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P61077

- UB2D3_HUMAN

UniProt

P61077 - UB2D3_HUMAN

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Protein
Ubiquitin-conjugating enzyme E2 D3
Gene
UBE2D3, UBC5C, UBCH5C
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 By similarity.14 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Glycyl thioester intermediate By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acid-amino acid ligase activity Source: InterPro
  3. protein binding Source: IntAct
  4. ubiquitin-protein transferase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. BMP signaling pathway Source: Reactome
  2. DNA repair Source: UniProtKB-KW
  3. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  4. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  5. apoptotic process Source: UniProtKB-KW
  6. cellular protein modification process Source: ProtInc
  7. cellular response to hypoxia Source: Reactome
  8. gene expression Source: Reactome
  9. innate immune response Source: Reactome
  10. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  11. negative regulation of type I interferon production Source: Reactome
  12. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  13. protein K11-linked ubiquitination Source: UniProtKB
  14. protein K48-linked ubiquitination Source: UniProtKB
  15. protein monoubiquitination Source: UniProtKB
  16. protein polyubiquitination Source: UniProtKB
  17. protein ubiquitination Source: UniProtKB
  18. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  19. toll-like receptor 3 signaling pathway Source: Reactome
  20. toll-like receptor 4 signaling pathway Source: Reactome
  21. toll-like receptor signaling pathway Source: Reactome
  22. transcription initiation from RNA polymerase II promoter Source: Reactome
  23. transcription, DNA-templated Source: Reactome
  24. transforming growth factor beta receptor signaling pathway Source: Reactome
  25. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12034. Signaling by BMP.
REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP61077.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 D3 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein D3
Ubiquitin-conjugating enzyme E2(17)KB 3
Ubiquitin-conjugating enzyme E2-17 kDa 3
Ubiquitin-protein ligase D3
Gene namesi
Name:UBE2D3
Synonyms:UBC5C, UBCH5C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:12476. UBE2D3.

Subcellular locationi

Cell membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endosome membrane Source: UniProtKB-SubCell
  3. nucleoplasm Source: Reactome
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi77 – 771N → S: Activity is restricted HECT-type and not RING-containing E3 ubiquitin-protein ligases. Exhibits ubiquitin transfer with ARIH1 and PARK2. 1 Publication
Mutagenesisi85 – 851C → A: Loss of function. 1 Publication
Mutagenesisi87 – 871D → E or P: Has intermediate lysine reactivity. 1 Publication
Mutagenesisi87 – 871D → K: Abolishes affect lysine reactivity. 1 Publication
Mutagenesisi87 – 871D → N: Does not affect lysine reactivity. 1 Publication
Mutagenesisi117 – 1171D → H: Strongly impairs lysine reactivity but retains some ability to transfer ubiquitin to BRCA1. 1 Publication

Organism-specific databases

PharmGKBiPA37126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Ubiquitin-conjugating enzyme E2 D3
PRO_0000082466Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 1071 Publication

Post-translational modificationi

Phosphorylated by AURKB By similarity.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP61077.
PRIDEiP61077.

PTM databases

PhosphoSiteiP61077.

Expressioni

Gene expression databases

ArrayExpressiP61077.
BgeeiP61077.
CleanExiHS_UBE2D3.
GenevestigatoriP61077.

Organism-specific databases

HPAiHPA003920.

Interactioni

Subunit structurei

Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex; when Cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened. Interacts with DAPK3. Interacts with BRCA1; the DNA damage checkpoint promotes the association with BRCA1 after ionizing radiation. Interacts non-covalently with ubiquitin. Interacts with E3 ubiquitin-protein ligase CBLC.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OTUB1Q96FW14EBI-348268,EBI-1058491
RNF11Q9Y3C53EBI-348268,EBI-396669
RNF126Q9BV683EBI-348268,EBI-357322
RNF43Q68DV72EBI-348268,EBI-1647060
RNF5Q999423EBI-348268,EBI-348482
TRAF6Q9Y4K32EBI-348268,EBI-359276
XIAPP981702EBI-348268,EBI-517127
ZNRF1Q8ND253EBI-348268,EBI-2129250

Protein-protein interaction databases

BioGridi113171. 191 interactions.
DIPiDIP-29062N.
IntActiP61077. 92 interactions.
MINTiMINT-1032046.
STRINGi9606.ENSP00000349722.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1515
Beta strandi21 – 266
Beta strandi32 – 387
Beta strandi41 – 433
Turni44 – 474
Beta strandi49 – 557
Turni58 – 614
Beta strandi66 – 694
Helixi87 – 893
Turni90 – 923
Helixi99 – 11113
Helixi121 – 1299
Helixi131 – 14515

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X23X-ray1.85A/B/C/D1-147[»]
2FUHNMR-A2-147[»]
3L1ZX-ray3.17A1-147[»]
3RPGX-ray2.65A2-147[»]
3UGBX-ray2.35A1-147[»]
4BVUX-ray2.70B1-147[»]
ProteinModelPortaliP61077.
SMRiP61077. Positions 1-147.

Miscellaneous databases

EvolutionaryTraceiP61077.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG063308.
KOiK06689.
OMAiSAGPCED.
OrthoDBiEOG7PCJGX.
PhylomeDBiP61077.
TreeFamiTF101108.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61077-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF    50
FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS 100
KVLLSICSLL CDPNPDDPLV PEIARIYKTD RDKYNRISRE WTQKYAM 147
Length:147
Mass (Da):16,687
Last modified:April 26, 2004 - v1
Checksum:iADD74A8A708EFEE3
GO
Isoform 2 (identifier: P61077-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-147: YNRISREWTQKYAM → YNRLAREWTEKYAML

Show »
Length:148
Mass (Da):16,785
Checksum:iE73DC194DB6D4EFE
GO
Isoform 3 (identifier: P61077-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MALKRINK → MLSNRKCLSK

Show »
Length:149
Mass (Da):16,893
Checksum:iF20F36FCD312444A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 88MALKRINK → MLSNRKCLSK in isoform 3.
VSP_038096
Alternative sequencei134 – 14714YNRIS…QKYAM → YNRLAREWTEKYAML in isoform 2.
VSP_038097Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501Missing in DB045280. 1 Publication
Sequence conflicti123 – 1231I → L in AAH66917. 1 Publication
Sequence conflicti137 – 1371I → V in CAG33197. 1 Publication
Sequence conflicti147 – 1471M → I in CAG33197. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U39318 mRNA. Translation: AAA91461.1.
AF213884 Genomic DNA. Translation: AAF35234.1.
AK095822 mRNA. Translation: BAC04632.1.
DB045280 mRNA. No translation available.
CR456916 mRNA. Translation: CAG33197.1.
AC018797 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06138.1.
CH471057 Genomic DNA. Translation: EAX06143.1.
BC003395 mRNA. Translation: AAH03395.1.
BC037894 mRNA. Translation: AAH37894.1.
BC066917 mRNA. Translation: AAH66917.1.
CCDSiCCDS3659.1. [P61077-3]
CCDS3660.1. [P61077-1]
CCDS3661.1. [P61077-2]
RefSeqiNP_003331.1. NM_003340.6. [P61077-1]
NP_871615.1. NM_181886.3. [P61077-1]
NP_871616.1. NM_181887.2. [P61077-1]
NP_871617.1. NM_181888.3. [P61077-1]
NP_871618.1. NM_181889.2. [P61077-1]
NP_871619.1. NM_181890.2. [P61077-1]
NP_871620.1. NM_181891.2. [P61077-1]
NP_871621.1. NM_181892.3. [P61077-2]
NP_871622.1. NM_181893.2. [P61077-3]
XP_005263257.1. XM_005263200.2. [P61077-2]
XP_006714360.1. XM_006714297.1. [P61077-2]
XP_006714361.1. XM_006714298.1. [P61077-2]
XP_006714362.1. XM_006714299.1. [P61077-2]
UniGeneiHs.518773.
Hs.595430.
Hs.621366.

Genome annotation databases

EnsembliENST00000321805; ENSP00000318494; ENSG00000109332. [P61077-1]
ENST00000338145; ENSP00000337208; ENSG00000109332. [P61077-1]
ENST00000343106; ENSP00000345285; ENSG00000109332. [P61077-2]
ENST00000349311; ENSP00000344069; ENSG00000109332. [P61077-1]
ENST00000357194; ENSP00000349722; ENSG00000109332. [P61077-3]
ENST00000394801; ENSP00000378280; ENSG00000109332. [P61077-1]
ENST00000394803; ENSP00000378282; ENSG00000109332. [P61077-1]
ENST00000394804; ENSP00000378283; ENSG00000109332. [P61077-1]
ENST00000453744; ENSP00000396901; ENSG00000109332. [P61077-1]
GeneIDi7323.
KEGGihsa:7323.
UCSCiuc003hwi.3. human. [P61077-2]
uc003hwk.3. human. [P61077-1]
uc003hwq.3. human. [P61077-3]

Polymorphism databases

DMDMi46577654.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U39318 mRNA. Translation: AAA91461.1 .
AF213884 Genomic DNA. Translation: AAF35234.1 .
AK095822 mRNA. Translation: BAC04632.1 .
DB045280 mRNA. No translation available.
CR456916 mRNA. Translation: CAG33197.1 .
AC018797 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06138.1 .
CH471057 Genomic DNA. Translation: EAX06143.1 .
BC003395 mRNA. Translation: AAH03395.1 .
BC037894 mRNA. Translation: AAH37894.1 .
BC066917 mRNA. Translation: AAH66917.1 .
CCDSi CCDS3659.1. [P61077-3 ]
CCDS3660.1. [P61077-1 ]
CCDS3661.1. [P61077-2 ]
RefSeqi NP_003331.1. NM_003340.6. [P61077-1 ]
NP_871615.1. NM_181886.3. [P61077-1 ]
NP_871616.1. NM_181887.2. [P61077-1 ]
NP_871617.1. NM_181888.3. [P61077-1 ]
NP_871618.1. NM_181889.2. [P61077-1 ]
NP_871619.1. NM_181890.2. [P61077-1 ]
NP_871620.1. NM_181891.2. [P61077-1 ]
NP_871621.1. NM_181892.3. [P61077-2 ]
NP_871622.1. NM_181893.2. [P61077-3 ]
XP_005263257.1. XM_005263200.2. [P61077-2 ]
XP_006714360.1. XM_006714297.1. [P61077-2 ]
XP_006714361.1. XM_006714298.1. [P61077-2 ]
XP_006714362.1. XM_006714299.1. [P61077-2 ]
UniGenei Hs.518773.
Hs.595430.
Hs.621366.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X23 X-ray 1.85 A/B/C/D 1-147 [» ]
2FUH NMR - A 2-147 [» ]
3L1Z X-ray 3.17 A 1-147 [» ]
3RPG X-ray 2.65 A 2-147 [» ]
3UGB X-ray 2.35 A 1-147 [» ]
4BVU X-ray 2.70 B 1-147 [» ]
ProteinModelPortali P61077.
SMRi P61077. Positions 1-147.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113171. 191 interactions.
DIPi DIP-29062N.
IntActi P61077. 92 interactions.
MINTi MINT-1032046.
STRINGi 9606.ENSP00000349722.

PTM databases

PhosphoSitei P61077.

Polymorphism databases

DMDMi 46577654.

Proteomic databases

MaxQBi P61077.
PRIDEi P61077.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321805 ; ENSP00000318494 ; ENSG00000109332 . [P61077-1 ]
ENST00000338145 ; ENSP00000337208 ; ENSG00000109332 . [P61077-1 ]
ENST00000343106 ; ENSP00000345285 ; ENSG00000109332 . [P61077-2 ]
ENST00000349311 ; ENSP00000344069 ; ENSG00000109332 . [P61077-1 ]
ENST00000357194 ; ENSP00000349722 ; ENSG00000109332 . [P61077-3 ]
ENST00000394801 ; ENSP00000378280 ; ENSG00000109332 . [P61077-1 ]
ENST00000394803 ; ENSP00000378282 ; ENSG00000109332 . [P61077-1 ]
ENST00000394804 ; ENSP00000378283 ; ENSG00000109332 . [P61077-1 ]
ENST00000453744 ; ENSP00000396901 ; ENSG00000109332 . [P61077-1 ]
GeneIDi 7323.
KEGGi hsa:7323.
UCSCi uc003hwi.3. human. [P61077-2 ]
uc003hwk.3. human. [P61077-1 ]
uc003hwq.3. human. [P61077-3 ]

Organism-specific databases

CTDi 7323.
GeneCardsi GC04M103717.
HGNCi HGNC:12476. UBE2D3.
HPAi HPA003920.
MIMi 602963. gene.
neXtProti NX_P61077.
PharmGKBi PA37126.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG063308.
KOi K06689.
OMAi SAGPCED.
OrthoDBi EOG7PCJGX.
PhylomeDBi P61077.
TreeFami TF101108.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_12034. Signaling by BMP.
REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki P61077.

Miscellaneous databases

ChiTaRSi UBE2D3. human.
EvolutionaryTracei P61077.
GeneWikii UBE2D3.
GenomeRNAii 7323.
NextBioi 28636.
PROi P61077.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61077.
Bgeei P61077.
CleanExi HS_UBE2D3.
Genevestigatori P61077.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a family of closely related human ubiquitin conjugating enzymes."
    Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M.
    J. Biol. Chem. 270:30408-30414(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Genome sequencing of the chromosome 4q region implicated in human hepatocellular carcinoma pathogenesis."
    Chang H.-M., Tsai S.-F.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Chondrocyte and Testis.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Placenta.
  8. "Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha."
    Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C., Yamanaka K., Pagano M., Iwai K., Ciechanover A.
    J. Biol. Chem. 274:14823-14830(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-85.
  9. "CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein."
    Murata S., Minami Y., Minami M., Chiba T., Tanaka K.
    EMBO Rep. 2:1133-1138(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Mammalian Numb is a target protein of Mdm2, ubiquitin ligase."
    Yogosawa S., Miyauchi Y., Honda R., Tanaka H., Yasuda H.
    Biochem. Biophys. Res. Commun. 302:869-872(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53."
    Rajendra R., Malegaonkar D., Pungaliya P., Marshall H., Rasheed Z., Brownell J., Liu L.F., Lutzker S., Saleem A., Rubin E.H.
    J. Biol. Chem. 279:36440-36444(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: FUNCTION.
  13. Cited for: FUNCTION.
  14. "A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites."
    Polanowska J., Martin J.S., Garcia-Muse T., Petalcorin M.I.R., Boulton S.J.
    EMBO J. 25:2178-2188(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRCA1, FUNCTION.
  15. Cited for: INTERACTION WITH DAPK3, FUNCTION.
  16. "PCNA is ubiquitinated by RNF8."
    Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.
    Cell Cycle 7:3399-3404(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation."
    Umebayashi K., Stenmark H., Yoshimori T.
    Mol. Biol. Cell 19:3454-3462(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  18. "Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation."
    Saha A., Deshaies R.J.
    Mol. Cell 32:21-31(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCF COMPLEX.
  19. "Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions."
    Kubori T., Hyakutake A., Nagai H.
    Mol. Microbiol. 67:1307-1319(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
    David Y., Ziv T., Admon A., Navon A.
    J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme."
    Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.
    J. Biol. Chem. 285:23687-23698(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBLC.
  22. "Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate."
    Wu K., Kovacev J., Pan Z.Q.
    Mol. Cell 37:784-796(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids."
    Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.
    Nature 474:105-108(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASN-77; ASP-87 AND ASP-117.
  25. "A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination."
    Brzovic P.S., Lissounov A., Christensen D.E., Hoyt D.W., Klevit R.E.
    Mol. Cell 21:873-880(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-147 IN COMPLEX WITH THE BRCA1/BARD1 RING-DOMAIN HETERODIMER, INTERACTION WITH BRCA1.
  26. "Crystal structure of UBCH5C."
    Nakanishi M., Teshima N., Mizushima T., Murata S., Tanaka K., Yamane T.
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-147, DISULFIDE BOND.
  27. "Crystal structure of the U-Box domain of human e4b ubiquitin ligase in complex with UBCH5C E2 ubiquitin conjugating enzyme."
    Benirschke R., Thompson J.R., Mer G.
    Submitted (MAY-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (3.17 ANGSTROMS) OF 1-147 IN COMPLEX WITH U-BOX DOMAIN OF UBE4B.

Entry informationi

Entry nameiUB2D3_HUMAN
AccessioniPrimary (citable) accession number: P61077
Secondary accession number(s): A6NJ93
, A6NJB1, A6NM99, P47986, Q6IB88, Q6NXS4, Q8N924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: September 3, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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