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Protein

Serine/threonine-protein kinase haspin

Gene

GSG2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+2 Publications

Enzyme regulationi

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).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei511 – 5111ATP
Active sitei649 – 6491Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi490 – 4989ATPPROSITE-ProRule annotationBy similarity
Nucleotide bindingi606 – 6116ATP
Nucleotide bindingi649 – 6546ATP
Nucleotide bindingi687 – 6893ATP

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • histone kinase activity (H3-T3 specific) Source: UniProtKB
  • protein kinase activity Source: UniProtKB

GO - Biological processi

  • histone H3-T3 phosphorylation involved in chromosome passenger complex localization to kinetochore Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • mitotic sister chromatid cohesion Source: UniProtKB
  • protein localization to chromosome, centromeric region Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of spindle checkpoint Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ8TF76.

Names & Taxonomyi

Protein namesi
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 namesi
Name:GSG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:19682. GSG2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • chromosome Source: UniProtKB-SubCell
  • cytoplasm Source: GO_Central
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi492 – 4921E → A: Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation. 1 Publication
Mutagenesisi511 – 5111K → A: Strongly reduced enzyme activity. 1 Publication
Mutagenesisi651 – 6511H → A: Strongly reduced enzyme activity, markedly reduced affinity for histone H3. 2 Publications
Mutagenesisi707 – 7071D → L: Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation. 1 Publication
Mutagenesisi709 – 7091D → N: Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation. 1 Publication
Mutagenesisi713 – 7131G → F: Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation. 1 Publication
Mutagenesisi716 – 7161D → L: Markedly reduced histone H3 phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA134909705.

Chemistry

ChEMBLiCHEMBL1075163.
GuidetoPHARMACOLOGYi2028.

Polymorphism and mutation databases

BioMutaiGSG2.
DMDMi296439330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 798798Serine/threonine-protein kinase haspinPRO_0000085989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei93 – 931Phosphoserine; by AURKBCombined sources1 Publication
Modified residuei97 – 971PhosphothreonineCombined sources
Modified residuei143 – 1431Phosphoserine; by AURKB1 Publication
Modified residuei147 – 1471PhosphoserineCombined sources

Post-translational modificationi

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.By similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8TF76.
MaxQBiQ8TF76.
PaxDbiQ8TF76.
PeptideAtlasiQ8TF76.
PRIDEiQ8TF76.

PTM databases

iPTMnetiQ8TF76.
PhosphoSiteiQ8TF76.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ8TF76.
CleanExiHS_GSG2.
GenevisibleiQ8TF76. HS.

Organism-specific databases

HPAiHPA027422.
HPA030698.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-1237328,EBI-352572

Protein-protein interaction databases

BioGridi123814. 22 interactions.
DIPiDIP-38174N.
IntActiQ8TF76. 9 interactions.
MINTiMINT-4774775.
STRINGi9606.ENSP00000325290.

Chemistry

BindingDBiQ8TF76.

Structurei

Secondary structure

1
798
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi452 – 46615Combined sources
Helixi475 – 4784Combined sources
Helixi481 – 4855Combined sources
Beta strandi488 – 4936Combined sources
Beta strandi496 – 5038Combined sources
Beta strandi506 – 51611Combined sources
Beta strandi518 – 5214Combined sources
Helixi529 – 54416Combined sources
Helixi545 – 5473Combined sources
Beta strandi549 – 5524Combined sources
Beta strandi554 – 5563Combined sources
Beta strandi559 – 56810Combined sources
Helixi571 – 58313Combined sources
Beta strandi599 – 6068Combined sources
Turni612 – 6187Combined sources
Helixi622 – 64322Combined sources
Helixi652 – 6543Combined sources
Beta strandi655 – 6595Combined sources
Beta strandi663 – 6697Combined sources
Beta strandi672 – 6776Combined sources
Beta strandi681 – 6855Combined sources
Beta strandi692 – 6954Combined sources
Beta strandi698 – 7003Combined sources
Helixi709 – 7113Combined sources
Helixi717 – 72913Combined sources
Helixi739 – 75416Combined sources
Beta strandi758 – 7603Combined sources
Helixi765 – 78016Combined sources
Helixi781 – 7833Combined sources
Beta strandi784 – 7863Combined sources
Helixi787 – 7937Combined sources
Helixi795 – 7973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VUWX-ray1.80A465-798[»]
2WB8X-ray2.15A452-798[»]
3DLZX-ray1.85A465-798[»]
3E7VX-ray2.00A471-798[»]
3F2NX-ray1.80A465-798[»]
3FMDX-ray2.00A470-798[»]
3IQ7X-ray2.00A465-798[»]
4OUCX-ray1.90A465-798[»]
4QTCX-ray1.40A465-798[»]
5HTBX-ray1.70A465-798[»]
5HTCX-ray1.50A465-798[»]
ProteinModelPortaliQ8TF76.
SMRiQ8TF76. Positions 469-798.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TF76.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini484 – 798315Protein kinasePROSITE-ProRule annotationCuratedAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Haspin subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2464. Eukaryota.
COG5072. LUCA.
GeneTreeiENSGT00390000013015.
HOGENOMiHOG000168256.
HOVERGENiHBG049009.
InParanoidiQ8TF76.
KOiK16315.
OMAiWGNVLLK.
OrthoDBiEOG744T89.
PhylomeDBiQ8TF76.
TreeFamiTF313895.

Family and domain databases

InterProiIPR024604. GSG2_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF12330. DUF3635. 1 hit.
[Graphical view]
SMARTiSM01331. DUF3635. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 12 Publications (identifier: Q8TF76-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAASLPGPGS RLFRTYGAAD GRRQRRPGRE AAQWFPPQDR RRFFNSSGSS
60 70 80 90 100
DASIGDPSQS DDPDDPDDPD FPGSPVRRRR RRPGGRVPKD RPSLTVTPKR
110 120 130 140 150
WKLRARPSLT VTPRRLGLRA RPPQKCSTPC GPLRLPPFPS RDSGRLSPDL
160 170 180 190 200
SVCGQPRDGD ELGISASLFS SLASPCPGSP TPRDSVISIG TSACLVAASA
210 220 230 240 250
VPSGLHLPEV SLDRASLPCS QEEATGGAKD TRMVHQTRAS LRSVLFGLMN
260 270 280 290 300
SGTPEDSEFR ADGKNMRESC CKRKLVVGNG PEGPGLSSTG KRRATGQDSC
310 320 330 340 350
QERGLQEAVR REHQEASVPK GRIVPRGIDR LERTRSSRKS KHQEATETSL
360 370 380 390 400
LHSHRFKKGQ KLGKDSFPTQ DLTPLQNVCF WTKTRASFSF HKKKIVTDVS
410 420 430 440 450
EVCSIYTTAT SLSGSLLSEC SNRPVMNRTS GAPSSWHSSS MYLLSPLNTL
460 470 480 490 500
SISNKKASDA EKVYGECSQK GPVPFSHCLP TEKLQRCEKI GEGVFGEVFQ
510 520 530 540 550
TIADHTPVAI KIIAIEGPDL VNGSHQKTFE EILPEIIISK ELSLLSGEVC
560 570 580 590 600
NRTEGFIGLN SVHCVQGSYP PLLLKAWDHY NSTKGSANDR PDFFKDDQLF
610 620 630 640 650
IVLEFEFGGI DLEQMRTKLS SLATAKSILH QLTASLAVAE ASLRFEHRDL
660 670 680 690 700
HWGNVLLKKT SLKKLHYTLN GKSSTIPSCG LQVSIIDYTL SRLERDGIVV
710 720 730 740 750
FCDVSMDEDL FTGDGDYQFD IYRLMKKENN NRWGEYHPYS NVLWLHYLTD
760 770 780 790
KMLKQMTFKT KCNTPAMKQI KRKIQEFHRT MLNFSSATDL LCQHSLFK
Length:798
Mass (Da):88,495
Last modified:May 18, 2010 - v3
Checksum:iE0EDF8F0C58ADA31
GO
Isoform 21 Publication (identifier: Q8TF76-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.Curated
Show »
Length:314
Mass (Da):33,850
Checksum:i7F8CC086036ED24E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731R → S in BAB71255 (PubMed:14702039).Curated
Sequence conflicti339 – 3391K → E in AAH47457 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761V → E.1 Publication
Corresponds to variant rs11653889 [ dbSNP | Ensembl ].
VAR_040540
Natural varianti82 – 821R → C.4 Publications
Corresponds to variant rs9907144 [ dbSNP | Ensembl ].
VAR_040541
Natural varianti145 – 1451R → H.1 Publication
Corresponds to variant rs55991903 [ dbSNP | Ensembl ].
VAR_040542
Natural varianti204 – 2041G → D.3 Publications
Corresponds to variant rs220462 [ dbSNP | Ensembl ].
VAR_027405
Natural varianti283 – 2831G → S.1 Publication
Corresponds to variant rs56224301 [ dbSNP | Ensembl ].
VAR_040543
Natural varianti301 – 3011Q → L.1 Publication
Corresponds to variant rs55649477 [ dbSNP | Ensembl ].
VAR_040544
Natural varianti328 – 3281I → T.3 Publications
Corresponds to variant rs220461 [ dbSNP | Ensembl ].
VAR_027406
Natural varianti378 – 3781V → A.3 Publications
Corresponds to variant rs3809806 [ dbSNP | Ensembl ].
VAR_027407
Natural varianti422 – 4221N → D.
Corresponds to variant rs7223226 [ dbSNP | Ensembl ].
VAR_027408
Natural varianti706 – 7061M → V.1 Publication
Corresponds to variant rs56134695 [ dbSNP | Ensembl ].
VAR_040545

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei314 – 3141Q → H in isoform 2. 1 PublicationVSP_050671
Alternative sequencei315 – 798484Missing in isoform 2. 1 PublicationVSP_050672Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11036.1. [Q8TF76-1]
RefSeqiNP_114171.2. NM_031965.2. [Q8TF76-1]
UniGeneiHs.534059.

Genome annotation databases

EnsembliENST00000325418; ENSP00000325290; ENSG00000177602. [Q8TF76-1]
GeneIDi83903.
KEGGihsa:83903.
UCSCiuc002fwp.4. human. [Q8TF76-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11036.1. [Q8TF76-1]
RefSeqiNP_114171.2. NM_031965.2. [Q8TF76-1]
UniGeneiHs.534059.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VUWX-ray1.80A465-798[»]
2WB8X-ray2.15A452-798[»]
3DLZX-ray1.85A465-798[»]
3E7VX-ray2.00A471-798[»]
3F2NX-ray1.80A465-798[»]
3FMDX-ray2.00A470-798[»]
3IQ7X-ray2.00A465-798[»]
4OUCX-ray1.90A465-798[»]
4QTCX-ray1.40A465-798[»]
5HTBX-ray1.70A465-798[»]
5HTCX-ray1.50A465-798[»]
ProteinModelPortaliQ8TF76.
SMRiQ8TF76. Positions 469-798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123814. 22 interactions.
DIPiDIP-38174N.
IntActiQ8TF76. 9 interactions.
MINTiMINT-4774775.
STRINGi9606.ENSP00000325290.

Chemistry

BindingDBiQ8TF76.
ChEMBLiCHEMBL1075163.
GuidetoPHARMACOLOGYi2028.

PTM databases

iPTMnetiQ8TF76.
PhosphoSiteiQ8TF76.

Polymorphism and mutation databases

BioMutaiGSG2.
DMDMi296439330.

Proteomic databases

EPDiQ8TF76.
MaxQBiQ8TF76.
PaxDbiQ8TF76.
PeptideAtlasiQ8TF76.
PRIDEiQ8TF76.

Protocols and materials databases

DNASUi83903.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325418; ENSP00000325290; ENSG00000177602. [Q8TF76-1]
GeneIDi83903.
KEGGihsa:83903.
UCSCiuc002fwp.4. human. [Q8TF76-1]

Organism-specific databases

CTDi83903.
GeneCardsiGSG2.
H-InvDBHIX0013433.
HGNCiHGNC:19682. GSG2.
HPAiHPA027422.
HPA030698.
MIMi609240. gene.
neXtProtiNX_Q8TF76.
PharmGKBiPA134909705.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2464. Eukaryota.
COG5072. LUCA.
GeneTreeiENSGT00390000013015.
HOGENOMiHOG000168256.
HOVERGENiHBG049009.
InParanoidiQ8TF76.
KOiK16315.
OMAiWGNVLLK.
OrthoDBiEOG744T89.
PhylomeDBiQ8TF76.
TreeFamiTF313895.

Enzyme and pathway databases

SignaLinkiQ8TF76.

Miscellaneous databases

EvolutionaryTraceiQ8TF76.
GeneWikiiGSG2.
GenomeRNAii83903.
PROiQ8TF76.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TF76.
CleanExiHS_GSG2.
GenevisibleiQ8TF76. HS.

Family and domain databases

InterProiIPR024604. GSG2_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF12330. DUF3635. 1 hit.
[Graphical view]
SMARTiSM01331. DUF3635. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: TestisImported.
  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 blood1 Publication.
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; THR-97 AND SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY.
  14. Cited for: ENZYME REGULATION.
  15. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  16. 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.
  17. "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.
  18. "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.

Entry informationi

Entry nameiHASP_HUMAN
AccessioniPrimary (citable) accession number: Q8TF76
Secondary accession number(s): Q5U5K3, Q96MN1, Q9BXS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.