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Q96LR5

- UB2E2_HUMAN

UniProt

Q96LR5 - UB2E2_HUMAN

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Protein
Ubiquitin-conjugating enzyme E2 E2
Gene
UBE2E2, UBCH8
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391Glycyl thioester intermediate By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ISG15 ligase activity Source: HGNC
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. ISG15-protein conjugation Source: HGNC
  2. protein K11-linked ubiquitination Source: UniProtKB
  3. protein K48-linked ubiquitination Source: UniProtKB
  4. 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

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: Chromosome 3

Organism-specific databases

HGNCiHGNC:12478. UBE2E2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37128.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 201200Ubiquitin-conjugating enzyme E2 E2
PRO_0000082472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei19 – 191Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96LR5.
PRIDEiQ96LR5.

PTM databases

PhosphoSiteiQ96LR5.

Expressioni

Gene expression databases

ArrayExpressiQ96LR5.
BgeeiQ96LR5.
CleanExiHS_UBE2E2.
GenevestigatoriQ96LR5.

Organism-specific databases

HPAiHPA003303.
HPA028872.
HPA030445.

Interactioni

Protein-protein interaction databases

BioGridi113173. 63 interactions.
IntActiQ96LR5. 37 interactions.
STRINGi9606.ENSP00000379931.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y6LX-ray1.85A/B/C55-201[»]
ProteinModelPortaliQ96LR5.
SMRiQ96LR5. Positions 54-201.

Miscellaneous databases

EvolutionaryTraceiQ96LR5.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

MSTEAQRVDD SPSTSGGSSD GDQRESVQQE PEREQVQPKK KEGKISSKTA    50
AKLSTSAKRI QKELAEITLD PPPNCSAGPK GDNIYEWRST ILGPPGSVYE 100
GGVFFLDITF SPDYPFKPPK VTFRTRIYHC NINSQGVICL DILKDNWSPA 150
LTISKVLLSI CSLLTDCNPA DPLVGSIATQ YMTNRAEHDR MARQWTKRYA 200
T 201
Length:201
Mass (Da):22,255
Last modified:December 1, 2001 - v1
Checksum:i3286FB51E2B9CD3E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi47606201.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK057886 mRNA. Translation: BAB71605.1 .
BC022332 mRNA. Translation: AAH22332.1 .
CCDSi CCDS2637.1.
RefSeqi NP_689866.1. NM_152653.3.
XP_005265489.1. XM_005265432.1.
UniGenei Hs.475688.
Hs.595802.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y6L X-ray 1.85 A/B/C 55-201 [» ]
ProteinModelPortali Q96LR5.
SMRi Q96LR5. Positions 54-201.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113173. 63 interactions.
IntActi Q96LR5. 37 interactions.
STRINGi 9606.ENSP00000379931.

PTM databases

PhosphoSitei Q96LR5.

Polymorphism databases

DMDMi 47606201.

Proteomic databases

MaxQBi Q96LR5.
PRIDEi Q96LR5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000396703 ; ENSP00000379931 ; ENSG00000182247 .
ENST00000425792 ; ENSP00000401053 ; ENSG00000182247 .
GeneIDi 7325.
KEGGi hsa:7325.
UCSCi uc003ccg.2. human.

Organism-specific databases

CTDi 7325.
GeneCardsi GC03P023221.
HGNCi HGNC:12478. UBE2E2.
HPAi HPA003303.
HPA028872.
HPA030445.
MIMi 602163. gene.
neXtProti NX_Q96LR5.
PharmGKBi PA37128.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi Q96LR5.
KOi K06689.
OMAi CNINSHG.
OrthoDBi EOG7PCJGX.
PhylomeDBi Q96LR5.
TreeFami TF101117.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki Q96LR5.

Miscellaneous databases

ChiTaRSi UBE2E2. human.
EvolutionaryTracei Q96LR5.
GeneWikii UBE2E2.
GenomeRNAii 7325.
NextBioi 28662.
PROi Q96LR5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96LR5.
Bgeei Q96LR5.
CleanExi HS_UBE2E2.
Genevestigatori Q96LR5.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 119 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

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