563,565,566,567,568,57 1,572,621,622,623,626,631,632,634,644,645,646,647, 648,650,651,653,654,655,656,657,658,659,660,661,66 2,664,666,679,681
P21802-4	1.033	652	1.031	2635.269	0.531	0.748	0.964	0.645	1.096	0.588	0.88	82,83,85,111,112,114,115,116,117,118,119,130,131,1 33,134,161,162,163,164,165,193,194,195,196,197,230 ,231,232,255,256,257,351,352,353,354,355,357,397,3 98,400,401,402,403,404,405,425,427,428,429,436,437 ,439,440,441,442,443,444,446,447,448,450,451,458,4 74,475,476,477,480,481,483,487,488,490,496,497,498 ,499,502,504,530,531,532,535,536,540,541,543,553,5 54,555,556,557,558,559,560,563,564,565,566,568,569 ,570,571,572,573,574,575,576,577,578,579,580,585,5 86,588,589,590,604,610,611,612,613,615,616,617,618 ,619,620,623
P21802-5	1.012	687	1.016	2280.607	0.58	0.716	0.923	0.503	1.086	0.463	0.696	172,174,186,187,188,189,190,191,193,197,198,199,20 0,201,202,203,204,205,206,207,208,209,210,211,212, 213,219,220,222,224,225,229,438,439,440,441,442,44 3,444,445,485,486,488,489,490,491,492,493,513,515, 516,517,524,525,527,528,529,530,531,532,534,535,53 8,546,562,563,564,565,568,569,571,572,575,576,578, 584,585,586,587,588,589,590,591,592,618,619,620,62 2,623,624,626,628,629,631,641,642,643,644,645,646, 647,648,650,651,652,653,654,656,657,658,659,660,66 1,662,663,664,665,666,667,668,676,677,678,692,698, 699,700,701,702,703,704,705,706,707,708,718,720,72 1
P21802-6	1.054	343	1.044	1179.577	0.472	0.779	1.063	0.813	1.113	0.73	0.945	347,440,441,442,443,445,488,489,490,491,492,493,51 5,516,517,524,525,527,528,529,530,531,532,534,535, 538,539,618,619,620,623,624,628,642,643,644,645,64 7,648,651,652,653,654,655,656,657,658,659,660,661, 662,663,664,668,674,675,676,677,678
P21802-8	1.07	204	1.014	672.966	0.541	0.803	0.972	0.469	1.249	0.375	0.529	170,171,172,173,223,250,251,253,284,347,348,528,53 1,623,624,644,645,647,651,652,654,655,656,657,658, 659,660,661,662,663,664,665,675,676,677,678

Protein Structure and Feature Comparision

Protein Structure Comparision Using Template Modeling Scores (TM-score).

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)

3D view using mol* of P21802-1_P21802-1_5eg3_A.pdb

Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of P21802-1_5eg3_A_P21802-14.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-15.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-16.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-17.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-18.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-19.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-2.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-20.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-21.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-22.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-23.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-3.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-4.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-5.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-6.pdb

3D view using mol* of P21802-1_5eg3_A_P21802-8.pdb

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of P21802-1_P21802-14.pdb

3D view using mol* of P21802-1_P21802-15.pdb

3D view using mol* of P21802-1_P21802-16.pdb

3D view using mol* of P21802-1_P21802-17.pdb

3D view using mol* of P21802-1_P21802-18.pdb

3D view using mol* of P21802-1_P21802-19.pdb

3D view using mol* of P21802-1_P21802-2.pdb

3D view using mol* of P21802-1_P21802-20.pdb

3D view using mol* of P21802-1_P21802-21.pdb

3D view using mol* of P21802-1_P21802-22.pdb

3D view using mol* of P21802-1_P21802-23.pdb

3D view using mol* of P21802-1_P21802-3.pdb

3D view using mol* of P21802-1_P21802-4.pdb

3D view using mol* of P21802-1_P21802-5.pdb

3D view using mol* of P21802-1_P21802-6.pdb

3D view using mol* of P21802-1_P21802-8.pdb

Protein Feature Comparison of the protein sequendary structures among the protiens.

./stats/secondary_structure/figure/P21802-1_vs_P21802-14.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-15.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-16.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-17.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-18.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-19.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-2.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-20.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-21.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-22.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-23.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-3.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-4.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-5.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-6.png

./stats/secondary_structure/figure/P21802-1_vs_P21802-8.png

Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.

./stats/relative_asa/P21802-1_vs_P21802-14.png

./stats/relative_asa/P21802-1_vs_P21802-15.png

./stats/relative_asa/P21802-1_vs_P21802-16.png

./stats/relative_asa/P21802-1_vs_P21802-17.png

./stats/relative_asa/P21802-1_vs_P21802-18.png

./stats/relative_asa/P21802-1_vs_P21802-19.png

./stats/relative_asa/P21802-1_vs_P21802-2.png

./stats/relative_asa/P21802-1_vs_P21802-20.png

./stats/relative_asa/P21802-1_vs_P21802-21.png

./stats/relative_asa/P21802-1_vs_P21802-22.png

./stats/relative_asa/P21802-1_vs_P21802-23.png

./stats/relative_asa/P21802-1_vs_P21802-3.png

./stats/relative_asa/P21802-1_vs_P21802-4.png

./stats/relative_asa/P21802-1_vs_P21802-5.png

./stats/relative_asa/P21802-1_vs_P21802-6.png

./stats/relative_asa/P21802-1_vs_P21802-8.png

Protein-Protein Interaction

Interactors from UniProt.

Accession_id

Subsection

Start

End

Funcitonal feature

Splicing information

Interactors from STRING.

Gene name

Interactors

Related Drugs to FGFR2

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession	Gene name	DrugBank ID	Drug name	Drug group	Actions
P21802	FGFR2	DB12010	Fostamatinib	approved, investigational	inhibitor
P21802	FGFR2	DB00039	Palifermin	approved	agonist, binder
P21802	FGFR2	DB15685	Selpercatinib	approved, investigational	inhibitor
P21802	FGFR2	DB11886	Infigratinib	approved, investigational	inhibitor
P21802	FGFR2	DB17587	KIN-3248	investigational	inhibitor
P21802	FGFR2	DB08896	Regorafenib	approved	inhibitor
P21802	FGFR2	DB01109	Heparin	approved, investigational
P21802	FGFR2	DB12147	Erdafitinib	approved, investigational	inhibitor
P21802	FGFR2	DB01901	Sucrosofate	experimental	ligand
P21802	FGFR2	DB09078	Lenvatinib	approved, investigational	inhibitor
P21802	FGFR2	DB02491	4-[4-(1-Amino-1-Methylethyl)Phenyl]-5-Chloro-N-[4-(2-Morpholin-4-Ylethyl)Phenyl]Pyrimidin-2-Amine	experimental
P21802	FGFR2	DB15822	Pralsetinib	approved, investigational	inhibitor
P21802	FGFR2	DB15102	Pemigatinib	approved, investigational	inhibitor
P21802	FGFR2	DB09079	Nintedanib	approved	inhibitor
P21802	FGFR2	DB02058	3-[4-(1-formylpiperazin-4-yl)-benzylidenyl]-2-indolinone	experimental
P21802	FGFR2	DB08901	Ponatinib	approved, investigational	inhibitor
P21802	FGFR2	DB10772	Foreskin keratinocyte (neonatal)	approved	agonist
P21802	FGFR2	DB10770	Foreskin fibroblast (neonatal)	approved	agonist
P21802	FGFR2	DB15149	Futibatinib	approved, investigational	inhibitor

Related Diseases to FGFR2

Previous studies relating to the alternative splicing of FGFR2 and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
FGFR2	1648704	Multiple mRNAs code for proteins related to the BEK fibroblast growth factor receptor.	The BEK transmembrane protein tyrosine kinase is a receptor for both acidic and basic fibroblast growth factors. We identify several different transcripts which code for BEK-related proteins. These proteins differ from BEK in regions expected to control receptor activity. Thus, some of the proteins have altered extracellular, ligand-binding domains, and others an altered carboxy-terminal tail. Still other forms of BEK differ only in their juxtamembrane domains. Sequencing of parts of the BEK gene shows that alternative splicing of the premessenger can account for at least some of this diversity. In particular, an apparently tissue specific, mutually exclusive splicing of two internal exons permits both the previously described K-SAM mRNA and the BEK mRNA to be derived from the same premessenger.	D000230	Adenocarcinoma
FGFR2	1648704	Multiple mRNAs code for proteins related to the BEK fibroblast growth factor receptor.	The BEK transmembrane protein tyrosine kinase is a receptor for both acidic and basic fibroblast growth factors. We identify several different transcripts which code for BEK-related proteins. These proteins differ from BEK in regions expected to control receptor activity. Thus, some of the proteins have altered extracellular, ligand-binding domains, and others an altered carboxy-terminal tail. Still other forms of BEK differ only in their juxtamembrane domains. Sequencing of parts of the BEK gene shows that alternative splicing of the premessenger can account for at least some of this diversity. In particular, an apparently tissue specific, mutually exclusive splicing of two internal exons permits both the previously described K-SAM mRNA and the BEK mRNA to be derived from the same premessenger.	D001943	Breast Neoplasms
FGFR2	1648704	Multiple mRNAs code for proteins related to the BEK fibroblast growth factor receptor.	The BEK transmembrane protein tyrosine kinase is a receptor for both acidic and basic fibroblast growth factors. We identify several different transcripts which code for BEK-related proteins. These proteins differ from BEK in regions expected to control receptor activity. Thus, some of the proteins have altered extracellular, ligand-binding domains, and others an altered carboxy-terminal tail. Still other forms of BEK differ only in their juxtamembrane domains. Sequencing of parts of the BEK gene shows that alternative splicing of the premessenger can account for at least some of this diversity. In particular, an apparently tissue specific, mutually exclusive splicing of two internal exons permits both the previously described K-SAM mRNA and the BEK mRNA to be derived from the same premessenger.	D002583	Uterine Cervical Neoplasms
FGFR2	1652059	The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain.	To determine the mechanisms by which multiple forms of fibroblast growth factor (FGF) receptors are generated, we have mapped the arrangement of exons and introns in the human FGF receptor 1 (FGFR 1) gene (flg). We found three alternative exons encoding a portion of the third immunoglobulin (Ig)-like domain of the receptor. One of these alternatives encodes a sequence that is part of a secreted form of FGFR 1. The other two encode sequences that are likely part of transmembrane forms of FGFR 1. One of these forms has not been previously reported in published cDNAs. Also, we have determined the structural organization of a portion of the human FGFR 2 gene (bek) and found a similar arrangement of alternative exons for the third Ig-like domain. The arrangement of these genes suggests that there are conserved mechanisms governing the expression of secreted FGF receptors as well as the expression of at least two distinct membrane-spanning forms of the FGF receptors. The diverse forms appear to be generated by alternative splicing of mRNA and selective use of polyadenylation signals.	D001254	Astrocytoma
FGFR2	1652059	The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain.	To determine the mechanisms by which multiple forms of fibroblast growth factor (FGF) receptors are generated, we have mapped the arrangement of exons and introns in the human FGF receptor 1 (FGFR 1) gene (flg). We found three alternative exons encoding a portion of the third immunoglobulin (Ig)-like domain of the receptor. One of these alternatives encodes a sequence that is part of a secreted form of FGFR 1. The other two encode sequences that are likely part of transmembrane forms of FGFR 1. One of these forms has not been previously reported in published cDNAs. Also, we have determined the structural organization of a portion of the human FGFR 2 gene (bek) and found a similar arrangement of alternative exons for the third Ig-like domain. The arrangement of these genes suggests that there are conserved mechanisms governing the expression of secreted FGF receptors as well as the expression of at least two distinct membrane-spanning forms of the FGF receptors. The diverse forms appear to be generated by alternative splicing of mRNA and selective use of polyadenylation signals.	D009447	Neuroblastoma
FGFR2	1652059	The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain.	To determine the mechanisms by which multiple forms of fibroblast growth factor (FGF) receptors are generated, we have mapped the arrangement of exons and introns in the human FGF receptor 1 (FGFR 1) gene (flg). We found three alternative exons encoding a portion of the third immunoglobulin (Ig)-like domain of the receptor. One of these alternatives encodes a sequence that is part of a secreted form of FGFR 1. The other two encode sequences that are likely part of transmembrane forms of FGFR 1. One of these forms has not been previously reported in published cDNAs. Also, we have determined the structural organization of a portion of the human FGFR 2 gene (bek) and found a similar arrangement of alternative exons for the third Ig-like domain. The arrangement of these genes suggests that there are conserved mechanisms governing the expression of secreted FGF receptors as well as the expression of at least two distinct membrane-spanning forms of the FGF receptors. The diverse forms appear to be generated by alternative splicing of mRNA and selective use of polyadenylation signals.	D012509	Sarcoma
FGFR2	18593464	Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.	Despite the advent of biological therapies for the treatment of rheumatoid arthritis, there is a compelling need to develop alternative therapeutic targets for nonresponders to existing treatments. Soluble receptors occur naturally in vivo, such as the splice variant of the cell surface receptor for vascular endothelial growth factor (VEGF)--a key regulator of angiogenesis in rheumatoid arthritis. Bioinformatics analyses predict that the majority of human genes undergo alternative splicing, generating proteins--many of which may have regulatory functions. The objective of the present study was to identify alternative splice variants (ASV) from cell surface receptor genes, and to determine whether the novel proteins encoded exert therapeutic activity in an in vivo model of arthritis.	D001172	Arthritis, Rheumatoid
FGFR2	18593464	Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.	Despite the advent of biological therapies for the treatment of rheumatoid arthritis, there is a compelling need to develop alternative therapeutic targets for nonresponders to existing treatments. Soluble receptors occur naturally in vivo, such as the splice variant of the cell surface receptor for vascular endothelial growth factor (VEGF)--a key regulator of angiogenesis in rheumatoid arthritis. Bioinformatics analyses predict that the majority of human genes undergo alternative splicing, generating proteins--many of which may have regulatory functions. The objective of the present study was to identify alternative splice variants (ASV) from cell surface receptor genes, and to determine whether the novel proteins encoded exert therapeutic activity in an in vivo model of arthritis.	D004195	Disease Models, Animal
FGFR2	22345151	FGFR2 isoforms support epithelial-stromal interactions in thyroid cancer progression.	Alternate splicing yields two distinct isoforms of the fibroblast growth factor (FGF) receptor FGFR2-IIIb and FGFR2-IIIc varying their extracellular structure in human thyroid cancer, in which FGFR expression is commonly dysregulated. In this study, we characterized the function of these variants in modulating thyroid cancer behavior. Enforced expression of either FGFR2-IIIb or FGFR2-IIIc in thyroid epithelial cancer cells reduced expression of fibronectin, MAGE-A3 and MMP9, while increasing p21 and enhancing Rb dephosphorylation. Consistent with these tumor-suppressive properties, FGFR2-IIIb and FGFR2-IIIc each diminished invasive behavior in vitro and reduced tumor growth and metastasis in vivo. Notably, these effects contrasted with those produced by expression of these FGFR isoforms in fibroblasts, in which they both stimulated cell growth. Moreover, in xenograft tumors generated by coimplantation of epithelial and fibroblast cells expressing that same isoform, there was no significant effect on tumor progression. Conversely, FGFR2-IIIb expression in epithelial cells yielded higher FGF4/FGF7 expression that, in the presence of FGFR2-IIIc-expressing fibroblasts, enhanced tumor progression. Together, our findings highlight the importance of cellular context in assigning growth properties to growth factor receptor isoforms. More specifically, they show how alternative splicing of FGFR2 yields heteroisoforms critical to the growth-promoting actions of FGFs that exert distinct epithelial-stromal effects in thyroid cancer.	D018450	Disease Progression
FGFR2	22345151	FGFR2 isoforms support epithelial-stromal interactions in thyroid cancer progression.	Alternate splicing yields two distinct isoforms of the fibroblast growth factor (FGF) receptor FGFR2-IIIb and FGFR2-IIIc varying their extracellular structure in human thyroid cancer, in which FGFR expression is commonly dysregulated. In this study, we characterized the function of these variants in modulating thyroid cancer behavior. Enforced expression of either FGFR2-IIIb or FGFR2-IIIc in thyroid epithelial cancer cells reduced expression of fibronectin, MAGE-A3 and MMP9, while increasing p21 and enhancing Rb dephosphorylation. Consistent with these tumor-suppressive properties, FGFR2-IIIb and FGFR2-IIIc each diminished invasive behavior in vitro and reduced tumor growth and metastasis in vivo. Notably, these effects contrasted with those produced by expression of these FGFR isoforms in fibroblasts, in which they both stimulated cell growth. Moreover, in xenograft tumors generated by coimplantation of epithelial and fibroblast cells expressing that same isoform, there was no significant effect on tumor progression. Conversely, FGFR2-IIIb expression in epithelial cells yielded higher FGF4/FGF7 expression that, in the presence of FGFR2-IIIc-expressing fibroblasts, enhanced tumor progression. Together, our findings highlight the importance of cellular context in assigning growth properties to growth factor receptor isoforms. More specifically, they show how alternative splicing of FGFR2 yields heteroisoforms critical to the growth-promoting actions of FGFs that exert distinct epithelial-stromal effects in thyroid cancer.	D013964	Thyroid Neoplasms

Clinically important variants in FGFR2

(ClinVar, 04/20/2024)

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