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P61077 (UB2D3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBE2D3
Synonyms:UBC5C, UBCH5C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.24

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.14 Ref.15 Ref.18 Ref.21 Ref.25

Subcellular location

Cell membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein Ref.17.

Post-translational modification

Phosphorylated by AURKB By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processApoptosis
DNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCell membrane
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Traceable author statement. Source: Reactome

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein modification process

Traceable author statement PubMed 8090726. Source: ProtInc

cellular response to hypoxia

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

negative regulation of type I interferon production

Traceable author statement. Source: Reactome

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.22. Source: UniProtKB

protein K11-linked ubiquitination

Inferred from direct assay Ref.20. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from direct assay Ref.20. Source: UniProtKB

protein monoubiquitination

Inferred from direct assay Ref.22. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay PubMed 14765125PubMed 16522193. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.24. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 14765125PubMed 16522193Ref.20Ref.22Ref.24. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61077-1)

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.
Isoform 2 (identifier: P61077-2)

The sequence of this isoform differs from the canonical sequence as follows:
     134-147: YNRISREWTQKYAM → YNRLAREWTEKYAML
Isoform 3 (identifier: P61077-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 147147Ubiquitin-conjugating enzyme E2 D3
PRO_0000082466

Sites

Active site851Glycyl thioester intermediate By similarity

Amino acid modifications

Disulfide bond21 ↔ 107 Ref.26

Natural variations

Alternative sequence1 – 88MALKRINK → MLSNRKCLSK in isoform 3.
VSP_038096
Alternative sequence134 – 14714YNRIS…QKYAM → YNRLAREWTEKYAML in isoform 2.
VSP_038097

Experimental info

Mutagenesis771N → S: Activity is restricted HECT-type and not RING-containing E3 ubiquitin-protein ligases. Exhibits ubiquitin transfer with ARIH1 and PARK2. Ref.24
Mutagenesis851C → A: Loss of function. Ref.8
Mutagenesis871D → E or P: Has intermediate lysine reactivity. Ref.24
Mutagenesis871D → K: Abolishes affect lysine reactivity. Ref.24
Mutagenesis871D → N: Does not affect lysine reactivity. Ref.24
Mutagenesis1171D → H: Strongly impairs lysine reactivity but retains some ability to transfer ubiquitin to BRCA1. Ref.24
Sequence conflict501Missing in DB045280. Ref.3
Sequence conflict1231I → L in AAH66917. Ref.7
Sequence conflict1371I → V in CAG33197. Ref.3
Sequence conflict1471M → I in CAG33197. Ref.3

Secondary structure

........................ 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: ADD74A8A708EFEE3

FASTA14716,687
        10         20         30         40         50         60 
MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY 

        70         80         90        100        110        120 
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV 

       130        140 
PEIARIYKTD RDKYNRISRE WTQKYAM 

« Hide

Isoform 2 [UniParc].

Checksum: E73DC194DB6D4EFE
Show »

FASTA14816,785
Isoform 3 [UniParc].

Checksum: F20F36FCD312444A
Show »

FASTA14916,893

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo."
Saville M.K., Sparks A., Xirodimas D.P., Wardrop J., Stevenson L.F., Bourdon J.C., Woods Y.L., Lane D.P.
J. Biol. Chem. 279:42169-42181(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"The poxvirus p28 virulence factor is an E3 ubiquitin ligase."
Huang J., Huang Q., Zhou X., Shen M.M., Yen A., Yu S.X., Dong G., Qu K., Huang P., Anderson E.M., Daniel-Issakani S., Buller R.M., Payan D.G., Lu H.H.
J. Biol. Chem. 279:54110-54116(2004) [PubMed] [Europe PMC] [Abstract]
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]"Physical and functional interactions between ZIP kinase and UbcH5."
Ohbayashi N., Okada K., Kawakami S., Togi S., Sato N., Ikeda O., Kamitani S., Muromoto R., Sekine Y., Kawai T., Akira S., Matsuda T.
Biochem. Biophys. Res. Commun. 372:708-712(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003331.1. NM_003340.6.
NP_871615.1. NM_181886.3.
NP_871616.1. NM_181887.2.
NP_871617.1. NM_181888.3.
NP_871618.1. NM_181889.2.
NP_871619.1. NM_181890.2.
NP_871620.1. NM_181891.2.
NP_871621.1. NM_181892.3.
NP_871622.1. NM_181893.2.
XP_005263257.1. XM_005263200.2.
UniGeneHs.518773.
Hs.595430.
Hs.621366.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP61077.
SMRP61077. Positions 1-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113171. 190 interactions.
DIPDIP-29062N.
IntActP61077. 92 interactions.
MINTMINT-1032046.
STRING9606.ENSP00000349722.

PTM databases

PhosphoSiteP61077.

Polymorphism databases

DMDM46577654.

Proteomic databases

PRIDEP61077.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321805; 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]
GeneID7323.
KEGGhsa:7323.
UCSCuc003hwi.3. human. [P61077-2]
uc003hwk.3. human. [P61077-1]
uc003hwq.3. human. [P61077-3]

Organism-specific databases

CTD7323.
GeneCardsGC04M103717.
HGNCHGNC:12476. UBE2D3.
HPAHPA003920.
MIM602963. gene.
neXtProtNX_P61077.
PharmGKBPA37126.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG063308.
KOK06689.
OMASAGPCED.
OrthoDBEOG7PCJGX.
PhylomeDBP61077.
TreeFamTF101108.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_6900. Immune System.
REACT_71. Gene Expression.
REACT_98458. Immune System.
SignaLinkP61077.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP61077.
BgeeP61077.
CleanExHS_UBE2D3.
GenevestigatorP61077.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2D3. human.
EvolutionaryTraceP61077.
GeneWikiUBE2D3.
GenomeRNAi7323.
NextBio28636.
PROP61077.
SOURCESearch...

Entry information

Entry nameUB2D3_HUMAN
AccessionPrimary (citable) accession number: P61077
Secondary accession number(s): A6NJ93 expand/collapse secondary AC list , A6NJB1, A6NM99, P47986, Q6IB88, Q6NXS4, Q8N924
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM