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Q9D479

- UVSSA_MOUSE

UniProt

Q9D479 - UVSSA_MOUSE

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Protein
UV-stimulated scaffold protein A
Gene
Uvssa, Kiaa1530
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Factor involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage. TC-NER allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Acts by promoting stabilization of ERCC6 by recruiting deubiquitinating enzyme USP7 to TC-NER complexes, preventing UV-induced degradation of ERCC6 by the proteasome. Interacts with the elongating form of RNA polymerase II (RNA pol IIo) and facilitates its ubiquitination at UV damage sites, leading to promote RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery. Not involved in processing oxidative damage By similarity.

GO - Molecular functioni

  1. RNA polymerase II core binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. protein ubiquitination Source: UniProtKB
  2. response to UV Source: UniProtKB
  3. transcription-coupled nucleotide-excision repair Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
UV-stimulated scaffold protein A
Gene namesi
Name:Uvssa
Synonyms:Kiaa1530
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1918351. Uvssa.

Subcellular locationi

Chromosome By similarity
Note: Accumulates at UV DNA damage sites By similarity.

GO - Cellular componenti

  1. chromosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 717717UV-stimulated scaffold protein A
PRO_0000317283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei284 – 2841Phosphoserine By similarity
Modified residuei291 – 2911Phosphoserine By similarity

Post-translational modificationi

Monoubiquitinated: ubiquitination does not increase in response to UV By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9D479.

PTM databases

PhosphoSiteiQ9D479.

Expressioni

Gene expression databases

ArrayExpressiQ9D479.
BgeeiQ9D479.
CleanExiMM_4933407H18RIK.
GenevestigatoriQ9D479.

Interactioni

Subunit structurei

Interacts with the elongating form of RNA polymerase II (RNA pol IIo). Interacts with ERCC6, ERCC8 and USP7 By similarity.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000085170.

Structurei

3D structure databases

ProteinModelPortaliQ9D479.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 145144VHS-like
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili169 – 19931 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi654 – 6629Poly-Lys

Sequence similaritiesi

Belongs to the UVSSA family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG313134.
GeneTreeiENSGT00390000000377.
HOVERGENiHBG076421.
InParanoidiQ9D479.
OMAiRMDQKKH.
OrthoDBiEOG7X0VHQ.
PhylomeDBiQ9D479.
TreeFamiTF321660.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR018610. DUF2043.
IPR008942. ENTH_VHS.
[Graphical view]
PfamiPF09740. DUF2043. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D479-1 [UniParc]FASTAAdd to Basket

« Hide

MDQKLSQLIE ELTTSGESQL NAQKMKELKK ICKSSEEQLS HAYRLLITQL    50
TQGHAEIRLS AFQIVDELFT RSHQFRMLLV SDFQEFLELT LGTDSDRPLP 100
PPREAAQRLR QAAMQAVEGW NEKFGQAYKK LALGYHFLKH TKKVDFRDIN 150
VRTVAERKRE EEKQKHLDKI HRESADRAKR EMEEMYDEIE CCLTEVENCF 200
KLLVPLDFVP CPEDKFFGEA SSMTEGYAPC PLSPDLATPR ESGLSGPQDE 250
EQPCCSKDLV ASAYHVGSVV GLKALPQTAM KDSSRDEDEP SDPDDFLRSH 300
GLGSHKYTLD VEVPSDGLKV QENEDNLAVL HAARDSLKLI QNKFLPTVCS 350
WVQRFTRAGT YSAHLKQAID LKMELELALK KYEELNIEPG RGQRSRTEAL 400
EDSEDEDQDF VEVPEKEGYE PRIPDHLRAE YGLEPKAPLK TLEKGTAVCK 450
LQERTRMRRE EEASDPTSAA AQMLRLQDCL SSPSPSSTRV LPGPEEAQKQ 500
AERARAPIVP FGVDLCYWGQ EQLTAGKILK SDSQHRFWKP SEVEEEVDSA 550
HVSEMLHSRH ITFSGTFEPV QHKCRALRPN GRLCERQDRL KCPFHGKIIP 600
RDDKGQPLNP EDRAREQRQQ LQRQQAHPDW QDPEFLKDVE AATGVDLGSS 650
RSSKKGKGKK KKHPNLTDLR ERTNTARARL EKKVFAKAAV QRVVAAMNQM 700
DQKKHEKFAN QFNYALK 717
Length:717
Mass (Da):81,759
Last modified:June 13, 2012 - v2
Checksum:iACC97A8DFAB47BB5
GO

Sequence cautioni

The sequence BAB30399.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAC98194.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821D → G in AAI44921. 1 Publication
Sequence conflicti397 – 44246Missing in BAC98194. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK016722 mRNA. Translation: BAB30399.1. Different initiation.
AK156117 mRNA. Translation: BAE33591.1.
AC145072 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37418.1.
BC061483 mRNA. Translation: AAH61483.1.
BC137803 mRNA. Translation: AAI37804.1.
BC144920 mRNA. Translation: AAI44921.1.
AK129384 Transcribed RNA. Translation: BAC98194.1. Different initiation.
CCDSiCCDS39064.1.
RefSeqiNP_001074570.1. NM_001081101.2.
XP_006504171.1. XM_006504108.1.
UniGeneiMm.132178.

Genome annotation databases

EnsembliENSMUST00000087864; ENSMUSP00000085170; ENSMUSG00000037355.
GeneIDi71101.
KEGGimmu:71101.
UCSCiuc008xas.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK016722 mRNA. Translation: BAB30399.1 . Different initiation.
AK156117 mRNA. Translation: BAE33591.1 .
AC145072 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37418.1 .
BC061483 mRNA. Translation: AAH61483.1 .
BC137803 mRNA. Translation: AAI37804.1 .
BC144920 mRNA. Translation: AAI44921.1 .
AK129384 Transcribed RNA. Translation: BAC98194.1 . Different initiation.
CCDSi CCDS39064.1.
RefSeqi NP_001074570.1. NM_001081101.2.
XP_006504171.1. XM_006504108.1.
UniGenei Mm.132178.

3D structure databases

ProteinModelPortali Q9D479.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000085170.

PTM databases

PhosphoSitei Q9D479.

Proteomic databases

PRIDEi Q9D479.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000087864 ; ENSMUSP00000085170 ; ENSMUSG00000037355 .
GeneIDi 71101.
KEGGi mmu:71101.
UCSCi uc008xas.2. mouse.

Organism-specific databases

CTDi 57654.
MGIi MGI:1918351. Uvssa.
Rougei Search...

Phylogenomic databases

eggNOGi NOG313134.
GeneTreei ENSGT00390000000377.
HOVERGENi HBG076421.
InParanoidi Q9D479.
OMAi RMDQKKH.
OrthoDBi EOG7X0VHQ.
PhylomeDBi Q9D479.
TreeFami TF321660.

Miscellaneous databases

NextBioi 333027.
PROi Q9D479.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9D479.
Bgeei Q9D479.
CleanExi MM_4933407H18RIK.
Genevestigatori Q9D479.

Family and domain databases

Gene3Di 1.25.40.90. 1 hit.
InterProi IPR018610. DUF2043.
IPR008942. ENTH_VHS.
[Graphical view ]
Pfami PF09740. DUF2043. 1 hit.
[Graphical view ]
SUPFAMi SSF48464. SSF48464. 1 hit.
ProtoNeti Search...

Publicationsi

  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].
    Strain: C57BL/6J and NOD.
    Tissue: Spleen and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Brain and Limb.
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-717.
    Tissue: Brain.

Entry informationi

Entry nameiUVSSA_MOUSE
AccessioniPrimary (citable) accession number: Q9D479
Secondary accession number(s): B2RQ84
, B7ZN03, Q3U1A8, Q6P7V8, Q6ZPN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 13, 2012
Last modified: July 9, 2014
This is version 75 of the entry and version 2 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

Similar proteinsi