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YCV1_YEAST
ID   YCV1_YEAST              Reviewed;         631 AA.
AC   P25639; D6VR66; P25363; Q8NIL7;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Uncharacterized membrane protein YCR061W;
DE   Flags: Precursor;
GN   OrderedLocusNames=YCR061W; ORFNames=YCR062W, YCR61W, YCR62W, YCR904;
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=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Valles G., Volckaerts G.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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] OF 512-631.
RX   PubMed=1561837; DOI=10.1002/yea.320080209;
RA   Benit P., Chanet R., Fabre F., Faye G., Fukuhara H., Sor F.;
RT   "Sequence of the sup61-RAD18 region on chromosome III of Saccharomyces
RT   cerevisiae.";
RL   Yeast 8:147-153(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-631.
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   [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   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, 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).
RN   [10]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-250, 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14562095}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:14562095}. Note=Localizes to
CC       cytoplasmic punctate structures.
CC   -!- SIMILARITY: To S.pombe SpBC3B8.06. {ECO:0000305}.
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DR   EMBL; X59720; CAC42986.1; -; Genomic_DNA.
DR   EMBL; AY693356; AAT93375.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07535.1; -; Genomic_DNA.
DR   PIR; S19476; S19476.
DR   PIR; S19477; S19477.
DR   RefSeq; NP_009987.2; NM_001178772.1.
DR   AlphaFoldDB; P25639; -.
DR   SMR; P25639; -.
DR   BioGRID; 31038; 163.
DR   DIP; DIP-8245N; -.
DR   IntAct; P25639; 22.
DR   MINT; P25639; -.
DR   STRING; 4932.YCR061W; -.
DR   iPTMnet; P25639; -.
DR   PaxDb; P25639; -.
DR   PRIDE; P25639; -.
DR   EnsemblFungi; YCR061W_mRNA; YCR061W; YCR061W.
DR   GeneID; 850425; -.
DR   KEGG; sce:YCR061W; -.
DR   SGD; S000000657; YCR061W.
DR   VEuPathDB; FungiDB:YCR061W; -.
DR   eggNOG; ENOG502QW3E; Eukaryota.
DR   GeneTree; ENSGT00940000176688; -.
DR   HOGENOM; CLU_012543_1_0_1; -.
DR   InParanoid; P25639; -.
DR   OMA; VSISIMF; -.
DR   BioCyc; YEAST:G3O-29366-MON; -.
DR   PRO; PR:P25639; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25639; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR   InterPro; IPR018825; DUF2427.
DR   InterPro; IPR018827; Uncharacterised_YCR061W_C.
DR   Pfam; PF10348; DUF2427; 1.
DR   Pfam; PF10355; Ytp1; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Isopeptide bond; Membrane; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..631
FT                   /note="Uncharacterized membrane protein YCR061W"
FT                   /id="PRO_0000014313"
FT   TOPO_DOM        21..105
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..170
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..322
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        344..351
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        373..407
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..451
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        473..529
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        551..598
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        599..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        620..631
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          216..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        250
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   631 AA;  70922 MW;  24B33124635FB508 CRC64;
     MVRFVSILSL FGCAATLVTA HDDMDMDMDM DMDMDMNIDT TTSQSIDVSS TASIVPVPHE
     PKHLHGLPIL QSPSLTPAER LYWENYNTTT YFTTQAGNRS ALRYHIITLL LVAFVLYPVS
     LALSAARSRW YLPLLFVNLC ICISSVMALS VFKNTFPEED WYAHNIYGTT SVLLLVFMLV
     HFFAAVLSVP VSLASKKEYR PVDTIPLNDL ESTPVMVNSA RGSPSPSSNR DTLFSLSSDT
     TTATATNNNK RRRAEGEDEG DNTSNHDTLR DEDYDNDDDE IASIEAPPLL PQDIPVFRIL
     FTNTKYQMLA AHLSCVANVV FHMLTYPLFM YIFVDLIIGF AVGNLLGKGI RIFNLLAHWI
     KGGVFFTLGV VSLARYCGFA AKYGWAWNNI SFTSQLTQTR SSNLLFRFAP AGTFTMEFVE
     SFLIFFYGST NIFLEHLAGN GGAWTAKDLQ HVSIAFMFIG TGLCGLLTEY KLNHWRFEHA
     RKRPQTDVVA ATPGYSPNPF PAFTIFWTGI LMSQHAQSSQ FSTTIHTQWG YLLSYGSFFR
     LLTFLILFLV PNTNSAASKP FTELITSFCL LCGGLVFMES TDQSIEAMEY RGFTPMFTFN
     LSVGFVSLLM AWEMILFIWK DWLIKTRKTS L
 
 
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