HASP_MOUSE
ID HASP_MOUSE Reviewed; 754 AA.
AC Q9Z0R0; Q99MU9; Q9JJJ4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase haspin;
DE EC=2.7.11.1;
DE AltName: Full=Germ cell-specific gene 2 protein;
DE AltName: Full=Haploid germ cell-specific nuclear protein kinase;
GN Name=Haspin; Synonyms=Gsg2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAA75494.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:7957958};
RC TISSUE=Testis {ECO:0000312|EMBL:BAA75494.1};
RX PubMed=7957958; DOI=10.1016/0014-5793(94)01155-9;
RA Tanaka H., Yoshimura Y., Nishina Y., Nozaki M., Nojima H., Nishimune Y.;
RT "Isolation and characterization of cDNA clones specifically expressed in
RT testicular germ cells.";
RL FEBS Lett. 355:4-10(1994).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:10358056};
RC TISSUE=Testis {ECO:0000312|EMBL:BAA75494.1};
RX PubMed=10358056; DOI=10.1074/jbc.274.24.17049;
RA Tanaka H., Yoshimura Y., Nozaki M., Yomogida K., Tsuchida J., Tosaka Y.,
RA Habu T., Nakanishi T., Okada M., Nojima H., Nishimune Y.;
RT "Identification and characterization of a haploid germ cell-specific
RT nuclear protein kinase (Haspin) in spermatid nuclei and its effects on
RT somatic cells.";
RL J. Biol. Chem. 274:17049-17057(1999).
RN [3] {ECO:0000312|EMBL:BAB00640.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11311555; DOI=10.1016/s0378-1119(01)00386-9;
RA Yoshimura Y., Tanaka H., Nozaki M., Yomogida K., Yasunaga T., Nishimune Y.;
RT "Nested genomic structure of haploid germ cell specific haspin gene.";
RL Gene 267:49-54(2001).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv {ECO:0000312|EMBL:AAK30301.1};
RX PubMed=11311556; DOI=10.1016/s0378-1119(01)00387-0;
RA Higgins J.M.G.;
RT "The Haspin gene: location in an intron of the Integrin Alpha-E gene,
RT associated transcription of an Integrin alpha-E-derived RNA and expression
RT in diploid as well as haploid cells.";
RL Gene 267:55-69(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP FUNCTION.
RX PubMed=15681610; DOI=10.1101/gad.1267105;
RA Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
RT "The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation
RT and normal metaphase chromosome alignment.";
RL Genes Dev. 19:472-488(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase that phosphorylates histone
CC H3 at 'Thr-3' (H3T3ph) during mitosis. May act through H3T3ph to both
CC position and modulate activation of AURKB and other components of the
CC chromosomal passenger complex (CPC) at centromeres to ensure proper
CC chromatid cohesion, metaphase alignment and normal progression through
CC the cell cycle. {ECO:0000250|UniProtKB:Q8TF76}.
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:0000250|UniProtKB:Q8TF76};
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:0000250|UniProtKB:Q8TF76};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8TF76};
CC -!- ACTIVITY REGULATION: Constitutive activity that does not require
CC phosphorylation. Specifically inhibited by 3-(1H-indazol-5-yl)-N-
CC propylimidazo[1,2-b]pyridazin-6-amine (CHR-6494).
CC {ECO:0000250|UniProtKB:Q8TF76}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10358056}. Chromosome
CC {ECO:0000250|UniProtKB:Q8TF76}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q8TF76}. Note=Nuclear during interphase and
CC associates with the chromosomes and spindle apparatus during mitosis.
CC {ECO:0000250|UniProtKB:Q8TF76}.
CC -!- TISSUE SPECIFICITY: Expressed in germ cells within the testis of adults
CC and of embryos from day 24 onwards. Also present in adult thymus and
CC weakly expressed in spleen, lung and whole embryo.
CC {ECO:0000269|PubMed:10358056, ECO:0000269|PubMed:11311556,
CC ECO:0000269|PubMed:7957958}.
CC -!- PTM: Autophosphorylated on both serine and threonine residues (By
CC similarity). Strongly phosphorylated during mitosis but this does not
CC appear to significantly affect its intrinsic kinase activity.
CC Phosphorylation by AURKB is required for full activity toward histone
CC H3 at 'Ser-3' in mitosis (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8TF76}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Haspin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; D87326; BAA75494.1; -; mRNA.
DR EMBL; AB036930; BAB00640.1; -; Genomic_DNA.
DR EMBL; AF289866; AAK30301.1; -; Genomic_DNA.
DR EMBL; AL670399; CAI24789.1; -; Genomic_DNA.
DR CCDS; CCDS24997.1; -.
DR RefSeq; NP_034483.1; NM_010353.2.
DR AlphaFoldDB; Q9Z0R0; -.
DR SMR; Q9Z0R0; -.
DR BioGRID; 200084; 1.
DR IntAct; Q9Z0R0; 1.
DR MINT; Q9Z0R0; -.
DR STRING; 10090.ENSMUSP00000055806; -.
DR iPTMnet; Q9Z0R0; -.
DR PhosphoSitePlus; Q9Z0R0; -.
DR EPD; Q9Z0R0; -.
DR jPOST; Q9Z0R0; -.
DR MaxQB; Q9Z0R0; -.
DR PaxDb; Q9Z0R0; -.
DR PRIDE; Q9Z0R0; -.
DR ProteomicsDB; 269811; -.
DR DNASU; 14841; -.
DR GeneID; 14841; -.
DR KEGG; mmu:14841; -.
DR UCSC; uc007jzz.2; mouse.
DR CTD; 83903; -.
DR MGI; MGI:1194498; Haspin.
DR eggNOG; KOG2464; Eukaryota.
DR InParanoid; Q9Z0R0; -.
DR OrthoDB; 1374355at2759; -.
DR PhylomeDB; Q9Z0R0; -.
DR TreeFam; TF313895; -.
DR BioGRID-ORCS; 14841; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Haspin; mouse.
DR PRO; PR:Q9Z0R0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z0R0; protein.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0035173; F:histone kinase activity; IMP:MGI.
DR GO; GO:0072354; F:histone kinase activity (H3-T3 specific); ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:2000751; P:histone H3-T3 phosphorylation involved in chromosome passenger complex localization to kinetochore; ISO:MGI.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR InterPro; IPR024604; GSG2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR SMART; SM01331; DUF3635; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Chromatin regulator; Chromosome; Cytoplasm;
KW Cytoskeleton; Kinase; Magnesium; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..754
FT /note="Serine/threonine-protein kinase haspin"
FT /id="PRO_0000085990"
FT DOMAIN 440..754
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 605
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 446..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24941,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24941,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 562..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 605..610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 643..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF76"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 104
FT /note="P -> L (in Ref. 1; BAA75494 and 5; CAI24789)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="Q -> R (in Ref. 2; BAB00640 and 4; AAK30301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 84181 MW; 4D093D7C95E65308 CRC64;
MAQAHPRSGT RLFRTYAARG VRGSQRQPGG LAEQWFQPPN LKRAFSSSLS DSNESPAVAS
DDPDDPDFPG SLVGQRRRRP RGSGSRNQRT LTNTPRVQRL RPRPPQKCST PCSRLRPPPF
PNCSPGCLGS DHSVCIQSRD SNELGTSASL FSSPASPGAP DPLYADSAVP GSFHLPAASL
SEPSVPCPQV AATGDRYTGR ALRAEASFRS SLFSLVNSGA TEENKFGTDG ENVKESCCER
RQQMGNRLTD PDLTSPGKRK AACKKVVSQG VDQRDYEESS ACKDLRVPGE ISRPKRTGPL
RKRKQQEATG TPPRHYHQSK KKRKASVSLW NLNTSQRDSW TKTRASFGFH KKKIITSVIE
VCSSVASSSS RSLLSECSTP PIKNRAHLTV SSRCSSVYLL SPLKTLHVTD QRPSYAEKVY
GECNQEGPIP FSDCLSTEKL ERCEKIGEGV FGEVFQIIND QAPVALKIIA IEGLDLVNGS
HQKTFEEILP EIIISKELSL LSSEAYNRTE GFIGLNSVHC VQGLYPPLLL KAWDHYNTTK
RSANDRPDFF QEDQLFIILE FEFGGVDLER MKTKLSSVAT AKSILHQITA SLAVAEASLH
FEHRDLHWGN VLLKKTNLKE LRYTLNGKTS TIPTHGLQVN IIDYTLSRLE RDGIVVFCDI
SAEEDLFTGE GDYQFEIYRL MRKENKNCWG EYHPYNNVLW LHYLTDKILN KMKFKTKCQS
AAMKQIRKNL QHFHRTVLSF SSATDLLCQH SLFR
