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Protein

Ubiquitin-conjugating enzyme E2 E2

Gene

UBE2E2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Catalyzes the ISGylation of influenza A virus NS1 protein.3 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ISG15 transferase activity Source: HGNC
  • ligase activity Source: UniProtKB-KW
  • ubiquitin conjugating enzyme activity Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: MGI
  • ISG15-protein conjugation Source: HGNC
  • positive regulation of G1/S transition of mitotic cell cycle Source: MGI
  • protein K11-linked ubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96LR5.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:UBE2E2
Synonyms:UBCH8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:12478. UBE2E2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37128.

Polymorphism and mutation databases

BioMutaiUBE2E2.
DMDMi47606201.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 201200Ubiquitin-conjugating enzyme E2 E2PRO_0000082472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei11 – 111Phosphoserine1 Publication
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei18 – 181Phosphoserine1 Publication
Modified residuei19 – 191Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96LR5.
PRIDEiQ96LR5.

PTM databases

PhosphoSiteiQ96LR5.

Expressioni

Gene expression databases

BgeeiQ96LR5.
CleanExiHS_UBE2E2.
ExpressionAtlasiQ96LR5. baseline and differential.
GenevestigatoriQ96LR5.

Organism-specific databases

HPAiCAB073417.
HPA028872.
HPA030445.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRDC3Q96B673EBI-2129763,EBI-2875665
DAZAP2Q150383EBI-2129763,EBI-724310
FAM9BQ8IZU03EBI-2129763,EBI-10175124
MID1O153445EBI-2129763,EBI-2340316
MID2Q9UJV3-23EBI-2129763,EBI-10172526
ospGQ99PZ62EBI-2129763,EBI-9316527From a different organism.
RNF5Q999425EBI-2129763,EBI-348482
TRIM39Q9HCM95EBI-2129763,EBI-739510

Protein-protein interaction databases

BioGridi113173. 72 interactions.
DIPiDIP-52704N.
IntActiQ96LR5. 45 interactions.
STRINGi9606.ENSP00000379931.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi55 – 6915Combined sources
Beta strandi75 – 828Combined sources
Beta strandi86 – 927Combined sources
Turni98 – 1014Combined sources
Beta strandi103 – 1097Combined sources
Turni112 – 1154Combined sources
Beta strandi120 – 1256Combined sources
Helixi141 – 1433Combined sources
Turni144 – 1463Combined sources
Helixi153 – 16513Combined sources
Helixi175 – 1839Combined sources
Helixi185 – 19915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y6LX-ray1.85A/B/C55-201[»]
ProteinModelPortaliQ96LR5.
SMRiQ96LR5. Positions 54-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96LR5.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ96LR5.
KOiK06689.
OMAiCNINSHG.
OrthoDBiEOG7PCJGX.
PhylomeDBiQ96LR5.
TreeFamiTF101117.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96LR5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTEAQRVDD SPSTSGGSSD GDQRESVQQE PEREQVQPKK KEGKISSKTA
60 70 80 90 100
AKLSTSAKRI QKELAEITLD PPPNCSAGPK GDNIYEWRST ILGPPGSVYE
110 120 130 140 150
GGVFFLDITF SPDYPFKPPK VTFRTRIYHC NINSQGVICL DILKDNWSPA
160 170 180 190 200
LTISKVLLSI CSLLTDCNPA DPLVGSIATQ YMTNRAEHDR MARQWTKRYA

T
Length:201
Mass (Da):22,255
Last modified:December 1, 2001 - v1
Checksum:i3286FB51E2B9CD3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK057886 mRNA. Translation: BAB71605.1.
BC022332 mRNA. Translation: AAH22332.1.
CCDSiCCDS2637.1.
RefSeqiNP_689866.1. NM_152653.3.
XP_005265489.1. XM_005265432.1.
UniGeneiHs.475688.
Hs.595802.

Genome annotation databases

EnsembliENST00000396703; ENSP00000379931; ENSG00000182247.
ENST00000425792; ENSP00000401053; ENSG00000182247.
GeneIDi7325.
KEGGihsa:7325.
UCSCiuc003ccg.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK057886 mRNA. Translation: BAB71605.1.
BC022332 mRNA. Translation: AAH22332.1.
CCDSiCCDS2637.1.
RefSeqiNP_689866.1. NM_152653.3.
XP_005265489.1. XM_005265432.1.
UniGeneiHs.475688.
Hs.595802.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y6LX-ray1.85A/B/C55-201[»]
ProteinModelPortaliQ96LR5.
SMRiQ96LR5. Positions 54-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113173. 72 interactions.
DIPiDIP-52704N.
IntActiQ96LR5. 45 interactions.
STRINGi9606.ENSP00000379931.

PTM databases

PhosphoSiteiQ96LR5.

Polymorphism and mutation databases

BioMutaiUBE2E2.
DMDMi47606201.

Proteomic databases

MaxQBiQ96LR5.
PRIDEiQ96LR5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396703; ENSP00000379931; ENSG00000182247.
ENST00000425792; ENSP00000401053; ENSG00000182247.
GeneIDi7325.
KEGGihsa:7325.
UCSCiuc003ccg.2. human.

Organism-specific databases

CTDi7325.
GeneCardsiGC03P023221.
HGNCiHGNC:12478. UBE2E2.
HPAiCAB073417.
HPA028872.
HPA030445.
MIMi602163. gene.
neXtProtiNX_Q96LR5.
PharmGKBiPA37128.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ96LR5.
KOiK06689.
OMAiCNINSHG.
OrthoDBiEOG7PCJGX.
PhylomeDBiQ96LR5.
TreeFamiTF101117.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96LR5.

Miscellaneous databases

ChiTaRSiUBE2E2. human.
EvolutionaryTraceiQ96LR5.
GeneWikiiUBE2E2.
GenomeRNAii7325.
NextBioi28662.
PROiQ96LR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96LR5.
CleanExiHS_UBE2E2.
ExpressionAtlasiQ96LR5. baseline and differential.
GenevestigatoriQ96LR5.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  5. "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.
  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. "ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells."
    Zhao C., Hsiang T.Y., Kuo R.L., Krug R.M.
    Proc. Natl. Acad. Sci. U.S.A. 107:2253-2258(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15 AND SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiUB2E2_HUMAN
AccessioniPrimary (citable) accession number: Q96LR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 1, 2001
Last modified: April 29, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.