KIN2_YEAST
ID KIN2_YEAST Reviewed; 1147 AA.
AC P13186; D6VY96; Q12384;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Serine/threonine-protein kinase KIN2;
DE EC=2.7.11.1;
GN Name=KIN2; OrderedLocusNames=YLR096W; ORFNames=L8004.3;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-609 AND SER-888, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-549, AND
RP 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: 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: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 P13186; P33306: BCK2; NbExp=4; IntAct=EBI-9723, EBI-3480;
CC P13186; P27637: BUD14; NbExp=4; IntAct=EBI-9723, EBI-20747;
CC P13186; P43565: RIM15; NbExp=2; IntAct=EBI-9723, EBI-15150;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side.
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; M69018; AAA34723.1; -; Genomic_DNA.
DR EMBL; Z73268; CAA97659.1; -; Genomic_DNA.
DR EMBL; Z73269; CAA97661.1; -; Genomic_DNA.
DR EMBL; U53876; AAB67540.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09412.1; -; Genomic_DNA.
DR PIR; S64930; S64930.
DR RefSeq; NP_013197.1; NM_001181983.1.
DR AlphaFoldDB; P13186; -.
DR SMR; P13186; -.
DR BioGRID; 31369; 232.
DR DIP; DIP-6276N; -.
DR IntAct; P13186; 66.
DR MINT; P13186; -.
DR STRING; 4932.YLR096W; -.
DR iPTMnet; P13186; -.
DR MaxQB; P13186; -.
DR PaxDb; P13186; -.
DR PRIDE; P13186; -.
DR EnsemblFungi; YLR096W_mRNA; YLR096W; YLR096W.
DR GeneID; 850785; -.
DR KEGG; sce:YLR096W; -.
DR SGD; S000004086; KIN2.
DR VEuPathDB; FungiDB:YLR096W; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000176540; -.
DR HOGENOM; CLU_002664_5_0_1; -.
DR InParanoid; P13186; -.
DR OMA; GGHRRKF; -.
DR BioCyc; YEAST:G3O-32246-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P13186; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P13186; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA: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..1147
FT /note="Serine/threonine-protein kinase KIN2"
FT /id="PRO_0000086133"
FT DOMAIN 99..377
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1098..1147
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 105..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 216..217
FT /note="QH -> HD (in Ref. 1; AAA34723)"
FT /evidence="ECO:0000305"
FT CONFLICT 675..707
FT /note="QEPLPEREPPTYMSKSNEISIKVPKSHSRTISD -> SGTYSSKENLQHICQ
FT NQMKFPSKYRKAIVVLYQT (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 756..758
FT /note="NAE -> KRQ (in Ref. 1; AAA34723)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="P -> PLSVP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034..1037
FT /note="ATNT -> TTNSI (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041..1042
FT /note="NS -> KT (in Ref. 1; AAA34723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1147 AA; 128338 MW; AC2660BF3CA69600 CRC64;
MPNPNTADYL VNPNFRTSKG GSLSPTPEAF NDTRVAAPAT LRMMGKQSGP RNDQQQAPLM
PPADIKQGKE QAAQRQNDAS RPNGAVELRQ FHRRSLGDWE FLETVGAGSM GKVKLVKHRQ
TKEICVIKIV NRASKAYLHK QHSLPSPKNE SEILERQKRL EKEIARDKRT VREASLGQIL
YHPHICRLFE MCTMSNHFYM LFEYVSGGQL LDYIIQHGSL KEHHARKFAR GIASALQYLH
ANNIVHRDLK IENIMISSSG EIKIIDFGLS NIFDYRKQLH TFCGSLYFAA PELLKAQPYT
GPEVDIWSFG IVLYVLVCGK VPFDDENSSI LHEKIKKGKV DYPSHLSIEV ISLLTRMIVV
DPLRRATLKN VVEHPWMNRG YDFKAPSYVP NRVPLTPEMI DSQVLKEMYR LEFIDDIEDT
RRSLIRLVTE KEYIQLSQEY WDKLSNAKGL SSSLNNNYLN STAQQTLIQN HITSNPSQSG
YNEPDSNFED PTLAYHPLLS IYHLVSEMVA RKLAKLQRRQ ALALQAQAQQ RQQQQQVALG
TKVALNNNSP DIMTKMRSPQ KEVVPNPGIF QVPAIGTSGT SNNTNTSNKP PLHVMVPPKL
TIPEQAHTSP TSRKSSDIHT ELNGVLKSTP VPVSGEYQQR SASPVVGEHQ EKNTIGGIFR
RISQSGQSQH PTRQQEPLPE REPPTYMSKS NEISIKVPKS HSRTISDYIP SARRYPSYVP
NSVDVKQKPA KNTTIAPPIR SVSQKQNSDL PALPQNAELI VQKQRQKLLQ ENLDKLQIND
NDNNNVNAVV DGINNDNSDH YLSVPKGRKL HPSARAKSVG HARRESLKFT RPPIPAALPP
SDMTNDNGFL GEANKERYNP VSSNFSTVPE DSTTYSNDTN NRLTSVYSQE LTEKQILEEA
SKAPPGSMPS IDYPKSMFLK GFFSVQTTSS KPLPIVRHNI ISVLTRMNID FKEVKGGFIC
VQQRPSIETA AVPVITTTGV GLDSGKAMDL QNSLDSQLSS SYHSTASSAS RNSSIKRQGS
YKRGQNNIPL TPLATNTHQR NSSIPMSPNY GNQSNGTSGE LSSMSLDYVQ QQDDILTTSR
AQNINNVNGQ TEQTNTSGIK ERPPIKFEIH IVKVRIVGLA GVHFKKVSGN TWLYKELASY
ILKELNL
