Q96LR5 (UB2E2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
UbcH8
Ubiquitin carrier protein E2
Ubiquitin-protein ligase E2

Gene names

Name:	UBE2E2
Synonyms:	UBCH8

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	201 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'-, as well as 'Lys-63'-linked polyubiquitination. 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	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ISG15-protein conjugation Inferred from direct assay PubMed 16428300. Source: HGNC protein K11-linked ubiquitination Inferred from direct assay Ref.5. Source: UniProtKB protein K48-linked ubiquitination Inferred from direct assay Ref.5. Source: UniProtKB protein K63-linked ubiquitination Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ISG15 ligase activity Inferred from direct assay PubMed 16428300. Source: HGNC 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 – 201

201

Ubiquitin-conjugating enzyme E2 E2

PRO_0000082472

Sites

Active site

139

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

19

1

Phosphoserine Ref.7

Secondary structure

1

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201

Helix Strand Turn

Details...

Helix

55 – 69

15

Beta strand

75 – 82

8

Beta strand

86 – 92

7

Turn

98 – 101

4

Beta strand

103 – 109

7

Turn

112 – 115

4

Beta strand

120 – 125

6

Helix

141 – 143

3

Turn

144 – 146

3

Helix

153 – 165

13

Helix

175 – 183

9

Helix

185 – 199

15

Sequences

	Sequence		Length	Mass (Da)
	Q96LR5 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 3286FB51E2B9CD3E	FASTA	201	22,255
	10 20 30 40 50 60 MSTEAQRVDD SPSTSGGSSD GDQRESVQQE PEREQVQPKK KEGKISSKTA AKLSTSAKRI 70 80 90 100 110 120 QKELAEITLD PPPNCSAGPK GDNIYEWRST ILGPPGSVYE GGVFFLDITF SPDYPFKPPK 130 140 150 160 170 180 VTFRTRIYHC NINSQGVICL DILKDNWSPA LTISKVLLSI CSLLTDCNPA DPLVGSIATQ 190 200 YMTNRAEHDR MARQWTKRYA T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme." Kimura M., Hattori T., Matsuda Y., Yoshioka T., Sumi N., Umeda Y., Nakashima S., Okano Y. Cytogenet. Cell Genet. 78:107-111(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"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. , 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]. Tissue: Brain.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[4]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK057886 mRNA. Translation: BAB71605.1.
BC022332 mRNA. Translation: AAH22332.1.

IPI

IPI00102173.

RefSeq

NP_689866.1. NM_152653.3.

UniGene

Hs.475688.
Hs.595802.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y6L	X-ray	1.85	A/B/C	54-201	[»]

ProteinModelPortal

Q96LR5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96LR5. 35 interactions.

STRING

9606.ENSP00000379931.

PTM databases

PhosphoSite

Q96LR5.

Polymorphism databases

DMDM

47606201.

Proteomic databases

PRIDE

Q96LR5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000396703; ENSP00000379931; ENSG00000182247.
ENST00000425792; ENSP00000401053; ENSG00000182247.

GeneID

7325.

KEGG

hsa:7325.

UCSC

uc003ccg.2. human.

Organism-specific databases

CTD

7325.

GeneCards

GC03P023221.

HGNC

HGNC:12478. UBE2E2.

HPA

HPA003303.
HPA028872.
HPA030445.

MIM

602163. gene.

neXtProt

NX_Q96LR5.

PharmGKB

PA37128.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HOG000233455.

HOVERGEN

HBG063308.

InParanoid

Q96LR5.

KO

K06689.

OMA

FTNREEH.

OrthoDB

EOG48SGV9.

PhylomeDB

Q96LR5.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q96LR5.

Bgee

Q96LR5.

CleanEx

HS_UBE2E2.

Genevestigator

Q96LR5.

GermOnline

ENSG00000182247. 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

ChiTaRS

UBE2E2. human.

EvolutionaryTrace

Q96LR5.

GenomeRNAi

7325.

NextBio

28662.

SOURCE

Search...

Entry information

Entry name

UB2E2_HUMAN

Accession

Primary (citable) accession number: Q96LR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 107 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.