ALK2_YEAST
ID ALK2_YEAST Reviewed; 676 AA.
AC P32789; D6VPZ0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Serine/threonine-protein kinase Haspin homolog ALK2;
DE EC=2.7.11.1;
GN Name=ALK2; OrderedLocusNames=YBL009W; ORFNames=YBL0317;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441753; DOI=10.1002/yea.320080909;
RA Delaveau T., Jacq C., Perea J.;
RT "Sequence of a 12.7 kb segment of yeast chromosome II identifies a PDR-like
RT gene and several new open reading frames.";
RL Yeast 8:761-768(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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, INDUCTION, PHOSPHORYLATION, DOMAINS, AND MUTAGENESIS OF
RP 528-E--L-532.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 ALK2 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. {ECO:0000269|PubMed:16855400}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Haspin subfamily. {ECO:0000305}.
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DR EMBL; Z35770; CAA84828.1; -; Genomic_DNA.
DR EMBL; S47695; AAB23988.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07110.1; -; Genomic_DNA.
DR PIR; S41217; S41217.
DR RefSeq; NP_009544.1; NM_001178249.1.
DR AlphaFoldDB; P32789; -.
DR BioGRID; 32690; 194.
DR DIP; DIP-5484N; -.
DR IntAct; P32789; 9.
DR MINT; P32789; -.
DR STRING; 4932.YBL009W; -.
DR iPTMnet; P32789; -.
DR MaxQB; P32789; -.
DR PaxDb; P32789; -.
DR PRIDE; P32789; -.
DR EnsemblFungi; YBL009W_mRNA; YBL009W; YBL009W.
DR GeneID; 852274; -.
DR KEGG; sce:YBL009W; -.
DR SGD; S000000105; ALK2.
DR VEuPathDB; FungiDB:YBL009W; -.
DR eggNOG; KOG2464; Eukaryota.
DR GeneTree; ENSGT00940000167518; -.
DR HOGENOM; CLU_022568_0_0_1; -.
DR InParanoid; P32789; -.
DR OMA; NQCENDQ; -.
DR BioCyc; YEAST:G3O-28915-MON; -.
DR Reactome; R-SCE-9020702; Interleukin-1 signaling.
DR PRO; PR:P32789; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32789; 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; IMP: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..676
FT /note="Serine/threonine-protein kinase Haspin homolog ALK2"
FT /id="PRO_0000202464"
FT DOMAIN 383..672
FT /note="Protein kinase"
FT REGION 53..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 116..118
FT /note="KEN box"
FT MOTIF 150..158
FT /note="D box"
FT COMPBIAS 57..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 528..532
FT /note="EHRNL->AAAAA: Reduces strongly kinase activity."
FT /evidence="ECO:0000269|PubMed:16855400"
SQ SEQUENCE 676 AA; 76372 MW; 0E7B84FC74142206 CRC64;
MNFDAVADQQ MTDRRYFALE VAESDDADSS LNSSSMGSPA VDVGRKVYKI TSHKGSAEDE
SQSFFTSSDS PTSKTRPVGK TIENDDYYGK RSSTGSSLKQ LFNKININDT AHSSNKENVS
QSVLSENKLL SPSKRLSKQG LTKVTNSKFR TPLRPISNQS TLSRDEPVKD FRSLKFRSGS
DFKCWGDEKT SSHVHSSSVN SVNSFTSTTS SSKWKFWKND NLLSRSLSSR SVNDQDPNFV
QPKPTNSLQK KSSISSFHNS IFGGGKHTEK KRNSGFIMPD HQSTKELNHK HSSSNLSFRS
LKHKTSHSSL NKLKVRRKGN TQELNHPIKK TCQISLPVPD QVSKDKIQLK LKNSTSLASL
SSEVTPINTL DYNDSILQQI LQLCDVKYIL HDLREAQSLG LFTLNTRSVQ LSHNFWQTYH
SDMQTSLICK KVCLGALSDL TTSNLISLHE LKSLRLIQGT SGVANLLQAY VVPSNQCEND
QNLILYLFFK YQGTPLSRCS NIDYSQALSI FWQCSSILYV AESKFQLEHR NLTLDHILID
SKGNVTLIDM KCCRFLNIDN NKASYTRLDH HYFFQGRGTL QFEIYELMRS MLPQPISWAT
FEPRTNLLWL YHLSSSLLKM AKKAVVSGAL NREENILIEL THLLDPARKH SKTIFKKELV
IRTCGDLLSL KGEIMQ
