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Protein

Sporulation-specific protein 2

Gene

SPS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in middle stages of meiosis. Redundant with SPS22 for the organization of the beta-glucan layer of the spore wall.3 Publications

GO - Biological processi

  1. ascospore formation Source: SGD
  2. ascospore wall assembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

Meiosis, Sporulation

Enzyme and pathway databases

BioCyciYEAST:G3O-30038-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sporulation-specific protein 2
Gene namesi
Name:SPS2
Ordered Locus Names:YDR522C
ORF Names:D9719.26
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR522c.
SGDiS000002930. SPS2.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. fungal-type cell wall Source: SGD
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5656Sequence AnalysisAdd
BLAST
Chaini57 – 475419Sporulation-specific protein 2PRO_0000033195Add
BLAST
Propeptidei476 – 50227Removed in mature formSequence AnalysisPRO_0000277471Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
Lipidationi475 – 4751GPI-anchor amidated asparagineSequence Analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP08459.

Expressioni

Gene expression databases

GenevestigatoriP08459.

Interactioni

Protein-protein interaction databases

BioGridi32572. 42 interactions.
DIPiDIP-7764N.
IntActiP08459. 3 interactions.
STRINGi4932.YDR522C.

Structurei

3D structure databases

ProteinModelPortaliP08459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SPS2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG309463.
GeneTreeiENSGT00530000065410.
HOGENOMiHOG000057088.
InParanoidiP08459.
OMAiGLMIANN.
OrthoDBiEOG75XGWQ.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIWKTQTFF TSISVIQIVN KETKVSTKKE KDSMLNQLNT ILRFLFLFLQ
60 70 80 90 100
LIKSSAAVEP NGGPNILDHN IMLVNTNATI PKKEQTDFEV ISPTKQTQVD
110 120 130 140 150
EDCKKGLYHI ENAGNLIELQ AKCWKVVGNI EISSNYSGSL IDLGLIREIE
160 170 180 190 200
GDLIIKNNKH IFRIQGYNLE SLGKLELDSL TSFVSLDFPA LKEVETVDWR
210 220 230 240 250
VLPILSSVVI NGNIKKIKNI IISDTALTSI DYFNNVKKVD IFNINNNRFL
260 270 280 290 300
ENLFASLESV TKQLTVHSNA KELELDLSNL HTVENMTIKD VSEIKLAKLS
310 320 330 340 350
SVNSSLEFIE NQFSSLELPL LAKVQGTLGL IDNKNLKKLN FSNATDIQGG
360 370 380 390 400
LMIANNTELA KIDFFPKLRQ IGGAIYFEGS FDKIDLPELK LVKGSAYIKS
410 420 430 440 450
SSEELNCEEF TSPKAGRSII RGGKIECTSG MKSKMLNVDE EGNVLGKQET
460 470 480 490 500
DNDNGKKEKG KNGAKSQGSS KKMENSAPKN IFIDAFKMSV YAVFTVLFSI

IF
Length:502
Mass (Da):55,939
Last modified:October 1, 1996 - v2
Checksum:i11F9EFB11CD4D59C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031P → L in AAA35080 (PubMed:9169867).Curated
Sequence conflicti210 – 2101I → S in AAA35080 (PubMed:9169867).Curated
Sequence conflicti324 – 3241V → G in AAA35080 (PubMed:9169867).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33057 Genomic DNA. Translation: AAB64962.1.
M13629 Genomic DNA. Translation: AAA35080.1.
BK006938 Genomic DNA. Translation: DAA12352.1.
PIRiS69578.
RefSeqiNP_010810.1. NM_001180830.1.

Genome annotation databases

EnsemblFungiiYDR522C; YDR522C; YDR522C.
GeneIDi852134.
KEGGisce:YDR522C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33057 Genomic DNA. Translation: AAB64962.1.
M13629 Genomic DNA. Translation: AAA35080.1.
BK006938 Genomic DNA. Translation: DAA12352.1.
PIRiS69578.
RefSeqiNP_010810.1. NM_001180830.1.

3D structure databases

ProteinModelPortaliP08459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32572. 42 interactions.
DIPiDIP-7764N.
IntActiP08459. 3 interactions.
STRINGi4932.YDR522C.

Proteomic databases

PaxDbiP08459.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR522C; YDR522C; YDR522C.
GeneIDi852134.
KEGGisce:YDR522C.

Organism-specific databases

CYGDiYDR522c.
SGDiS000002930. SPS2.

Phylogenomic databases

eggNOGiNOG309463.
GeneTreeiENSGT00530000065410.
HOGENOMiHOG000057088.
InParanoidiP08459.
OMAiGLMIANN.
OrthoDBiEOG75XGWQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-30038-MONOMER.

Miscellaneous databases

NextBioi970537.

Gene expression databases

GenevestigatoriP08459.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Characterization and mutational analysis of a cluster of three genes expressed preferentially during sporulation of Saccharomyces cerevisiae."
    Percival-Smith A., Segall J.
    Mol. Cell. Biol. 6:2443-2451(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-502.
  4. "Increased copy number of the 5' end of the SPS2 gene inhibits sporulation of Saccharomyces cerevisiae."
    Percival-Smith A., Segall J.
    Mol. Cell. Biol. 7:2484-2490(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Stimulation of later functions of the yeast meiotic protein kinase Ime2p by the IDS2 gene product."
    Sia R.A., Mitchell A.P.
    Mol. Cell. Biol. 15:5279-5287(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Morphogenetic pathway of spore wall assembly in Saccharomyces cerevisiae."
    Coluccio A., Bogengruber E., Conrad M.N., Dresser M.E., Briza P., Neiman A.M.
    Eukaryot. Cell 3:1464-1475(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSPS2_YEAST
AccessioniPrimary (citable) accession number: P08459
Secondary accession number(s): D6VTE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 238 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.