HER1_YEAST
ID HER1_YEAST Reviewed; 1246 AA.
AC Q12276; D6W2T1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=HMG2-induced ER-remodeling protein 1;
GN Name=HER1; OrderedLocusNames=YOR227W; ORFNames=YOR50-17;
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 96604 / S288c / FY1679;
RX PubMed=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-277, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP FUNCTION.
RX PubMed=18667535; DOI=10.1091/mbc.e07-11-1188;
RA Federovitch C.M., Jones Y.Z., Tong A.H., Boone C., Prinz W.A.,
RA Hampton R.Y.;
RT "Genetic and structural analysis of Hmg2p-induced endoplasmic reticulum
RT remodeling in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 19:4506-4520(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-1013 AND THR-1130,
RP AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-277; SER-1013;
RP SER-1200; SER-1204 AND SER-1207, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Required for HMG2-induced endoplasmic reticulum-remodeling.
CC {ECO:0000269|PubMed:18667535}.
CC -!- SUBUNIT: May interact with ribosomes.
CC -!- INTERACTION:
CC Q12276; P32598: GLC7; NbExp=4; IntAct=EBI-35056, EBI-13715;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GIP3/HER1 family. {ECO:0000305}.
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DR EMBL; X92441; CAA63190.1; -; Genomic_DNA.
DR EMBL; Z75135; CAA99447.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10997.1; -; Genomic_DNA.
DR PIR; S60954; S60954.
DR RefSeq; NP_014870.1; NM_001183646.1.
DR AlphaFoldDB; Q12276; -.
DR BioGRID; 34620; 55.
DR DIP; DIP-6547N; -.
DR IntAct; Q12276; 8.
DR MINT; Q12276; -.
DR STRING; 4932.YOR227W; -.
DR iPTMnet; Q12276; -.
DR MaxQB; Q12276; -.
DR PaxDb; Q12276; -.
DR PRIDE; Q12276; -.
DR EnsemblFungi; YOR227W_mRNA; YOR227W; YOR227W.
DR GeneID; 854402; -.
DR KEGG; sce:YOR227W; -.
DR SGD; S000005753; HER1.
DR VEuPathDB; FungiDB:YOR227W; -.
DR eggNOG; ENOG502QYHN; Eukaryota.
DR GeneTree; ENSGT00940000176518; -.
DR HOGENOM; CLU_007231_0_0_1; -.
DR InParanoid; Q12276; -.
DR OMA; EILPDCP; -.
DR BioCyc; YEAST:G3O-33725-MON; -.
DR PRO; PR:Q12276; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12276; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IGI:SGD.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1246
FT /note="HMG2-induced ER-remodeling protein 1"
FT /id="PRO_0000237668"
FT REGION 19..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1246 AA; 139458 MW; 1AE4AC2EC0DE728E CRC64;
MSSKLKYTDI DVPLDWLYKG KRRNRTKSAA STRTSEATTT SVKKTATLPS TAAVPTKTIA
SPQRPLSGQN VNNELSNSKP AVSAEKVSQQ GQVPTRRTRS HSVSYGLLQK KNNNDDTTDS
PKISRIRTAQ DQPVKETKSS TLAEPIVSKK GRSRSSSIST SLNERSKKSL FGSLFGRRPS
TTPSHVVERP LSSQNDHKKS TELPPIDTRQ SKISTPTSTP TTASSKPSSS GGNRHSDGSL
TSKLLSIPHN ILETSSTNFN AHHHIQSHHS SGREQDSPHS ESSDLPPILE KETTQKQLQK
VSKVNLKRVT IAVQEFNSDP PQQLPSRKPK RGNVLIPEDM ISAPPLISLG ITNSSDQSSF
QSNISPSYSK DSKEYKLALE NFKKAAKEAE KHQKDAYYVA ERMAQEVANY KARQLKTSPL
TGATNSAADS ATDQESSSLD ARASKLHIDK PINVGAHPFE THQDDNIKYS SHLEQTLDVA
YTRCCHLREI LPIPSTLRQV KGKTAPLQTL KFLNPKPTLV DILSFCDFIA ITPIHNIIFD
NVSLTHDMFK IVICSLVTSP VVEKLGLRNV VINEQSWKLL CKFLLQNKTL IKLDISQTKA
RTDLNDSNYR DQMDWELFCE VLRNREGRPL EELLLNGLRF DKMSFSHFKN ILLTFAQMNP
KNPIRLGMAN VEFSTECFDF LFNWMSEYNV QGVDLAYNNL ESLAKRMIKK LARLPYKHLE
YFTLNSTNIT SVDDMSYILK YLSRLPSIKF LDLSNLPQLF PGILTSGYKY FPQFPQLKRI
HFDFDDLSIK ETTMLVSILA KCETLSHVSL IGQSPMPDAS KISDSTDEPD KSKDEKKEQI
VFMRNTLWAS LYAFVRDSHN LVSLDVDYDQ VPDEIQSRIA LCLMHNMKRI MDSSFKLDEL
TVQDDLIFDG SLITETAEEV LKRLNDKSLL QNDVGKKYLL KKYFEKMEKV HHNVQNTIDS
MFEKRKSGEL PLQEKENLLR LLLLEKNLSN ILDIFASMPN IADVVPFSKA DNSFPNIGDS
TVSANYNDGI RPSLKHLDSD RLINDVSIPE NDSSIRPHLM ATDSGRIIDV TTGKALLFKS
SSNTSLAGKR QEEEEGELHK WGVFVQHQSS RHNSGLPSSA NSSRISGSLT PDSSVAGGKK
GESSRTSGTR PKILPKIPTG AELRDAIIKA KGIDSVDDLI KNVTSEKVGL ESLYGDELNS
RSPSNDSLQE SQQKAPLQRP LVEDETVTKK YDKLLNDLSN VRHSKT
