Q8TF76 (HASP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase haspin
EC=2.7.11.1

Alternative name(s):
Germ cell-specific gene 2 protein
H-haspin
Haploid germ cell-specific nuclear protein kinase

Gene names

Name:

GSG2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase that phosphorylates histone H3 at 'Ser-3' (H3T3ph) during mitosis. This positions and activates AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle. Ref.1 Ref.7 Ref.8 Ref.11 Ref.12
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.15 Ref.16
Cofactor	Magnesium. Ref.1 Ref.15
Enzyme regulation	Constitutive activity that does not require phosphorylation. Specifically inhibited by 3-(1H-indazol-5-yl)-N-propylimidazo[1,2-b]pyridazin-6-amine (CHR-6494). Ref.13 Ref.14 Ref.15
Subcellular location	Nucleus. Chromosome. Cytoplasm › cytoskeleton › spindle. Note: Nuclear during interphase and associates with the chromosomes and spindle apparatus during mitosis. Ref.1 Ref.7
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. Strongly phosphorylated during mitosis but this does not appear to significantly affect its intrinsic kinase activity. Phosphorylation by AURKB is required for full activity toward histone H3 at 'Ser-3' in mitosis. Ref.7 Ref.13 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	Chromosome Cytoplasm Cytoskeleton 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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3-T3 phosphorylation involved in chromosome passenger complex localization to kinetochore Inferred from mutant phenotype PubMed 23071153. Source: UniProtKB intracellular protein kinase cascade Inferred from direct assay Ref.1. Source: UniProtKB mitotic sister chromatid cohesion Inferred from mutant phenotype Ref.11. Source: UniProtKB protein localization to chromosome, centromeric region Inferred from mutant phenotype Ref.11. Source: UniProtKB regulation of spindle checkpoint Inferred from mutant phenotype Ref.11. Source: UniProtKB
Cellular_component	centrosome Inferred from direct assay Ref.1. Source: UniProtKB chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay. Source: HPA nuclear membrane Inferred from direct assay. Source: HPA spindle Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.1. Source: UniProtKB DNA binding Inferred from electronic annotation. Source: Compara histone kinase activity (H3-T3 specific) Inferred from mutant phenotype Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-1237328,EBI-352572

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

Nucleotide binding

606 – 611

6

ATP

Nucleotide binding

649 – 654

6

ATP

Nucleotide binding

687 – 689

3

ATP

Sites

Active site

649

1

Proton acceptor By similarity UniProtKB P24941

Binding site

511

1

ATP UniProtKB P24941

Amino acid modifications

Modified residue

58

1

Phosphoserine Ref.10

Modified residue

93

1

Phosphoserine; by AURKB Ref.9 Ref.13

Modified residue

97

1

Phosphothreonine Ref.9

Modified residue

143

1

Phosphoserine; by AURKB Ref.13

Modified residue

147

1

Phosphoserine Ref.9

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.17
Corresponds to variant rs11653889 [ dbSNP | Ensembl ].

VAR_040540

Natural variant

82

1

R → C. Ref.3 Ref.4 Ref.6 Ref.17
Corresponds to variant rs9907144 [ dbSNP | Ensembl ].

VAR_040541

Natural variant

145

1

R → H. Ref.17
Corresponds to variant rs55991903 [ dbSNP | Ensembl ].

VAR_040542

Natural variant

204

1

G → D. Ref.3 Ref.6 Ref.17
Corresponds to variant rs220462 [ dbSNP | Ensembl ].

VAR_027405

Natural variant

283

1

G → S. Ref.17
Corresponds to variant rs56224301 [ dbSNP | Ensembl ].

VAR_040543

Natural variant

301

1

Q → L. Ref.17
Corresponds to variant rs55649477 [ dbSNP | Ensembl ].

VAR_040544

Natural variant

328

1

I → T. Ref.3 Ref.6 Ref.17
Corresponds to variant rs220461 [ dbSNP | Ensembl ].

VAR_027406

Natural variant

378

1

V → A. Ref.3 Ref.6 Ref.17
Corresponds to variant rs3809806 [ dbSNP | Ensembl ].

VAR_027407

Natural variant

422

1

N → D.
Corresponds to variant rs7223226 [ dbSNP | Ensembl ].

VAR_027408

Natural variant

706

1

M → V. Ref.17
Corresponds to variant rs56134695 [ dbSNP | Ensembl ].

VAR_040545

Experimental info

Mutagenesis

492

1

E → A: Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation. Ref.16

Mutagenesis

511

1

K → A: Strongly reduced enzyme activity. Ref.15

Mutagenesis

651

1

H → A: Strongly reduced enzyme activity, markedly reduced affinity for histone H3. Ref.15 Ref.16

Mutagenesis

707

1

D → L: Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation. Ref.16

Mutagenesis

709

1

D → N: Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation. Ref.16

Mutagenesis

713

1

G → F: Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation. Ref.16

Mutagenesis

716

1

D → L: Markedly reduced histone H3 phosphorylation. Ref.16

Sequence conflict

273

1

R → S in BAB71255. Ref.4

Sequence conflict

339

1

K → E in AAH47457. Ref.6

Secondary structure

1

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798

Helix Strand Turn

Details...

Helix

452 – 466

15

Helix

475 – 478

4

Helix

481 – 485

5

Beta strand

488 – 493

6

Beta strand

496 – 503

8

Beta strand

506 – 516

11

Helix

529 – 544

16

Helix

545 – 547

3

Beta strand

549 – 552

4

Beta strand

554 – 556

3

Beta strand

559 – 568

10

Helix

571 – 583

13

Beta strand

599 – 606

8

Helix

613 – 615

3

Turn

616 – 618

3

Helix

622 – 643

22

Helix

652 – 654

3

Beta strand

655 – 659

5

Beta strand

663 – 669

7

Beta strand

672 – 677

6

Beta strand

681 – 685

5

Beta strand

692 – 695

4

Beta strand

698 – 700

3

Helix

709 – 711

3

Helix

717 – 729

13

Helix

739 – 754

16

Beta strand

758 – 760

3

Helix

765 – 780

16

Helix

781 – 783

3

Beta strand

784 – 786

3

Helix

787 – 793

7

Helix

795 – 797

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: E0EDF8F0C58ADA31	FASTA	798	88,495
	10 20 30 40 50 60 MAASLPGPGS RLFRTYGAAD GRRQRRPGRE AAQWFPPQDR RRFFNSSGSS DASIGDPSQS 70 80 90 100 110 120 DDPDDPDDPD FPGSPVRRRR RRPGGRVPKD RPSLTVTPKR WKLRARPSLT VTPRRLGLRA 130 140 150 160 170 180 RPPQKCSTPC GPLRLPPFPS RDSGRLSPDL SVCGQPRDGD ELGISASLFS SLASPCPGSP 190 200 210 220 230 240 TPRDSVISIG TSACLVAASA VPSGLHLPEV SLDRASLPCS QEEATGGAKD TRMVHQTRAS 250 260 270 280 290 300 LRSVLFGLMN SGTPEDSEFR ADGKNMRESC CKRKLVVGNG PEGPGLSSTG KRRATGQDSC 310 320 330 340 350 360 QERGLQEAVR REHQEASVPK GRIVPRGIDR LERTRSSRKS KHQEATETSL LHSHRFKKGQ 370 380 390 400 410 420 KLGKDSFPTQ DLTPLQNVCF 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 [UniParc]. Checksum: 7F8CC086036ED24E	FASTA	314	33,850
	10 20 30 40 50 60 MAASLPGPGS RLFRTYGAAD GRRQRRPGRE AAQWFPPQDR RRFFNSSGSS DASIGDPSQS 70 80 90 100 110 120 DDPDDPDDPD FPGSPVRRRR RRPGGRVPKD RPSLTVTPKR WKLRARPSLT VTPRRLGLRA 130 140 150 160 170 180 RPPQKCSTPC GPLRLPPFPS RDSGRLSPDL SVCGQPRDGD ELGISASLFS SLASPCPGSP 190 200 210 220 230 240 TPRDSVISIG TSACLVAASA VPSGLHLPEV 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHROMOSOMAL LOCATION. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS CYS-82; ASP-204; THR-328 AND ALA-378. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT CYS-82. Tissue: Peripheral blood.
[5]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS CYS-82; ASP-204; THR-328 AND ALA-378. Tissue: Testis.
[7]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[8]	"Regulation of mitotic chromosome cohesion by Haspin and Aurora B." Dai J., Sullivan B.A., Higgins J.M. Dev. Cell 11:741-750(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CHROMOSOME COHESION.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; THR-97 AND SER-147, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Histone H3 Thr-3 phosphorylation by Haspin positions Aurora B at centromeres in mitosis." Wang F., Dai J., Daum J.R., Niedzialkowska E., Banerjee B., Stukenberg P.T., Gorbsky G.J., Higgins J.M. Science 330:231-235(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Two histone marks establish the inner centromere and chromosome bi-orientation." Yamagishi Y., Honda T., Tanno Y., Watanabe Y. Science 330:239-243(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"A positive feedback loop involving Haspin and Aurora B promotes CPC accumulation at centromeres in mitosis." Wang F., Ulyanova N.P., van der Waal M.S., Patnaik D., Lens S.M., Higgins J.M. Curr. Biol. 21:1061-1069(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-93 AND SER-143 BY AURKB, ENZYME REGULATION, MASS SPECTROMETRY.
[14]	"Antitumor activity of a small-molecule inhibitor of the histone kinase Haspin." Huertas D., Soler M., Moreto J., Villanueva A., Martinez A., Vidal A., Charlton M., Moffat D., Patel S., McDermott J., Owen J., Brotherton D., Krige D., Cuthill S., Esteller M. Oncogene 31:1408-1418(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[15]	"Structure and functional characterization of the atypical human kinase haspin." Eswaran J., Patnaik D., Filippakopoulos P., Wang F., Stein R.L., Murray J.W., Higgins J.M., Knapp S. Proc. Natl. Acad. Sci. U.S.A. 106:20198-20203(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 465-798 IN COMPLEX WITH AMP AND INHIBITOR IODOTUBERCIDIN, COFACTOR, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF LYS-511 AND HIS-651.
[16]	"Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization." Villa F., Capasso P., Tortorici M., Forneris F., de Marco A., Mattevi A., Musacchio A. Proc. Natl. Acad. Sci. U.S.A. 106:20204-20209(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 452-798, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-492; HIS-651; ASP-707; ASP-709; GLY-713 AND ASP-716.
[17]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-76; CYS-82; HIS-145; ASP-204; SER-283; LEU-301; THR-328; ALA-378 AND VAL-706.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB039834 mRNA. Translation: BAB21938.3.
AF289865 mRNA. Translation: AAK30300.1.
AK056691 mRNA. Translation: BAB71255.1.
AC116914 Genomic DNA. No translation available.
BC047457 mRNA. Translation: AAH47457.1.

IPI

IPI00397836.
IPI00401554.

RefSeq

NP_114171.2. NM_031965.2.

UniGene

Hs.534059.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VUW	X-ray	1.80	A	465-798	[»]
2WB8	X-ray	2.15	A	452-798	[»]
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	[»]
3IQ7	X-ray	2.00	A	465-798	[»]

ProteinModelPortal

Q8TF76.

SMR

Q8TF76. Positions 470-798.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38174N.

IntAct

Q8TF76. 2 interactions.

STRING

9606.ENSP00000325290.

PTM databases

PhosphoSite

Q8TF76.

Polymorphism databases

DMDM

296439330.

Proteomic databases

PaxDb

Q8TF76.

PRIDE

Q8TF76.

Protocols and materials databases

DNASU

83903.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325418; ENSP00000325290; ENSG00000177602.

GeneID

83903.

KEGG

hsa:83903.

UCSC

uc002fwp.3. human.

Organism-specific databases

CTD

83903.

GeneCards

GC17P003627.

H-InvDB

HIX0013433.

HGNC

HGNC:19682. GSG2.

HPA

HPA027422.

MIM

609240. gene.

neXtProt

NX_Q8TF76.

PharmGKB

PA134909705.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5072.

HOGENOM

HOG000168256.

HOVERGEN

HBG049009.

InParanoid

Q8TF76.

KO

K16315.

OMA

ASFSFHK.

OrthoDB

EOG4548Z0.

PhylomeDB

Q8TF76.

Gene expression databases

Bgee

Q8TF76.

CleanEx

HS_GSG2.

Genevestigator

Q8TF76.

GermOnline

ENSG00000177602. Homo sapiens.

Family and domain databases

InterPro

IPR024604. DUF3635.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]

Pfam

PF12330. DUF3635. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

BindingDB

Q8TF76.

ChEMBL

CHEMBL1075163.

EvolutionaryTrace

Q8TF76.

GenomeRNAi

83903.

NextBio

73035.

SOURCE

Search...

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:	May 18, 2010
Last modified:	May 1, 2013
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.