ID UBX1_YEAST Reviewed; 423 AA. AC P34223; D6VPU2; E9P8S9; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 193. DE RecName: Full=UBX domain-containing protein 1; DE AltName: Full=Suppressor of high-copy PP1 protein; GN Name=SHP1; Synonyms=UBX1; OrderedLocusNames=YBL058W; GN ORFNames=YBL0509, YBL0515; 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 [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8154187; DOI=10.1002/yea.320091210; RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.; RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm RT of yeast chromosome II. Identification of 26 open reading frames, including RT the KIP1 and SEC17 genes."; RL Yeast 9:1355-1371(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP IDENTIFICATION. RX PubMed=7891699; DOI=10.1128/mcb.15.4.2037; RA Zhang S., Guha S., Volkert F.C.; RT "The Saccharomyces SHP1 gene, which encodes a regulator of phosphoprotein RT phosphatase 1 with differential effects on glycogen metabolism, meiotic RT differentiation, and mitotic cell cycle progression."; RL Mol. Cell. Biol. 15:2037-2050(1995). RN [6] 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 [7] 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 [8] RP FUNCTION, AND 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [10] RP IDENTIFICATION IN A COMPLEX WITH NPL4; UFD1; CDC48; OTU1 AND DOA1. RX PubMed=16427015; DOI=10.1016/j.molcel.2005.12.014; RA Rumpf S., Jentsch S.; RT "Functional division of substrate processing cofactors of the ubiquitin- RT selective Cdc48 chaperone."; RL Mol. Cell 21:261-269(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-322, AND RP IDENTIFICATION BY 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-210; SER-224; RP SER-315; SER-321; SER-322 AND THR-331, AND IDENTIFICATION BY MASS RP 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). RN [14] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-241, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). CC -!- FUNCTION: Involved in CDC48-dependent protein degradation through the CC ubiquitin/proteasome pathway. Direct or indirect positive regulator of CC GLC7 activity. {ECO:0000269|PubMed:15258615}. CC -!- SUBUNIT: Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and CC deubiquitinase OTU1 (PubMed:16427015). Interacts with CDC48 CC (PubMed:15258615). {ECO:0000269|PubMed:15258615, CC ECO:0000269|PubMed:16427015}. CC -!- INTERACTION: CC P34223; P25694: CDC48; NbExp=10; IntAct=EBI-17093, EBI-4308; CC P34223; Q12743: DFM1; NbExp=2; IntAct=EBI-17093, EBI-33192; CC P34223; P54860: UFD2; NbExp=3; IntAct=EBI-17093, EBI-20003; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm CC {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 3200 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z23261; CAA80789.1; -; Genomic_DNA. DR EMBL; Z35819; CAA84878.1; -; Genomic_DNA. DR EMBL; AY557717; AAS56043.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07062.1; -; Genomic_DNA. DR PIR; S39830; S39830. DR RefSeq; NP_009495.1; NM_001178298.1. DR PDB; 6OPC; EM; 3.70 A; Z=1-423. DR PDBsum; 6OPC; -. DR AlphaFoldDB; P34223; -. DR EMDB; EMD-20149; -. DR SMR; P34223; -. DR BioGRID; 32641; 456. DR ComplexPortal; CPX-8127; CDC48-SHP1 AAA ATPase complex. DR DIP; DIP-2789N; -. DR IntAct; P34223; 24. DR MINT; P34223; -. DR STRING; 4932.YBL058W; -. DR iPTMnet; P34223; -. DR MaxQB; P34223; -. DR PaxDb; 4932-YBL058W; -. DR PeptideAtlas; P34223; -. DR TopDownProteomics; P34223; -. DR EnsemblFungi; YBL058W_mRNA; YBL058W; YBL058W. DR GeneID; 852222; -. DR KEGG; sce:YBL058W; -. DR AGR; SGD:S000000154; -. DR SGD; S000000154; SHP1. DR VEuPathDB; FungiDB:YBL058W; -. DR eggNOG; KOG2086; Eukaryota. DR GeneTree; ENSGT00520000055567; -. DR HOGENOM; CLU_029402_4_1_1; -. DR InParanoid; P34223; -. DR OMA; REVLHCN; -. DR OrthoDB; 5483331at2759; -. DR BioCyc; YEAST:G3O-28956-MONOMER; -. DR BioGRID-ORCS; 852222; 10 hits in 10 CRISPR screens. DR PRO; PR:P34223; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P34223; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005829; C:cytosol; HDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0019888; F:protein phosphatase regulator activity; IMP:SGD. DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central. DR GO; GO:0030437; P:ascospore formation; IMP:SGD. DR GO; GO:0000045; P:autophagosome assembly; IMP:SGD. DR GO; GO:0005977; P:glycogen metabolic process; IMP:SGD. DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central. DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central. DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD. DR GO; GO:0031134; P:sister chromatid biorientation; IMP:SGD. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD. DR CDD; cd14351; UBA_Ubx1_like; 1. DR CDD; cd01770; UBX_UBXN2; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.30.420.210; SEP domain; 1. DR InterPro; IPR036241; NSFL1C_SEP_dom_sf. DR InterPro; IPR012989; SEP_domain. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR001012; UBX_dom. DR PANTHER; PTHR23333:SF20; NSFL1 COFACTOR P47; 1. DR PANTHER; PTHR23333; UBX DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF08059; SEP; 1. DR Pfam; PF14555; UBA_4; 1. DR Pfam; PF00789; UBX; 1. DR SMART; SM00553; SEP; 1. DR SMART; SM00166; UBX; 1. DR SUPFAM; SSF102848; NSFL1 (p97 ATPase) cofactor p47, SEP domain; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS51399; SEP; 1. DR PROSITE; PS50033; UBX; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..423 FT /note="UBX domain-containing protein 1" FT /id="PRO_0000210998" FT DOMAIN 232..297 FT /note="SEP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732" FT DOMAIN 344..421 FT /note="UBX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215" FT REGION 44..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 299..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 45..63 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 64..81 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 91..130 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 148..162 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 128 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 210 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15665377, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 322 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 331 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT CROSSLNK 241 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CONFLICT 223 FT /note="T -> A (in Ref. 4; AAS56043)" FT /evidence="ECO:0000305" SQ SEQUENCE 423 AA; 46987 MW; AB46C88D7ED4F11C CRC64; MAEIPDETIQ QFMALTNVSH NIAVQYLSEF GDLNEALNSY YASQTDDQKD RREEAHWNRQ QEKALKQEAF STNSSNKAIN TEHVGGLCPK PGSSQGSNEY LKRKGSTSPE PTKGSSRSGS GNNSRFMSFS DMVRGQADDD DEDQPRNTFA GGETSGLEVT DPSDPNSLLK DLLEKARRGG QMGAENGFRD DEDHEMGANR FTGRGFRLGS TIDAADEVVE DNTSQSQRRP EKVTREITFW KEGFQVADGP LYRYDDPANS FYLSELNQGR APLKLLDVQF GQEVEVNVYK KLDESYKAPT RKLGGFSGQG QRLGSPIPGE SSPAEVPKNE TPAAQEQPMP DNEPKQGDTS IQIRYANGKR EVLHCNSTDT VKFLYEHVTS NANTDPSRNF TLNYAFPIKP ISNDETTLKD ADLLNSVVVQ RWA //