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:CAMK2G

Protein Summary

Gene summary

Gene name: CAMK2G
ASpdb.0 ID: 818
	Gene
Gene symbol	CAMK2G
Gene ID	818
Gene name	calcium/calmodulin dependent protein kinase II gamma
Synonyms	CAMK\|CAMK-II\|CAMKG\|MRD59
Cytomap	10q22.2
Type of gene	protein-coding
Description	calcium/calmodulin-dependent protein kinase type II subunit gammacaMK-II subunit gammacalcium/calmodulin-dependent protein kinase (CaM kinase) II gamma
Modification date	20240403
UniProtAcc	Q13555

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	CAMK2G	GO:0005954	calcium- and calmodulin-dependent protein kinase complex	20668654

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
Q13555-1	Q13555-1_2v7o_A.pdb	2V7O	X-ray	2.25	A	5	302

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
Q13555	CAMK2G	Q13555-1	Q13555-10	558	495	331	364	Deletion	none	none	330	330
Q13555	CAMK2G	Q13555-1	Q13555-10	558	495	396	425	Substitution	GRVPEGRSSRDRTAPSAGMQPQPSLCSSAM	V	362	362
Q13555	CAMK2G	Q13555-1	Q13555-11	558	539	316	316	Substitution	A	VGRQSSAPASPAASAAGLAGQA	316	337
Q13555	CAMK2G	Q13555-1	Q13555-11	558	539	331	341	Deletion	none	none	351	351
Q13555	CAMK2G	Q13555-1	Q13555-11	558	539	396	426	Substitution	GRVPEGRSSRDRTAPSAGMQPQPSLCSSAMR	VR	406	407
Q13555	CAMK2G	Q13555-1	Q13555-2	558	547	331	341	Deletion	none	none	330	330
Q13555	CAMK2G	Q13555-1	Q13555-3	558	524	331	364	Deletion	none	none	330	330
Q13555	CAMK2G	Q13555-1	Q13555-4	558	529	396	425	Substitution	GRVPEGRSSRDRTAPSAGMQPQPSLCSSAM	V	396	396
Q13555	CAMK2G	Q13555-1	Q13555-5	558	527	315	315	Substitution	S	SVGRQSSAPASPAASAAGLAGQ	315	336
Q13555	CAMK2G	Q13555-1	Q13555-5	558	527	341	363	Deletion	none	none	361	361
Q13555	CAMK2G	Q13555-1	Q13555-5	558	527	396	425	Substitution	GRVPEGRSSRDRTAPSAGMQPQPSLCSSAM	V	394	394
Q13555	CAMK2G	Q13555-1	Q13555-6	558	588	315	315	Substitution	S	SVGRQSSAPASPAASAAGLAGQ	315	336
Q13555	CAMK2G	Q13555-1	Q13555-6	558	588	397	398	Substitution	RV	APLRTGNGSSV	418	428
Q13555	CAMK2G	Q13555-1	Q13555-7	558	533	331	364	Deletion	none	none	330	330
Q13555	CAMK2G	Q13555-1	Q13555-7	558	533	397	398	Substitution	RV	APLRTGNGSSV	363	373
Q13555	CAMK2G	Q13555-1	Q13555-8	558	556	331	341	Deletion	none	none	330	330
Q13555	CAMK2G	Q13555-1	Q13555-8	558	556	397	398	Substitution	RV	APLRTGNGSSV	386	396
Q13555	CAMK2G	Q13555-1	Q13555-9	558	542	331	341	Deletion	none	none	330	330
Q13555	CAMK2G	Q13555-1	Q13555-9	558	542	351	364	Deletion	none	none	339	339
Q13555	CAMK2G	Q13555-1	Q13555-9	558	542	397	398	Substitution	RV	APLRTGNGSSV	372	382

Multiple sequence alignment of our canonical and alternatively spliced CAMK2G

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CAMK2G

UniProt-id	ENSG	ENST	ENSP
Q13555-10	ENSG00000148660.22	ENST00000351293.7	ENSP00000277853.5
Q13555-11	ENSG00000148660.22	ENST00000680035.1	ENSP00000505103.1
Q13555-4	ENSG00000148660.22	ENST00000305762.11	ENSP00000307082.7
Q13555-5	ENSG00000148660.22	ENST00000322635.7	ENSP00000315599.3

UniProt-id	NM ID	NP ID
Q13555-10	NM_001222.3	NP_001213.2
Q13555-11	NM_001204492.1	NP_001191421.1
Q13555-5	NM_172169.2	NP_751909.1

Amino acid sequences of our canonical and alternatively spliced CAMK2G

accession_id	Protein sequence
Q13555-1	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKKRKSSSSVHLMPQSNNKNSLVSPAQEPAPL QTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKGRVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYT KICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDG
Q13555-10	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKEPQTTVVHNATDGIKGSTESCNTTTEDEDL KVRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIR
Q13555-11	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSVGRQSSAPASPAASAAGLAGQAAKSLLNKKSDGGVKPQSNNKNSL VSPAQEPAPLQTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKVRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLV
Q13555-2	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKPQSNNKNSLVSPAQEPAPLQTAMEPQTTVV HNATDGIKGSTESCNTTTEDEDLKGRVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFE PEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWLNVHYHCSG
Q13555-3	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKEPQTTVVHNATDGIKGSTESCNTTTEDEDL KGRVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLS
Q13555-4	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKKRKSSSSVHLMPQSNNKNSLVSPAQEPAPL QTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKVRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYF
Q13555-5	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSVGRQSSAPASPAASAAGLAGQAAKSLLNKKSDGGVKKRKSSSSVH LMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKVRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFEN
Q13555-6	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSVGRQSSAPASPAASAAGLAGQAAKSLLNKKSDGGVKKRKSSSSVH LMPQSNNKNSLVSPAQEPAPLQTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKGAPLRTGNGSSVPEGRSSRDRTAPSAGMQPQPSL CSSAMRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIA
Q13555-7	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKEPQTTVVHNATDGIKGSTESCNTTTEDEDL KGAPLRTGNGSSVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFH
Q13555-8	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKPQSNNKNSLVSPAQEPAPLQTAMEPQTTVV HNATDGIKGSTESCNTTTEDEDLKGAPLRTGNGSSVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYTKI CDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKW
Q13555-9	MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGY LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHP WVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKPQSNNKNSLEPQTTVVHNATDGIKGSTESC NTTTEDEDLKGAPLRTGNGSSVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALG NLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWLNVHYHCSGAPAAP

Protein Functional Features

Main function of this protein. (from UniProt)

CAMK2G (go to UniProt):Q13555

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
Q13555	Region	294	316	Note=Calmodulin-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:20668654;Dbxref=PMID:20668654	Type=Substitution;Start=316;End=316
Q13555	Region	294	316	Note=Calmodulin-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:20668654;Dbxref=PMID:20668654	Type=Substitution;Start=315;End=315
Q13555	Region	294	316	Note=Calmodulin-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:20668654;Dbxref=PMID:20668654	Type=Substitution;Start=315;End=315
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=364
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=341
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=341
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=364
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=341;End=363
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=364
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=341
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=341
Q13555	Region	324	353	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=351;End=364
Q13555	Region	376	423	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425
Q13555	Region	376	423	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=426
Q13555	Region	376	423	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425
Q13555	Region	376	423	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425
Q13555	Region	376	423	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=397;End=398
Q13555	Region	376	423	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=397;End=398
Q13555	Region	376	423	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=397;End=398
Q13555	Region	376	423	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=397;End=398
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=364
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=341
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=341
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=364
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=341;End=363
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=364
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=341
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=331;End=341
Q13555	Compositional bias	336	353	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=351;End=364
Q13555	Compositional bias	386	404	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425
Q13555	Compositional bias	386	404	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=426
Q13555	Compositional bias	386	404	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425
Q13555	Compositional bias	386	404	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425
Q13555	Compositional bias	386	404	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=397;End=398
Q13555	Compositional bias	386	404	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=397;End=398
Q13555	Compositional bias	386	404	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=397;End=398
Q13555	Compositional bias	386	404	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=397;End=398
Q13555	Compositional bias	408	423	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425
Q13555	Compositional bias	408	423	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=426
Q13555	Compositional bias	408	423	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425
Q13555	Compositional bias	408	423	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=396;End=425

Gene Isoform Structures and Expression Levels for CAMK2G

Gene structures of our canonical and alternative spliced genes of CAMK2G
* 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 Q13555-1

3D view using mol* of Q13555-10

3D view using mol* of Q13555-11

3D view using mol* of Q13555-2

3D view using mol* of Q13555-3

3D view using mol* of Q13555-4

3D view using mol* of Q13555-5

3D view using mol* of Q13555-6

3D view using mol* of Q13555-7

3D view using mol* of Q13555-8

3D view using mol* of Q13555-9

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 Q13555-1

pLDDT distribution across the protein length of Q13555-10

pLDDT distribution across the protein length of Q13555-11

pLDDT distribution across the protein length of Q13555-2

pLDDT distribution across the protein length of Q13555-3

pLDDT distribution across the protein length of Q13555-4

pLDDT distribution across the protein length of Q13555-5

pLDDT distribution across the protein length of Q13555-6

pLDDT distribution across the protein length of Q13555-7

pLDDT distribution across the protein length of Q13555-8

pLDDT distribution across the protein length of Q13555-9

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 Q13555-1

Ramachandran plot of Q13555-11

Ramachandran plot of Q13555-2

Ramachandran plot of Q13555-3

Ramachandran plot of Q13555-5

Ramachandran plot of Q13555-6

Ramachandran plot of Q13555-8

Ramachandran plot of Q13555-9

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
Q13555-1	1.03	588	1.069	2472.001	0.627	0.701	0.852	0.77	0.896	0.859	1.003	20,21,22,23,24,25,26,28,41,43,45,49,50,51,53,54,57 ,58,60,61,65,74,90,91,92,93,94,96,135,138,139,140, 141,143,156,157,158,159,160,162,171,172,173,174,17 5,176,177,178,179,180,181,202,206,211,212,213,214, 215,216,217,219,222,290,293,294,297,298,299,300,30 1,302,304,305,306,308,309,310,312,313,315,316,363, 364,365,366,367,368,369,370,371,422,424,425,426,42 8,429,431,432,433,435,438,439,442,443,451,452,483, 486,487,488,489,490,491,492,516,517,518,524,525,53 7,540,541,542,543
Q13555-10	1.121	147	1.043	290.178	0.46	0.88	1.198	1.14	1.304	0.874	0.795	378,379,386,398,400,412,415,416,419,420,422,423,42 5,426,427,450,452,454,455,456,457,458,464,466,468, 470,484,490,491,492,493,494,495
Q13555-11	1.074	126	1.12	486.717	0.584	0.743	0.938	1	0.814	1.229	0.804	138,140,177,178,179,180,202,206,210,211,212,213,21 4,215,216,217,218,219,222,290,293,294,297,298,299, 301,302,303,305,306,409
Q13555-2	1.059	162	1.089	691.488	0.601	0.755	0.882	0.953	0.932	1.023	0.534	20,21,23,24,25,26,28,41,43,45,50,53,54,56,57,58,60 ,61,74,90,91,92,93,135,138,140,141,143,156,157,158 ,159,160,162,171,172,173,174,175,176,357,358,359
Q13555-3	1.12	182	1.164	507.64	0.483	0.808	1.029	1.308	0.802	1.631	0.87	407,408,415,427,428,429,441,444,445,448,449,452,45 4,456,479,481,483,484,485,486,487,491,493,495,497, 499,513,515,518,519,520,521,522,523
Q13555-4	1.041	479	1.077	2257.283	0.614	0.72	0.88	0.791	0.903	0.876	0.718	20,21,22,23,24,25,26,28,30,41,43,45,50,51,53,54,56 ,57,58,60,61,74,90,91,92,93,94,96,97,135,138,139,1 40,141,143,156,157,158,159,160,161,162,172,173,174 ,175,176,177,178,179,180,202,206,211,212,213,214,2 15,216,217,218,219,222,223,290,293,294,296,297,298 ,299,300,301,302,303,304,305,306,308,309,312,313,3 16,362,363,364,365,366,367,368,369,370,371,373,374 ,395,396,398,399,400,402,403,406,467,468,469,470
Q13555-5	1.08	287	1.136	1208.389	0.596	0.734	0.885	1.064	0.75	1.419	1.131	20,23,24,25,26,28,41,43,45,50,54,57,58,61,65,74,90 ,91,92,93,94,96,134,136,138,139,140,141,143,156,15 7,158,159,160,177,178,179,180,202,205,206,211,212, 213,214,215,216,217,219,222,230,231,232,234,290,29 3,294,297,298,301,302,305,306,309,313
Q13555-6	1.131	152	1.166	426.006	0.42	0.841	1.051	1.102	0.854	1.29	1.918	471,472,479,491,492,493,505,508,509,512,513,516,51 8,519,520,543,545,547,548,557,558,559,561,563,577, 579,582,583,584,585,586
Q13555-7	1.115	197	1.16	507.64	0.476	0.802	1.019	1.165	0.803	1.451	1.388	416,417,424,436,437,438,450,453,454,457,458,461,46 5,488,490,492,493,494,495,500,502,503,504,506,508, 522,524,527,528,529,530,531,532
Q13555-8	1.178	94	1.185	132.398	0.329	0.971	1.223	2.643	0.948	2.789	0.459	20,28,41,43,74,90,91,92,93,140,141,143,156,157,158 ,356,357,358,359,360
Q13555-9	1.158	128	1.099	234.269	0.319	0.934	1.199	1.206	1.231	0.979	0.863	24,25,26,43,45,50,54,57,58,60,61,134,136,138,140,1 41,157,158,159,160,161,340,341,342,343,344,345

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 Q13555-1_Q13555-1_2v7o_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 Q13555-1_2v7o_A_Q13555-10.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-11.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-2.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-3.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-4.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-5.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-6.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-7.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-8.pdb

3D view using mol* of Q13555-1_2v7o_A_Q13555-9.pdb

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

3D view using mol* of Q13555-1_Q13555-10.pdb

3D view using mol* of Q13555-1_Q13555-11.pdb

3D view using mol* of Q13555-1_Q13555-2.pdb

3D view using mol* of Q13555-1_Q13555-3.pdb

3D view using mol* of Q13555-1_Q13555-4.pdb

3D view using mol* of Q13555-1_Q13555-5.pdb

3D view using mol* of Q13555-1_Q13555-6.pdb

3D view using mol* of Q13555-1_Q13555-7.pdb

3D view using mol* of Q13555-1_Q13555-8.pdb

3D view using mol* of Q13555-1_Q13555-9.pdb

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

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-10.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-11.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-2.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-3.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-4.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-5.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-6.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-7.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-8.png

./stats/secondary_structure/figure/Q13555-1_vs_Q13555-9.png

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

./stats/relative_asa/Q13555-1_vs_Q13555-10.png

./stats/relative_asa/Q13555-1_vs_Q13555-11.png

./stats/relative_asa/Q13555-1_vs_Q13555-2.png

./stats/relative_asa/Q13555-1_vs_Q13555-3.png

./stats/relative_asa/Q13555-1_vs_Q13555-4.png

./stats/relative_asa/Q13555-1_vs_Q13555-5.png

./stats/relative_asa/Q13555-1_vs_Q13555-6.png

./stats/relative_asa/Q13555-1_vs_Q13555-7.png

./stats/relative_asa/Q13555-1_vs_Q13555-8.png

./stats/relative_asa/Q13555-1_vs_Q13555-9.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 CAMK2G

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession	Gene name	DrugBank ID	Drug name	Drug group	Actions
Q13555	CAMK2G	DB06616	Bosutinib	approved	inhibitor
Q13555	CAMK2G	DB12010	Fostamatinib	approved, investigational	inhibitor
Q13555	CAMK2G	DB08699	1-tert-butyl-3-(3-methylbenzyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine	experimental

Related Diseases to CAMK2G

Previous studies relating to the alternative splicing of CAMK2G and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
CAMK2G	22612808	Neuronal excitability and calcium/calmodulin-dependent protein kinase type II: location, location, location.	Calcium/calmodulin-dependent protein kinase type II (CaMKII) is a highly abundant serine/threonine kinase comprising a significant fraction of total protein in mammalian forebrain and forming a major component of the postsynaptic density. CaMKII is essential for certain forms of synaptic plasticity and memory consolidation and this is mediated through substrate binding and intramolecular phosphorylation of holoenzyme subunits. CaMKII is multifunctional; it targets a variety of cellular substrates, and this diversity depends on holoenzyme subunit composition. CaMKII comprises homooligomeric and heterooligomeric complexes generated from four subunits (Î±, Î², Î´, and Î³) encoded by separate genes that are further expanded by extensive alternative splicing to more than 30 different isoforms. Much attention has been paid to understanding the regulation of CaMKII function through its structural diversity and/or substrate specificity. However, given the importance of subunit composition to holoenzyme activity, it is likely that specificity of cellular expression of CaMKII isoforms also plays a major role in regulation of enzyme function. Herein we review the cellular colocalization of CaMKII isoforms with special regard to the cell-type specificity of isoform expression in brain. In addition, we highlight the remarkable specificity of subcellular localization by the CaMKIIÎ± isoform. In addition, we discuss the role that this cellular specificity of expression might play in propagating the type of recurrent neuronal activity associated with disorders such as temporal lobe epilepsy.	D004827	Epilepsy

Clinically important variants in CAMK2G

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance