ID UBX5_YEAST Reviewed; 500 AA.
AC Q06682; D6VSW2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=UBX domain-containing protein 5;
GN Name=UBX5; OrderedLocusNames=YDR330W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP INTERACTION WITH CDC48.
RX PubMed=15258615; DOI=10.1038/sj.embor.7400203;
RA Schuberth C., Richly H., Rumpf S., Buchberger A.;
RT "Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent
RT protein degradation.";
RL EMBO Rep. 5:818-824(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in CDC48-dependent protein degradation through the
CC ubiquitin/proteasome pathway. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC48. {ECO:0000269|PubMed:15258615}.
CC -!- INTERACTION:
CC Q06682; P25694: CDC48; NbExp=4; IntAct=EBI-32041, EBI-4308;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 6630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U32517; AAB64765.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12172.1; -; Genomic_DNA.
DR PIR; S59795; S59795.
DR RefSeq; NP_010617.1; NM_001180638.1.
DR AlphaFoldDB; Q06682; -.
DR SMR; Q06682; -.
DR BioGRID; 32387; 89.
DR DIP; DIP-3938N; -.
DR IntAct; Q06682; 14.
DR MINT; Q06682; -.
DR STRING; 4932.YDR330W; -.
DR iPTMnet; Q06682; -.
DR MaxQB; Q06682; -.
DR PaxDb; 4932-YDR330W; -.
DR PeptideAtlas; Q06682; -.
DR EnsemblFungi; YDR330W_mRNA; YDR330W; YDR330W.
DR GeneID; 851930; -.
DR KEGG; sce:YDR330W; -.
DR AGR; SGD:S000002738; -.
DR SGD; S000002738; UBX5.
DR VEuPathDB; FungiDB:YDR330W; -.
DR eggNOG; KOG1364; Eukaryota.
DR GeneTree; ENSGT00390000018687; -.
DR HOGENOM; CLU_021255_2_1_1; -.
DR InParanoid; Q06682; -.
DR OMA; PAIFDCQ; -.
DR OrthoDB; 5482878at2759; -.
DR BioCyc; YEAST:G3O-29886-MONOMER; -.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR BioGRID-ORCS; 851930; 5 hits in 10 CRISPR screens.
DR PRO; PR:Q06682; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06682; Protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR CDD; cd02958; UAS; 1.
DR CDD; cd14346; UBA_Ubx5_like; 1.
DR CDD; cd01767; UBX; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR PANTHER; PTHR23322; FAS-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23322:SF6; UBX DOMAIN-CONTAINING PROTEIN 7; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR Pfam; PF14555; UBA_4; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..500
FT /note="UBX domain-containing protein 5"
FT /id="PRO_0000211002"
FT DOMAIN 415..493
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 50..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 500 AA; 56737 MW; 6B3DD79D98950523 CRC64;
MSEGKVDEFM AITGADDAAI ATQFIEMADG NLNTAISLFF ENGGAALLSS NNTPTPSNST
PMAPTSVDSD ADAQLAERLQ REAYQQQQPD QDYVRPPDEA RHEVLTETSG FPISYGGIGG
RFEPLHRVND MFDEGRPESI FNQRLDDTNT NTYINDNSSD SLDSEEENDD DEYEYVEEPV
IELDEDGNIK EYTKLVRKPK TISKEQKLAL LFRPPFSIMS KLDLDAAKQK ARAKQKWIMI
NIQDSGIFQC QALNRDLWSS RPVKTIIKEN FVFLQYQYES RNAQPYLQFY HLNNKDDLPH
IAILDPITGE RVKQWNRVVP IPEQFISEIN EFLASFSLDP KVPNPTVNEP LPKVDPTTLT
EEQQMELAIK ESLNNNSSKS NQEEVPSTGE EQKRVQEPDP FSTIEARVHP EPPNKPGITT
RIQIRTGDGS RLVRRFNALE DTVRTIYEVI KTEMDGFADS RFTLNDHQRE DLIDKLNMTI
ADAGLKNSSL LLEKLDPEIE
//
