EKC1_SCHPO
ID EKC1_SCHPO Reviewed; 838 AA.
AC O74511; O74554;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Extragenic suppressor of kinetochore protein 1;
GN Name=ekc1; ORFNames=SPCC663.01c, SPCC777.16c;
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], FUNCTION, INTERACTION WITH PPE1 AND
RP MIS12, AND SUBCELLULAR LOCATION.
RX PubMed=12773390; DOI=10.1093/emboj/cdg266;
RA Goshima G., Iwasaki O., Obuse C., Yanagida M.;
RT "The role of Ppe1/PP6 phosphatase for equal chromosome segregation in
RT fission yeast kinetochore.";
RL EMBO J. 22:2752-2763(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-418; THR-419;
RP SER-425; SER-459; SER-468; SER-491; THR-493; SER-494; SER-711 AND SER-713,
RP AND 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: Has a role in chromosome segregation. May provide a dynamic
CC connection between kinetochore microtubules and kinetochore chromatin.
CC {ECO:0000269|PubMed:12773390}.
CC -!- SUBUNIT: Interacts with ppe1 and mis12. {ECO:0000269|PubMed:12773390}.
CC -!- INTERACTION:
CC O74511; P36614: ppe1; NbExp=2; IntAct=EBI-1153096, EBI-1153118;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773390}.
CC Note=Associated with chromatin.
CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU329672; CAA20720.2; -; Genomic_DNA.
DR PIR; T41532; T41532.
DR RefSeq; NP_588263.2; NM_001023253.2.
DR AlphaFoldDB; O74511; -.
DR SMR; O74511; -.
DR BioGRID; 276073; 19.
DR IntAct; O74511; 2.
DR STRING; 4896.SPCC663.01c.1; -.
DR iPTMnet; O74511; -.
DR MaxQB; O74511; -.
DR PaxDb; O74511; -.
DR PRIDE; O74511; -.
DR EnsemblFungi; SPCC663.01c.1; SPCC663.01c.1:pep; SPCC663.01c.
DR GeneID; 2539511; -.
DR KEGG; spo:SPCC663.01c; -.
DR PomBase; SPCC663.01c; ekc1.
DR VEuPathDB; FungiDB:SPCC663.01c; -.
DR eggNOG; KOG2073; Eukaryota.
DR HOGENOM; CLU_003676_2_0_1; -.
DR InParanoid; O74511; -.
DR OMA; TYDPIYL; -.
DR PhylomeDB; O74511; -.
DR PRO; PR:O74511; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IPI:PomBase.
DR GO; GO:0072542; F:protein phosphatase activator activity; IMP:PomBase.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator 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 GO; GO:1905341; P:negative regulation of protein localization to kinetochore; IMP:PomBase.
DR GO; GO:1903379; P:regulation of mitotic chromosome condensation; IGI:PomBase.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..838
FT /note="Extragenic suppressor of kinetochore protein 1"
FT /id="PRO_0000046105"
FT REGION 411..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..825
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 493
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 838 AA; 94967 MW; A4E40D2CC1DE8F65 CRC64;
MFWRLGQGFG FQSSSAIEAI LDKPEDEINL KELLEENGVL DECKSHNPKL LEYLCKPEVL
SQLIDYILEV DETEIPSADG GYEEPEHTRL SYIASEILSS DVWSICEACV ENKTLMVKLW
SFLDSEGPLN PLQASYFAKV NEHFLDKKTE ETVAFIQSID NFVEKILRHA ETSAIMDLLL
KFISMDRCNT AIGIADWLYS QGLIQSLLRL LSPYVDPDVQ FTVADVIKAI IAISANSNEP
GVIGPNSLSR ELVSRQTITT LTDYMTDSKA PHSATSLING VSIVIELIRK NNSDYDVTPV
LQMPLDTHPP TTRDPIYLGT MLRLFAEKIP VFQKILLKPS TESDLMPTSF GKIKPLGFER
FRICELYAEL LHCSNMSLLS DPNGEAMVMQ RDHLRDYLFR HNSCARDLVM SDEDDDDSTF
SDKNSKDFKE TEDMNGAEDM HGRAPQITKD NLNLTTTDSP MSEAEPVSEE EYKDVMETAK
ALHHGDDDAA SDTSYEPLPE SVIEDAKKLP VIGDFLKIEF IQNNVIPTIL DHFFDYPWNN
FLHNVVYDVV QQVLNAPMDK DQNYALAVDM FKQGKITEKI VYGQELNDKK VAKPSGFRAG
YMGHLTIIAD EVVKFVEHYS STFDQELLNL INDEKWQNFV NKTLVETRNR DNQLLGGLEP
SMVGYLEDMD EGEMLDANNL PEMQFALEQE LESNSSDDDV VEVHRELSHN SSSNDEDDGN
DEDPLSREMS RRLSFESAND SDQDNRDHFA QYMSQQISDN NANQFSSSDE DDDDDDEVVE
WVSRGNENKY PRSNFFINGS DREDFSDSEE EDGNDSSDDD RGFAEEEYSD GLVLNHGK
