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P62837 (UB2D2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. 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 D2

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein D2
Ubiquitin-conjugating enzyme E2(17)KB 2
Ubiquitin-conjugating enzyme E2-17 kDa 2
Ubiquitin-protein ligase D2
p53-regulated ubiquitin-conjugating enzyme 1
Gene names
Name:UBE2D2
Synonyms:PUBC1, UBC4, UBC5B, UBCH4, UBCH5B
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-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3. Ref.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

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. Interacts with CNOT4 (via RING domain). Interacts with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts with PDZRN3. Ref.11 Ref.12 Ref.14 Ref.21

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

cellular protein modification process

Traceable author statement PubMed 8090726. Source: ProtInc

cellular response to hypoxia

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

protein K48-linked ubiquitination

Inferred from direct assay Ref.20. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay PubMed 15247280. Source: BHF-UCL

protein ubiquitination

Inferred from direct assay PubMed 9990509. Source: BHF-UCL

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

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

ubiquitin ligase complex

Inferred from direct assay PubMed 15247280. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from direct assay Ref.17Ref.16Ref.20. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62837-1)

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: P62837-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 147147Ubiquitin-conjugating enzyme E2 D2
PRO_0000082462

Sites

Active site851Glycyl thioester intermediate By similarity

Natural variations

Alternative sequence1 – 2929Missing in isoform 2.
VSP_045180

Experimental info

Mutagenesis631K → A or E: Strongly reduced interaction with CNTO4. Ref.14
Mutagenesis851C → A: Catalytically inactive. Loss of ability to promote FBXW2-mediated GCM1 ubiquitination. Inhibition of TNF-alpha-induced degradation of NFKBIA. Ref.10 Ref.16 Ref.21
Sequence conflict1281K → Q in AAC41750. Ref.2

Secondary structure

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

Details...

Sequences

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

Last modified August 16, 2004. Version 1.
Checksum: C942BE7853CBC355

FASTA14716,735
        10         20         30         40         50         60 
MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY 

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

       130        140 
PEIARIYKTD REKYNRIARE WTQKYAM 

« Hide

Isoform 2 [UniParc].

Checksum: CC29567199FE8084
Show »

FASTA11813,635

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).
Tissue: Peripheral blood lymphocyte.
[2]"Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP)."
Rolfe M., Beer-Romero P., Glass S., Eckstein J., Berdo I., Theodoras A., Pagano M., Draetta G.
Proc. Natl. Acad. Sci. U.S.A. 92:3264-3268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia."
Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., Wells J.W., Banham A.H., Mufti G.J.
Biochem. Biophys. Res. Commun. 335:1293-1304(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"Cloning and identification of a p53-regulated ubiquitin-conjugating enzyme, PUBC1."
Yin Y.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"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] (ISOFORM 1).
Tissue: Teratocarcinoma.
[6]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Testis.
[9]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 73-90, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[10]"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.
[11]"SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I kappa B alpha catalyzed by Ubc3 and Ubc4."
Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., Benfield P., Brizuela L., Rolfe M.
Oncogene 19:3529-3536(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCF COMPLEX.
[12]"PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain."
Yu P., Chen Y., Tagle D.A., Cai T.
Genomics 79:869-874(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PJA1 AND PJA2.
[13]"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.
[14]"An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair."
Winkler G.S., Albert T.K., Dominguez C., Legtenberg Y.I., Boelens R., Timmers H.T.
J. Mol. Biol. 337:157-165(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CNOT4, MUTAGENESIS OF LYS-63.
[15]"Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology."
Windheim M., Peggie M., Cohen P.
Biochem. J. 409:723-729(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation."
Chiang M.H., Chen L.F., Chen H.
Biol. Reprod. 79:914-920(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-85.
[17]"Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor."
Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., Meyer H.E., Warscheid B., Sa-Miranda C., Azevedo J.E.
J. Biol. Chem. 283:14190-14197(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3."
Zeng W., Xu M., Liu S., Sun L., Chen Z.J.
Mol. Cell 36:315-325(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
[19]"Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity."
Zeng W., Sun L., Jiang X., Chen X., Hou F., Adhikari A., Xu M., Chen Z.J.
Cell 141:315-330(2010) [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: FUNCTION, INTERACTION WITH CBLC, MUTAGENESIS OF CYS-85.
[22]"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].
[23]"Solution structure of the ubiquitin-conjugating enzyme UbcH5B."
Houben K., Dominguez C., van Schaik F.M., Timmers H.T., Bonvin A.M., Boelens R.
J. Mol. Biol. 344:513-526(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[24]"Crystal structure of UbcH5b~ubiquitin intermediate: insight into the formation of the self-assembled E2~Ub conjugates."
Sakata E., Satoh T., Yamamoto S., Yamaguchi Y., Yagi-Utsumi M., Kurimoto E., Tanaka K., Wakatsuki S., Kato K.
Structure 18:138-147(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39317 mRNA. Translation: AAA91460.1.
L40146 Genomic DNA. Translation: AAC41750.1.
AY651263 mRNA. Translation: AAX35690.1.
AF317220 mRNA. Translation: AAK93958.1.
AK001311 mRNA. Translation: BAG50891.1.
AK001428 mRNA. Translation: BAG50911.1.
AC010378 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62095.1.
CH471062 Genomic DNA. Translation: EAW62096.1.
CH471062 Genomic DNA. Translation: EAW62097.1.
BC033349 mRNA. Translation: AAH33349.1.
PIRI59365.
RefSeqNP_003330.1. NM_003339.2.
NP_862821.1. NM_181838.1.
UniGeneHs.108332.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UR6NMR-A1-147[»]
1W4UNMR-A1-147[»]
2C4OX-ray1.94A/B/C/D1-147[»]
2CLWX-ray1.94A/B/C/D1-147[»]
2ESKX-ray1.36A1-147[»]
2ESOX-ray1.50A1-147[»]
2ESPX-ray1.52A1-147[»]
2ESQX-ray1.44A1-147[»]
3A33X-ray2.20A1-147[»]
3JVZX-ray3.30A/B4-147[»]
3JW0X-ray3.10A/B4-147[»]
3L1YX-ray1.60A1-147[»]
3TGDX-ray1.80A1-147[»]
3ZNIX-ray2.21C/G/K/O2-147[»]
4A49X-ray2.21B1-147[»]
4A4BX-ray2.79C1-147[»]
4A4CX-ray2.70C1-147[»]
4AUQX-ray2.18A/D1-147[»]
4DDGX-ray3.30A/B/C/J/K/L1-147[»]
4LDTX-ray1.90C1-147[»]
ProteinModelPortalP62837.
SMRP62837. Positions 1-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113170. 200 interactions.
DIPDIP-29267N.
IntActP62837. 96 interactions.
MINTMINT-1035011.
STRING9606.ENSP00000381717.

Protein family/group databases

TCDB3.A.20.1.1. the peroxisomal protein importer (ppi) family.

PTM databases

PhosphoSiteP62837.

Polymorphism databases

DMDM51338685.

Proteomic databases

PaxDbP62837.
PRIDEP62837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253815; ENSP00000253815; ENSG00000131508. [P62837-2]
ENST00000398733; ENSP00000381717; ENSG00000131508. [P62837-1]
ENST00000398734; ENSP00000381718; ENSG00000131508. [P62837-1]
ENST00000505548; ENSP00000424941; ENSG00000131508. [P62837-2]
ENST00000511725; ENSP00000429613; ENSG00000131508. [P62837-2]
GeneID7322.
KEGGhsa:7322.
UCSCuc003leq.3. human. [P62837-1]

Organism-specific databases

CTD7322.
GeneCardsGC05P138920.
H-InvDBHIX0019025.
HIX0028451.
HGNCHGNC:12475. UBE2D2.
HPAHPA003920.
MIM602962. gene.
neXtProtNX_P62837.
PharmGKBPA37125.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
HOVERGENHBG063308.
KOK06689.
OMAIAHIYKQ.
OrthoDBEOG7PCJGX.
PhylomeDBP62837.
TreeFamTF101108.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_6900. Immune System.
REACT_98458. Immune System.
SignaLinkP62837.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP62837.
BgeeP62837.
CleanExHS_UBE2D2.
GenevestigatorP62837.

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

EvolutionaryTraceP62837.
GeneWikiUBE2D2.
GenomeRNAi7322.
NextBio28630.
PROP62837.
SOURCESearch...

Entry information

Entry nameUB2D2_HUMAN
AccessionPrimary (citable) accession number: P62837
Secondary accession number(s): D3DQC9 expand/collapse secondary AC list , P51669, Q3MN78, Q96RP6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 119 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 5

Human chromosome 5: entries, gene names and cross-references to MIM