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Q9CZY3

- UB2V1_MOUSE

UniProt

Q9CZY3 - UB2V1_MOUSE

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Protein

Ubiquitin-conjugating enzyme E2 variant 1

Gene

Ube2v1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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 (By similarity). 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 (By similarity).By similarity

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ubiquitin conjugating enzyme binding Source: MGI
  3. ubiquitin-protein transferase activity Source: MGI

GO - Biological processi

  1. error-free postreplication DNA repair Source: MGI
  2. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  3. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  4. protein K63-linked ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_198543. IRAK1 recruits IKK complex.
REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_205561. FCERI mediated NF-kB activation.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 variant 1
Short name:
UEV-1
Alternative name(s):
CROC-1
Gene namesi
Name:Ube2v1
Synonyms:Croc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1913839. Ube2v1.

Subcellular locationi

Nucleus By similarity
Note: Excluded from the nucleolus.By similarity

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-KW
  4. protein complex Source: MGI
  5. UBC13-UEV1A complex Source: UniProtKB
  6. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 147146Ubiquitin-conjugating enzyme E2 variant 1PRO_0000082601Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CZY3.
PaxDbiQ9CZY3.
PRIDEiQ9CZY3.

PTM databases

PhosphoSiteiQ9CZY3.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in heart, brain, liver, skeletal msucle, kidney and testis. Detected at lower levels in lung and spleen.1 Publication

Gene expression databases

BgeeiQ9CZY3.
CleanExiMM_UBE2V1.
ExpressionAtlasiQ9CZY3. baseline and differential.
GenevestigatoriQ9CZY3.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi211575. 3 interactions.
IntActiQ9CZY3. 1 interaction.
MINTiMINT-1869924.

Structurei

3D structure databases

ProteinModelPortaliQ9CZY3.
SMRiQ9CZY3. Positions 8-146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG239185.
GeneTreeiENSGT00740000115534.
HOGENOMiHOG000036561.
HOVERGENiHBG054552.
InParanoidiQ9CZY3.
KOiK10704.
OrthoDBiEOG77M8R5.
PhylomeDBiQ9CZY3.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9CZY3-1) [UniParc]FASTAAdd to Basket

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 SVRFVTRVNM SGVSSSNGVV
110 120 130 140
DPRATAVLAK WQNSHSIKVI LQELRRLMMS KENMKLPQPP EGQCYSN
Length:147
Mass (Da):16,355
Last modified:June 1, 2001 - v1
Checksum:iE66E83EEE9D08E92
GO
Isoform 2 (identifier: Q9CZY3-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:105
Mass (Da):11,725
Checksum:iCCCF79601969C719
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591I → M in AAG22085. (PubMed:11406273)Curated
Sequence conflicti66 – 661S → G in AAG22085. (PubMed:11406273)Curated
Sequence conflicti78 – 781A → P in AAG22085. (PubMed:11406273)Curated
Sequence conflicti100 – 1001V → M in AAG22085. (PubMed:11406273)Curated
Sequence conflicti108 – 1081L → P in AAH19372. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 9942Missing in isoform 2. 1 PublicationVSP_011528Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012021 mRNA. Translation: BAB27978.1.
AL589870 Genomic DNA. Translation: CAM13830.1.
BC003449 mRNA. Translation: AAH03449.1.
BC019372 mRNA. Translation: AAH19372.1.
AF303829 mRNA. Translation: AAG22085.1.
CCDSiCCDS17103.1. [Q9CZY3-1]
RefSeqiNP_075719.1. NM_023230.2. [Q9CZY3-1]
XP_006500078.1. XM_006500015.1. [Q9CZY3-2]
UniGeneiMm.278783.
Mm.360108.

Genome annotation databases

EnsembliENSMUST00000060645; ENSMUSP00000053109; ENSMUSG00000078923. [Q9CZY3-2]
ENSMUST00000109207; ENSMUSP00000104830; ENSMUSG00000078923. [Q9CZY3-1]
GeneIDi66589.
KEGGimmu:66589.
UCSCiuc008oaa.1. mouse. [Q9CZY3-1]
uc008oab.1. mouse. [Q9CZY3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012021 mRNA. Translation: BAB27978.1 .
AL589870 Genomic DNA. Translation: CAM13830.1 .
BC003449 mRNA. Translation: AAH03449.1 .
BC019372 mRNA. Translation: AAH19372.1 .
AF303829 mRNA. Translation: AAG22085.1 .
CCDSi CCDS17103.1. [Q9CZY3-1 ]
RefSeqi NP_075719.1. NM_023230.2. [Q9CZY3-1 ]
XP_006500078.1. XM_006500015.1. [Q9CZY3-2 ]
UniGenei Mm.278783.
Mm.360108.

3D structure databases

ProteinModelPortali Q9CZY3.
SMRi Q9CZY3. Positions 8-146.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211575. 3 interactions.
IntActi Q9CZY3. 1 interaction.
MINTi MINT-1869924.

PTM databases

PhosphoSitei Q9CZY3.

Proteomic databases

MaxQBi Q9CZY3.
PaxDbi Q9CZY3.
PRIDEi Q9CZY3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000060645 ; ENSMUSP00000053109 ; ENSMUSG00000078923 . [Q9CZY3-2 ]
ENSMUST00000109207 ; ENSMUSP00000104830 ; ENSMUSG00000078923 . [Q9CZY3-1 ]
GeneIDi 66589.
KEGGi mmu:66589.
UCSCi uc008oaa.1. mouse. [Q9CZY3-1 ]
uc008oab.1. mouse. [Q9CZY3-2 ]

Organism-specific databases

CTDi 7335.
MGIi MGI:1913839. Ube2v1.

Phylogenomic databases

eggNOGi NOG239185.
GeneTreei ENSGT00740000115534.
HOGENOMi HOG000036561.
HOVERGENi HBG054552.
InParanoidi Q9CZY3.
KOi K10704.
OrthoDBi EOG77M8R5.
PhylomeDBi Q9CZY3.
TreeFami TF316971.

Enzyme and pathway databases

Reactomei REACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_198543. IRAK1 recruits IKK complex.
REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_205561. FCERI mediated NF-kB activation.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.

Miscellaneous databases

NextBioi 322088.
PROi Q9CZY3.
SOURCEi Search...

Gene expression databases

Bgeei Q9CZY3.
CleanExi MM_UBE2V1.
ExpressionAtlasi Q9CZY3. baseline and differential.
Genevestigatori Q9CZY3.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORMS 1 AND 2).
    Strain: NMRI.
    Tissue: Mammary tumor.
  4. "Molecular cloning and functional characterization of two murine cDNAs which encode Ubc variants involved in DNA repair and mutagenesis."
    Franko J., Ashley C., Xiao W.
    Biochim. Biophys. Acta 1519:70-77(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-147 (ISOFORM 1), FUNCTION, INTERACTION WITH UBE2N, TISSUE SPECIFICITY.
  5. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STUB1 AND UBE2N.

Entry informationi

Entry nameiUB2V1_MOUSE
AccessioniPrimary (citable) accession number: Q9CZY3
Secondary accession number(s): A2A467, Q8VEB5, Q9ERI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3