HASP_BOVIN
ID HASP_BOVIN Reviewed; 781 AA.
AC Q2KIP2;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Serine/threonine-protein kinase haspin;
DE EC=2.7.11.1;
DE AltName: Full=Germ cell-specific gene 2 protein;
GN Name=HASPIN; Synonyms=GSG2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q8TF76}.
CC Chromosome {ECO:0000250|UniProtKB:Q8TF76}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q8TF76}. Note=Nuclear during interphase
CC and associates with the chromosomes and spindle apparatus during
CC mitosis. {ECO:0000250|UniProtKB:Q8TF76}.
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).
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; BC112565; AAI12566.1; -; mRNA.
DR RefSeq; NP_001070012.1; NM_001076544.2.
DR AlphaFoldDB; Q2KIP2; -.
DR SMR; Q2KIP2; -.
DR STRING; 9913.ENSBTAP00000043277; -.
DR PaxDb; Q2KIP2; -.
DR PRIDE; Q2KIP2; -.
DR GeneID; 767819; -.
DR KEGG; bta:767819; -.
DR CTD; 83903; -.
DR eggNOG; KOG2464; Eukaryota.
DR InParanoid; Q2KIP2; -.
DR OrthoDB; 1374355at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0072354; F:histone kinase activity (H3-T3 specific); ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006325; P:chromatin organization; 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:0007064; P:mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISS: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 2: Evidence at transcript 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..781
FT /note="Serine/threonine-protein kinase haspin"
FT /id="PRO_0000413975"
FT DOMAIN 467..781
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 632
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 473..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 589..594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 632..637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 670..672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF76"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF76"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF76"
SQ SEQUENCE 781 AA; 86411 MW; 2CB8FEBBFE2FD6E0 CRC64;
MAASLPLPAS GLFRTYGAAG GGRPRRRQGL AAVQWFPPQD RKRFFSSSSS DTSSGGPSQS
VVSDDPDDPD FPGSPVGQRR RRAGARLAKG RPSQIATPRR LRLRSRCPQK CSTPCGALEP
PSFPNGNPGS LSPDLRVCGQ PRDGGELGTS ASLFSSLASP GPGFPAPEDS ICTDPSTFLD
AASEAPSNFH LPEASLDQAP LPCSQDAATG GGRFTRLAHQ AQASLRSALF SFLDPGNPED
SELGTDGKNL QEFCHDRELV GRRLESPGLS GRGKKRTTDQ DSCREIESQE SVQIEYEEAR
GCKGGIASGK SNGPERTRLS RKRKHQGTAE TSLLHHCQVT KGQKMEDGSC VTQDLTRLQN
ACSWTKTRAS FSFHKKKIVT AVSEVCSCDT LAGSLSESLM SEYSHHPVQN RTSCALSPWH
SSSMYLLTPL KTQQVTDKRT SDAEKLYGEC NQVGPIPFSD YLSEEKLECC EKIGEGVFGE
VFQTVTNHTP VALKIIAIEG QNLVNGAHQK TFEEILPEII ISKELSLLSD EACNRTEGFI
GLNSVHCVQG SYPPLLLQAW DHYHSTKGSA NDRPDFFRED QLFIVLEFEF GGIDLEQMRK
KLSSIATAKS ILHQITASLA VAEASLHFEH RDLHWGNVLL KKTSLKELHY TLNGKKSSIP
TRGLQVNIID YTLSRLERDG IVVFCDISRD EDLFMGQGDY QFEIYRLMRK ENNNCWGEYH
PYNNVLWLHY LTDKILNQMT FKSKHNTPAL KRMKKQIQHF YQTMLNFSSA TDLLCQHSLF
K
