Q5VVX9 (UBE2U_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 U
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein U
Ubiquitin-protein ligase U

Gene names

Name:

UBE2U

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins By similarity.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5VVX9-1)

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: Q5VVX9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     227-321: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 321

321

Ubiquitin-conjugating enzyme E2 U

PRO_0000082512

Sites

Active site

89

1

Glycyl thioester intermediate By similarity

Natural variations

Alternative sequence

227 – 321

95

Missing in isoform 2.

VSP_016003

Natural variant

90

1

I → T.
Corresponds to variant rs7532933 [ dbSNP | Ensembl ].

VAR_057323

Secondary structure

1

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321

Helix Strand Turn

Details...

Helix

4 – 19

16

Beta strand

24 – 28

5

Beta strand

35 – 41

7

Turn

47 – 50

4

Beta strand

52 – 58

7

Beta strand

69 – 74

6

Turn

83 – 85

3

Helix

91 – 94

4

Helix

96 – 98

3

Helix

105 – 116

12

Helix

127 – 134

8

Helix

137 – 147

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 8104FE91620417BB	FASTA	321	37,741
	10 20 30 40 50 60 MHGRAYLLLH RDFCDLKENN YKGITAKPVS EDMMEWEVEI EGLQNSVWQG LVFQLTIHFT 70 80 90 100 110 120 SEYNYAPPVV KFITIPFHPN VDPHTGQPCI DFLDNPEKWN TNYTLSSILL ALQVMLSNPV 130 140 150 160 170 180 LENPVNLEAA RILVKDESLY RTILRLFNRP LQMKDDSQEL PKDPRKCIRP IKTTSFSDYY 190 200 210 220 230 240 QTWSRIATSK ATEYYRTPLL KVPNFIGQYY KWKKMDLQHQ KEWNLKYSVI KCWLARKRMP 250 260 270 280 290 300 HEVTHSMEEI KLCPTLIPTT DEIFLESPTA INSITDIYET EEEGWKSDTS LYENDTDEPR 310 320 EEEVEDLISW TNTLNTNTSE D
	Isoform 2 [UniParc]. Checksum: 2DFF8434DD9452FB	FASTA	226	26,689
	10 20 30 40 50 60 MHGRAYLLLH RDFCDLKENN YKGITAKPVS EDMMEWEVEI EGLQNSVWQG LVFQLTIHFT 70 80 90 100 110 120 SEYNYAPPVV KFITIPFHPN VDPHTGQPCI DFLDNPEKWN TNYTLSSILL ALQVMLSNPV 130 140 150 160 170 180 LENPVNLEAA RILVKDESLY RTILRLFNRP LQMKDDSQEL PKDPRKCIRP IKTTSFSDYY 190 200 210 220 QTWSRIATSK ATEYYRTPLL KVPNFIGQYY KWKKMDLQHQ KEWNLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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 2). Tissue: Brain.
[3]	"Novel ubiquitin-conjugating enzyme." Avvakumov G.V., Walker J.R., Choe J., Newman E.M., MacKenzie F., Bochkarev A., Dhe-Paganon S. Submitted (FEB-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 1-150.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL445205, AL161916 Genomic DNA. Translation: CAH71707.1.
AL445205, AL161916 Genomic DNA. Translation: CAH71708.1.
AL161916, AL445205 Genomic DNA. Translation: CAI22119.1.
AL161916, AL445205 Genomic DNA. Translation: CAI22120.1.
BC029895 mRNA. Translation: AAH29895.1.

IPI

IPI00166140.
IPI00645714.

RefSeq

NP_689702.1. NM_152489.1.

UniGene

Hs.388746.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YRV	X-ray	2.18	A	1-150	[»]

ProteinModelPortal

Q5VVX9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q5VVX9. 65 interactions.

STRING

9606.ENSP00000360116.

Polymorphism databases

DMDM

74747311.

Proteomic databases

PaxDb

Q5VVX9.

PRIDE

Q5VVX9.

Protocols and materials databases

DNASU

148581.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371076; ENSP00000360116; ENSG00000177414.
ENST00000371077; ENSP00000360117; ENSG00000177414.

GeneID

148581.

KEGG

hsa:148581.

UCSC

uc001dbn.1. human.

Organism-specific databases

CTD

148581.

GeneCards

GC01P064669.

HGNC

HGNC:28559. UBE2U.

HPA

HPA020472.
HPA021660.

neXtProt

NX_Q5VVX9.

PharmGKB

PA142670656.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000049184.

HOVERGEN

HBG080217.

InParanoid

Q5VVX9.

KO

K10584.

OMA

HPNVDPH.

OrthoDB

EOG4KPTBX.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

Bgee

Q5VVX9.

CleanEx

HS_UBE2U.

Genevestigator

Q5VVX9.

GermOnline

ENSG00000177414. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5VVX9.

GenomeRNAi

148581.

NextBio

85955.

Entry information

Entry name

UBE2U_HUMAN

Accession

Primary (citable) accession number: Q5VVX9
Secondary accession number(s): Q8N1D4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	December 7, 2004
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.