UVSSA_MOUSE
ID UVSSA_MOUSE Reviewed; 717 AA.
AC Q9D479; B2RQ84; B7ZN03; Q3U1A8; Q6P7V8; Q6ZPN7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=UV-stimulated scaffold protein A;
GN Name=Uvssa; Synonyms=Kiaa1530;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-717.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Factor involved in transcription-coupled nucleotide excision
CC repair (TC-NER) in response to UV damage. TC-NER allows RNA polymerase
CC II-blocking lesions to be rapidly removed from the transcribed strand
CC of active genes. Acts by promoting stabilization of ERCC6 by recruiting
CC deubiquitinating enzyme USP7 to TC-NER complexes, preventing UV-induced
CC degradation of ERCC6 by the proteasome. Interacts with the elongating
CC form of RNA polymerase II (RNA pol IIo) and facilitates its
CC ubiquitination at UV damage sites, leading to promote RNA pol IIo
CC backtracking to allow access to the nucleotide excision repair
CC machinery. Not involved in processing oxidative damage (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the elongating form of RNA polymerase II (RNA
CC pol IIo). Interacts with ERCC6, ERCC8 and USP7 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250}. Note=Accumulates at UV
CC DNA damage sites. {ECO:0000250}.
CC -!- PTM: Monoubiquitinated: ubiquitination does not increase in response to
CC UV. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UVSSA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30399.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98194.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK016722; BAB30399.1; ALT_INIT; mRNA.
DR EMBL; AK156117; BAE33591.1; -; mRNA.
DR EMBL; AC145072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466524; EDL37418.1; -; Genomic_DNA.
DR EMBL; BC061483; AAH61483.1; -; mRNA.
DR EMBL; BC137803; AAI37804.1; -; mRNA.
DR EMBL; BC144920; AAI44921.1; -; mRNA.
DR EMBL; AK129384; BAC98194.1; ALT_INIT; Transcribed_RNA.
DR CCDS; CCDS39064.1; -.
DR RefSeq; NP_001074570.1; NM_001081101.2.
DR RefSeq; XP_006504171.1; XM_006504108.3.
DR AlphaFoldDB; Q9D479; -.
DR SMR; Q9D479; -.
DR BioGRID; 214478; 1.
DR STRING; 10090.ENSMUSP00000085170; -.
DR iPTMnet; Q9D479; -.
DR PhosphoSitePlus; Q9D479; -.
DR EPD; Q9D479; -.
DR jPOST; Q9D479; -.
DR MaxQB; Q9D479; -.
DR PaxDb; Q9D479; -.
DR PeptideAtlas; Q9D479; -.
DR PRIDE; Q9D479; -.
DR ProteomicsDB; 300099; -.
DR Antibodypedia; 22237; 52 antibodies from 18 providers.
DR Ensembl; ENSMUST00000087864; ENSMUSP00000085170; ENSMUSG00000037355.
DR Ensembl; ENSMUST00000202816; ENSMUSP00000144400; ENSMUSG00000037355.
DR GeneID; 71101; -.
DR KEGG; mmu:71101; -.
DR UCSC; uc008xar.1; mouse.
DR CTD; 57654; -.
DR MGI; MGI:1918351; Uvssa.
DR VEuPathDB; HostDB:ENSMUSG00000037355; -.
DR eggNOG; KOG2374; Eukaryota.
DR GeneTree; ENSGT00390000000377; -.
DR HOGENOM; CLU_023577_0_0_1; -.
DR InParanoid; Q9D479; -.
DR OMA; TSEHRFW; -.
DR OrthoDB; 996127at2759; -.
DR PhylomeDB; Q9D479; -.
DR TreeFam; TF321660; -.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR BioGRID-ORCS; 71101; 1 hit in 107 CRISPR screens.
DR ChiTaRS; Uvssa; mouse.
DR PRO; PR:Q9D479; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D479; protein.
DR Bgee; ENSMUSG00000037355; Expressed in manus and 217 other tissues.
DR ExpressionAtlas; Q9D479; baseline and differential.
DR Genevisible; Q9D479; MM.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR018610; UVSSA.
DR PANTHER; PTHR28670; PTHR28670; 1.
DR Pfam; PF09740; DUF2043; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; DNA damage; DNA repair; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..717
FT /note="UV-stimulated scaffold protein A"
FT /id="PRO_0000317283"
FT REGION 2..145
FT /note="VHS-like"
FT REGION 231..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..199
FT /evidence="ECO:0000255"
FT COMPBIAS 280..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2YD98"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2YD98"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 82
FT /note="D -> G (in Ref. 4; AAI44921)"
FT /evidence="ECO:0000305"
FT CONFLICT 397..442
FT /note="Missing (in Ref. 5; BAC98194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 81759 MW; ACC97A8DFAB47BB5 CRC64;
MDQKLSQLIE ELTTSGESQL NAQKMKELKK ICKSSEEQLS HAYRLLITQL TQGHAEIRLS
AFQIVDELFT RSHQFRMLLV SDFQEFLELT LGTDSDRPLP PPREAAQRLR QAAMQAVEGW
NEKFGQAYKK LALGYHFLKH TKKVDFRDIN VRTVAERKRE EEKQKHLDKI HRESADRAKR
EMEEMYDEIE CCLTEVENCF KLLVPLDFVP CPEDKFFGEA SSMTEGYAPC PLSPDLATPR
ESGLSGPQDE EQPCCSKDLV ASAYHVGSVV GLKALPQTAM KDSSRDEDEP SDPDDFLRSH
GLGSHKYTLD VEVPSDGLKV QENEDNLAVL HAARDSLKLI QNKFLPTVCS WVQRFTRAGT
YSAHLKQAID LKMELELALK KYEELNIEPG RGQRSRTEAL EDSEDEDQDF VEVPEKEGYE
PRIPDHLRAE YGLEPKAPLK TLEKGTAVCK LQERTRMRRE EEASDPTSAA AQMLRLQDCL
SSPSPSSTRV LPGPEEAQKQ AERARAPIVP FGVDLCYWGQ EQLTAGKILK SDSQHRFWKP
SEVEEEVDSA HVSEMLHSRH ITFSGTFEPV QHKCRALRPN GRLCERQDRL KCPFHGKIIP
RDDKGQPLNP EDRAREQRQQ LQRQQAHPDW QDPEFLKDVE AATGVDLGSS RSSKKGKGKK
KKHPNLTDLR ERTNTARARL EKKVFAKAAV QRVVAAMNQM DQKKHEKFAN QFNYALK
