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:DENND1A

Protein Summary

Gene summary

Gene name: DENND1A
ASpdb.0 ID: 57706
	Gene
Gene symbol	DENND1A
Gene ID	57706
Gene name	DENN domain containing 1A
Synonyms	FAM31A\|KIAA1608
Cytomap	9q33.3
Type of gene	protein-coding
Description	DENN domain-containing protein 1ADENN/MADD domain containing 1Aconnecdenn 1
Modification date	20240403
UniProtAcc	Q8TEH3

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	DENND1A	GO:0005085	guanyl-nucleotide exchange factor activity	20937701
Gene	DENND1A	GO:0005829	cytosol	-
Gene	DENND1A	GO:0030136	clathrin-coated vesicle	20937701
Gene	DENND1A	GO:0032483	regulation of Rab protein signal transduction	20937701
Gene	DENND1A	GO:0043231	intracellular membrane-bounded organelle	-

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
Q8TEH3-1	Q8TEH3-1_6ekk_B.pdb	6EKK	X-ray	1.82	B	2	394

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
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-2	1009	559	527	559	Substitution	PQPYRTLRESDSAEGDEAESPEQQVRKSTGPVP	NTIATPATLHILQKSITHFAAKFPTRGWTSSSH	527	559
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-2	1009	559	560	1009	Deletion	none	none	559	559
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-3	1009	498	497	498	Substitution	VR	AL	497	498
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-3	1009	498	499	1009	Deletion	none	none	498	498
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-4	1009	466	1	32	Deletion	none	none	0	0
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-4	1009	466	33	60	Substitution	VQRQFPEDYSDQEVLQTLTKFCFPFYVD	MLKWPIPGQVALFQILRCRGNSRRTTVT	1	28
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-4	1009	466	497	498	Substitution	VR	AL	465	466
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-4	1009	466	499	1009	Deletion	none	none	466	466
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-5	1009	529	1	30	Deletion	none	none	0	0
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-5	1009	529	31	43	Substitution	PEVQRQFPEDYSD	MLKWPIPGQVALF	1	13
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-5	1009	529	527	559	Substitution	PQPYRTLRESDSAEGDEAESPEQQVRKSTGPVP	NTIATPATLHILQKSITHFAAKFPTRGWTSSSH	497	529
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-5	1009	529	560	1009	Deletion	none	none	529	529
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-7	1009	1010	290	331	Deletion	none	none	289	289
Q8TEH3	DENND1A	Q8TEH3-1	Q8TEH3-7	1009	1010	526	526	Substitution	Q	HLVKPLRHYAVFLSEDSSDDECQREEGPSSGFTESFFFSAPFEW	484	527

Multiple sequence alignment of our canonical and alternatively spliced DENND1A

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of DENND1A

UniProt-id	ENSG	ENST	ENSP
Q8TEH3-1	ENSG00000119522.18	ENST00000373624.6	ENSP00000362727.2
Q8TEH3-2	ENSG00000119522.18	ENST00000373620.7	ENSP00000362722.3
Q8TEH3-4	ENSG00000119522.18	ENST00000373618.1	ENSP00000362720.1

UniProt-id	NM ID	NP ID
Q8TEH3-1	NM_020946.1	NP_065997.1
Q8TEH3-2	NM_024820.2	NP_079096.2

Amino acid sequences of our canonical and alternatively spliced DENND1A

accession_id	Protein sequence
Q8TEH3-1	MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLS SGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVD VNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNV DTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQ LQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLK QKDIAENGCAPTPEEQLPKTAPSPLVEAKDPKLREDRRPITVHFGQVRPPRPHVVKRPKSNIAVEGRRTSVPSPEQPQPYRTLRESDSAE GDEAESPEQQVRKSTGPVPAPPDRAASIDLLEDVFSNLDMEAALQPLGQAKSLEDLRAPKDLREQPGTFDYQRLDLGGSERSRGVTVALK LTHPYNKLWSLGQDDMAIPSKPPAASPEKPSALLGNSLALPRRPQNRDSILNPSDKEEVPTPTLGSITIPRPQGRKTPELGIVPPPPIPR PAKLQAAGAALGDVSERLQTDRDRRAALSPGLLPGVVPQGPTELLQPLSPGPGAAGTSSDALLALLDPLSTAWSGSTLPSRPATPNVATP FTPQFSFPPAGTPTPFPQPPLNPFVPSMPAAPPTLPLVSTPAGPFGAPPASLGPAFASGLLLSSAGFCAPHRSQPNLSALSMPNLFGQMP MGTHTSPLQPLGPPAVAPSRIRTLPLARSSARAAETKQGLALRPGDPPLLPPRPPQGLEPTLQPSAPQQARDPFEDLLQKTKQDVSPSPA
Q8TEH3-2	MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLS SGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVD VNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNV DTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQ LQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLK QKDIAENGCAPTPEEQLPKTAPSPLVEAKDPKLREDRRPITVHFGQVRPPRPHVVKRPKSNIAVEGRRTSVPSPEQNTIATPATLHILQK
Q8TEH3-3	MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLS SGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVD VNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNV DTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQ LQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLK
Q8TEH3-4	MLKWPIPGQVALFQILRCRGNSRRTTVTSLTVSQVGQNFTFVLTDIDSKQRFGFCRLSSGAKSCFCILSYLPWFEVFYKLLNILADYTTK RQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVDVNNMLHLYASMLYERRILIICSKLSTLTACIH GSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNVDTNTLETPFDDLQSLPNDVISSLKNRLKKVST TTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQLQLFKQFIDGRLDLLNSGEGFSDVFEEEINMG EYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDIAENGCAPTPEEQLPKTAPSPLVEAKDPK
Q8TEH3-5	MLKWPIPGQVALFQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLSSGAKSCFCILSYLPWFEVFYKLLNILADYT TKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVDVNNMLHLYASMLYERRILIICSKLSTLTAC IHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNVDTNTLETPFDDLQSLPNDVISSLKNRLKKV STTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQLQLFKQFIDGRLDLLNSGEGFSDVFEEEIN MGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDIAENGCAPTPEEQLPKTAPSPLVEAKD
Q8TEH3-7	MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLS SGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVD VNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNV DTNTLETPFDDLQSLPNDVEEPITFCEEAFVSHYRSGAMRQFLQNATQLQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYH QWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDIAENGCAPTPEEQLPKTAPSPLVEAKDPKLREDRRPITV HFGQVRPPRPHVVKRPKSNIAVEGRRTSVPSPEHLVKPLRHYAVFLSEDSSDDECQREEGPSSGFTESFFFSAPFEWPQPYRTLRESDSA EGDEAESPEQQVRKSTGPVPAPPDRAASIDLLEDVFSNLDMEAALQPLGQAKSLEDLRAPKDLREQPGTFDYQRLDLGGSERSRGVTVAL KLTHPYNKLWSLGQDDMAIPSKPPAASPEKPSALLGNSLALPRRPQNRDSILNPSDKEEVPTPTLGSITIPRPQGRKTPELGIVPPPPIP RPAKLQAAGAALGDVSERLQTDRDRRAALSPGLLPGVVPQGPTELLQPLSPGPGAAGTSSDALLALLDPLSTAWSGSTLPSRPATPNVAT PFTPQFSFPPAGTPTPFPQPPLNPFVPSMPAAPPTLPLVSTPAGPFGAPPASLGPAFASGLLLSSAGFCAPHRSQPNLSALSMPNLFGQM PMGTHTSPLQPLGPPAVAPSRIRTLPLARSSARAAETKQGLALRPGDPPLLPPRPPQGLEPTLQPSAPQQARDPFEDLLQKTKQDVSPSP

Protein Functional Features

Main function of this protein. (from UniProt)

DENND1A (go to UniProt):Q8TEH3

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
Q8TEH3	Domain	13	145	Note=UDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00304	Type=Deletion;Start=1;End=32
Q8TEH3	Domain	13	145	Note=UDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00304	Type=Substitution;Start=33;End=60
Q8TEH3	Domain	13	145	Note=UDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00304	Type=Deletion;Start=1;End=30
Q8TEH3	Domain	13	145	Note=UDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00304	Type=Substitution;Start=31;End=43
Q8TEH3	Domain	162	298	Note=CDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00304	Type=Deletion;Start=290;End=331
Q8TEH3	Domain	300	378	Note=DDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00304	Type=Deletion;Start=290;End=331
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=527;End=559
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=497;End=498
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=497;End=498
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=527;End=559
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Region	453	564	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=526;End=526
Q8TEH3	Region	648	714	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Region	648	714	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Region	648	714	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Region	648	714	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Region	796	831	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Region	796	831	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Region	796	831	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Region	796	831	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Region	928	1009	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Region	928	1009	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Region	928	1009	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Region	928	1009	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Motif	569	578	Note=Clathrin box;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:20154091;Dbxref=PMID:20154091	Type=Deletion;Start=560;End=1009
Q8TEH3	Motif	569	578	Note=Clathrin box;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:20154091;Dbxref=PMID:20154091	Type=Deletion;Start=499;End=1009
Q8TEH3	Motif	569	578	Note=Clathrin box;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:20154091;Dbxref=PMID:20154091	Type=Deletion;Start=499;End=1009
Q8TEH3	Motif	569	578	Note=Clathrin box;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:20154091;Dbxref=PMID:20154091	Type=Deletion;Start=560;End=1009
Q8TEH3	Compositional bias	535	549	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=527;End=559
Q8TEH3	Compositional bias	535	549	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Compositional bias	535	549	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Compositional bias	535	549	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=527;End=559
Q8TEH3	Compositional bias	796	815	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Compositional bias	796	815	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Compositional bias	796	815	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Compositional bias	796	815	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Compositional bias	816	831	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Compositional bias	816	831	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Compositional bias	816	831	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Compositional bias	816	831	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Compositional bias	945	961	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009
Q8TEH3	Compositional bias	945	961	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Compositional bias	945	961	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=499;End=1009
Q8TEH3	Compositional bias	945	961	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=560;End=1009

Gene Isoform Structures and Expression Levels for DENND1A

Gene structures of our canonical and alternative spliced genes of DENND1A
* 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 Q8TEH3-1

3D view using mol* of Q8TEH3-2

3D view using mol* of Q8TEH3-3

3D view using mol* of Q8TEH3-4

3D view using mol* of Q8TEH3-5

3D view using mol* of Q8TEH3-7

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 Q8TEH3-1

pLDDT distribution across the protein length of Q8TEH3-2

pLDDT distribution across the protein length of Q8TEH3-3

pLDDT distribution across the protein length of Q8TEH3-4

pLDDT distribution across the protein length of Q8TEH3-5

pLDDT distribution across the protein length of Q8TEH3-7

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 Q8TEH3-1

Ramachandran plot of Q8TEH3-2

Ramachandran plot of Q8TEH3-4

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
Q8TEH3-1	1.061	284	1.083	937.762	0.543	0.773	0.953	0.659	0.983	0.67	0.806	1,2,3,4,5,6,7,9,82,84,103,104,105,106,107,108,140, 141,143,156,157,158,159,160,161,162,163,164,165,16 8,169,171,212,213,215,216,217,219,220,221,222,223, 224,227,309,312,313,366,367,370,371,373,374,383,38 4
Q8TEH3-2	1.075	97	1.084	238.385	0.529	0.822	1.102	1.347	1.026	1.313	0.789	1,2,3,4,74,75,76,77,78,79,80,81,224,225,226,227,22 8,231,235,238,243,366,538,541,542,544,545,548,549
Q8TEH3-3	1.067	207	1.114	1120.238	0.562	0.732	0.911	0.969	0.813	1.191	0.853	1,3,4,45,46,49,53,74,75,76,77,78,79,80,81,83,224,2 25,226,227,228,231,234,235,237,238,240,241,242,243 ,362,366,435,438,439,442,443,445,446,448,449,450,4 53,490,491,492,493,494
Q8TEH3-4	1.041	152	1.092	503.181	0.584	0.691	0.866	0.869	0.805	1.08	1.288	296,297,298,299,300,301,302,303,337,340,341,343,34 4,345,346,368,371,372,375,376,383,386,387,388,390, 391,392,395,396,399
Q8TEH3-5	1.044	870	1.09	3188.528	0.581	0.705	0.892	0.772	0.839	0.921	0.862	4,6,7,9,10,12,13,15,16,18,19,22,23,44,45,46,47,48, 49,50,51,52,53,54,70,71,72,73,74,75,76,77,78,81,82 ,85,106,108,109,110,111,112,113,114,125,126,127,12 8,129,130,131,132,133,134,135,138,139,141,182,183, 185,186,187,188,189,190,191,192,193,194,195,196,19 7,198,203,204,205,206,207,208,211,213,226,230,276, 279,282,304,305,306,307,309,329,332,333,334,335,33 6,337,338,339,340,341,342,343,344,346,347,353,354, 389,390,392,393,394,397,398,400,401,404,405,407,40 8,409,410,411,412,413,415,416,419,420,422,423,426, 427,509,510,511,512,513,514,515,516,517,518,519,52 0,521,522
Q8TEH3-7	1.072	366	1.143	1203.244	0.58	0.697	0.915	1.322	0.661	2	1.374	188,192,218,219,220,221,285,286,289,290,291,292,29 3,294,295,296,297,298,300,309,312,313,316,317,319, 321,322,323,325,326,329,330,332,333,334,336,337,33 8,339,343,344,346,347,348,350,351,352,353,354,358, 359,361,362,363,365,366,367,369,370,372,373,376,37 7

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 Q8TEH3-1_Q8TEH3-1_6ekk_B.pdb

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

3D view using mol* of Q8TEH3-1_6ekk_B_Q8TEH3-2.pdb

3D view using mol* of Q8TEH3-1_6ekk_B_Q8TEH3-3.pdb

3D view using mol* of Q8TEH3-1_6ekk_B_Q8TEH3-4.pdb

3D view using mol* of Q8TEH3-1_6ekk_B_Q8TEH3-5.pdb

3D view using mol* of Q8TEH3-1_6ekk_B_Q8TEH3-7.pdb

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

3D view using mol* of Q8TEH3-1_Q8TEH3-2.pdb

3D view using mol* of Q8TEH3-1_Q8TEH3-3.pdb

3D view using mol* of Q8TEH3-1_Q8TEH3-4.pdb

3D view using mol* of Q8TEH3-1_Q8TEH3-5.pdb

3D view using mol* of Q8TEH3-1_Q8TEH3-7.pdb

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

./stats/secondary_structure/figure/Q8TEH3-1_vs_Q8TEH3-2.png