Search by BoMiProt ID - Bomi9047


Primary Information

BoMiProt ID Bomi9047
Protein Name Serine/threonine-protein kinase haspin/Germ cell-specific gene 2 protein
Organism Bos taurus
Uniprot IdQ2KIP2
Milk FractionWhey
Ref Sequence Id NP_001070012.1
Aminoacid Length 781
Molecular Weight 86411
Fasta Sequence https://www.uniprot.org/uniprot/Q2KIP2.fasta
Gene Name HASPIN/GSG2
Gene Id 767819
Protein Existence Status reviewed

Secondary Information

Protein Function is responsible for phosphorylation of histone H3 at threonine 3 (H3T3ph) during mitosis, in mammals and yeast.Also involved in sister chromatid cohesion during mitosis.
Biochemical Properties Mg2+ as cofactor.
PTMs Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q2KIP2|HASP_BOVIN Serine/threonine-protein kinase haspin OS=Bos taurus OX=9913 GN=HASPIN PE=2 SV=1 MAASLPLPASGLFRTYGAAGGGRPRRRQGLAAVQWFPPQDRKRFFSSSSSDTSSGGPS*58QS VVSDDPDDPDFPGSPVGQRRRRAGARLAKGRPS*93QIATPRRLRLRSRCPQKCSTPCGALEP PSFPNGNPGSLS*132PDLRVCGQPRDGGELGTSASLFSSLASPGPGFPAPEDSICTDPSTFLD AASEAPSNFHLPEASLDQAPLPCSQDAATGGGRFTRLAHQAQASLRSALFSFLDPGNPED SELGTDGKNLQEFCHDRELVGRRLESPGLSGRGKKRTTDQDSCREIESQESVQIEYEEAR GCKGGIASGKSNGPERTRLSRKRKHQGTAETSLLHHCQVTKGQKMEDGSCVTQDLTRLQN ACSWTKTRASFSFHKKKIVTAVSEVCSCDTLAGSLSESLMSEYSHHPVQNRTSCALSPWH SSSMYLLTPLKTQQVTDKRTSDAEKLYGECNQVGPIPFSDYLSEEKLECCEKIGEGVFGE VFQTVTNHTPVALKIIAIEGQNLVNGAHQKTFEEILPEIIISKELSLLSDEACNRTEGFI GLNSVHCVQGSYPPLLLQAWDHYHSTKGSANDRPDFFREDQLFIVLEFEFGGIDLEQMRK KLSSIATAKSILHQITASLAVAEASLHFEHRDLHWGNVLLKKTSLKELHYTLNGKKSSIP TRGLQVNIIDYTLSRLERDGIVVFCDISRDEDLFMGQGDYQFEIYRLMRKENNNCWGEYH PYNNVLWLHYLTDKILNQMTFKSKHNTPALKRMKKQIQHFYQTMLNFSSATDLLCQHSLF K
Predicted Disorder Regions 39-95, 110-115, 143-210, 238-242, 265-289, 310-333
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Autophosphorylated on both serine and threonine residues which is imp for cell cycle regulation.Approx 30 mitotic phosphorylation sites in the N-terminal domain of human haspin have been identified.Phosphorylation by AURKB is required for full activity toward histone H3 at 'Ser-3' in mitosis.Phosphorylation of haspin on its N-domain may alter the access of haspin to its substrates, or might regulate the interaction of haspin with putative regulatory proteins that control its activity in cells.
Bibliography 1.Fresán U, Rodríguez-Sánchez MA, Reina O, Corces VG, Espinàs ML. Haspin kinase modulates nuclear architecture and Polycomb-dependent gene silencing. PLoS Genet. 2020 Aug 4;16(8):e1008962. doi: 10.1371/journal.pgen.1008962. PMID: 32750047; PMCID: PMC7428214. 2.Higgins JM. Haspin: a newly discovered regulator of mitotic chromosome behavior. Chromosoma. 2010 Apr;119(2):137-47. doi: 10.1007/s00412-009-0250-4. Epub 2009 Dec 8. PMID: 19997740; PMCID: PMC2839057.