UIP4_YEAST
ID UIP4_YEAST Reviewed; 304 AA.
AC Q08926; D6W3I3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=ULP1-interacting protein 4;
GN Name=UIP4; OrderedLocusNames=YPL186C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 INTERACTION WITH ULP1.
RX PubMed=11056382; DOI=10.1093/oxfordjournals.jbchem.a022807;
RA Takahashi Y., Mizoi J., Toh-e A., Kikuchi Y.;
RT "Yeast Ulp1, an Smt3-specific protease, associates with nucleoporins.";
RL J. Biochem. 128:723-725(2000).
RN [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-185 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-205, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-205, AND
RP IDENTIFICATION BY 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 -!- SUBUNIT: Interacts with ULP1. {ECO:0000269|PubMed:11056382}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16407407}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16407407}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16407407}. Nucleus envelope
CC {ECO:0000269|PubMed:16407407}.
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DR EMBL; Z73542; CAA97897.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11249.1; -; Genomic_DNA.
DR PIR; S65198; S65198.
DR RefSeq; NP_015138.1; NM_001184000.1.
DR AlphaFoldDB; Q08926; -.
DR BioGRID; 35997; 29.
DR IntAct; Q08926; 8.
DR MINT; Q08926; -.
DR STRING; 4932.YPL186C; -.
DR iPTMnet; Q08926; -.
DR MaxQB; Q08926; -.
DR PaxDb; Q08926; -.
DR PRIDE; Q08926; -.
DR TopDownProteomics; Q08926; -.
DR EnsemblFungi; YPL186C_mRNA; YPL186C; YPL186C.
DR GeneID; 855916; -.
DR KEGG; sce:YPL186C; -.
DR SGD; S000006107; UIP4.
DR VEuPathDB; FungiDB:YPL186C; -.
DR eggNOG; ENOG502SASQ; Eukaryota.
DR HOGENOM; CLU_079707_0_0_1; -.
DR InParanoid; Q08926; -.
DR OMA; RECIFFR; -.
DR BioCyc; YEAST:G3O-34079-MON; -.
DR PRO; PR:Q08926; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08926; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..304
FT /note="ULP1-interacting protein 4"
FT /id="PRO_0000270927"
FT REGION 72..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 304 AA; 34222 MW; C46486ABE0073A61 CRC64;
MVTIVFDHPA EDFPELKIAG EFTNWEGVPM KINTSSGKWE YKFDESSVTK HNDKDKVHFK
FIDQNGNWFA DDEYPKEVDE HSNENNVATL NNEEDGGSAG EEKDEGDKTA HNTNENGSEL
YYEGPETPTP SLKGNVTFPS PKTAISQDGS AFAKETTRKE RKYEHAPLNE VPVERDPKEE
NKELSPNFSQ EQTENKQDKG LDNLSEGNDN DNTRVNEDTD VTDTQESEHE INGSDTENTD
MSEQEEIQKI DKPADQNAKS IVKEGDANTE DYESVLKKLL GALGRFFGSW FSWLTTKMSS
SEAS
