KIC1_YEAST
ID KIC1_YEAST Reviewed; 1080 AA.
AC P38692; D3DL52;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Serine/threonine-protein kinase KIC1;
DE EC=2.7.11.1;
DE AltName: Full=Kinase that interacts with CDC31;
DE AltName: Full=N-rich kinase 1;
GN Name=KIC1; Synonyms=NRK1; OrderedLocusNames=YHR102W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 64665 / S288c / DC5;
RA Fukami Y.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INTERACTION WITH CDC31.
RX PubMed=9813095; DOI=10.1083/jcb.143.3.751;
RA Sullivan D.S., Biggins S., Rose M.D.;
RT "The yeast centrin, cdc31p, and the interacting protein kinase, Kic1p, are
RT required for cell integrity.";
RL J. Cell Biol. 143:751-765(1998).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Protein kinase involved in morphogenesis and cell integrity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with CDC31. {ECO:0000269|PubMed:9813095}.
CC -!- INTERACTION:
CC P38692; P32464: HYM1; NbExp=4; IntAct=EBI-12253, EBI-8859;
CC P38692; Q00772: SLT2; NbExp=3; IntAct=EBI-12253, EBI-17372;
CC P38692; Q08817: SOG2; NbExp=5; IntAct=EBI-12253, EBI-30849;
CC -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D29980; BAA06250.1; -; Genomic_DNA.
DR EMBL; U00059; AAB68860.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06796.1; -; Genomic_DNA.
DR PIR; S48944; S48944.
DR RefSeq; NP_011970.1; NM_001179232.1.
DR AlphaFoldDB; P38692; -.
DR SMR; P38692; -.
DR BioGRID; 36535; 39.
DR DIP; DIP-1999N; -.
DR IntAct; P38692; 18.
DR MINT; P38692; -.
DR STRING; 4932.YHR102W; -.
DR iPTMnet; P38692; -.
DR MaxQB; P38692; -.
DR PaxDb; P38692; -.
DR PRIDE; P38692; -.
DR EnsemblFungi; YHR102W_mRNA; YHR102W; YHR102W.
DR GeneID; 856502; -.
DR KEGG; sce:YHR102W; -.
DR SGD; S000001144; KIC1.
DR VEuPathDB; FungiDB:YHR102W; -.
DR eggNOG; KOG0201; Eukaryota.
DR HOGENOM; CLU_009125_0_0_1; -.
DR InParanoid; P38692; -.
DR OMA; LQMPSPT; -.
DR BioCyc; YEAST:G3O-31147-MON; -.
DR Reactome; R-SCE-75153; Apoptotic execution phase.
DR PRO; PR:P38692; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38692; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd06917; STKc_NAK1_like; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035062; STK_Kic1p-like.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1080
FT /note="Serine/threonine-protein kinase KIC1"
FT /id="PRO_0000086127"
FT DOMAIN 23..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 308..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1080 AA; 117062 MW; 9989EAF315EE0B94 CRC64;
MTTKPQNSKQ GLAEGEMDVS SLFKRTEVIG RGKFGVVYKG YNVKTGRVYA IKVLNLDSDS
DEVEDVQREI QFLASLKQIS NITRYYGSYL KDTSLWIIME HCAGGSLRSL LRPGKIDEKY
IGVIMRELLV ALKCIHKDNV IHRDIKAANV LITNEGNVKL CDFGVAAQVN QTSLRRQTMA
GTPYWMAPEV IMEGVYYDTK VDIWSLGITT YEIATGNPPY CDVEALRAMQ LIIKSKPPRL
EDRSYSTSLK EFIALCLDED PKERLSADDL LKSKFIRAHK ATPTSILKEL ISRYLLFRDK
NKNKYKIEGS IPENEPSKPS EAPKPSQNGG GDEAQKSIAS NDNEIKRVNE GDVEMKWDFD
SLSSSDYIIE NNINLDALAE DNNEWATAQH DLFNYAYPDE DSYYFDPTSH NTRPFVYQGT
TIGKGYPGTI AQNSTLNAPV TNNYTNSKYP SKMVAGTTNT SGTHTAGPMT SSKRLESKAP
KQLLELFEDN EIITAENDVN TEAPKISKSI SSLNAGNSSR DDFIPSISNE VNGNINNNKM
RPHLPPLSSG NNYYSQSTPA LPLLQTKFNK TSKGPPTSGL TTAPTSIEIE IPEELPNSAL
PTPASADPVL IPSTKARSST VTAGTPSSSS SIQYKSPSNV PRRLTVSNNR PEHCPSTITN
QKLGSAVASN SGISSTPNNS NNYNNNTDSE NSRGSSGSNT ANSTQMGITN PGNVTKLSTH
KASSPSRPLF GVGTSPNRKP AGSPTQNIGH NSTHTNLAPP PTMKPMANSK DNKDILLQPL
NSIPSSSTLN TISGNSSNNL TSSNYFSNEK EGSRVNGDFK RNNPNLKLQM PLPTPVVRNK
LLDPNTATSQ NNNGMPGSAG ISTNENINQF GFNTSSASNI PVSMTPISEK HIDFGGKIKR
SQSISNRKNS SASEHPLNIL GSSVSGNVSG IGNNNVGSNN NSGPNNSVPL SANTGNTTIK
ANSTTIATSS SAAASTTAPI SQQTIPSGTQ FNHILSSAAT AANSVNSLGF GMCPPPQSLQ
MEMFLDLESF LPGKQRRVDR KPQVLKELEN LLQMFEEGLP CIEHALKEQL ISTPIKDNEH
