Reviewed, UniProtKB/Swiss-Prot Q8TF76 (HASP_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase haspin
    EC=2.7.11.1
Alternative name(s):
    Haploid germ cell-specific nuclear protein kinase
    H-haspin
    Germ cell-specific gene 2 protein

Gene names

Name:

GSG2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for normal alignment of chromosomes at metaphase. Phosphorylates histone H3 'Thr-3' during mitosis. Ref.1 Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium. Ref.1
Subcellular location	Nucleus. Ref.1 Ref.6
Tissue specificity	Strongly expressed in testis. Also present in thymus and bone marrow and low levels observed in prostate, intestine, lung, spleen and lymph node. Expressed in fetal skin, liver, kidney and small intestine and also in proliferating but not non-proliferating cell lines. Ref.1 Ref.3
Post-translational modification	Autophosphorylated on both serine and threonine residues By similarity. Phosphorylated during mitosis. Phosphorylated upon DNA damage, probably by ATM or ATR. UniProtKB Q9Z0R0
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Haspin subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Ref.1 Inferred from direct assay. Source: UniProtKB protein kinase cascade Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	nucleus Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Ref.1 Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 Ref.3 (identifier: Q8TF76-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 Ref.4 (identifier: Q8TF76-2)

The sequence of this isoform differs from the canonical sequence as follows:
     314-314: Q → H
     315-798: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 798	798	Serine/threonine-protein kinase haspin		PRO_0000085989
Regions
	Domain	484 – 798	315	Protein kinase
	Nucleotide binding	490 – 498	9	ATP By similarity UniProtKB P24941
Sites
	Active site	649	1	Proton acceptor By similarity UniProtKB P24941
	Binding site	511	1	ATP By similarity UniProtKB P24941
Amino acid modifications
	Modified residue	93	1	Phosphoserine Ref.9
	Modified residue	97	1	Phosphothreonine Ref.9
	Modified residue	143	1	Phosphoserine Ref.9
	Modified residue	147	1	Phosphoserine Ref.9
	Modified residue	220	1	Phosphoserine Ref.8
	Modified residue	253	1	Phosphothreonine Ref.7
Natural variations
	Alternative sequence	314	1	Q → H in isoform 2. Ref.4		VSP_050671
	Alternative sequence	315 – 798	484	Missing in isoform 2. Ref.4		VSP_050672
	Natural variant	76	1	V → E Ref.10		VAR_040540
	Natural variant	82	1	C → R Ref.1 Ref.10		VAR_040541
	Natural variant	145	1	R → H Ref.10		VAR_040542
	Natural variant	204	1	D → G: dbSNP rs220462. Ref.1 Ref.10 Ref.4		VAR_027405
	Natural variant	283	1	G → S Ref.10		VAR_040543
	Natural variant	301	1	Q → L Ref.10		VAR_040544
	Natural variant	328	1	T → I: dbSNP rs220461. Ref.1 Ref.10		VAR_027406
	Natural variant	378	1	A → V: dbSNP rs3809806. Ref.1 Ref.10		VAR_027407
	Natural variant	422	1	N → D: dbSNP rs7223226.		VAR_027408
	Natural variant	706	1	M → V Ref.10		VAR_040545
Experimental info
	Sequence conflict	273	1	R → S in BAB71255. Ref.4
	Sequence conflict	339	1	K → E in AAH47457. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 16, 2004. Version 2. Checksum: 0F6D2A3BAABE0CB0	FASTA	798	88,460
	10 20 30 40 50 60 MAASLPGPGS RLFRTYGAAD GRRQRRPGRE AAQWFPPQDR RRFFNSSGSS DASIGDPSQS 70 80 90 100 110 120 DDPDDPDDPD FPGSPVRRRR RCPGGRVPKD RPSLTVTPKR WKLRARPSLT VTPRRLGLRA 130 140 150 160 170 180 RPPQKCSTPC GPLRLPPFPS RDSGRLSPDL SVCGQPRDGD ELGISASLFS SLASPCPGSP 190 200 210 220 230 240 TPRDSVISIG TSACLVAASA VPSDLHLPEV SLDRASLPCS QEEATGGAKD TRMVHQTRAS 250 260 270 280 290 300 LRSVLFGLMN SGTPEDSEFR ADGKNMRESC CKRKLVVGNG PEGPGLSSTG KRRATGQDSC 310 320 330 340 350 360 QERGLQEAVR REHQEASVPK GRIVPRGTDR LERTRSSRKS KHQEATETSL LHSHRFKKGQ 370 380 390 400 410 420 KLGKDSFPTQ DLTPLQNACF WTKTRASFSF HKKKIVTDVS EVCSIYTTAT SLSGSLLSEC 430 440 450 460 470 480 SNRPVMNRTS GAPSSWHSSS MYLLSPLNTL SISNKKASDA EKVYGECSQK GPVPFSHCLP 490 500 510 520 530 540 TEKLQRCEKI GEGVFGEVFQ TIADHTPVAI KIIAIEGPDL VNGSHQKTFE EILPEIIISK 550 560 570 580 590 600 ELSLLSGEVC NRTEGFIGLN SVHCVQGSYP PLLLKAWDHY NSTKGSANDR PDFFKDDQLF 610 620 630 640 650 660 IVLEFEFGGI DLEQMRTKLS SLATAKSILH QLTASLAVAE ASLRFEHRDL HWGNVLLKKT 670 680 690 700 710 720 SLKKLHYTLN GKSSTIPSCG LQVSIIDYTL SRLERDGIVV FCDVSMDEDL FTGDGDYQFD 730 740 750 760 770 780 IYRLMKKENN NRWGEYHPYS NVLWLHYLTD KMLKQMTFKT KCNTPAMKQI KRKIQEFHRT 790 MLNFSSATDL LCQHSLFK
	Isoform 2. Checksum: 11B033493433A620	FASTA	314	33,855
	10 20 30 40 50 60 MAASLPGPGS RLFRTYGAAD GRRQRRPGRE AAQWFPPQDR RRFFNSSGSS DASIGDPSQS 70 80 90 100 110 120 DDPDDPDDPD FPGSPVRRRR RCPGGRVPKD RPSLTVTPKR WKLRARPSLT VTPRRLGLRA 130 140 150 160 170 180 RPPQKCSTPC GPLRLPPFPS RDSGRLSPDL SVCGQPRDGD ELGISASLFS SLASPCPGSP 190 200 210 220 230 240 TPRDSVISIG TSACLVAASA VPSDLHLPEV SLDRASLPCS QEEATGGAKD TRMVHQTRAS 250 260 270 280 290 300 LRSVLFGLMN SGTPEDSEFR ADGKNMRESC CKRKLVVGNG PEGPGLSSTG KRRATGQDSC 310 QERGLQEAVR REHH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of human haspin gene encoding haploid germ cell-specific nuclear protein kinase." Tanaka H., Iguchi N., Nakamura Y., Kohroki J., de Carvalho C.E., Nishimune Y. Mol. Hum. Reprod. 7:211-218(2001) [PubMed: 11228240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHROMOSOMAL LOCATION, VARIANTS ARG-82; GLY-204; ILE-328 AND VAL-378. Tissue: Testis.
[2]	Tanaka H. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 204; 328 AND 378.
[3]	"The Haspin gene: location in an intron of the Integrin Alpha-E gene, associated transcription of an Integrin alpha-E-derived RNA and expression in diploid as well as haploid cells." Higgins J.M.G. Gene 267:55-69(2001) [PubMed: 11311556] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Testis.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLY-204. Tissue: Peripheral blood.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[6]	"The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment." Dai J., Sultan S., Taylor S.S., Higgins J.M.G. Genes Dev. 19:472-488(2005) [PubMed: 15681610] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[7]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-253, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, MASS SPECTROMETRY.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; THR-97; SER-143 AND SER-147, MASS SPECTROMETRY.
[10]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-76; ARG-82; HIS-145; GLY-204; SER-283; LEU-301; ILE-328; VAL-378 AND VAL-706.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB039834 mRNA. Translation: BAB21938.3.
AF289865 mRNA. Translation: AAK30300.1.
AK056691 mRNA. Translation: BAB71255.1.
BC047457 mRNA. Translation: AAH47457.1.

IPI

IPI00397836.
IPI00401554.

UniGene

Hs.534059

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VUW	X-ray	1.80	A	465-798	[»]
3DLZ	X-ray	1.85	A	465-798	[»]
3E7V	X-ray	2.00	A	465-798	[»]
3F2N	X-ray	1.80	A	465-798	[»]
3FMD	X-ray	2.00	A	465-798	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q8TF76.

Proteomic databases

PRIDE

Q8TF76.

Genome annotation databases

Ensembl

ENSG00000177602. Homo sapiens. [Contig view]

Organism-specific databases

GeneCards

GC17P003573.

H-InvDB

HIX0013433.

HGNC

HGNC:19682. GSG2.

MIM

609240. gene.

PharmGKB

PA134909705.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q8TF76.

HOVERGEN

Q8TF76.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Gene expression databases

ArrayExpress

Q8TF76.

Bgee

Q8TF76.

CleanEx

HS_GSG2.

GermOnline

ENSG00000177602. Homo sapiens.

Family and domain databases

InterPro

IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser_thr_pkin_AS.
IPR001245. Tyr_pkinase.
[Graphical view]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

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Other Resources

SOURCE

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Entry information

Entry name

HASP_HUMAN

Accession

Primary (citable) accession number: Q8TF76
Secondary accession number(s): Q5U5K3, Q96MN1, Q9BXS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	February 16, 2004
Last modified:	May 26, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)