dbPTM

HASP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HASP_HUMAN
UniProt AC	Q8TF76
Protein Name	Serine/threonine-protein kinase haspin
Gene Name	HASPIN {ECO:0000312\|HGNC:HGNC:19682}
Organism	Homo sapiens (Human).
Sequence Length	798
Subcellular Localization	Nucleus . Chromosome . Cytoplasm, cytoskeleton, spindle . Nuclear during interphase and associates with the chromosomes and spindle apparatus during mitosis.
Protein Description	Serine/threonine-protein kinase that phosphorylates histone H3 at 'Thr-3' (H3T3ph) during mitosis. May act through H3T3ph to both position and modulate activation of 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..
Protein Sequence	MAASLPGPGSRLFRTYGAADGRRQRRPGREAAQWFPPQDRRRFFNSSGSSDASIGDPSQSDDPDDPDDPDFPGSPVRRRRRRPGGRVPKDRPSLTVTPKRWKLRARPSLTVTPRRLGLRARPPQKCSTPCGPLRLPPFPSRDSGRLSPDLSVCGQPRDGDELGISASLFSSLASPCPGSPTPRDSVISIGTSACLVAASAVPSGLHLPEVSLDRASLPCSQEEATGGAKDTRMVHQTRASLRSVLFGLMNSGTPEDSEFRADGKNMRESCCKRKLVVGNGPEGPGLSSTGKRRATGQDSCQERGLQEAVRREHQEASVPKGRIVPRGIDRLERTRSSRKSKHQEATETSLLHSHRFKKGQKLGKDSFPTQDLTPLQNVCFWTKTRASFSFHKKKIVTDVSEVCSIYTTATSLSGSLLSECSNRPVMNRTSGAPSSWHSSSMYLLSPLNTLSISNKKASDAEKVYGECSQKGPVPFSHCLPTEKLQRCEKIGEGVFGEVFQTIADHTPVAIKIIAIEGPDLVNGSHQKTFEEILPEIIISKELSLLSGEVCNRTEGFIGLNSVHCVQGSYPPLLLKAWDHYNSTKGSANDRPDFFKDDQLFIVLEFEFGGIDLEQMRTKLSSLATAKSILHQLTASLAVAEASLRFEHRDLHWGNVLLKKTSLKKLHYTLNGKSSTIPSCGLQVSIIDYTLSRLERDGIVVFCDVSMDEDLFTGDGDYQFDIYRLMKKENNNRWGEYHPYSNVLWLHYLTDKMLKQMTFKTKCNTPAMKQIKRKIQEFHRTMLNFSSATDLLCQHSLFK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAASLPGPGSR ----CCCCCCCCCCH	26.09	-
10	Phosphorylation	ASLPGPGSRLFRTYG CCCCCCCCHHHHHCC	29.01	-
46	Phosphorylation	DRRRFFNSSGSSDAS HHHHHCCCCCCCCCC	30.80	30624053
47	Phosphorylation	RRRFFNSSGSSDASI HHHHCCCCCCCCCCC	43.74	30624053
49	Phosphorylation	RFFNSSGSSDASIGD HHCCCCCCCCCCCCC	27.30	30624053
50	Phosphorylation	FFNSSGSSDASIGDP HCCCCCCCCCCCCCC	40.50	30624053
53	Phosphorylation	SSGSSDASIGDPSQS CCCCCCCCCCCCHHC	31.90	30624053
58	Phosphorylation	DASIGDPSQSDDPDD CCCCCCCHHCCCCCC	47.24	30576142
60	Phosphorylation	SIGDPSQSDDPDDPD CCCCCHHCCCCCCCC	48.60	30624053
74	Phosphorylation	DDPDFPGSPVRRRRR CCCCCCCCCCCCCCC	22.06	26329039
93	Phosphorylation	RVPKDRPSLTVTPKR CCCCCCCCCEECCCC	37.25	25159151
95	Phosphorylation	PKDRPSLTVTPKRWK CCCCCCCEECCCCEE	27.03	21815630
97	Phosphorylation	DRPSLTVTPKRWKLR CCCCCEECCCCEEEE	20.18	23401153
99	Ubiquitination	PSLTVTPKRWKLRAR CCCEECCCCEEEECC	62.62	-
108	Phosphorylation	WKLRARPSLTVTPRR EEEECCCCCEECCCH	30.99	26055452
110	Phosphorylation	LRARPSLTVTPRRLG EECCCCCEECCCHHC	27.03	30266825
112	Phosphorylation	ARPSLTVTPRRLGLR CCCCCEECCCHHCCC	13.07	30266825
127	Phosphorylation	ARPPQKCSTPCGPLR CCCCCCCCCCCCCCC	42.28	24719451
128	Phosphorylation	RPPQKCSTPCGPLRL CCCCCCCCCCCCCCC	31.88	28985074
140	Phosphorylation	LRLPPFPSRDSGRLS CCCCCCCCCCCCCCC	49.45	25159151
143	Phosphorylation	PPFPSRDSGRLSPDL CCCCCCCCCCCCCCC	25.38	29255136
147	Phosphorylation	SRDSGRLSPDLSVCG CCCCCCCCCCCCCCC	18.27	19664994
151	Phosphorylation	GRLSPDLSVCGQPRD CCCCCCCCCCCCCCC	23.81	22167270
165	Phosphorylation	DGDELGISASLFSSL CCCCCCCCHHHHHHH	15.26	-
170	Phosphorylation	GISASLFSSLASPCP CCCHHHHHHHCCCCC	29.72	28122231
171	Phosphorylation	ISASLFSSLASPCPG CCHHHHHHHCCCCCC	22.18	28122231
174	Phosphorylation	SLFSSLASPCPGSPT HHHHHHCCCCCCCCC	32.12	28122231
179	Phosphorylation	LASPCPGSPTPRDSV HCCCCCCCCCCCCCE	15.67	27422710
181	Phosphorylation	SPCPGSPTPRDSVIS CCCCCCCCCCCCEEE	32.43	30278072
185	Phosphorylation	GSPTPRDSVISIGTS CCCCCCCCEEEECHH	23.72	-
188	Phosphorylation	TPRDSVISIGTSACL CCCCCEEEECHHHHH	16.89	-
191	Phosphorylation	DSVISIGTSACLVAA CCEEEECHHHHHHHH	16.10	-
192	Phosphorylation	SVISIGTSACLVAAS CEEEECHHHHHHHHH	16.27	-
211	Phosphorylation	GLHLPEVSLDRASLP CCCCCCCCCCCCCCC	23.92	-
216	Phosphorylation	EVSLDRASLPCSQEE CCCCCCCCCCCCHHH	33.47	19691289
220	Phosphorylation	DRASLPCSQEEATGG CCCCCCCCHHHHCCC	38.39	17525332
229	Acetylation	EEATGGAKDTRMVHQ HHHCCCCCCHHHHHH	64.01	25953088
229	Ubiquitination	EEATGGAKDTRMVHQ HHHCCCCCCHHHHHH	64.01	-
231	Phosphorylation	ATGGAKDTRMVHQTR HCCCCCCHHHHHHHH	21.69	24719451
237	Phosphorylation	DTRMVHQTRASLRSV CHHHHHHHHHHHHHH	17.21	22210691
240	Phosphorylation	MVHQTRASLRSVLFG HHHHHHHHHHHHHHH	22.48	20860994
243	Phosphorylation	QTRASLRSVLFGLMN HHHHHHHHHHHHHHC	28.59	-
251	Phosphorylation	VLFGLMNSGTPEDSE HHHHHHCCCCCCCHH	30.03	22199227
253	Phosphorylation	FGLMNSGTPEDSEFR HHHHCCCCCCCHHHC	24.27	25159151
257	Phosphorylation	NSGTPEDSEFRADGK CCCCCCCHHHCCCCC	36.65	22199227
269	Phosphorylation	DGKNMRESCCKRKLV CCCCHHHHHHCCEEE	17.91	-
274	Ubiquitination	RESCCKRKLVVGNGP HHHHHCCEEEECCCC	31.00	-
287	Phosphorylation	GPEGPGLSSTGKRRA CCCCCCCCCCCCCCC	31.59	22199227
288	Phosphorylation	PEGPGLSSTGKRRAT CCCCCCCCCCCCCCC	46.34	25159151
289	Phosphorylation	EGPGLSSTGKRRATG CCCCCCCCCCCCCCC	43.26	25159151
291	Ubiquitination	PGLSSTGKRRATGQD CCCCCCCCCCCCCCC	38.51	-
291	Acetylation	PGLSSTGKRRATGQD CCCCCCCCCCCCCCC	38.51	25953088
295	Phosphorylation	STGKRRATGQDSCQE CCCCCCCCCCCHHHH	33.30	-
299	O-linked_Glycosylation	RRATGQDSCQERGLQ CCCCCCCHHHHHHHH	15.15	29351928
317	Phosphorylation	RREHQEASVPKGRIV HHHHHHHCCCCCCCC	37.89	28985074
340	Phosphorylation	RTRSSRKSKHQEATE HHHHCCHHHHHHHHH	33.97	-
341	Ubiquitination	TRSSRKSKHQEATET HHHCCHHHHHHHHHH	52.95	-
348	Phosphorylation	KHQEATETSLLHSHR HHHHHHHHHHHHHHC	21.96	29214152
349	Phosphorylation	HQEATETSLLHSHRF HHHHHHHHHHHHHCC	23.77	26425664
353	Phosphorylation	TETSLLHSHRFKKGQ HHHHHHHHHCCCCCC	19.14	26425664
366	Phosphorylation	GQKLGKDSFPTQDLT CCCCCCCCCCCCCCC	36.29	21712546
373	Phosphorylation	SFPTQDLTPLQNVCF CCCCCCCCCCCEEEE	30.18	21712546
384	Phosphorylation	NVCFWTKTRASFSFH EEEEEECCCCCEEEC	24.88	20860994
387	Phosphorylation	FWTKTRASFSFHKKK EEECCCCCEEECCCE	20.38	25159151
389	Phosphorylation	TKTRASFSFHKKKIV ECCCCCEEECCCEEE	24.76	25159151
429	Phosphorylation	NRPVMNRTSGAPSSW CCCCCCCCCCCCCCC	26.89	-
430	Phosphorylation	RPVMNRTSGAPSSWH CCCCCCCCCCCCCCC	29.71	-
434	Phosphorylation	NRTSGAPSSWHSSSM CCCCCCCCCCCCCCE	45.59	-
435	Phosphorylation	RTSGAPSSWHSSSMY CCCCCCCCCCCCCEE	27.96	-
445	Phosphorylation	SSSMYLLSPLNTLSI CCCEEEECCCCEEEC	25.42	-
453	Phosphorylation	PLNTLSISNKKASDA CCCEEECCCCCHHHH	38.94	-
456	Ubiquitination	TLSISNKKASDAEKV EEECCCCCHHHHHHH	58.32	-
462	Ubiquitination	KKASDAEKVYGECSQ CCHHHHHHHHHHHHC	42.34	-
470	Ubiquitination	VYGECSQKGPVPFSH HHHHHHCCCCCCHHH	49.22	-
483	Ubiquitination	SHCLPTEKLQRCEKI HHCCCHHHHHHHHHH	53.01	-
506	Phosphorylation	FQTIADHTPVAIKII HHHHHHCCCEEEEEE	21.72	24719451
584	Ubiquitination	WDHYNSTKGSANDRP HHHCCCCCCCCCCCC	51.17	-
618	Ubiquitination	DLEQMRTKLSSLATA CHHHHHHHHHHHHHH	35.69	-
620	Phosphorylation	EQMRTKLSSLATAKS HHHHHHHHHHHHHHH	25.51	24719451
621	Phosphorylation	QMRTKLSSLATAKSI HHHHHHHHHHHHHHH	32.24	28102081
624	Phosphorylation	TKLSSLATAKSILHQ HHHHHHHHHHHHHHH	39.65	24719451
627	Phosphorylation	SSLATAKSILHQLTA HHHHHHHHHHHHHHH	28.11	24719451
664	Ubiquitination	LKKTSLKKLHYTLNG EEECCCCEEEEECCC	45.87	-
759	Methylation	MLKQMTFKTKCNTPA HHHHCCCCCCCCCHH	37.60	-
764	Phosphorylation	TFKTKCNTPAMKQIK CCCCCCCCHHHHHHH	23.15	20860994
768	Ubiquitination	KCNTPAMKQIKRKIQ CCCCHHHHHHHHHHH	51.48	-
795	Phosphorylation	TDLLCQHSLFK---- HHHHHHHHHCC----	15.04	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
4	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
93	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
108	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
128	T	Phosphorylation	Kinase	CDK1	P06493	PSP
143	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
3	S	Phosphorylation		15681610
Phosphorylation by AURKB is required for full activity toward histone H3 at 'Ser-3' in mitosis.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HASP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
H31_HUMAN	HIST1H3A	physical	21397507
IMA7_HUMAN	KPNA6	physical	26496610
FBXL6_HUMAN	FBXL6	physical	26496610
HERC5_HUMAN	HERC5	physical	26496610
THA11_HUMAN	THAP11	physical	26496610
EHMT1_HUMAN	EHMT1	physical	26496610

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HASP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A positive feedback loop involving Haspin and Aurora B promotes CPCaccumulation 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). Cited for: PHOSPHORYLATION AT SER-93 AND SER-143 BY AURKB, ENZYME REGULATION, ANDMASS SPECTROMETRY.	21658950 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; THR-97; SER-143 ANDSER-147, AND MASS SPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASSSPECTROMETRY.	17525332 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-253, AND MASSSPECTROMETRY.	16565220 [Abstract]

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