HASP_ARATH
ID HASP_ARATH Reviewed; 599 AA.
AC O80528; Q84WE0;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Serine/threonine-protein kinase haspin homolog {ECO:0000305};
DE Short=AtHaspin {ECO:0000303|PubMed:21527018, ECO:0000303|PubMed:21749502};
DE EC=2.7.11.1 {ECO:0000305};
GN Name=HASPIN {ECO:0000305};
GN OrderedLocusNames=At1g09450 {ECO:0000312|Araport:AT1G09450};
GN ORFNames=F14J9.11 {ECO:0000312|EMBL:AAC33205.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND MUTAGENESIS OF LYS-310.
RX PubMed=21527018; DOI=10.1186/1471-2229-11-73;
RA Kurihara D., Matsunaga S., Omura T., Higashiyama T., Fukui K.;
RT "Identification and characterization of plant Haspin kinase as a histone H3
RT threonine kinase.";
RL BMC Plant Biol. 11:73-73(2011).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-310.
RX PubMed=21749502; DOI=10.1111/j.1365-313x.2011.04699.x;
RA Ashtiyani R.K., Moghaddam A.M., Schubert V., Rutten T., Fuchs J.,
RA Demidov D., Blattner F.R., Houben A.;
RT "AtHaspin phosphorylates histone H3 at threonine 3 during mitosis and
RT contributes to embryonic patterning in Arabidopsis.";
RL Plant J. 68:443-454(2011).
CC -!- FUNCTION: Threonine-protein kinase that phosphorylates histone H3 in
CC vitro at 'Thr-3' (H3T3ph) and 'Thr-11' (H3T11ph), but not at 'Ser-10'
CC (H3S10ph) or 'Ser-28' (H3S28ph). Plays a role in mitotic cell division
CC during plant growth (PubMed:21527018). Threonine-protein kinase that
CC phosphorylates histone H3 in vitro at 'Thr-3' (H3T3ph), but not at
CC 'Thr-11' (H3T11ph), 'Ser-10' (H3S10ph) or 'Ser-28' (H3S28ph). Involved
CC in histone H3 phosphorylation in mitotic cells. Contributes to organ
CC and plant development, as well as embryonic patterning
CC (PubMed:21749502). {ECO:0000269|PubMed:21527018,
CC ECO:0000269|PubMed:21749502}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21527018}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:21527018}. Nucleus
CC {ECO:0000269|PubMed:21527018}. Chromosome
CC {ECO:0000269|PubMed:21527018}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:21527018}. Note=During interphase, localized in the
CC cytoplasm and at the nuclear periphery. During prometaphase and
CC metaphase, localized on chromosomes, and around the cell plate during
CC cytokinesis. {ECO:0000269|PubMed:21527018}.
CC -!- TISSUE SPECIFICITY: Expressed in meristems and primordia of root tips,
CC lateral roots, shoot apex, leaves and flowers.
CC {ECO:0000269|PubMed:21527018}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, expressed in embryos and
CC suspensors from the one-cell stage to the four-cell stage. Expressed in
CC the embryo until the torpedo stage. {ECO:0000269|PubMed:21527018}.
CC -!- INDUCTION: Expression peaks at mitosis. {ECO:0000269|PubMed:21527018}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:21749502}.
CC -!- MISCELLANEOUS: Over-expression of an inactive kinase mutant decreases
CC the size of the root meristem and delays root growth.
CC {ECO:0000269|PubMed:21527018}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Haspin subfamily. {ECO:0000305}.
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DR EMBL; AC003970; AAC33205.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28444.1; -; Genomic_DNA.
DR EMBL; BT003923; AAO41970.1; -; mRNA.
DR PIR; H86227; H86227.
DR RefSeq; NP_172416.2; NM_100816.5.
DR AlphaFoldDB; O80528; -.
DR SMR; O80528; -.
DR STRING; 3702.AT1G09450.1; -.
DR iPTMnet; O80528; -.
DR PaxDb; O80528; -.
DR PRIDE; O80528; -.
DR ProteomicsDB; 230386; -.
DR EnsemblPlants; AT1G09450.1; AT1G09450.1; AT1G09450.
DR GeneID; 837468; -.
DR Gramene; AT1G09450.1; AT1G09450.1; AT1G09450.
DR KEGG; ath:AT1G09450; -.
DR Araport; AT1G09450; -.
DR TAIR; locus:2012340; AT1G09450.
DR eggNOG; KOG2464; Eukaryota.
DR HOGENOM; CLU_019002_1_0_1; -.
DR InParanoid; O80528; -.
DR OMA; DYWEGSF; -.
DR OrthoDB; 1374355at2759; -.
DR PhylomeDB; O80528; -.
DR PRO; PR:O80528; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80528; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035402; F:histone kinase activity (H3-T11 specific); IDA:TAIR.
DR GO; GO:0072354; F:histone kinase activity (H3-T3 specific); IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0035407; P:histone H3-T11 phosphorylation; IDA:TAIR.
DR GO; GO:0072355; P:histone H3-T3 phosphorylation; IDA:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:TAIR.
DR InterPro; IPR024604; GSG2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR SMART; SM01331; DUF3635; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Chromosome; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..599
FT /note="Serine/threonine-protein kinase haspin homolog"
FT /id="PRO_0000436998"
FT DOMAIN 287..599
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 448
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 293..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 407..412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TF76"
FT BINDING 448..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TF76"
FT BINDING 486..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TF76"
FT MUTAGEN 310
FT /note="K->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:21527018,
FT ECO:0000269|PubMed:21749502"
FT CONFLICT 455
FT /note="L -> P (in Ref. 3; AAO41970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 67930 MW; 2C9D4732C4E243A0 CRC64;
MGQRVDLWSE VIKSEEEDGD IPKIEAVFQR RKKPDKSSEA VNFGWLVKGA RTSSVNGPKR
DSWARSLSTR GRESIAVRAY VNNQPQKKAA GRKKPPIPKG KVVKAPDFQK EKEYFRDIDA
FELLEESPSP NKSSTWTMGE QVVPEMPHLS TRLEKWLISK KLNHTCGPSS TLSKILENSA
IHQESVCDND AFDSLSLKTP DKSSAGNTSV FRLIPSCDEN LAAEDVPVRK IKMESIDLED
ELKRLSLTSD LIPTHQDFDQ PILDLLSACG QMRPSNFIEA FSKFCEPESI VKIGEGTYGE
AFRAGSSVCK IVPIDGDFRV NGEVQKRADE LLEEVILSWT LNQLRECETT AQNLCPTYIK
TQDIKLCQGP YDPILIKAWE EWDAKHGSEN DHPDFPEKQC YVMFVLEHGG KDLESFVLLN
FDEARSLLVQ ATAGLAVAEA AFEFEHRDLH WGNILLSRNN SDTLPFILEG KQVCIKTFGV
QISIIDFTLS RINTGEKILF LDLTSDPYLF KGPKGDKQSE TYRKMKAVTE DYWEGSFART
NVLWLIYLVD ILLTKKSFER SSKHERELRS LKKRMEKYES AKEAVSDPFF SDMLMDQIS
