Q07653 (HBT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein HBT1

Alternative name(s):
HUB1 target protein 1

Gene names

Name:	HBT1
Synonyms:	Crem
Ordered Locus Names:	YDL223C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1046 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Polarity-determining protein which forms a conjugate with the ubiquitin-like modifier HUB1. Involved in bud site selection and cellular morphogenesis during conjugation. Required for survival during stationary phase. Ref.4 Ref.7
Subunit structure	Conjugated with HUB1. HUB1 has not the classical C-terminal Gly residue, so it is still unknown how conjugation may occur.
Subcellular location	Cytoplasm Ref.5.

Ontologies

Keywords
Biological process	Cell shape Conjugation
Cellular component	Cytoplasm
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell morphogenesis involved in conjugation with cellular fusion Inferred from mutant phenotype Ref.4. Source: SGD regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell mating projection Inferred from direct assay Ref.4. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1046	1046	Protein HBT1		PRO_0000233010
Regions
	Compositional bias	151 – 254	104	His-rich
	Compositional bias	967 – 1001	35	His-rich
Amino acid modifications
	Modified residue	28	1	Phosphoserine Ref.6
	Modified residue	41	1	Phosphoserine Ref.11
	Modified residue	44	1	Phosphothreonine Ref.6
	Modified residue	161	1	Phosphothreonine Ref.9
	Modified residue	189	1	Phosphoserine Ref.9
	Modified residue	299	1	Phosphothreonine Ref.10
	Modified residue	301	1	Phosphoserine Ref.6
	Modified residue	303	1	Phosphoserine Ref.6 Ref.10
	Modified residue	363	1	Phosphoserine Ref.9 Ref.10 Ref.11
	Modified residue	366	1	Phosphothreonine Ref.11
	Modified residue	400	1	Phosphoserine Ref.6
	Modified residue	595	1	Phosphoserine Ref.6
	Modified residue	857	1	Phosphoserine Ref.6
	Modified residue	889	1	Phosphothreonine Ref.6
	Modified residue	943	1	Phosphoserine Ref.6
	Modified residue	950	1	Phosphoserine Ref.11
	Modified residue	956	1	Phosphoserine Ref.10 Ref.11
	Modified residue	959	1	Phosphoserine Ref.3 Ref.10
	Modified residue	962	1	Phosphoserine Ref.3 Ref.10
	Modified residue	993	1	Phosphoserine Ref.3
	Modified residue	997	1	Phosphothreonine Ref.3
	Modified residue	1005	1	Phosphoserine Ref.10
	Modified residue	1034	1	Phosphoserine Ref.8 Ref.11
	Modified residue	1036	1	Phosphoserine Ref.6 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q07653 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: DC5E3EB5DDAFA405	FASTA	1,046	113,616
	10 20 30 40 50 60 MNMNESISKD GQGEEEQNNF SFGGKPGSYD SNSDSAQRKK SFSTTKPTEY NLPKEQPEST 70 80 90 100 110 120 SKNLETKAKN ILLPWRKKHN KDSETPHEDT EADANRRANV TSDVNPVSAD TKSSSGPNAT 130 140 150 160 170 180 ITTHGYSYVK TTTPAATSEQ SKVKTSPPTS HEHSNIKASP TAHRHSKGDA GHPSIATTHN 190 200 210 220 230 240 HSTSKAATSP VTHTHGHSSA TTSPVTHTHG HASVKTTSPT NTHEHSKANT GPSATATTHG 250 260 270 280 290 300 HINVKTTHPV SHGHSGSSTG PKSTAAAQDH SSTKTNPSVT HGHTSVKDNS SATKGYSNTD 310 320 330 340 350 360 SNSDRDVIPG SFRGMTGTDV NPVDPSVYTS TGPKSNVSSG MNAVDPSVYT DTSSKSADRR 370 380 390 400 410 420 KYSGNTATGP PQDTIKEIAQ NVKMDESEQT GLKNDQVSGS DAIQQQTMEP EPKAAVGTSG 430 440 450 460 470 480 FVSQQPSYHD SNKNIQHPEK NKVDNKNISE RAAEKFNIER DDILESADDY QQKNIKSKTD 490 500 510 520 530 540 SNWGPIEYSS SAGKNKNLQD VVIPSSMKEK FDSGTSGSQN MPKAGTELGH MKYNDNGRDN 550 560 570 580 590 600 LQYVAGSQAG SQNTNNNIDM SPRHEAEWSG LSNDATTRNN VVSPAMKDED MNEDSTKPHQ 610 620 630 640 650 660 YGLDYLDDVE DYHENDIDDY SNAKKNDLYS KKAYQGKPSD YNYEQREKIP GTFEPDTLSK 670 680 690 700 710 720 SVQKQDEDPL SPRQTTNRAG METARDESLG NYEYSNTSGN KKLSDLSKNK SGPTPTRSNF 730 740 750 760 770 780 IDQIEPRRAK TTQDIASDAK DFTNNPETGT TGNVDTTGRM GAKSKTFSSN PFDDSKNTDT 790 800 810 820 830 840 HLENANVAAF DNSRSGDTTY SKSGDAETAA YDNIKNADPT YAKSQDITGM THDQEPSSEQ 850 860 870 880 890 900 KASYGSGGNS QNQEYSSDDN IDVNKNAKVL EEDAPGYKRE VDLKNKRRTD LGGADASNAY 910 920 930 940 950 960 AAEVGNFPSL IDPHVPTYGF KDTNTSSSQK PSEGTYPETT SYSIHNETTS QGRKVSVGSM 970 980 990 1000 1010 1020 GSGKSKHHHN HHRHSRQNSS KGSDYDYNNS THSAEHTPRH HQYGSDEGEQ DYHDDEQGEE 1030 1040 QAGKQSFMGR VRKSISGGTF GFRSEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959; SER-962; SER-993 AND THR-997, MASS SPECTROMETRY. Strain: 2124.
[4]	"Role of a ubiquitin-like modification in polarized morphogenesis." Dittmar G.A.G., Wilkinson C.R.M., Jedrzejewski P.T., Finley D. Science 295:2442-2446(2002) [PubMed: 11923536] [Abstract] Cited for: FUNCTION, MASS SPECTROMETRY, CONJUGATION TO HUB1.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-44; SER-301; SER-303; SER-400; SER-595; SER-857; THR-889; SER-943 AND SER-1036, MASS SPECTROMETRY. Strain: SUB592.
[7]	"Genomic analysis of stationary-phase and exit in Saccharomyces cerevisiae: gene expression and identification of novel essential genes." Martinez M.J., Roy S., Archuletta A.B., Wentzell P.D., Anna-Arriola S.S., Rodriguez A.L., Aragon A.D., Quinones G.A., Allen C., Werner-Washburne M. Mol. Biol. Cell 15:5295-5305(2004) [PubMed: 15456898] [Abstract] Cited for: FUNCTION.
[8]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, MASS SPECTROMETRY. Strain: ADR376.
[9]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; SER-189 AND SER-363, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-299; SER-303; SER-363; SER-956; SER-959; SER-962 AND SER-1005, MASS SPECTROMETRY.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-363; THR-366; SER-950; SER-956; SER-1034 AND SER-1036, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z74271 Genomic DNA. Translation: CAA98802.1. BK006938 Genomic DNA. Translation: DAA11642.1.
PIR	S67786.
RefSeq	NP_010058.1. NM_001180283.1.
3D structure databases
ProteinModelPortal	Q07653.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q07653. 4 interactions.
STRING	Q07653.
Proteomic databases
PeptideAtlas	Q07653.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL223C; YDL223C; YDL223C.
GeneID	851303.
KEGG	sce:YDL223C.
NMPDR	fig|4932.3.peg.791.
Organism-specific databases
CYGD	YDL223c.
SGD	S000002382. HBT1.
Phylogenomic databases
eggNOG	fuNOG16229.
OrthoDB	EOG4HDX47.
Gene expression databases
ArrayExpress	Q07653.
Genevestigator	Q07653.
GermOnline	YDL223C. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other
NextBio	968313.

Entry information

Entry name

HBT1_YEAST

Accession

Primary (citable) accession number: Q07653
Secondary accession number(s): D6VRD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program