KCC4_YEAST
ID KCC4_YEAST Reviewed; 1037 AA.
AC P25389; D6VQZ2; P87005; Q8NKJ8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Probable serine/threonine-protein kinase KCC4;
DE EC=2.7.11.1;
GN Name=KCC4; OrderedLocusNames=YCL024W; ORFNames=YCL24W;
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], AND SUBCELLULAR LOCATION.
RX PubMed=9925642; DOI=10.1101/gad.13.2.176;
RA Barral Y., Parra M., Bidlingmaier S., Snyder M.;
RT "Nim1-related kinases coordinate cell cycle progression with the
RT organization of the peripheral cytoskeleton in yeast.";
RL Genes Dev. 13:176-187(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH SWE1.
RX PubMed=12773812; DOI=10.1266/ggs.78.113;
RA Okuzaki D., Watanabe T., Tanaka S., Nojima H.;
RT "The Saccharomyces cerevisiae bud-neck proteins Kcc4 and Gin4 have distinct
RT but partially-overlapping cellular functions.";
RL Genes Genet. Syst. 78:113-126(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP SEQUENCE REVISION.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SEQUENCE REVISION.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP INTERACTION WITH SEPTIN PROTEINS, AND SUBCELLULAR LOCATION.
RX PubMed=11165249; DOI=10.1016/s0014-5793(01)02104-4;
RA Okuzaki D., Nojima H.;
RT "Kcc4 associates with septin proteins of Saccharomyces cerevisiae.";
RL FEBS Lett. 489:197-201(2001).
RN [8]
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 [9]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675; SER-822 AND SER-825, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-707; SER-777 AND
RP SER-871, AND IDENTIFICATION BY 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: Involved in regulation of bud growth during cell cycle and in
CC septin organization. Plays a role in cell wall synthesis.
CC {ECO:0000269|PubMed:12773812}.
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 septin proteins, primarily with CDC11.
CC Interacts with SWE1 and NAP1. {ECO:0000269|PubMed:11165249,
CC ECO:0000269|PubMed:12773812, ECO:0000269|PubMed:18086883}.
CC -!- INTERACTION:
CC P25389; P25293: NAP1; NbExp=5; IntAct=EBI-9607, EBI-11850;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:11165249,
CC ECO:0000269|PubMed:9925642}.
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR EMBL; X59720; CAC42961.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07461.1; -; Genomic_DNA.
DR PIR; S74283; S74283.
DR RefSeq; NP_009907.2; NM_001178670.1.
DR PDB; 3OSM; X-ray; 1.70 A; A=917-1037.
DR PDB; 3OST; X-ray; 1.69 A; A=917-1037.
DR PDBsum; 3OSM; -.
DR PDBsum; 3OST; -.
DR AlphaFoldDB; P25389; -.
DR SMR; P25389; -.
DR BioGRID; 30960; 145.
DR DIP; DIP-1779N; -.
DR IntAct; P25389; 14.
DR MINT; P25389; -.
DR STRING; 4932.YCL024W; -.
DR CarbonylDB; P25389; -.
DR iPTMnet; P25389; -.
DR MaxQB; P25389; -.
DR PaxDb; P25389; -.
DR PRIDE; P25389; -.
DR EnsemblFungi; YCL024W_mRNA; YCL024W; YCL024W.
DR GeneID; 850334; -.
DR KEGG; sce:YCL024W; -.
DR SGD; S000000529; KCC4.
DR VEuPathDB; FungiDB:YCL024W; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000166887; -.
DR HOGENOM; CLU_005276_1_0_1; -.
DR InParanoid; P25389; -.
DR BioCyc; YEAST:G3O-29286-MON; -.
DR EvolutionaryTrace; P25389; -.
DR PRO; PR:P25389; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25389; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0032174; C:cellular bud neck septin collar; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; HDA: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:0007117; P:budding cell bud growth; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0044879; P:mitotic morphogenesis checkpoint signaling; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0000921; P:septin ring assembly; IMP:SGD.
DR Gene3D; 3.30.310.220; -; 1.
DR InterPro; IPR031850; Fungal_KA1_dom.
DR InterPro; IPR043024; KA1_sf_fungal.
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 Pfam; PF16797; Fungal_KA1; 1.
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 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1037
FT /note="Probable serine/threonine-protein kinase KCC4"
FT /id="PRO_0000086109"
FT DOMAIN 21..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 372..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 921..924
FT /evidence="ECO:0007829|PDB:3OST"
FT HELIX 925..927
FT /evidence="ECO:0007829|PDB:3OST"
FT STRAND 930..933
FT /evidence="ECO:0007829|PDB:3OST"
FT STRAND 938..942
FT /evidence="ECO:0007829|PDB:3OST"
FT HELIX 944..956
FT /evidence="ECO:0007829|PDB:3OST"
FT HELIX 959..961
FT /evidence="ECO:0007829|PDB:3OST"
FT STRAND 963..969
FT /evidence="ECO:0007829|PDB:3OST"
FT TURN 970..973
FT /evidence="ECO:0007829|PDB:3OST"
FT STRAND 974..979
FT /evidence="ECO:0007829|PDB:3OST"
FT STRAND 984..986
FT /evidence="ECO:0007829|PDB:3OST"
FT STRAND 990..998
FT /evidence="ECO:0007829|PDB:3OST"
FT STRAND 1004..1013
FT /evidence="ECO:0007829|PDB:3OST"
FT HELIX 1015..1031
FT /evidence="ECO:0007829|PDB:3OST"
SQ SEQUENCE 1037 AA; 116475 MW; 2F5FF36DA8C5B1A3 CRC64;
MTVANTETHS AAKPSSTIGP WKLGETLGFG STGKVQLAQH ERTGHRTAVK VISKSIFNNN
GNHSNDDSVL PYNIEREIVI MKLLSHPNVL SLYDVWETNN NLYLILEYAE KGELFNLLVD
HGPLPEREAI NCFRQIIIGI SYCHALGIVH RDLKPENLLL DSFYNIKIAD FGMAALQTDA
DLLETSCGSP HYAAPEIVSG LPYEGFASDV WSCGVILFAL LTGRLPFDEE NGNVRDLLLK
VQKGQFEMPN DTEISRDAQD LIGKILVVDP RQRIKIRDIL SHPLLKKYQT IKDSKSIKDL
PRENTYLYPL ADSNNHTSAS IDDSILQNLV VLWHGRHADD IVSKLKENGT NKEKILYALL
YRFKLDSVRG SNKKNRNKIK KTKKNKRSST LSSSSSLLLN NRSIQSTPRR RTSKRHSREF
SSSRKRSSFL LSSNPTDSSP IPLRSSKRIT HINVASANTQ ATPSGVPNPH KRNSKKRSSK
RLSYMPNTKR SSLTSKSLSN FTNLIDDDDW EYIEKDAKRT SSNFATLIDE IFEPEKFELA
KREKAELQRK VQEAKRQSVN AQKINEDEFG SEVSDGMKEL KKINDKVSSP LINYEFSQQE
LLQDIDTLLT NRYQLSSYTR PISRLDPGLT PVTETLPNNL KEKTALLQDT EKKIIETIRR
SKFLGSLLNV RGGLSPGKSE LAPIEESPIV STTPLIYNDR MEPRRISDVE VPHFTRKSKH
FTTANNRRSV LSLYAKDSIK DLNEFLIKED PDLPPQGSTD NESRSEDPEI AESITDSRNI
QYDEDDSKDG DNVNNDNILS DFPQGVGISQ EYDMKDKNPN QSPISKSAEP TLVVKLPSLS
SFQGKNASGL GLYQREPSKV TLPSLTSNNS SVGENIEDGA EKGTESEKIA ASLSDDDLKE
DNDKKDNDTV NAPTTVKKPP NSVLLKKFSK GKILELEIHA KIPEKRLYEG LHKLLEGWKQ
YGLKNLVFNI TNMIITGKLV NDSILFLRST LFEIMVLPNG DGRSLIKFNK KTGSTKTLTK
LATEIQIILQ KEGVLDK
