AVEN_HUMAN - dbPTM
AVEN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AVEN_HUMAN
UniProt AC Q9NQS1
Protein Name Cell death regulator Aven
Gene Name AVEN
Organism Homo sapiens (Human).
Sequence Length 362
Subcellular Localization Endomembrane system
Peripheral membrane protein. Associated with intracellular membranes.
Protein Description Protects against apoptosis mediated by Apaf-1..
Protein Sequence MQAERGARGGRGRRPGRGRPGGDRHSERPGAAAAVARGGGGGGGGDGGGRRGRGRGRGFRGARGGRGGGGAPRGSRREPGGWGAGASAPVEDDSDAETYGEENDEQGNYSKRKIVSNWDRYQDIEKEVNNESGESQRGTDFSVLLSSAGDSFSQFRFAEEKEWDSEASCPKQNSAFYVDSELLVRALQELPLCLRLNVAAELVQGTVPLEVPQVKPKRTDDGKGLGMQLKGPLGPGGRGPIFELKSVAAGCPVLLGKDNPSPGPSRDSQKPTSPLQSAGDHLEEELDLLLNLDAPIKEGDNILPDQTSQDLKSKEDGEVVQEEEVCAKPSVTEEKNMEPEQPSTSKNVTEEELEDWLDSMIS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
17DimethylationGRGRRPGRGRPGGDR
CCCCCCCCCCCCCCC
40.40-
28DimethylationGGDRHSERPGAAAAV
CCCCCCCCCCCCCHH
37.66-
28MethylationGGDRHSERPGAAAAV
CCCCCCCCCCCCCHH
37.66-
37DimethylationGAAAAVARGGGGGGG
CCCCHHHCCCCCCCC
37.38-
37MethylationGAAAAVARGGGGGGG
CCCCHHHCCCCCCCC
37.38-
50MethylationGGGDGGGRRGRGRGR
CCCCCCCCCCCCCCC
40.95-
87PhosphorylationGGWGAGASAPVEDDS
CCCCCCCCCCCCCCC
31.9930206219
94PhosphorylationSAPVEDDSDAETYGE
CCCCCCCCCHHHHCC
51.5522167270
98PhosphorylationEDDSDAETYGEENDE
CCCCCHHHHCCCCCC
38.2522167270
99PhosphorylationDDSDAETYGEENDEQ
CCCCHHHHCCCCCCC
17.6622167270
109PhosphorylationENDEQGNYSKRKIVS
CCCCCCCCCCHHCCC
23.5323403867
110PhosphorylationNDEQGNYSKRKIVSN
CCCCCCCCCHHCCCC
29.9523403867
116PhosphorylationYSKRKIVSNWDRYQD
CCCHHCCCCHHHHHH
35.36-
121PhosphorylationIVSNWDRYQDIEKEV
CCCCHHHHHHHHHHH
14.2028796482
129UbiquitinationQDIEKEVNNESGESQ
HHHHHHHHCCCCCCC
47.8722817900
131UbiquitinationIEKEVNNESGESQRG
HHHHHHCCCCCCCCC
55.7222817900
135PhosphorylationVNNESGESQRGTDFS
HHCCCCCCCCCCCHH
28.8018571408
140UbiquitinationGESQRGTDFSVLLSS
CCCCCCCCHHHEECC
36.3322817900
142UbiquitinationSQRGTDFSVLLSSAG
CCCCCCHHHEECCCC
18.0522817900
144UbiquitinationRGTDFSVLLSSAGDS
CCCCHHHEECCCCCC
3.5823000965
150UbiquitinationVLLSSAGDSFSQFRF
HEECCCCCCHHHCCC
46.3422817900
151PhosphorylationLLSSAGDSFSQFRFA
EECCCCCCHHHCCCC
26.3628348404
152UbiquitinationLSSAGDSFSQFRFAE
ECCCCCCHHHCCCCH
8.7222817900
155UbiquitinationAGDSFSQFRFAEEKE
CCCCHHHCCCCHHHC
7.2223000965
161UbiquitinationQFRFAEEKEWDSEAS
HCCCCHHHCCCCCCC
56.4629967540
165UbiquitinationAEEKEWDSEASCPKQ
CHHHCCCCCCCCCCC
35.8123000965
177PhosphorylationPKQNSAFYVDSELLV
CCCCCCEEECHHHHH
11.7627642862
215UbiquitinationPLEVPQVKPKRTDDG
CCCCCCCCCCCCCCC
39.3022817900
217UbiquitinationEVPQVKPKRTDDGKG
CCCCCCCCCCCCCCC
63.3122817900
230MethylationKGLGMQLKGPLGPGG
CCCCCEEECCCCCCC
41.4124129315
230UbiquitinationKGLGMQLKGPLGPGG
CCCCCEEECCCCCCC
41.4123000965
238MethylationGPLGPGGRGPIFELK
CCCCCCCCCCCHHHH
54.34-
245MethylationRGPIFELKSVAAGCP
CCCCHHHHHHHCCCC
35.37-
245UbiquitinationRGPIFELKSVAAGCP
CCCCHHHHHHHCCCC
35.3729967540
246PhosphorylationGPIFELKSVAAGCPV
CCCHHHHHHHCCCCE
29.6124732914
261PhosphorylationLLGKDNPSPGPSRDS
EECCCCCCCCCCCCC
49.0625159151
265PhosphorylationDNPSPGPSRDSQKPT
CCCCCCCCCCCCCCC
55.4223401153
268PhosphorylationSPGPSRDSQKPTSPL
CCCCCCCCCCCCCCC
38.7123663014
272PhosphorylationSRDSQKPTSPLQSAG
CCCCCCCCCCCCCCC
50.4325159151
273PhosphorylationRDSQKPTSPLQSAGD
CCCCCCCCCCCCCCC
31.9425159151
277PhosphorylationKPTSPLQSAGDHLEE
CCCCCCCCCCCCHHH
41.7323663014
307PhosphorylationDNILPDQTSQDLKSK
CCCCCCCCCHHHHHC
35.4220068231
308PhosphorylationNILPDQTSQDLKSKE
CCCCCCCCHHHHHCC
18.9618571408
328AcetylationQEEEVCAKPSVTEEK
CHHHCCCCCCCCCCC
32.4726051181
330PhosphorylationEEVCAKPSVTEEKNM
HHCCCCCCCCCCCCC
40.7523312004
332PhosphorylationVCAKPSVTEEKNMEP
CCCCCCCCCCCCCCC
42.6423312004

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
135SPhosphorylationKinaseATMQ13315
PSP
308SPhosphorylationKinaseATMQ13315
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AVEN_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AVEN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
B2CL1_HUMANBCL2L1physical
10949025
BCL2_HUMANBCL2physical
10949025
APAF_HUMANAPAF1physical
10949025

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AVEN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.

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