HECD3_HUMAN - dbPTM
HECD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HECD3_HUMAN
UniProt AC Q5T447
Protein Name E3 ubiquitin-protein ligase HECTD3
Gene Name HECTD3
Organism Homo sapiens (Human).
Sequence Length 861
Subcellular Localization Cytoplasm, perinuclear region.
Protein Description E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity)..
Protein Sequence MAGPGPGAVLESPRQLLGRVRFLAEAARSLRAGRPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAAGPAPGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLGDCGLQEGWLLVCRPAEGGARLVPIDTPNHLQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYAEAVQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNLKKLSDVSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPTSLVRYPRLEGTDPEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPGLVAQCLRDSESSKPSFMPRLYINRRLAMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSADTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPAVDSVLVKLLEVMEGMDKETFEFKFGKELTFTTVLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEESKEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPARIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE
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
2Acetylation------MAGPGPGAV
------CCCCCCCCC
32.6522223895
12PhosphorylationGPGAVLESPRQLLGR
CCCCCCCCHHHHHHH
22.6321815630
49PhosphorylationFVPREVLYKLYKDPA
CCCHHHHHHHHCCCC
12.2429496907
50AcetylationVPREVLYKLYKDPAG
CCHHHHHHHHCCCCC
40.9725953088
50UbiquitinationVPREVLYKLYKDPAG
CCHHHHHHHHCCCCC
40.97-
52PhosphorylationREVLYKLYKDPAGPS
HHHHHHHHCCCCCCC
14.8129496907
53UbiquitinationEVLYKLYKDPAGPSR
HHHHHHHCCCCCCCC
68.61-
59PhosphorylationYKDPAGPSRVLLPVW
HCCCCCCCCEEEEEE
33.82-
84PhosphorylationAAGPAPGTGSGPLRA
ECCCCCCCCCCCCHH
27.4128555341
86PhosphorylationGPAPGTGSGPLRAAR
CCCCCCCCCCCHHHH
36.7627251275
95PhosphorylationPLRAARDSIELRRGA
CCHHHHHHHHHCCCC
16.65-
157PhosphorylationARLVPIDTPNHLQRQ
CCEEECCCCCHHHHH
27.0628555341
192PhosphorylationTYSHRLGSRPQPAEA
HHHCCCCCCCCCHHH
45.43-
289PhosphorylationRLTMKKGTIVKKLLL
HHEECCCCEEEEEEE
31.3225690035
308UbiquitinationTDDNFMPKRVVVYGG
CCCCCCCCEEEEECC
46.14-
321UbiquitinationGGEGDNLKKLSDVSI
CCCCCCCHHHCCCCC
58.90-
322UbiquitinationGEGDNLKKLSDVSID
CCCCCCHHHCCCCCC
57.29-
327PhosphorylationLKKLSDVSIDETLIG
CHHHCCCCCCCCCCC
29.3426074081
331PhosphorylationSDVSIDETLIGDVCV
CCCCCCCCCCCCEEE
21.6726074081
343PhosphorylationVCVLEDMTVHLPIIE
EEEECCCEEEECEEE
19.6626074081
372PhosphorylationLRGVKIKSSRQRELG
EECEEECCHHHHHCC
33.9427174698
373PhosphorylationRGVKIKSSRQRELGL
ECEEECCHHHHHCCC
27.6827174698
388PhosphorylationNADLFQPTSLVRYPR
CCCCCCCCCCCCCCC
24.7427174698
389PhosphorylationADLFQPTSLVRYPRL
CCCCCCCCCCCCCCC
31.3927174698
393PhosphorylationQPTSLVRYPRLEGTD
CCCCCCCCCCCCCCC
5.8027174698
467UbiquitinationLRDSESSKPSFMPRL
HCCCCCCCCCCCCHH
54.69-
507UbiquitinationTQVYEGLKPSDKYEK
HHHHCCCCCCCCCCC
54.02-
511UbiquitinationEGLKPSDKYEKPLDY
CCCCCCCCCCCCCCC
60.70-
512PhosphorylationGLKPSDKYEKPLDYR
CCCCCCCCCCCCCCC
33.8928634298
518PhosphorylationKYEKPLDYRWPMRYD
CCCCCCCCCCCCCCC
23.4328634298
586PhosphorylationTGEARDMYVPNPSCR
CCCCCEEECCCCCHH
19.62-
636UbiquitinationGEEVSWSKDFPAVDS
CCCCCCCCCCHHHHH
58.07-
643PhosphorylationKDFPAVDSVLVKLLE
CCCHHHHHHHHHHHH
15.6821406692
663UbiquitinationDKETFEFKFGKELTF
CCCEEEEECCCEEEE
46.11-
705UbiquitinationRFIQLVQKARLEESK
HHHHHHHHHCHHHHH
28.17-
712UbiquitinationKARLEESKEQVAAMQ
HHCHHHHHHHHHHHH
56.28-
742UbiquitinationTWQELEKKVCGDPEV
CHHHHHHHHCCCCCC
33.12-
793PhosphorylationSRFLRFVTGRSRLPA
HHHHHHHHCCCCCCE
24.9424719451
808UbiquitinationRIYIYPDKLGYETTD
EEEECCCCCCCCCCC
39.03-
841UbiquitinationSAKVCEEKLRYAAYN
CHHHHHHHHHHHHHC
18.90-
854PhosphorylationYNCVAIDTDMSPWEE
HCCEEEECCCCCCCC
27.7327251275
857PhosphorylationVAIDTDMSPWEE---
EEEECCCCCCCC---
29.6627251275

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
157TPhosphorylationKinaseMAPK1P28482
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HECD3_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 HECD3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STX8_HUMANSTX8physical
18821010
P53_HUMANTP53physical
23358872
MALT1_HUMANMALT1physical
23358872
CASP8_HUMANCASP8physical
24287696
RS4X_HUMANRPS4Xphysical
28514442

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 HECD3_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP