NIF1_SCHPO
ID NIF1_SCHPO Reviewed; 681 AA.
AC P87159;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Mitosis inhibitor nif1;
DE AltName: Full=Nim1-interacting factor 1;
GN Name=nif1; ORFNames=SPBC23G7.04c;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=9135149; DOI=10.1093/emboj/16.6.1342;
RA Wu L., Russell P.;
RT "Nif1, a novel mitotic inhibitor in Schizosaccharomyces pombe.";
RL EMBO J. 16:1342-1350(1997).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-196, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Functions as a negative regulator of mitosis. It interacts
CC with the C-terminal of nim1, thereby inhibiting its kinase activity
CC which phosphorylates wee1. {ECO:0000269|PubMed:9135149}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; U64574; AAC49705.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22620.1; -; Genomic_DNA.
DR PIR; T39950; T39950.
DR RefSeq; NP_595862.1; NM_001021767.2.
DR AlphaFoldDB; P87159; -.
DR SMR; P87159; -.
DR BioGRID; 276996; 8.
DR STRING; 4896.SPBC23G7.04c.1; -.
DR iPTMnet; P87159; -.
DR MaxQB; P87159; -.
DR PaxDb; P87159; -.
DR PRIDE; P87159; -.
DR EnsemblFungi; SPBC23G7.04c.1; SPBC23G7.04c.1:pep; SPBC23G7.04c.
DR GeneID; 2540468; -.
DR KEGG; spo:SPBC23G7.04c; -.
DR PomBase; SPBC23G7.04c; nif1.
DR VEuPathDB; FungiDB:SPBC23G7.04c; -.
DR HOGENOM; CLU_408893_0_0_1; -.
DR InParanoid; P87159; -.
DR OMA; WGITRDR; -.
DR PRO; PR:P87159; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; EXP:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IMP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0023052; P:signaling; IC:PomBase.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SMART; SM00671; SEL1; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..681
FT /note="Mitosis inhibitor nif1"
FT /id="PRO_0000096819"
FT REPEAT 547..582
FT /note="Sel1-like 1"
FT REPEAT 583..618
FT /note="Sel1-like 2"
FT REGION 22..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 681 AA; 75449 MW; 163400FFAC5B8BAB CRC64;
METMQSRTYA GLTKLNTTTA LLNKKDGNDD DKAEHSKRSG YHGLSPLDAL ALKHRDLNRK
LNLRAMMSKS EDNLQILKET TSGSSSDLLN IESPASPAEA SSPFTVRTPT VHDPEHYFVA
QKLSSVFGTP DLEDETDFFD YFSAAPDVHP NDIFDSYNSN NIAESFDDDN YYNSLLPPNA
PYYHEIEPPR TASNTSPTPN SIKSAHPAEP PKRPAFTRSA TSPDKILPTR IKSKDTVSSG
DSTPLSGSSS SKGMLMSMST SENHSLSSNP ELSNSNLLAK NESPADVSNN ESGNESSKEP
DKEHSTPIHP TTPVSRCARP SSRQQTISIL QAQSPFLKKS DKERANLNKT MVSINKSINI
HQSIHEISCP HHSSSDNCLF ILISLMDRLH SPVLKQLDVS LQSLTMTAIR YIDLNYVDVQ
YTNLRGGAYG NGNNSESSDN AQLKKEEHLN LAIHFHLLND HDKCFWHTGM ASSYEDYTAT
FIYGLYLRHG LACSPKTHVS FLFLLKTATQ LLNKLVECLH SSDLGLNDTT PNEKLSTEYN
QQRLLLALIL YELGVCFMHG WGITRDRYLA LHLIKLSGAW GDADAQFEAG LQMSLGAVSD
KDSHMAAYYY RLAGFQGISP PSKCKWVYKS KYSLAANHKV PAASEVAYVS AIVENLESHS
LKFSTKPKAK LRSLITSVRY L
