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HRI1_YEAST
ID   HRI1_YEAST              Reviewed;         244 AA.
AC   Q05905; D6VYU5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Protein HRI1;
DE   AltName: Full=HRR25-interacting protein 1;
GN   Name=HRI1; OrderedLocusNames=YLR301W;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   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   [4]
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   [5]
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   [6]
RP   INTERACTION WITH SEC72.
RX   PubMed=12518317; DOI=10.1002/yea.954;
RA   Willer M., Jermy A.J., Young B.P., Stirling C.J.;
RT   "Identification of novel protein-protein interactions at the cytosolic
RT   surface of the Sec63 complex in the yeast ER membrane.";
RL   Yeast 20:133-148(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, 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-143, 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   INTERACTION WITH HRR25.
RX   PubMed=21460040; DOI=10.1101/gad.1998811;
RA   Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M.,
RA   Gerstein M., Snyder M.;
RT   "Diverse protein kinase interactions identified by protein microarrays
RT   reveal novel connections between cellular processes.";
RL   Genes Dev. 25:767-778(2011).
CC   -!- FUNCTION: Unknown. Non essential.
CC   -!- SUBUNIT: Interacts with HRR25. May interact with SEC72.
CC       {ECO:0000269|PubMed:12518317, ECO:0000269|PubMed:21460040}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 15400 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HRI1 family. {ECO:0000305}.
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DR   EMBL; U17243; AAB67346.1; -; Genomic_DNA.
DR   EMBL; AY558217; AAS56543.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09611.1; -; Genomic_DNA.
DR   PIR; S50385; S50385.
DR   RefSeq; NP_013404.1; NM_001182189.1.
DR   PDB; 3RBY; X-ray; 2.30 A; A/B=1-244.
DR   PDBsum; 3RBY; -.
DR   AlphaFoldDB; Q05905; -.
DR   SMR; Q05905; -.
DR   BioGRID; 31565; 89.
DR   DIP; DIP-4329N; -.
DR   IntAct; Q05905; 2.
DR   STRING; 4932.YLR301W; -.
DR   iPTMnet; Q05905; -.
DR   MaxQB; Q05905; -.
DR   PaxDb; Q05905; -.
DR   PRIDE; Q05905; -.
DR   TopDownProteomics; Q05905; -.
DR   EnsemblFungi; YLR301W_mRNA; YLR301W; YLR301W.
DR   GeneID; 851008; -.
DR   KEGG; sce:YLR301W; -.
DR   SGD; S000004292; HRI1.
DR   VEuPathDB; FungiDB:YLR301W; -.
DR   eggNOG; ENOG502QTYD; Eukaryota.
DR   HOGENOM; CLU_097607_0_0_1; -.
DR   InParanoid; Q05905; -.
DR   OMA; NVPNTHR; -.
DR   BioCyc; YEAST:G3O-32392-MON; -.
DR   PRO; PR:Q05905; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05905; protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IPI:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006612; P:protein targeting to membrane; IPI:SGD.
DR   CDD; cd11692; HRI1_N_like; 1.
DR   Gene3D; 2.40.128.320; -; 1.
DR   InterPro; IPR031818; Hri1.
DR   InterPro; IPR038744; Hri1_N.
DR   InterPro; IPR043047; Hri1_N_sf.
DR   Pfam; PF16815; HRI1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..244
FT                   /note="Protein HRI1"
FT                   /id="PRO_0000245329"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   STRAND          3..14
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          32..40
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          50..56
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          67..75
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   HELIX           81..85
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          107..113
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          123..132
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          165..172
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          175..184
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          191..198
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          204..211
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:3RBY"
FT   STRAND          235..243
FT                   /evidence="ECO:0007829|PDB:3RBY"
SQ   SEQUENCE   244 AA;  27501 MW;  80D813586A1930BB CRC64;
     MPALLKRLLF QVGPHPNERT FTLSSVSTDG HYISLRPFVK PSGDELSFPF EWAFAGTNET
     VKANDQGNGV VTQDFNFWLD TNVYLNVPNT HRGEVNTTWK NWDSGCVEET GAVYPFGADK
     ESVSFRELWQ PVDPSREDLV IVSPNNEKFS SNARSIVLKV TDEAYDGLVI VIGRWIQGFL
     SQKNNNTIEG LNFIRLLEKD SGKSEFLLSY GKEVNKIPQS YENLKKGSTV TSNGLNWEVI
     EYHA
 
 
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