UB2D3_HUMAN - dbPTM
UB2D3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UB2D3_HUMAN
UniProt AC P61077
Protein Name Ubiquitin-conjugating enzyme E2 D3
Gene Name UBE2D3
Organism Homo sapiens (Human).
Sequence Length 147
Subcellular Localization Cell membrane
Peripheral membrane protein . Endosome membrane
Peripheral membrane protein .
Protein Description Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction..
Protein Sequence MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM
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
3 (in isoform 3)Phosphorylation-3.5520068231
8 (in isoform 2)Ubiquitination-58.6321890473
8 (in isoform 1)Ubiquitination-58.6321890473
8UbiquitinationMALKRINKELSDLAR
CCHHHHHHHHHHHHH
58.6321906983
8AcetylationMALKRINKELSDLAR
CCHHHHHHHHHHHHH
58.6326051181
9 (in isoform 3)Phosphorylation-49.3620068231
11PhosphorylationKRINKELSDLARDPP
HHHHHHHHHHHHCCC
31.5028857561
13 (in isoform 3)Phosphorylation-3.6520068231
74PhosphorylationVAFTTRIYHPNINSN
EEEEEEEECCCCCCC
14.1328152594
80PhosphorylationIYHPNINSNGSICLD
EECCCCCCCCEEHHH
38.4824076635
83PhosphorylationPNINSNGSICLDILR
CCCCCCCEEHHHHHH
17.8725849741
94PhosphorylationDILRSQWSPALTISK
HHHHHCCCCCHHHHH
7.83-
98PhosphorylationSQWSPALTISKVLLS
HCCCCCHHHHHHHHH
25.8821712546
101UbiquitinationSPALTISKVLLSICS
CCCHHHHHHHHHHHH
32.81-
105PhosphorylationTISKVLLSICSLLCD
HHHHHHHHHHHHHCC
19.86-
128UbiquitinationPEIARIYKTDRDKYN
HHHHHHHCCCHHHHH
41.39-
128SuccinylationPEIARIYKTDRDKYN
HHHHHHHCCCHHHHH
41.3923954790
130 (in isoform 3)Ubiquitination-53.26-
133AcetylationIYKTDRDKYNRISRE
HHCCCHHHHHHHCHH
45.3726051181
133UbiquitinationIYKTDRDKYNRISRE
HHCCCHHHHHHHCHH
45.37-
144UbiquitinationISREWTQKYAM----
HCHHHHHHHCC----
27.8321906983
144AcetylationISREWTQKYAM----
HCHHHHHHHCC----
27.8321791702
145PhosphorylationSREWTQKYAM-----
CHHHHHHHCC-----
9.70-
146 (in isoform 3)Ubiquitination-12.30-

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UB2D3_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 UB2D3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI39_HUMANTRIM39physical
16189514
RN126_HUMANRNF126physical
16189514
NEDD4_HUMANNEDD4physical
9990509
UBE3A_HUMANUBE3Aphysical
9990509
MEX3B_HUMANMEX3Bphysical
16169070
DAPK3_HUMANDAPK3physical
18515077
DDX58_HUMANDDX58physical
17719635
RN125_HUMANRNF125physical
17719635
ISG15_HUMANISG15physical
17719635
STAM2_HUMANSTAM2physical
17588522
EPS15_HUMANEPS15physical
17588522
DPOLM_HUMANPOLMphysical
17588522
DPOLL_HUMANPOLLphysical
17588522
HDAC6_HUMANHDAC6physical
17588522
UBS3B_HUMANUBASH3Bphysical
17588522
UFM1_HUMANUFM1physical
19690564
AMFR_HUMANAMFRphysical
19690564
MUL1_HUMANMUL1physical
19690564
CAPS2_HUMANCADPS2physical
19690564
CNOT4_HUMANCNOT4physical
19690564
DTX1_HUMANDTX1physical
19690564
UBE4A_HUMANUBE4Aphysical
19690564
RN103_HUMANRNF103physical
19690564
RN181_HUMANRNF181physical
19690564
M3K1_HUMANMAP3K1physical
19690564
MIB1_HUMANMIB1physical
19690564
PJA2_HUMANPJA2physical
19690564
RFWD3_HUMANRFWD3physical
19690564
RMD5B_HUMANRMND5Bphysical
19690564
RNF11_HUMANRNF11physical
19690564
RN111_HUMANRNF111physical
19690564
RNF13_HUMANRNF13physical
19690564
GOLI_HUMANRNF130physical
19690564
RN150_HUMANRNF150physical
19690564
RN165_HUMANRNF165physical
19690564
RN167_HUMANRNF167physical
19690564
RNF25_HUMANRNF25physical
19690564
RNF26_HUMANRNF26physical
19690564
RNF43_HUMANRNF43physical
19690564
SIAH1_HUMANSIAH1physical
19690564
RNF4_HUMANRNF4physical
19690564
TOPRS_HUMANTOPORSphysical
19690564
UHRF2_HUMANUHRF2physical
19690564
RN115_HUMANRNF115physical
19690564
ZNRF1_HUMANZNRF1physical
19690564
ZNRF2_HUMANZNRF2physical
19690564
ZNRF4_HUMANZNRF4physical
19690564
XIAP_HUMANXIAPphysical
19549727
RN126_HUMANRNF126physical
19549727
RNF37_HUMANUBOX5physical
19549727
RNF5_HUMANRNF5physical
19549727
DTX3_HUMANDTX3physical
19549727
RNF14_HUMANRNF14physical
19549727
ZNRF1_HUMANZNRF1physical
19549727
RN114_HUMANRNF114physical
19549727
RNF11_HUMANRNF11physical
19549727
TRIM8_HUMANTRIM8physical
19549727
DTX3L_HUMANDTX3Lphysical
19549727
DZIP3_HUMANDZIP3physical
19549727
TRI18_HUMANMID1physical
19549727
MKRN3_HUMANMKRN3physical
19549727
TRI39_HUMANTRIM39physical
19549727
TRI27_HUMANTRIM27physical
19549727
RFWD3_HUMANRFWD3physical
19549727
RNF10_HUMANRNF10physical
19549727
RN111_HUMANRNF111physical
19549727
RN166_HUMANRNF166physical
19549727
RN185_HUMANRNF185physical
19549727
RING2_HUMANRNF2physical
19549727
RNF25_HUMANRNF25physical
19549727
TRI43_HUMANTRIM43physical
19549727
TRAF6_HUMANTRAF6physical
19549727
BIRC8_HUMANBIRC8physical
19549727
RN125_HUMANRNF125physical
19549727
BFAR_HUMANBFARphysical
19549727
RNF4_HUMANRNF4physical
19549727
RING1_HUMANRING1physical
19549727
MARH3_HUMANMARCH3physical
19549727
RSPRY_HUMANRSPRY1physical
19549727
RNF12_HUMANRLIMphysical
19549727
LRSM1_HUMANLRSAM1physical
19549727
AMFR_HUMANAMFRphysical
19549727
SIAH1_HUMANSIAH1physical
19549727
CHFR_HUMANCHFRphysical
19549727
ARI2_HUMANARIH2physical
19549727
MGRN1_HUMANMGRN1physical
19549727
TRI55_HUMANTRIM55physical
19549727
RNF38_HUMANRNF38physical
19549727
TRI17_HUMANTRIM17physical
19549727
TRIM2_HUMANTRIM2physical
19549727
TRI25_HUMANTRIM25physical
19549727
TRI26_HUMANTRIM26physical
19549727
TRI31_HUMANTRIM31physical
19549727
TRI35_HUMANTRIM35physical
19549727
TRIM5_HUMANTRIM5physical
19549727
DREB_HUMANDBN1physical
21900206
STAU1_HUMANSTAU1physical
21900206
K1107_HUMANKIAA1107physical
21900206
FOCAD_HUMANFOCADphysical
21900206
TBA1A_HUMANTUBA1Aphysical
21900206
MKRN1_HUMANMKRN1physical
21900206
RLA1_HUMANRPLP1physical
21900206
XPP1_HUMANXPNPEP1physical
21900206
MEX3B_HUMANMEX3Bphysical
21900206
STK25_HUMANSTK25physical
21900206
PDCD5_HUMANPDCD5physical
21900206
TRAF6_HUMANTRAF6physical
17709375
IKBA_HUMANNFKBIAphysical
10329681
CHIP_HUMANSTUB1physical
22551455
TRIM1_HUMANMID2physical
21143188
TRI10_HUMANTRIM10physical
21143188
TRI11_HUMANTRIM11physical
21143188
TRI18_HUMANMID1physical
21143188
TRI27_HUMANTRIM27physical
21143188
TRI50_HUMANTRIM50physical
21143188
TRI37_HUMANTRIM37physical
21143188
TF65_HUMANRELAphysical
14690596
FBX25_HUMANFBXO25physical
16714087
PCNA_HUMANPCNAphysical
22989887
NEDD4_HUMANNEDD4physical
23644597
NED4L_HUMANNEDD4Lphysical
23644597
ITCH_HUMANITCHphysical
23644597
SMUF2_HUMANSMURF2physical
23644597
WWP2_HUMANWWP2physical
23644597
TERT_HUMANTERTphysical
23741361
UBC_HUMANUBCphysical
21900206
UB2D3_HUMANUBE2D3physical
12438698
UBC_HUMANUBCphysical
24446487
SMUF1_HUMANSMURF1physical
24821572
IKBA_HUMANNFKBIAphysical
20347421
UB2D3_HUMANUBE2D3physical
20061386
RNF26_HUMANRNF26physical
19549727
RN115_HUMANRNF115physical
25416956
RN111_HUMANRNF111physical
25416956
OTUB1_HUMANOTUB1physical
25416956
TRI39_HUMANTRIM39physical
25416956
DTX2_HUMANDTX2physical
25416956
TRI25_HUMANTRIM25physical
22350887
MDM2_HUMANMDM2physical
15280377
BRCA1_HUMANBRCA1physical
11927591
BARD1_HUMANBARD1physical
11927591
OTUB1_HUMANOTUB1physical
24403071
UBC_HUMANUBCphysical
24403071
UBC_HUMANUBCphysical
17170710
NEDD8_HUMANNEDD8physical
26344197
UBE2C_HUMANUBE2Cphysical
26344197
FA12_HUMANF12physical
18838541
KDM1B_HUMANKDM1Bphysical
25773598
RBX2_HUMANRNF7physical
27910872
RBX1_HUMANRBX1physical
27910872
UB2R1_HUMANCDC34physical
27910872
TF_HUMANF3physical
27599717
RN168_HUMANRNF168physical
28244869
RNF8_HUMANRNF8physical
28244869
RN114_HUMANRNF114physical
28625874
SQSTM_HUMANSQSTM1physical
28322253

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UB2D3_HUMAN

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Related Literatures of Post-Translational Modification

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