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Q8WVN8 (UB2Q2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 Q2

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein Q2
Ubiquitin-protein ligase Q2
Gene names
Name:UBE2Q2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 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. Ref.6

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Cytoplasm Ref.5.

Tissue specificity

Detected in hypopharyngeal head and neck squamous cell carcinoma, in tumor masses and invasive epithelium. Ref.5

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence AAH34342.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein K48-linked ubiquitination

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein transferase activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WVN8-1)

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: Q8WVN8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     296-314: YVLGGGALCMELLTKQGWS → LVHPSKGRWLNMLTVVCLD
     315-375: Missing.
Isoform 3 (identifier: Q8WVN8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MSVSGLKAEL...PPLTLHCNIT → MRMDSLTEEK...ERSIVPSLRQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Ubiquitin-conjugating enzyme E2 Q2
PRO_0000223879

Regions

Compositional bias134 – 17845Glu-rich

Sites

Active site3041Glycyl thioester intermediate By similarity

Natural variations

Alternative sequence1 – 6060MSVSG…HCNIT → MRMDSLTEEKLECRLWCCLS DPSPPGLAARCCVLERSIVP SLRQ in isoform 3.
VSP_044817
Alternative sequence296 – 31419YVLGG…KQGWS → LVHPSKGRWLNMLTVVCLD in isoform 2.
VSP_017298
Alternative sequence315 – 37561Missing in isoform 2.
VSP_017299

Experimental info

Sequence conflict1611E → K in BAH12288. Ref.1

Secondary structure

............................. 375
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2002. Version 1.
Checksum: 7DE07315E89178A3

FASTA37542,818
        10         20         30         40         50         60 
MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PQQGSPHSLP PPLTLHCNIT 

        70         80         90        100        110        120 
ESYPSSSPIW FVDSEDPNLT SVLERLEDTK NNNLLRQQLK WLICELCSLY NLPKHLDVEM 

       130        140        150        160        170        180 
LDQPLPTGQN GTTEEVTSEE EEEEEEMAED IEDLDHYEMK EEEPISGKKS EDEGIEKENL 

       190        200        210        220        230        240 
AILEKIRKTQ RQDHLNGAVS GSVQASDRLM KELRDIYRSQ SYKTGIYSVE LINDSLYDWH 

       250        260        270        280        290        300 
VKLQKVDPDS PLHSDLQILK EKEGIEYILL NFSFKDNFPF DPPFVRVVLP VLSGGYVLGG 

       310        320        330        340        350        360 
GALCMELLTK QGWSSAYSIE SVIMQINATL VKGKARVQFG ANKNQYNLAR AQQSYNSIVQ 

       370 
IHEKNGWYTP PKEDG 

« Hide

Isoform 2 [UniParc].

Checksum: 2C8943AFD4F6EE8A
Show »

FASTA31436,135
Isoform 3 [UniParc].

Checksum: 6C596548409AEFEB
Show »

FASTA35940,956

References

« Hide 'large scale' references
[1]"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 3).
Tissue: Thalamus.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Melanoma.
[3]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-375 (ISOFORM 2).
Tissue: Ovary, Placenta and Uterus.
[5]"Analysis of a novel human gene, LOC92912, over-expressed in hypopharyngeal tumours."
Seghatoleslam A., Zambrano A., Millon R., Ganguli G., Argentini M., Cromer A., Abecassis J., Wasylyk B.
Biochem. Biophys. Res. Commun. 339:422-429(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"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.
[7]"Structure of human ubiquitin-conjugating enzyme (UBCI) involved in embryo attachment and implantation."
Structural genomics consortium (SGC)
Submitted (JAN-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 197-363.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK296234 mRNA. Translation: BAH12288.1.
AL832429 mRNA. Translation: CAH10654.1.
AC019294 Genomic DNA. No translation available.
AC027104 Genomic DNA. No translation available.
BC006827 mRNA. Translation: AAH06827.1.
BC017708 mRNA. Translation: AAH17708.1.
BC034342 mRNA. Translation: AAH34342.1. Different initiation.
CCDSCCDS10286.1. [Q8WVN8-1]
CCDS45309.1. [Q8WVN8-3]
RefSeqNP_001138807.1. NM_001145335.1. [Q8WVN8-3]
NP_001271311.1. NM_001284382.1.
NP_775740.1. NM_173469.3. [Q8WVN8-1]
UniGeneHs.23033.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZUOX-ray1.80A/B197-363[»]
ProteinModelPortalQ8WVN8.
SMRQ8WVN8. Positions 201-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124986. 15 interactions.
IntActQ8WVN8. 8 interactions.
STRING9606.ENSP00000267938.

PTM databases

PhosphoSiteQ8WVN8.

Polymorphism databases

DMDM74751557.

Proteomic databases

MaxQBQ8WVN8.
PaxDbQ8WVN8.
PRIDEQ8WVN8.

Protocols and materials databases

DNASU92912.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267938; ENSP00000267938; ENSG00000140367. [Q8WVN8-1]
ENST00000561851; ENSP00000456229; ENSG00000140367. [Q8WVN8-3]
GeneID92912.
KEGGhsa:92912.
UCSCuc002bbg.2. human. [Q8WVN8-1]

Organism-specific databases

CTD92912.
GeneCardsGC15P076135.
H-InvDBHIX0172650.
HGNCHGNC:19248. UBE2Q2.
MIM612501. gene.
neXtProtNX_Q8WVN8.
PharmGKBPA142670652.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320521.
HOGENOMHOG000007757.
HOVERGENHBG061368.
InParanoidQ8WVN8.
KOK10582.
OMASYKAGIY.
OrthoDBEOG76DTSS.
PhylomeDBQ8WVN8.
TreeFamTF313338.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ8WVN8.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8WVN8.
BgeeQ8WVN8.
CleanExHS_UBE2Q2.
GenevestigatorQ8WVN8.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR006575. RWD-domain.
IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF05773. RWD. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SMARTSM00591. RWD. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 2 hits.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2Q2. human.
EvolutionaryTraceQ8WVN8.
GenomeRNAi92912.
NextBio77912.
PROQ8WVN8.
SOURCESearch...

Entry information

Entry nameUB2Q2_HUMAN
AccessionPrimary (citable) accession number: Q8WVN8
Secondary accession number(s): B7Z3Q2 expand/collapse secondary AC list , H3BRG2, Q8N4G6, Q96J08
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 117 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 15

Human chromosome 15: entries, gene names and cross-references to MIM