KIN1_YEAST
ID KIN1_YEAST Reviewed; 1064 AA.
AC P13185; D6VSA8; Q04606;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Serine/threonine protein kinase KIN1;
DE EC=2.7.11.1;
GN Name=KIN1; OrderedLocusNames=YDR122W; ORFNames=YD9727.17;
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].
RX PubMed=2957690; DOI=10.1073/pnas.84.17.6035;
RA Levin D.E., Hammond C.I., Ralston R.O., Bishop J.M.;
RT "Two yeast genes that encode unusual protein kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6035-6039(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 FUNCTION, AND PHOSPHORYLATION.
RX PubMed=1652871; DOI=10.1002/yea.320070304;
RA Lamb A., Tibbetts M., Hammond C.I.;
RT "The product of the KIN1 locus in Saccharomyces cerevisiae is a
RT serine/threonine-specific protein kinase.";
RL Yeast 7:219-228(1991).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=8020610; DOI=10.1006/excr.1994.1177;
RA Tibbetts M., Donovan M., Roe S., Stiltner A.M., Hammond C.I.;
RT "KIN1 and KIN2 protein kinases localize to the cytoplasmic face of the
RT yeast plasma membrane.";
RL Exp. Cell Res. 213:93-99(1994).
RN [6]
RP FUNCTION.
RX PubMed=8203145; DOI=10.1002/yea.320100111;
RA Donovan M., Romano P., Tibbetts M., Hammond C.I.;
RT "Characterization of the KIN2 gene product in Saccharomyces cerevisiae and
RT comparison between the kinase activities of p145KIN1 and p145KIN2.";
RL Yeast 10:113-124(1994).
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC9 AND SRO7.
RX PubMed=15563607; DOI=10.1091/mbc.e04-07-0549;
RA Elbert M., Rossi G., Brennwald P.;
RT "The yeast par-1 homologs kin1 and kin2 show genetic and physical
RT interactions with components of the exocytic machinery.";
RL Mol. Biol. Cell 16:532-549(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593; SER-764 AND SER-986, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534 AND SER-764, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-764, 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: Serine/threonine protein kinase involved in the regulation of
CC exocytosis. Induces phosphorylation of SEC9 and its release from the
CC plasma membrane to the cytosol. {ECO:0000269|PubMed:15563607,
CC ECO:0000269|PubMed:1652871, ECO:0000269|PubMed:8203145}.
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 SEC9 and SRO7. {ECO:0000269|PubMed:15563607}.
CC -!- INTERACTION:
CC P13185; P32944: SWE1; NbExp=3; IntAct=EBI-9716, EBI-18607;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:1652871}.
CC -!- MISCELLANEOUS: Present with 279 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; M69017; AAA34722.1; -; Genomic_DNA.
DR EMBL; Z48758; CAA88675.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11968.1; -; Genomic_DNA.
DR PIR; S52687; S52687.
DR RefSeq; NP_010407.1; NM_001180430.1.
DR AlphaFoldDB; P13185; -.
DR SMR; P13185; -.
DR BioGRID; 32178; 125.
DR DIP; DIP-1406N; -.
DR IntAct; P13185; 26.
DR MINT; P13185; -.
DR STRING; 4932.YDR122W; -.
DR iPTMnet; P13185; -.
DR MaxQB; P13185; -.
DR PaxDb; P13185; -.
DR PRIDE; P13185; -.
DR EnsemblFungi; YDR122W_mRNA; YDR122W; YDR122W.
DR GeneID; 851700; -.
DR KEGG; sce:YDR122W; -.
DR SGD; S000002529; KIN1.
DR VEuPathDB; FungiDB:YDR122W; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000176540; -.
DR HOGENOM; CLU_002664_0_2_1; -.
DR InParanoid; P13185; -.
DR OMA; MFDFYKR; -.
DR BioCyc; YEAST:G3O-29722-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P13185; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P13185; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IPI:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IDA:SGD.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045921; P:positive regulation of exocytosis; IGI:SGD.
DR GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
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; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 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; Cell membrane; Cytoplasm; Exocytosis; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1064
FT /note="Serine/threonine protein kinase KIN1"
FT /id="PRO_0000086131"
FT DOMAIN 120..398
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1015..1064
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 126..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 25
FT /note="S -> R (in Ref. 1; AAA34722)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="T -> H (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="V -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="A -> R (in Ref. 1; AAA34722)"
FT /evidence="ECO:0000305"
FT CONFLICT 920..921
FT /note="NI -> IN (in Ref. 1; AAA34722)"
FT /evidence="ECO:0000305"
FT CONFLICT 976
FT /note="T -> A (in Ref. 1; AAA34722)"
FT /evidence="ECO:0000305"
FT CONFLICT 979..980
FT /note="SI -> T (in Ref. 1; AAA34722)"
FT /evidence="ECO:0000305"
FT CONFLICT 984..985
FT /note="KT -> NS (in Ref. 1; AAA34722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1064 AA; 120071 MW; E4104B84A8E45C36 CRC64;
MDDYHVNTAF SMGRGNQQDD GNSESNSMHT QPSTMAPATL RMMGKSPQQQ QQQNTPLMPP
ADIKYANNGN SHQAEQKERQ VELEGKSREN APKPNTTSQS RVSSSQGMPK QFHRKSLGDW
EFVETVGAGS MGKVKLAKHR YTNEVCAVKI VNRATKAFLH KEQMLPPPKN EQDVLERQKK
LEKEISRDKR TIREASLGQI LYHPHICRLF EMCTLSNHFY MLFEYVSGGQ LLDYIIQHGS
IREHQARKFA RGIASALIYL HANNIVHRDL KIENIMISDS SEIKIIDFGL SNIYDSRKQL
HTFCGSLYFA APELLKANPY TGPEVDVWSF GVVLFVLVCG KVPFDDENSS VLHEKIKQGK
VEYPQHLSIE VISLLSKMLV VDPKRRATLK QVVEHHWMVR GFNGPPPSYL PKRVPLTIEM
LDINVLKEMY RLEFIDDVEE TRSVLVSIIT DPTYVLLSRQ YWTLAAKMNA ESSDNGNAPN
ITESFEDPTR AYHPMISIYY LTSEMLDRKH AKIRNQQQRQ SHENIEKLSE IPESVKQRDV
EVNTTAMKSE PEATLATKDT SVPFTPKNSD GTEPPLHVLI PPRLAMPEQA HTSPTSRKSS
DNQRREMEYA LSPTPQGNDY QQFRVPSTTG DPSEKAKFGN IFRKLSQRRK KTIEQTSVNS
NNSINKPVQK THSRAVSDFV PGFAKPSYDS NYTMNEPVKT NDSRGGNKGD FPALPADAEN
MVEKQREKQI EEDIMKLHDI NKQNNEVAKG SGREAYAAQK FEGSDDDENH PLPPLNVAKG
RKLHPSARAK SVGHARRESL KYMRPPMPSS AYPQQELIDT GFLESSDDNK SDSLGNVTSQ
TNDSVSVHSV NAHINSPSVE KELTDEEILQ EASRAPAGSM PSIDFPRSLF LKGFFSVQTT
SSKPLPIVRY KIMFVLRKMN IEFKEVKGGF VCMQRFSSNN VAAKREGTPR SIMPLSHHES
IRRQGSNKYS PSSPLTTNSI HQRKTSITET YGDDKHSGTS LENIHQQGDG SEGMTTTEKE
PIKFEIHIVK VRIVGLAGVH FKKISGNTWL YKELASSILK ELKL
