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 27-MAR-2024, entry version 165. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000055806; -. DR ProteomicsDB; 269811; -. DR Pumba; Q9Z0R0; -. DR DNASU; 14841; -. DR GeneID; 14841; -. DR KEGG; mmu:14841; -. DR UCSC; uc007jzz.2; mouse. DR AGR; MGI:1194498; -. DR CTD; 83903; -. DR MGI; MGI:1194498; Haspin. DR eggNOG; KOG2464; Eukaryota. DR InParanoid; Q9Z0R0; -. DR OrthoDB; 5491350at2759; -. DR PhylomeDB; Q9Z0R0; -. DR TreeFam; TF313895; -. DR BioGRID-ORCS; 14841; 2 hits in 85 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:0072354; F:histone H3T3 kinase activity; ISS:UniProtKB. DR GO; GO:0035173; F:histone kinase activity; IMP:MGI. 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:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:MGI. DR GO; GO:0010467; P:gene expression; IMP: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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1. DR PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1. DR Pfam; PF12330; Haspin_kinase; 1. DR SMART; SM01331; DUF3635; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //