P27574 (PYP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase 1
EC=3.1.3.48

Alternative name(s):
Protein-tyrosine phosphatase 1
Short name=PTPase 1

Gene names

Name:	pyp1
ORF Names:	SPAC26F1.10c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in inhibiting the onset of mitosis. Dephosphorylates sty1/spc1 and wis1/spc2/sty2.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of G2/M transition of mitotic cell cycle Inferred from mutant phenotype Ref.3PubMed 22624651. Source: PomBase negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion Inferred from mutant phenotype PubMed 12172965. Source: PomBase negative regulation of stress-activated MAPK cascade Traceable author statement PubMed 8649397. Source: PomBase negative regulation of transcription by glucose Inferred from mutant phenotype PubMed 8832414. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	protein tyrosine phosphatase activity Traceable author statement PubMed 8649397. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 550	550	Tyrosine-protein phosphatase 1		PRO_0000094858
Regions
	Domain	260 – 539	280	Tyrosine-protein phosphatase
Sites
	Active site	470	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	318	1	Phosphoserine Ref.5
	Modified residue	320	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P27574 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 5DB770AEAAA59F03	FASTA	550	61,588
	10 20 30 40 50 60 MNFSNGSKSS TFTIAPSGSC IALPPQRGVA TSKYAVHASC LQEYLDKEAW KDDTLIIDLR 70 80 90 100 110 120 PVSEFSKSRI KGSVNLSLPA TLIKRPAFSV ARIISNLHDV DDKRDFQNWQ EFSSILVCVP 130 140 150 160 170 180 AWIANYVTNA EVIGEKFRKE SYSGDFGILD LDYSKVSGKY PSVIDNSPVK SKLGALPSAR 190 200 210 220 230 240 PRLSYSAAQT APISLSSEGS DYFSRPPPTP NVAGLSLNNF FCPLPENKDN KSSPFGSATV 250 260 270 280 290 300 QTPCLHSVPD AFTNPDVATL YQKFLRLQSL EHQRLVSCSD RNSQWSTVDS LSNTSYKKNR 310 320 330 340 350 360 YTDIVPYNCT RVHLKRTSPS ELDYINASFI KTETSNYIAC QGSISRSISD FWHMVWDNVE 370 380 390 400 410 420 NIGTIVMLGS LFEAGREMCT AYWPSNGIGD KQVYGDYCVK QISEENVDNS RFILRKFEIQ 430 440 450 460 470 480 NANFPSVKKV HHYQYPNWSD CNSPENVKSM VEFLKYVNNS HGSGNTIVHC SAGVGRTGTF 490 500 510 520 530 540 IVLDTILRFP ESKLSGFNPS VADSSDVVFQ LVDHIRKQRM KMVQTFTQFK YVYDLIDSLQ 550 KSQVHFPVLT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases." Ottilie S., Chernoff J., Hannig G., Hoffman C.S., Erikson R.L. Proc. Natl. Acad. Sci. U.S.A. 88:3455-3459(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"Negative regulation of mitosis by two functionally overlapping PTPases in fission yeast." Millar J.B.A., Russell P., Dixon J.E., Guan K.L. EMBO J. 11:4943-4952(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[4]	"Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell size at division in fission yeast." Millar J.B.A., Buck V., Wilkinson M.G. Genes Dev. 9:2117-2130(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318 AND SER-320, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63257 mRNA. Translation: AAA35328.1. CU329670 Genomic DNA. Translation: CAA97367.1.
PIR	A40449.
RefSeq	NP_594885.1. NM_001020314.2.
3D structure databases
ProteinModelPortal	P27574.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC26F1.10c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC26F1.10c.1; SPAC26F1.10c.1:pep; SPAC26F1.10c.
GeneID	2542677.
KEGG	spo:SPAC26F1.10c.
Organism-specific databases
PomBase	SPAC26F1.10c.
Phylogenomic databases
eggNOG	COG5599.
KO	K01104.
OrthoDB	EOG4ZPJ48.
Family and domain databases
Gene3D	3.40.250.10. 1 hit.
InterPro	IPR001763. Rhodanese-like_dom. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
Pfam	PF00581. Rhodanese. 1 hit. PF00102. Y_phosphatase. 1 hit. [Graphical view]
PRINTS	PR00700. PRTYPHPHTASE.
SMART	SM00194. PTPc. 1 hit. [Graphical view]
SUPFAM	SSF52821. Rhodanese-like. 1 hit.
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20803725.

Entry information

Entry name

PYP1_SCHPO

Accession

Primary (citable) accession number: P27574

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program