P62256 (UBE2H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
UbcH2
Ubiquitin carrier protein H
Ubiquitin-conjugating enzyme E2-20K
Ubiquitin-protein ligase H

Gene names

Name:

UBE2H

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Protein existence	Evidence 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'- and 'Lys-48'-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A. Ref.1 Ref.5
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
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein K11-linked ubiquitination Inferred from direct assay Ref.5. Source: UniProtKB protein K48-linked ubiquitination Inferred from direct assay Ref.5. Source: UniProtKB ubiquitin-dependent protein catabolic process Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 183

183

Ubiquitin-conjugating enzyme E2 H

PRO_0000082486

Sites

Active site

87

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

60

1

N6-acetyllysine Ref.4

Modified residue

64

1

N6-acetyllysine Ref.4

Secondary structure

1

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183

Helix Strand Turn

Details...

Helix

6 – 20

15

Beta strand

21 – 23

3

Beta strand

25 – 30

6

Beta strand

33 – 39

7

Turn

45 – 48

4

Beta strand

50 – 56

7

Turn

59 – 63

5

Beta strand

67 – 72

6

Turn

81 – 83

3

Helix

88 – 94

7

Helix

103 – 106

4

Helix

108 – 114

7

Helix

124 – 132

9

Helix

134 – 148

15

Helix

151 – 154

4

Sequences

	Sequence		Length	Mass (Da)
	P62256 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 3DD5D365945F708C	FASTA	183	20,655
	10 20 30 40 50 60 MSSPSPGKRR MDTDVVKLIE SKHEVTILGG LNEFVVKFYG PQGTPYEGGV WKVRVDLPDK 70 80 90 100 110 120 YPFKSPSIGF MNKIFHPNID EASGTVCLDV INQTWTALYD LTNIFESFLP QLLAYPNPID 130 140 150 160 170 180 PLNGDAAAMY LHRPEEYKQK IKEYIQKYAT EEALKEQEEG TGDSSSESSM SDFSEDEAQD MEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human ubiquitin-conjugating enzyme homologous to yeast UBC8." Kaiser P., Seufert W., Hoefferer L., Kofler B., Sachsenmaier C., Herzog H., Jentsch S., Schweiger M., Schneider R. J. Biol. Chem. 269:8797-8802(1994) [PubMed: 8132613] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[4]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60 AND LYS-64, MASS SPECTROMETRY.
[5]	"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: 20061386] [Abstract] Cited for: FUNCTION.
[6]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z29328 mRNA. Translation: CAA82525.1.
Z29330 mRNA. Translation: CAA82527.1.
Z29331 mRNA. Translation: CAA82528.1.
BT006756 mRNA. Translation: AAP35402.1.
BC006277 mRNA. Translation: AAH06277.1.

IPI

IPI00020965.

PIR

A53516.

RefSeq

NP_001189427.1. NM_001202498.1.
NP_003335.1. NM_003344.3.

UniGene

Hs.643548.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Z5D	X-ray	2.10	A/B	1-160	[»]

ProteinModelPortal

P62256.

SMR

P62256. Positions 4-155.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62256. 41 interactions.

STRING

P62256.

PTM databases

PhosphoSite

P62256.

Polymorphism databases

DMDM

51338683.

Proteomic databases

PRIDE

P62256.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355621; ENSP00000347836; ENSG00000186591.
ENST00000486424; ENSP00000417644; ENSG00000186591.

GeneID

7328.

KEGG

hsa:7328.

UCSC

uc003vpf.1. human.

Organism-specific databases

CTD

7328.

GeneCards

GC07M129470.

H-InvDB

HIX0007069.

HGNC

HGNC:12484. UBE2H.

HPA

HPA003302.

MIM

601082. gene.

neXtProt

NX_P62256.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000004852.

HOGENOM

HBG756483.

HOVERGEN

HBG063308.

InParanoid

P62256.

OMA

AGKRRMD.

OrthoDB

EOG4D52ZV.

PhylomeDB

P62256.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P62256.

Bgee

P62256.

CleanEx

HS_UBE2H.

Genevestigator

P62256.

GermOnline

ENSG00000186591. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

KO

K10576.

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

NextBio

28676.

SOURCE

Search...

Entry information

Entry name

UBE2H_HUMAN

Accession

Primary (citable) accession number: P62256
Secondary accession number(s): P37286

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 86 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.