IBP1_SCHPO
ID IBP1_SCHPO Reviewed; 138 AA.
AC Q8WZK3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Dual specificity phosphatase ibp1;
DE EC=3.1.3.48;
DE AltName: Full=Cdc25-like phosphatase ibp1;
DE AltName: Full=Itsy bitsy phosphatase 1;
GN Name=ibp1; ORFNames=SPBC839.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF CYS-70; SER-73 AND
RP ARG-76.
RX PubMed=14508607; DOI=10.1007/s00294-003-0424-1;
RA Snaith H.A., Marlett J., Forsburg S.L.;
RT "Ibp1p, a novel Cdc25-related phosphatase, suppresses Schizosaccharomyces
RT pombe hsk1 (cdc7).";
RL Curr. Genet. 44:38-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: May play a role in DNA replication checkpoint via regulation
CC of hsk1 or may act downstream of hsk1 in an S phase regulatory pathway.
CC {ECO:0000269|PubMed:14508607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR EMBL; CU329671; CAB46700.1; -; Genomic_DNA.
DR PIR; T40714; T40714.
DR RefSeq; NP_595247.1; NM_001021153.2.
DR AlphaFoldDB; Q8WZK3; -.
DR SMR; Q8WZK3; -.
DR BioGRID; 277728; 14.
DR IntAct; Q8WZK3; 2.
DR STRING; 4896.SPBC839.07.1; -.
DR MaxQB; Q8WZK3; -.
DR PaxDb; Q8WZK3; -.
DR EnsemblFungi; SPBC839.07.1; SPBC839.07.1:pep; SPBC839.07.
DR GeneID; 2541214; -.
DR KEGG; spo:SPBC839.07; -.
DR PomBase; SPBC839.07; ibp1.
DR VEuPathDB; FungiDB:SPBC839.07; -.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_107716_1_1_1; -.
DR InParanoid; Q8WZK3; -.
DR OMA; PSIYILH; -.
DR PhylomeDB; Q8WZK3; -.
DR PRO; PR:Q8WZK3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:PomBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Hydrolase; Mitosis; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..138
FT /note="Dual specificity phosphatase ibp1"
FT /id="PRO_0000256254"
FT DOMAIN 19..133
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 70
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT MUTAGEN 70
FT /note="C->S: No catalytic activity."
FT /evidence="ECO:0000269|PubMed:14508607"
FT MUTAGEN 73
FT /note="S->A: No catalytic activity."
FT /evidence="ECO:0000269|PubMed:14508607"
FT MUTAGEN 76
FT /note="R->A: No catalytic activity."
FT /evidence="ECO:0000269|PubMed:14508607"
SQ SEQUENCE 138 AA; 15778 MW; 48B69E211539AECF CRC64;
MSTLSYVSPD ALKGWLMESP NEISIIDVRD YDYEGERIPG SVRIPSDTFL ASVDQHVDDL
MKKRSLIVHC TYSQVRGPKA ARVLSEILRN RITESKEKLS LSQKEKLFQN LPTVYILHGG
FSAWKRRYGG QQGLIEYD
