HBT1_YEAST
ID HBT1_YEAST Reviewed; 1046 AA.
AC Q07653; D6VRD2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein HBT1;
DE AltName: Full=HUB1 target protein 1;
GN Name=HBT1; Synonyms=Crem; OrderedLocusNames=YDL223C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND CONJUGATION TO HUB1.
RX PubMed=11923536; DOI=10.1126/science.1069989;
RA Dittmar G.A.G., Wilkinson C.R.M., Jedrzejewski P.T., Finley D.;
RT "Role of a ubiquitin-like modification in polarized morphogenesis.";
RL Science 295:2442-2446(2002).
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 FUNCTION.
RX PubMed=15456898; DOI=10.1091/mbc.e03-11-0856;
RA Martinez M.J., Roy S., Archuletta A.B., Wentzell P.D., Anna-Arriola S.S.,
RA Rodriguez A.L., Aragon A.D., Quinones G.A., Allen C., Werner-Washburne M.;
RT "Genomic analysis of stationary-phase and exit in Saccharomyces cerevisiae:
RT gene expression and identification of novel essential genes.";
RL Mol. Biol. Cell 15:5295-5305(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, 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 IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-363; SER-491;
RP SER-561; SER-671; TYR-855; SER-857; SER-1005 AND SER-1034, 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 -!- FUNCTION: Polarity-determining protein which forms a conjugate with the
CC ubiquitin-like modifier HUB1. Involved in bud site selection and
CC cellular morphogenesis during conjugation. Required for survival during
CC stationary phase. {ECO:0000269|PubMed:11923536,
CC ECO:0000269|PubMed:15456898}.
CC -!- SUBUNIT: Conjugated with HUB1. HUB1 has not the classical C-terminal
CC Gly residue, so it is still unknown how conjugation may occur.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
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DR EMBL; Z74271; CAA98802.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11642.1; -; Genomic_DNA.
DR PIR; S67786; S67786.
DR RefSeq; NP_010058.1; NM_001180283.1.
DR AlphaFoldDB; Q07653; -.
DR BioGRID; 31823; 119.
DR IntAct; Q07653; 3.
DR STRING; 4932.YDL223C; -.
DR CarbonylDB; Q07653; -.
DR iPTMnet; Q07653; -.
DR MaxQB; Q07653; -.
DR PaxDb; Q07653; -.
DR PRIDE; Q07653; -.
DR TopDownProteomics; Q07653; -.
DR EnsemblFungi; YDL223C_mRNA; YDL223C; YDL223C.
DR GeneID; 851303; -.
DR KEGG; sce:YDL223C; -.
DR SGD; S000002382; HBT1.
DR VEuPathDB; FungiDB:YDL223C; -.
DR eggNOG; ENOG502SEJI; Eukaryota.
DR HOGENOM; CLU_012135_0_0_1; -.
DR InParanoid; Q07653; -.
DR OMA; PVTHTHG; -.
DR BioCyc; YEAST:G3O-29603-MON; -.
DR PRO; PR:Q07653; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07653; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005937; C:mating projection; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0000753; P:cell morphogenesis involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell shape; Conjugation; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1046
FT /note="Protein HBT1"
FT /id="PRO_0000233010"
FT REGION 1..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 855
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1046 AA; 113616 MW; DC5E3EB5DDAFA405 CRC64;
MNMNESISKD GQGEEEQNNF SFGGKPGSYD SNSDSAQRKK SFSTTKPTEY NLPKEQPEST
SKNLETKAKN ILLPWRKKHN KDSETPHEDT EADANRRANV TSDVNPVSAD TKSSSGPNAT
ITTHGYSYVK TTTPAATSEQ SKVKTSPPTS HEHSNIKASP TAHRHSKGDA GHPSIATTHN
HSTSKAATSP VTHTHGHSSA TTSPVTHTHG HASVKTTSPT NTHEHSKANT GPSATATTHG
HINVKTTHPV SHGHSGSSTG PKSTAAAQDH SSTKTNPSVT HGHTSVKDNS SATKGYSNTD
SNSDRDVIPG SFRGMTGTDV NPVDPSVYTS TGPKSNVSSG MNAVDPSVYT DTSSKSADRR
KYSGNTATGP PQDTIKEIAQ NVKMDESEQT GLKNDQVSGS DAIQQQTMEP EPKAAVGTSG
FVSQQPSYHD SNKNIQHPEK NKVDNKNISE RAAEKFNIER DDILESADDY QQKNIKSKTD
SNWGPIEYSS SAGKNKNLQD VVIPSSMKEK FDSGTSGSQN MPKAGTELGH MKYNDNGRDN
LQYVAGSQAG SQNTNNNIDM SPRHEAEWSG LSNDATTRNN VVSPAMKDED MNEDSTKPHQ
YGLDYLDDVE DYHENDIDDY SNAKKNDLYS KKAYQGKPSD YNYEQREKIP GTFEPDTLSK
SVQKQDEDPL SPRQTTNRAG METARDESLG NYEYSNTSGN KKLSDLSKNK SGPTPTRSNF
IDQIEPRRAK TTQDIASDAK DFTNNPETGT TGNVDTTGRM GAKSKTFSSN PFDDSKNTDT
HLENANVAAF DNSRSGDTTY SKSGDAETAA YDNIKNADPT YAKSQDITGM THDQEPSSEQ
KASYGSGGNS QNQEYSSDDN IDVNKNAKVL EEDAPGYKRE VDLKNKRRTD LGGADASNAY
AAEVGNFPSL IDPHVPTYGF KDTNTSSSQK PSEGTYPETT SYSIHNETTS QGRKVSVGSM
GSGKSKHHHN HHRHSRQNSS KGSDYDYNNS THSAEHTPRH HQYGSDEGEQ DYHDDEQGEE
QAGKQSFMGR VRKSISGGTF GFRSEI
