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Protein

Protein PSP1

Gene

PSP1

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

DNA polymerase alpha mutation suppressor.

Enzyme and pathway databases

BioCyciYEAST:G3O-30026-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PSP1
Alternative name(s):
Growth inhibitory protein 5
Polymerase suppressor protein 1
Gene namesi
Name:PSP1
Synonyms:GIN5
Ordered Locus Names:YDR505C
ORF Names:D9719.11
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR505C.
SGDiS000002913. PSP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: SGD
  • mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 841841Protein PSP1PRO_0000097068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei237 – 2371PhosphoserineCombined sources
Modified residuei334 – 3341PhosphothreonineCombined sources
Modified residuei520 – 5201PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP50896.

PTM databases

iPTMnetiP50896.

Interactioni

Protein-protein interaction databases

BioGridi32556. 69 interactions.
DIPiDIP-5018N.
IntActiP50896. 7 interactions.
MINTiMINT-508587.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini653 – 765113PSP1 C-terminalPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi98 – 1014Poly-Gln
Compositional biasi139 – 1446Poly-Asn
Compositional biasi314 – 3207Poly-Asn
Compositional biasi348 – 35912Poly-GlnAdd
BLAST

Sequence similaritiesi

Belongs to the PSP1 family.Curated
Contains 1 PSP1 C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000067658.
InParanoidiP50896.
OrthoDBiEOG78PVJF.

Family and domain databases

InterProiIPR007557. PSP1_C.
[Graphical view]
PfamiPF04468. PSP1. 1 hit.
[Graphical view]
PROSITEiPS51411. PSP1_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLPTVNSTT SISDNVDLKN YYEDLLFKNN SGKSLSDLPR KLNDNSNNSG
60 70 80 90 100
SDTVDPLAGL NNLRNSIKSA GNGMENRRTF DDIDFMGRFP YLPPVPNQQQ
110 120 130 140 150
QPFSHQNGFI QEHPSSNLTS FQMSSSNSEP MSAPPISSNN NNLNSTQMGN
160 170 180 190 200
YQAQQRSFPQ FNGNSFHSNG NDLMGNRMDS DYMRLMNKTN IGFTSNSGSN
210 220 230 240 250
FAAPSHSAGN PSSMNNQQVP SFNWQQPSHP ESTIRRSSYI SDTLINHQMP
260 270 280 290 300
DARQKQTSQV QQQHAQGFNL FNSRFNYDNL NSTHLTAKGV PEFGNGVQPP
310 320 330 340 350
YPYDNEPNNA SISNSNNNNN SHNMVPMQQF RRNTQPVASF NPSLPTFQQQ
360 370 380 390 400
QQQPQQPQQP RNVNVPTSFN GERVDDVQLV QLQRSSSVPS STNSHNLQNE
410 420 430 440 450
NSNEGNVSLD NGLVLIQGKH LTSSKTLHDL YSDCGSGYFA SSAVFEFTDN
460 470 480 490 500
IKKMLKLHDS NESYDAKNMG LIDEEGNTYQ SLLNFLDILR SCNMNYVNDP
510 520 530 540 550
ESNNGIVSNN GGNKNRRKGS FTTELSCRNA NNSFLPYTPL VLVALKNGKL
560 570 580 590 600
ELLSTPQATN LLLKRGDLVI IDGDRGRDLV LVVEPSVDLN LALFINFLKK
610 620 630 640 650
KIHFDSLITS ESQHYRNDEF IQMLIDSKNG QKKKLNPKLY DVVELTELII
660 670 680 690 700
PSKQVLRFAT PWEVTTNLHN KFEDELKALH IAQSKLQALN DNSKSQNTND
710 720 730 740 750
SSSNNFTNAA TYSKPKLNIK ILNAEFQFDR KKLTFYYVCE ERNDFRDLIK
760 770 780 790 800
ELFKYYKTRI WLCAIPNNLS IDSKYYDKQQ KELKLYQNIV KNYNAEDLMN
810 820 830 840
VNEFSQNRGN NRVNFAPPLN EIELDNFQIA VYEELVHELF H
Length:841
Mass (Da):95,348
Last modified:July 27, 2011 - v2
Checksum:i03B5C27F96F71F2C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161S → C in AAA93076 (PubMed:9529527).Curated
Sequence conflicti122 – 13312QMSSS…EPMSA → KCLRLIQSCVP in AAA93076 (PubMed:9529527).CuratedAdd
BLAST
Sequence conflicti198 – 21013GSNFA…HSAGN → RAILLPHHTVLAT in AAA93076 (PubMed:9529527).CuratedAdd
BLAST
Sequence conflicti732 – 7321K → E in AAB64947 (PubMed:9169867).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33115 Genomic DNA. Translation: AAA93076.1.
U33057 Genomic DNA. Translation: AAB64947.1.
BK006938 Genomic DNA. Translation: DAA12337.2.
PIRiS69563.
RefSeqiNP_010793.2. NM_001180813.2.

Genome annotation databases

EnsemblFungiiYDR505C; YDR505C; YDR505C.
GeneIDi852116.
KEGGisce:YDR505C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33115 Genomic DNA. Translation: AAA93076.1.
U33057 Genomic DNA. Translation: AAB64947.1.
BK006938 Genomic DNA. Translation: DAA12337.2.
PIRiS69563.
RefSeqiNP_010793.2. NM_001180813.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32556. 69 interactions.
DIPiDIP-5018N.
IntActiP50896. 7 interactions.
MINTiMINT-508587.

PTM databases

iPTMnetiP50896.

Proteomic databases

MaxQBiP50896.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR505C; YDR505C; YDR505C.
GeneIDi852116.
KEGGisce:YDR505C.

Organism-specific databases

EuPathDBiFungiDB:YDR505C.
SGDiS000002913. PSP1.

Phylogenomic databases

GeneTreeiENSGT00530000067658.
InParanoidiP50896.
OrthoDBiEOG78PVJF.

Enzyme and pathway databases

BioCyciYEAST:G3O-30026-MONOMER.

Miscellaneous databases

PROiP50896.

Family and domain databases

InterProiIPR007557. PSP1_C.
[Graphical view]
PfamiPF04468. PSP1. 1 hit.
[Graphical view]
PROSITEiPS51411. PSP1_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Suppressors of the temperature sensitivity of DNA polymerase alpha mutations in Saccharomyces cerevisiae."
    Formosa T., Nittis T.
    Mol. Gen. Genet. 257:461-468(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 732.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. "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-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "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-31; SER-34 AND SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-34; SER-36; SER-237; THR-334 AND SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSP1_YEAST
AccessioniPrimary (citable) accession number: P50896
Secondary accession number(s): D6VTC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 111 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 259 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

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 one 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.