位置:首页 > 蛋白库 > KCC4_YEAST
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024