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Protein

Ubiquitin-conjugating enzyme E2 variant 1

Gene

UBE2V1

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

Functioni

Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes.7 Publications

GO - Molecular functioni

  1. ubiquitin-like protein transferase activity Source: GO_Central
  2. ubiquitin protein ligase activity Source: GO_Central
  3. ubiquitin protein ligase binding Source: GO_Central

GO - Biological processi

  1. cell differentiation Source: UniProtKB
  2. error-free postreplication DNA repair Source: Ensembl
  3. Fc-epsilon receptor signaling pathway Source: Reactome
  4. innate immune response Source: Reactome
  5. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  6. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  7. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: HGNC
  9. positive regulation of NF-kappaB transcription factor activity Source: HGNC
  10. positive regulation of transcription, DNA-templated Source: UniProtKB
  11. postreplication repair Source: GO_Central
  12. protein K63-linked ubiquitination Source: UniProtKB
  13. protein polyubiquitination Source: ProtInc
  14. regulation of DNA repair Source: ProtInc
  15. regulation of transcription, DNA-templated Source: UniProtKB
  16. T cell receptor signaling pathway Source: Reactome
  17. toll-like receptor 10 signaling pathway Source: Reactome
  18. toll-like receptor 2 signaling pathway Source: Reactome
  19. toll-like receptor 4 signaling pathway Source: Reactome
  20. toll-like receptor 5 signaling pathway Source: Reactome
  21. toll-like receptor 9 signaling pathway Source: Reactome
  22. toll-like receptor signaling pathway Source: Reactome
  23. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  24. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_22442. Interleukin-1 signaling.
REACT_24918. IRAK1 recruits IKK complex.
REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ13404.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 variant 1
Short name:
UEV-1
Alternative name(s):
CROC-1
TRAF6-regulated IKK activator 1 beta Uev1A
Gene namesi
Name:UBE2V1
Synonyms:CROC1, UBE2V, UEV1
ORF Names:P/OKcl.19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:12494. UBE2V1.

Subcellular locationi

Nucleus 2 Publications
Note: Excluded from the nucleolus.

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. protein complex Source: MGI
  6. UBC13-UEV1A complex Source: UniProtKB
  7. ubiquitin conjugating enzyme complex Source: HGNC
  8. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37142.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 147146Ubiquitin-conjugating enzyme E2 variant 1PRO_0000082600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ13404.
PaxDbiQ13404.
PRIDEiQ13404.

Expressioni

Tissue specificityi

Highly expressed in thyroid, pancreas, spinal cord, lymph node, trachea, adrenal gland, bone marrow and pancreas. Detected at low levels in heart, breast, placenta, brain, liver, kidney, stomach and lung.2 Publications

Inductioni

Down-regulated during differentiation of cultured colon adenocarcinoma cells.1 Publication

Gene expression databases

BgeeiQ13404.
GenevestigatoriQ13404.

Interactioni

Subunit structurei

Heterodimer with UBE2N. Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with TRAF6.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RNF111Q6ZNA42EBI-1050671,EBI-2129175
UBE2NP6108818EBI-1050671,EBI-1052908
XIAPP981703EBI-1050671,EBI-517127
ZNRF1Q8ND252EBI-1050671,EBI-2129250

Protein-protein interaction databases

BioGridi113183. 70 interactions.
132321. 1 interaction.
DIPiDIP-41911N.
IntActiQ13404. 108 interactions.
MINTiMINT-5002796.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2515Combined sources
Beta strandi31 – 399Combined sources
Beta strandi47 – 537Combined sources
Beta strandi56 – 583Combined sources
Turni59 – 624Combined sources
Beta strandi64 – 707Combined sources
Turni73 – 775Combined sources
Beta strandi81 – 866Combined sources
Beta strandi91 – 933Combined sources
Turni95 – 973Combined sources
Helixi102 – 1043Combined sources
Helixi106 – 1094Combined sources
Helixi117 – 12812Combined sources
Turni131 – 1355Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A4DX-ray1.69A8-147[»]
2C2VX-ray2.90C/F/I/L8-147[»]
2HLWNMR-A8-147[»]
ProteinModelPortaliQ13404.
SMRiQ13404. Positions 8-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13404.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG119330.
GeneTreeiENSGT00740000115534.
HOGENOMiHOG000036561.
HOVERGENiHBG054552.
InParanoidiQ13404.
KOiK10704.
OMAiPPNTAYE.
OrthoDBiEOG77M8R5.
TreeFamiTF316971.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 3 (identifier: Q13404-4) [UniParc]FASTAAdd to basket

Also known as: Isoform 2

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.

« Hide

        10         20         30         40         50
MAATTGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG
60 70 80 90 100
MIIGPPRTIY ENRIYSLKIE CGPKYPEAPP FVRFVTKINM NGVNSSNGVV
110 120 130 140
DPRAISVLAK WQNSYSIKVV LQELRRLMMS KENMKLPQPP EGQCYSN
Length:147
Mass (Da):16,495
Last modified:September 22, 2009 - v2
Checksum:iBA53837F21977B3F
GO
Isoform 1 (identifier: Q13404-1) [UniParc]FASTAAdd to basket

Also known as: CROC-1B, UEV-1B, Isoform 4

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MAATTGS → MAYKFRTHSP...PHETYFCITT

Show »
Length:221
Mass (Da):25,797
Checksum:i6EE5C0FCC8CBBEE6
GO
Isoform 2 (identifier: Q13404-2) [UniParc]FASTAAdd to basket

Also known as: CROC-1A, UEV-1A

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MAATTGSGVKVPRN → MPGEVQASYLKSQSKLSDEGRLEPRKFHCKGSKSPSQ

Show »
Length:170
Mass (Da):19,228
Checksum:i9D3A8AC1EBEB22A6
GO
Isoform 4 (identifier: Q13404-6) [UniParc]FASTAAdd to basket

Also known as: UEV-1As

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-57: LTRWTGMIIGPPR → MKEDLNLENFTAK

Show »
Length:103
Mass (Da):11,842
Checksum:i76C152A73DE9AC40
GO
Isoform 5 (identifier: Q13404-7) [UniParc]FASTAAdd to basket

Also known as: Isoform 3

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MAATTGS → MPGEVQASYLKSQSKLSDEGRLEPRKFHCK

Show »
Length:170
Mass (Da):19,307
Checksum:i5B2E8C6FFDF51510
GO
Isoform 6 (identifier: Q13404-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-99: Missing.

Note: No experimental confirmation available.

Show »
Length:105
Mass (Da):11,766
Checksum:iD7C2659FBA3FC719
GO

Sequence cautioni

The sequence AAH08944.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC16955.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 1 (identifier: Q13404-1)
Sequence conflicti71 – 8111SPHETYFCITT → WPTSSAQCYSP in AAC02755 (PubMed:9418904).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444Missing in isoform 4. 1 PublicationVSP_038032Add
BLAST
Alternative sequencei1 – 1414MAATT…KVPRN → MPGEVQASYLKSQSKLSDEG RLEPRKFHCKGSKSPSQ in isoform 2. 2 PublicationsVSP_038033Add
BLAST
Alternative sequencei1 – 77MAATTGS → MAYKFRTHSPEALEQLYPWE CFVFCLIIFGTFTNQIHKWS HTYFGLPRWVTLLQDWHVIL PRKHHRIHHVSPHETYFCIT T in isoform 1. 3 PublicationsVSP_038034
Alternative sequencei1 – 77MAATTGS → MPGEVQASYLKSQSKLSDEG RLEPRKFHCK in isoform 5. 1 PublicationVSP_038035
Alternative sequencei45 – 5713LTRWT…IGPPR → MKEDLNLENFTAK in isoform 4. 1 PublicationVSP_038036Add
BLAST
Alternative sequencei58 – 9942Missing in isoform 6. 1 PublicationVSP_044818Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39360 mRNA. Translation: AAB72015.1.
U39361 mRNA. Translation: AAB72016.1.
U49278 mRNA. Translation: AAC02757.1.
U97279 mRNA. Translation: AAC02780.1.
U97280 mRNA. Translation: AAC02755.1.
U97281 mRNA. Translation: AAC02756.1.
AY008273 mRNA. Translation: AAG24229.1.
BT007382 mRNA. Translation: AAP36046.1.
DA580976 mRNA. No translation available.
AL034423 Genomic DNA. Translation: CAB76864.1.
AL034423 Genomic DNA. Translation: CAB76865.1.
AL034423 Genomic DNA. Translation: CAC16954.1.
AL034423 Genomic DNA. Translation: CAC16955.2. Different initiation.
AL034423 Genomic DNA. Translation: CAI19382.1.
AL034423 Genomic DNA. Translation: CAI19383.1.
CH471077 Genomic DNA. Translation: EAW75635.1.
CH471077 Genomic DNA. Translation: EAW75634.1.
CH471077 Genomic DNA. Translation: EAW75636.1.
BC000468 mRNA. Translation: AAH00468.1.
BC008944 mRNA. Translation: AAH08944.2. Different initiation.
CCDSiCCDS13426.1. [Q13404-7]
CCDS13427.1. [Q13404-6]
CCDS33483.1. [Q13404-4]
CCDS58775.1. [Q13404-8]
RefSeqiNP_001027459.1. NM_001032288.2. [Q13404-4]
NP_001244322.1. NM_001257393.1. [Q13404-7]
NP_001244323.1. NM_001257394.1. [Q13404-6]
NP_001244325.1. NM_001257396.1. [Q13404-8]
NP_068823.2. NM_021988.5. [Q13404-7]
NP_071887.1. NM_022442.5. [Q13404-6]
NP_954595.1. NM_199144.2. [Q13404-7]
NP_954673.1. NM_199203.2.
UniGeneiHs.420529.
Hs.744839.

Genome annotation databases

EnsembliENST00000340309; ENSP00000340305; ENSG00000244687. [Q13404-7]
ENST00000371657; ENSP00000360720; ENSG00000244687. [Q13404-8]
ENST00000371674; ENSP00000360739; ENSG00000244687. [Q13404-4]
ENST00000371677; ENSP00000360742; ENSG00000244687. [Q13404-7]
ENST00000415862; ENSP00000407770; ENSG00000244687. [Q13404-6]
GeneIDi387522.
7335.
KEGGihsa:387522.
hsa:7335.
UCSCiuc002xva.4. human. [Q13404-4]
uc002xvc.4. human. [Q13404-6]
uc002xvd.4. human. [Q13404-7]
uc031rtz.1. human.

Polymorphism databases

DMDMi259016163.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39360 mRNA. Translation: AAB72015.1.
U39361 mRNA. Translation: AAB72016.1.
U49278 mRNA. Translation: AAC02757.1.
U97279 mRNA. Translation: AAC02780.1.
U97280 mRNA. Translation: AAC02755.1.
U97281 mRNA. Translation: AAC02756.1.
AY008273 mRNA. Translation: AAG24229.1.
BT007382 mRNA. Translation: AAP36046.1.
DA580976 mRNA. No translation available.
AL034423 Genomic DNA. Translation: CAB76864.1.
AL034423 Genomic DNA. Translation: CAB76865.1.
AL034423 Genomic DNA. Translation: CAC16954.1.
AL034423 Genomic DNA. Translation: CAC16955.2. Different initiation.
AL034423 Genomic DNA. Translation: CAI19382.1.
AL034423 Genomic DNA. Translation: CAI19383.1.
CH471077 Genomic DNA. Translation: EAW75635.1.
CH471077 Genomic DNA. Translation: EAW75634.1.
CH471077 Genomic DNA. Translation: EAW75636.1.
BC000468 mRNA. Translation: AAH00468.1.
BC008944 mRNA. Translation: AAH08944.2. Different initiation.
CCDSiCCDS13426.1. [Q13404-7]
CCDS13427.1. [Q13404-6]
CCDS33483.1. [Q13404-4]
CCDS58775.1. [Q13404-8]
RefSeqiNP_001027459.1. NM_001032288.2. [Q13404-4]
NP_001244322.1. NM_001257393.1. [Q13404-7]
NP_001244323.1. NM_001257394.1. [Q13404-6]
NP_001244325.1. NM_001257396.1. [Q13404-8]
NP_068823.2. NM_021988.5. [Q13404-7]
NP_071887.1. NM_022442.5. [Q13404-6]
NP_954595.1. NM_199144.2. [Q13404-7]
NP_954673.1. NM_199203.2.
UniGeneiHs.420529.
Hs.744839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A4DX-ray1.69A8-147[»]
2C2VX-ray2.90C/F/I/L8-147[»]
2HLWNMR-A8-147[»]
ProteinModelPortaliQ13404.
SMRiQ13404. Positions 8-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113183. 70 interactions.
132321. 1 interaction.
DIPiDIP-41911N.
IntActiQ13404. 108 interactions.
MINTiMINT-5002796.

Polymorphism databases

DMDMi259016163.

Proteomic databases

MaxQBiQ13404.
PaxDbiQ13404.
PRIDEiQ13404.

Protocols and materials databases

DNASUi387522.
7335.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340309; ENSP00000340305; ENSG00000244687. [Q13404-7]
ENST00000371657; ENSP00000360720; ENSG00000244687. [Q13404-8]
ENST00000371674; ENSP00000360739; ENSG00000244687. [Q13404-4]
ENST00000371677; ENSP00000360742; ENSG00000244687. [Q13404-7]
ENST00000415862; ENSP00000407770; ENSG00000244687. [Q13404-6]
GeneIDi387522.
7335.
KEGGihsa:387522.
hsa:7335.
UCSCiuc002xva.4. human. [Q13404-4]
uc002xvc.4. human. [Q13404-6]
uc002xvd.4. human. [Q13404-7]
uc031rtz.1. human.

Organism-specific databases

CTDi387522.
7335.
GeneCardsiGC20M048698.
HGNCiHGNC:12494. UBE2V1.
MIMi602995. gene.
neXtProtiNX_Q13404.
PharmGKBiPA37142.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG119330.
GeneTreeiENSGT00740000115534.
HOGENOMiHOG000036561.
HOVERGENiHBG054552.
InParanoidiQ13404.
KOiK10704.
OMAiPPNTAYE.
OrthoDBiEOG77M8R5.
TreeFamiTF316971.

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_22442. Interleukin-1 signaling.
REACT_24918. IRAK1 recruits IKK complex.
REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ13404.

Miscellaneous databases

ChiTaRSiUBE2V1. human.
EvolutionaryTraceiQ13404.
GeneWikiiUBE2V1.
NextBioi101372.
PROiQ13404.
SOURCEiSearch...

Gene expression databases

BgeeiQ13404.
GenevestigatoriQ13404.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter."
    Rothofsky M.L., Lin S.L.
    Gene 195:141-149(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Brain.
  2. "Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells."
    Sancho E., Vila M.R., Sanchez-Pulido L., Lozano J.J., Paciucci R., Nadal M., Fox M., Harvey C., Bercovich B., Loukili N., Ciechanover A., Lin S.L., Sanz F., Estivill X., Valencia A., Thomson T.M.
    Mol. Cell. Biol. 18:576-589(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, INDUCTION, TISSUE SPECIFICITY.
    Tissue: Colon adenocarcinoma.
  3. "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain."
    Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., Chen Z.J.
    Cell 103:351-361(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH TRAF6 AND UBE2N, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "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 (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Lung.
  6. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Bienvenut W.V., Pchelintsev N., Adams P.D.
    Submitted (JUN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13 (ISOFORM 3), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung fibroblast.
  9. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-147 (ISOFORMS 1 AND 3).
    Tissue: Muscle.
  10. "Role of UEV-1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage."
    Thomson T.M., Khalid H., Lozano J.J., Sancho E., Arino J.
    FEBS Lett. 423:49-52(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family."
    Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F.
    Nucleic Acids Res. 26:3908-3914(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  12. "Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene."
    Thomson T.M., Lozano J.J., Loukili N., Carrio R., Serras F., Cormand B., Valeri M., Diaz V.M., Abril J., Burset M., Merino J., Macaya A., Corominas M., Guigo R.
    Genome Res. 10:1743-1756(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION OF TMEM189-UBE2V1 FUSION PROTEIN.
    Tissue: Colon cancer.
  13. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
    David Y., Ziv T., Admon A., Navon A.
    J. Biol. Chem. 285:8595-8604(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: FUNCTION.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
    Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
    Mol. Cell 20:525-538(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 8-147 IN COMPLEX WITH STUB1 AND UBE2N.

Entry informationi

Entry nameiUB2V1_HUMAN
AccessioniPrimary (citable) accession number: Q13404
Secondary accession number(s): E1P629
, Q13403, Q13532, Q5TGE0, Q5TGE3, Q96H34, Q9GZT0, Q9GZW1, Q9H4J3, Q9H4J4, Q9UKL1, Q9UM48, Q9UM49, Q9UM50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: September 22, 2009
Last modified: April 1, 2015
This is version 153 of the entry and version 2 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

Miscellaneous

In human, TMEM189/KUA and UBE2V1/UEV1 are adjacent genes which can produce independent proteins and can also be fused to form a TMEM189-UBE2V1 hybrid protein.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.