Protein SPA2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P23201 (SPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein SPA2

Gene names

Name:	SPA2
Synonyms:	PEA1
Ordered Locus Names:	YLL021W
ORF Names:	L1209

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1466 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in pheromone-induced morphogenesis and efficient mating, perhaps as a cytoskeletal protein.
Subunit structure	Interacts with SHS1. Ref.5
Subcellular location	Cell tip. Note: Localizes to a sharp patch at the shmoo tip (mating projection) which corresponds to the site of polarized cell growth.
Miscellaneous	Present with 274 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	Cell shape
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	invasive filamentous growth Inferred from genetic interaction PubMed 9443897. Source: SGD mating projection assembly Inferred from genetic interaction PubMed 9443897. Source: SGD pseudohyphal growth Inferred from mutant phenotype PubMed 9055077 PubMed 9443897. Source: SGD regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW regulation of initiation of mating projection growth Inferred from mutant phenotype PubMed 14734532. Source: SGD regulation of termination of mating projection growth Inferred from mutant phenotype PubMed 14734532. Source: SGD
Cellular_component	cell tip Inferred from electronic annotation. Source: UniProtKB-SubCell cellular bud neck Inferred from direct assay PubMed 9214378. Source: SGD cellular bud tip Inferred from direct assay PubMed 12361575 PubMed 2647769. Source: SGD incipient cellular bud site Inferred from direct assay PubMed 9214378. Source: SGD mating projection tip Inferred from direct assay PubMed 2647769 PubMed 9214378. Source: SGD polarisome Inferred from direct assay PubMed 9632790. Source: SGD
Molecular_function	cytoskeletal regulatory protein binding Traceable author statement PubMed 10639324. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1466

1466

Protein SPA2

PRO_0000072090

Regions

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Region

270

25 X 9 AA approximate tandem repeats

Coiled coil

286 – 388

103

Potential

Coiled coil

1169 – 1189

Potential

Coiled coil

1275 – 1302

Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Modified residue

102

Phosphoserine Ref.11

Modified residue

157

Phosphoserine Ref.11

Modified residue

182

Phosphoserine Ref.8

Modified residue

183

Phosphoserine Ref.8

Modified residue

220

Phosphothreonine Ref.10 Ref.11

Modified residue

222

Phosphoserine Ref.10 Ref.11

Modified residue

254

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11

Modified residue

274

Phosphoserine Ref.11

Modified residue

301

Phosphoserine Ref.11

Modified residue

544

Phosphoserine Ref.11

Modified residue

575

Phosphoserine Ref.10

Modified residue

585

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

599

Phosphoserine Ref.7 Ref.8 Ref.10 Ref.11

Modified residue

606

Phosphoserine Ref.11

Modified residue

646

Phosphoserine Ref.8

Modified residue

653

Phosphoserine Ref.11

Modified residue

657

Phosphoserine Ref.11

Modified residue

817

Phosphoserine Ref.9 Ref.11

Modified residue

820

Phosphoserine Ref.9 Ref.11

Modified residue

835

Phosphoserine Ref.11

Modified residue

865

Phosphoserine Ref.11

Modified residue

883

Phosphoserine Ref.8 Ref.11

Modified residue

887

Phosphothreonine Ref.11

Modified residue

910

Phosphoserine Ref.10 Ref.11

Modified residue

937

Phosphoserine Ref.8 Ref.9

Modified residue

961

Phosphoserine Ref.8 Ref.9 Ref.10

Modified residue

970

Phosphoserine Ref.10 Ref.11

Modified residue

971

Phosphoserine Ref.11

Modified residue

979

Phosphoserine Ref.8 Ref.10 Ref.11

Modified residue

986

Phosphoserine Ref.11

Modified residue

988

Phosphoserine Ref.7 Ref.11

Modified residue

1006

Phosphoserine Ref.10 Ref.11

Modified residue

1053

Phosphoserine Ref.9

Modified residue

1056

Phosphoserine Ref.9

Modified residue

1080

Phosphoserine Ref.7 Ref.10

Modified residue

1173

Phosphoserine Ref.11

Modified residue

1179

Phosphothreonine Ref.8 Ref.10 Ref.11

Modified residue

1180

Phosphoserine Ref.8 Ref.10 Ref.11

Modified residue

1262

Phosphotyrosine Ref.11

Modified residue

1263

Phosphoserine Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P23201 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 2EBB616152382C89
Show »

FASTA

1,466

163,143

        10         20         30         40         50         60 
MGTSSEVSLA HHRDIFHYYV SLKTFFEVTG ENRDRSNSTR AQKARAKLLK LSSSQFYELS 

        70         80         90        100        110        120 
TDVSDELQRR IGEDANQPDY LLPKANFHMK RNQARQKLAN LSQTRFNDLL DDILFEIKRR 

       130        140        150        160        170        180 
GFDKDLDAPR PPLPQPMKQE VSKDSDDTAR TSTNSSSVTQ VAPNVSVQPS LVIPKMASID 

       190        200        210        220        230        240 
WSSEEEEEEQ VKEKPNEPEG KQTSMDEKKE AKPALNPIVT DSDLPDSQVL ARDITSMART 

       250        260        270        280        290        300 
PTTTHKNYWD VNDSPIIKVD KDIDNEKGPE QLKSPEVQRA ENNNPNSEME DKVKELTDLN 

       310        320        330        340        350        360 
SDLHLQIEDL NAKLASLTSE KEKEKKEEKE EKEKEKNLKI NYTIDESFQK ELLSLNSQIG 

       370        380        390        400        410        420 
ELSIENENLK QKISEFELHQ KKNDNHNDLK ITDGFISKYS SADGLIPAQY ILNANNLIIQ 

       430        440        450        460        470        480 
FTTRLSAVPI GDSTAISHQI GEELFQILSQ LSNLISQLLL SADLLQYKDQ VILLKASLSH 

       490        500        510        520        530        540 
AITSIRYFSV YGPVLIPKIT VQAAVSEVCF AMCNLIDSAK IKSDSNGEST TSNEGNRQVL 

       550        560        570        580        590        600 
EYSSPTATTP MTPTFPSTSG INMKKGFINP RKPASFLNDV EEEESPVKPL KITQKAINSP 

       610        620        630        640        650        660 
IIRPSSSNGV PTTSRKPSGT GLFSLMIDSS IAKNSSHKED NDKYVSPIKA VTSASNSASS 

       670        680        690        700        710        720 
NISEIPKLTL PPQAKIGTVI PPSENQVPNI KIENTEEDNK RSDITNEISV KPTSSIADKL 

       730        740        750        760        770        780 
KQFEQSSEKK SSPKENPIAK EEMDSKPKLS NKFITSMNDV STDDSSSDGN ENDDADDDDD 

       790        800        810        820        830        840 
FTYMALKQTM KREGSKIEKN NDSKLPANIV ELDLHESPES VKIESPESIK EITSSEMSSE 

       850        860        870        880        890        900 
MPSSSLPKRL VEDVEPSEMP EKGASVESVR KKNFQEPLGN VESPDMTQKV KSLGMTGKAV 

       910        920        930        940        950        960 
GPESDSRVES PGMTGQIKSL NMAGKVVGPE ADSRVESPGM KEQIKSLGMT GKITAQESIK 

       970        980        990       1000       1010       1020 
SPEAARKLAS SGEVDKIESP RMVRESESLE AVGNTIPSNM TVKMESPNLK GNTVSEPQEI 

      1030       1040       1050       1060       1070       1080 
RRDIASSEPI ENVDPPKVLK KIVFPKAVNR TGSPKSVEKT PSSATLKKSG LPEPNSQIVS 

      1090       1100       1110       1120       1130       1140 
PELAKNSPLA PIKKNVELRE TNKPHTETIT SVEPTNKDAN TSWRDADLNR TIKREEEDED 

      1150       1160       1170       1180       1190       1200 
FDRVNHNIQI TGAYTKTGKI DYHKIPVDRK AKSEAEVHTS EEDIDESNNV NGKRADAQIH 

      1210       1220       1230       1240       1250       1260 
ITERKHAFVN PTENSQVKKT SHSPFLNSKP VQYENSESNG GINNHIKIKN TGETTAHDEK 

      1270       1280       1290       1300       1310       1320 
HYSDDDDSSY QFVPMKHEEQ EQEQNRSEEE ESEDDDEEEE DSDFDVDTFD IENPDNTLSE 

      1330       1340       1350       1360       1370       1380 
LLLYLEHQTM DVISTIQSLL TSIKKPQVTK GNLRGESNAI NQVIGQMVDA TSISMEQSRN 

      1390       1400       1410       1420       1430       1440 
ANLKKHGDWV VQSLRDCSRR MTILCQLTGD GILAKEKSDQ DYADKNFKQR LAGIAFDVAK 

      1450       1460 
CTKELVKTVE EASLKDEINY LNSKLK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The SPA2 gene of Saccharomyces cerevisiae is important for pheromone-induced morphogenesis and efficient mating." Gehrung S., Snyder M. J. Cell Biol. 111:1451-1464(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The sequence of 32kb on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABC transporter homologous to the human multidrug resistance protein." Purnelle B., Goffeau A. Yeast 13:183-188(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Shs1p: a novel member of septin that interacts with spa2p, involved in polarized growth in Saccharomyces cerevisiae." Mino A., Tanaka K., Kamei T., Umikawa M., Fujiwara T., Takai Y. Biochem. Biophys. Res. Commun. 251:732-736(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHS1.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-599; SER-988 AND SER-1080, MASS SPECTROMETRY. Strain: YAL6B.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-183; SER-254; SER-585; SER-599; SER-646; SER-883; SER-937; SER-961; SER-979; THR-1179; SER-1180 AND SER-1263, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-254; SER-585; SER-817; SER-820; SER-937; SER-961; SER-1053 AND SER-1056, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-222; SER-575; SER-585; SER-599; SER-910; SER-961; SER-970; SER-979; SER-1006; SER-1080; THR-1179 AND SER-1180, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-157; THR-220; SER-222; SER-254; SER-274; SER-301; SER-544; SER-585; SER-599; SER-606; SER-653; SER-657; SER-817; SER-820; SER-835; SER-865; SER-883; THR-887; SER-910; SER-970; SER-971; SER-979; SER-986; SER-988; SER-1006; SER-1173; THR-1179; SER-1180 AND TYR-1262, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53731 Genomic DNA. Translation: CAA37763.1. X97560 Genomic DNA. Translation: CAA66170.1. Z73126 Genomic DNA. Translation: CAA97469.1. BK006945 Genomic DNA. Translation: DAA09299.1.
PIR	A36426.
RefSeq	NP_013079.1. NM_001181841.1.
3D structure databases
ProteinModelPortal	P23201.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-99N.
IntAct	P23201. 12 interactions.
MINT	MINT-435928.
STRING	4932.YLL021W.
Proteomic databases
PaxDb	P23201.
PeptideAtlas	P23201.
PRIDE	P23201.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLL021W; YLL021W; YLL021W.
GeneID	850639.
KEGG	sce:YLL021W.
Organism-specific databases
CYGD	YLL021w.
SGD	S000003944. SPA2.
Phylogenomic databases
eggNOG	NOG84978.
GeneTree	ENSGT00650000094229.
OMA	DATSISM.
OrthoDB	EOG4RV61G.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32125-MONOMER.
Gene expression databases
Genevestigator	P23201.
GermOnline	YLL021W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013724. GIT_SHD. [Graphical view]
Pfam	PF08518. GIT_SHD. 2 hits. [Graphical view]
SMART	SM00555. GIT. 4 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	966570.

Entry information

Entry name

SPA2_YEAST

Accession

Primary (citable) accession number: P23201
Secondary accession number(s): D6VXY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 29, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents