ALK1_YEAST
ID ALK1_YEAST Reviewed; 760 AA.
AC P43633; D6VUB6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase Haspin homolog ALK1;
DE EC=2.7.11.1;
DE AltName: Full=DNA damage-responsive protein ALK1;
GN Name=ALK1; OrderedLocusNames=YGL021W; ORFNames=G3686;
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].
RA Moen C., Lindstedt B.A., Berdal K.G., Rognes T., Seeberg E.C.;
RT "A novel DNA damage-response gene from Saccharomyces cerevisiae with
RT homology to protein kinase.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [5]
RP FUNCTION, INDUCTION, DOMAINS, AND MUTAGENESIS OF 606-E--L-610.
RX PubMed=16855400; DOI=10.4161/cc.5.13.2914;
RA Nespoli A., Vercillo R., di Nola L., Diani L., Giannattasio M., Plevani P.,
RA Muzi-Falconi M.;
RT "Alk1 and Alk2 are two new cell cycle-regulated haspin-like proteins in
RT budding yeast.";
RL Cell Cycle 5:1464-1471(2006).
RN [6]
RP IDENTIFICATION BY 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-79, 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 haspin-like protein kinase involved in cell
CC cycle regulation. {ECO:0000269|PubMed:16855400}.
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 -!- INDUCTION: Absent in G1-arrested cells and accumulates in G2-M.
CC {ECO:0000269|PubMed:16855400}.
CC -!- DOMAIN: The KEN and D (destructive) boxes are required for the cell
CC cycle-controlled ALK1 degradation by the anaphase promoting complex
CC (APC) pathway. {ECO:0000269|PubMed:16855400}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. However, weak kinase activity was experimentally
CC demonstrated. {ECO:0000269|PubMed:16855400}.
CC -!- PTM: Periodically phosphorylated during the cell cycle with a
CC phosphorylation peak during mitosis and hyperphosphorylated after DNA
CC damage.
CC -!- MISCELLANEOUS: Present with 2190 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. Haspin subfamily. {ECO:0000305}.
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DR EMBL; X87672; CAA61012.1; -; Genomic_DNA.
DR EMBL; Z72543; CAA96721.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08077.1; -; Genomic_DNA.
DR PIR; S64023; S64023.
DR RefSeq; NP_011494.1; NM_001180886.1.
DR AlphaFoldDB; P43633; -.
DR BioGRID; 33225; 55.
DR DIP; DIP-4816N; -.
DR IntAct; P43633; 3.
DR MINT; P43633; -.
DR STRING; 4932.YGL021W; -.
DR iPTMnet; P43633; -.
DR MaxQB; P43633; -.
DR PaxDb; P43633; -.
DR PRIDE; P43633; -.
DR EnsemblFungi; YGL021W_mRNA; YGL021W; YGL021W.
DR GeneID; 852863; -.
DR KEGG; sce:YGL021W; -.
DR SGD; S000002989; ALK1.
DR VEuPathDB; FungiDB:YGL021W; -.
DR eggNOG; KOG2464; Eukaryota.
DR GeneTree; ENSGT00940000167518; -.
DR HOGENOM; CLU_022568_0_0_1; -.
DR InParanoid; P43633; -.
DR OMA; TKFQFEH; -.
DR BioCyc; YEAST:G3O-30541-MON; -.
DR Reactome; R-SCE-9020702; Interleukin-1 signaling.
DR PRO; PR:P43633; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P43633; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0072354; F:histone kinase activity (H3-T3 specific); IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR InterPro; IPR024604; GSG2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SMART; SM01331; DUF3635; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA damage; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..760
FT /note="Serine/threonine-protein kinase Haspin homolog ALK1"
FT /id="PRO_0000064557"
FT DOMAIN 468..760
FT /note="Protein kinase"
FT REGION 76..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 200..202
FT /note="KEN box"
FT MOTIF 224..232
FT /note="D box"
FT COMPBIAS 77..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..382
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474..482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 606..610
FT /note="EHRNL->AAAAA: Reduces strongly kinase activity."
FT /evidence="ECO:0000269|PubMed:16855400"
FT CONFLICT 758..760
FT /note="LYK -> AL (in Ref. 1; CAA61012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 86087 MW; 3FD169AD789ED60A CRC64;
MLLHFDIVIQ LLSSHTLKSH QVEPPMDFET SFEEFVEDKR FIALEVSDND DDCDTDLTAD
TADELESSAI LKMRESDASL NVTTGNNTSR KTTSNSKKRW SLLSNHSAVS SSKSKKRWSV
LSSSFTSESH KDRESRNVLQ QKRKSLQSYS SLDTVASNSS ISASSSLKRS STGLSLRQLF
TKIGINDDIS QPGIGIPQGK ENLPPTMGKK NSSIASTSSE NRLRTPLKPL VNHSKRPTSQ
PQQQQPLYNA SLSSRRSSIS STVSSSSSSK WRFWKRNKNQ TPALLQPDHH SLKTFPAVNR
RDSMTPVEPR NMVKHKTSFS DFHKTIFSSN TYSESSDTIS SMEITLKNKA SSSSLSLNVL
KKRNSQSSLK HKSSHASLQK FKRNKGKSSM IAPSTATNSS NDDSCSYSSK NSTLSHRISL
PVPDQVSRDK IQNKLRYSTS LLSLNSKSSL PMNKNDHDET LLRQILLNCD IKRILNPAKG
DVLPLINDVN HLSSIQLTSN VWQIGEVICK KVSLGTIDDI TWDRKFLSLQ ELEKLKIMQQ
KFDGIPQLLK SFVVKEANGG LYLYLLFKDH GTPISLISLK NWKQILKIFW SCAGIIHGLE
KNLKFEHRNL TLDNILIDGN GNITIIDFKC SRLQTPQDDV LYLRLDHPLF FLNGKDKSKI
NEYQYQFEFE IYQSMRILLN MDASAFEPMT NLYWLYYLSR VLLKFGDRKL GKNDANRDKM
ARVINHLEMN LAVHKRGGQL FKRLETEDIK NTGDLLKLYK
