HAT1_HUMAN - dbPTM
HAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAT1_HUMAN
UniProt AC O14929
Protein Name Histone acetyltransferase type B catalytic subunit
Gene Name HAT1
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization Isoform A: Nucleus matrix.
Isoform B: Cytoplasm. Nucleus. Nucleus matrix. Nucleus, nucleoplasm. Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redis
Protein Description Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage..
Protein Sequence MAGFGAMEKFLVEYKSAVEKKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGFCTNTNDFLSLLEKEVDFKPFGTLLHTYSVLSPTGGENFTFQIYKADMTCRGFREYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATVGYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPTVLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMAIEAQQKFKINKQHARRVYEILRLLVTDMSDAEQYRSYRLDIKRRLISPYKKKQRDLAKMRKCLRPEELTNQMNQIEISMQHEQLEESFQELVEDYRRVIERLAQE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAGFGAMEK
------CCCCCHHHH		23.2522223895
3Ubiquitination-----MAGFGAMEKF
-----CCCCCHHHHH		21.8823000965
9AcetylationAGFGAMEKFLVEYKS
CCCCHHHHHHHHHHH		30.8025953088
9UbiquitinationAGFGAMEKFLVEYKS
CCCCHHHHHHHHHHH		30.8023000965
14UbiquitinationMEKFLVEYKSAVEKK
HHHHHHHHHHHHHHH		11.6323000965
15SumoylationEKFLVEYKSAVEKKL
HHHHHHHHHHHHHHH		20.59-
152-HydroxyisobutyrylationEKFLVEYKSAVEKKL
HHHHHHHHHHHHHHH		20.59-
15SuccinylationEKFLVEYKSAVEKKL
HHHHHHHHHHHHHHH		20.5923954790
15NeddylationEKFLVEYKSAVEKKL
HHHHHHHHHHHHHHH		20.5932015554
15AcetylationEKFLVEYKSAVEKKL
HHHHHHHHHHHHHHH		20.5923954790
15UbiquitinationEKFLVEYKSAVEKKL
HHHHHHHHHHHHHHH		20.5923000965
20UbiquitinationEYKSAVEKKLAEYKC
HHHHHHHHHHHHCCC		46.6323000965
21UbiquitinationYKSAVEKKLAEYKCN
HHHHHHHHHHHCCCC		39.1523000965
262-HydroxyisobutyrylationEKKLAEYKCNTNTAI
HHHHHHCCCCCCCCE		16.71-
26UbiquitinationEKKLAEYKCNTNTAI
HHHHHHCCCCCCCCE		16.7121963094
36UbiquitinationTNTAIELKLVRFPED
CCCCEEEEEEECCHH		31.9529967540
50PhosphorylationDLENDIRTFFPEYTH
HHHHHHHHHCHHHHH		29.93-
55PhosphorylationIRTFFPEYTHQLFGD
HHHHCHHHHHHHHCC		15.12-
64UbiquitinationHQLFGDDETAFGYKG
HHHHCCCCCCCCHHH		46.9421890473
67UbiquitinationFGDDETAFGYKGLKI
HCCCCCCCCHHHHHH		16.7322817900
69PhosphorylationDDETAFGYKGLKILL
CCCCCCCHHHHHHHH		8.74-
70UbiquitinationDETAFGYKGLKILLY
CCCCCCHHHHHHHHH		59.1421906983
73UbiquitinationAFGYKGLKILLYYIA
CCCHHHHHHHHHHHH		39.7222817900
77PhosphorylationKGLKILLYYIAGSLS
HHHHHHHHHHHHHHH		6.8621601212
78PhosphorylationGLKILLYYIAGSLST
HHHHHHHHHHHHHHH		5.58-
82PhosphorylationLLYYIAGSLSTMFRV
HHHHHHHHHHHHHHH		15.3221601212
84PhosphorylationYYIAGSLSTMFRVEY
HHHHHHHHHHHHHHH		21.3721601212
91PhosphorylationSTMFRVEYASKVDEN
HHHHHHHHHCCCCCC		17.2029214152
93PhosphorylationMFRVEYASKVDENFD
HHHHHHHCCCCCCCC		32.1021712546
94AcetylationFRVEYASKVDENFDC
HHHHHHCCCCCCCCE		45.6026051181
94UbiquitinationFRVEYASKVDENFDC
HHHHHHCCCCCCCCE		45.6033845483
101GlutathionylationKVDENFDCVEADDVE
CCCCCCCEEECCCCC		2.3222555962
104UbiquitinationENFDCVEADDVEGKI
CCCCEEECCCCCCCE		9.6321963094
110UbiquitinationEADDVEGKIRQIIPP
ECCCCCCCEEECCCC		22.6221906983
128PhosphorylationTNTNDFLSLLEKEVD
CCCHHHHHHHHHCCC		30.7924719451
152PhosphorylationTYSVLSPTGGENFTF
EEEEECCCCCCCEEE		55.2122210691
158PhosphorylationPTGGENFTFQIYKAD
CCCCCCEEEEEEECC		26.6422210691
190PhosphorylationMWFIETASFIDVDDE
HHHHHHCCEECCCCC		30.1028143904
201PhosphorylationVDDERWHYFLVFEKY
CCCCCEEEEEEEEEC		7.5226437602
245PhosphorylationVSQMLILTPFQGQGH
EEEEEEEECCCCCCH		18.31-
274UbiquitinationFPTVLDITAEDPSKS
CCCEEEEECCCCCCC		24.5422817900
278UbiquitinationLDITAEDPSKSYVKL
EEEECCCCCCCCEEH		34.8522817900
280UbiquitinationITAEDPSKSYVKLRD
EECCCCCCCCEEHHH		51.7121906983
280AcetylationITAEDPSKSYVKLRD
EECCCCCCCCEEHHH		51.7125953088
284UbiquitinationDPSKSYVKLRDFVLV
CCCCCCEEHHHHHHH		29.5822817900
286MethylationSKSYVKLRDFVLVKL
CCCCEEHHHHHHHHH		29.60-
298UbiquitinationVKLCQDLPCFSREKL
HHHHCCCCCCCHHHH		25.9522817900
301PhosphorylationCQDLPCFSREKLMQG
HCCCCCCCHHHHHCC		46.3720068231
304UbiquitinationLPCFSREKLMQGFNE
CCCCCHHHHHCCCCH		48.4222817900
3042-HydroxyisobutyrylationLPCFSREKLMQGFNE
CCCCCHHHHHCCCCH		48.42-
306SulfoxidationCFSREKLMQGFNEDM
CCCHHHHHCCCCHHH		5.6221406390
314UbiquitinationQGFNEDMAIEAQQKF
CCCCHHHHHHHHHHH		14.5922817900
316UbiquitinationFNEDMAIEAQQKFKI
CCHHHHHHHHHHHCC		30.7822817900
319UbiquitinationDMAIEAQQKFKINKQ
HHHHHHHHHHCCCHH		61.2722817900
320UbiquitinationMAIEAQQKFKINKQH
HHHHHHHHHCCCHHH		36.2221906983
3202-HydroxyisobutyrylationMAIEAQQKFKINKQH
HHHHHHHHHCCCHHH		36.22-
322UbiquitinationIEAQQKFKINKQHAR
HHHHHHHCCCHHHHH		53.0222817900
325UbiquitinationQQKFKINKQHARRVY
HHHHCCCHHHHHHHH		47.1122817900
342SulfoxidationLRLLVTDMSDAEQYR
HHHHHCCCCHHHHHH		2.5930846556
343PhosphorylationRLLVTDMSDAEQYRS
HHHHCCCCHHHHHHH		36.1630624053
350PhosphorylationSDAEQYRSYRLDIKR
CHHHHHHHHHHHHHH		15.0722817900
351PhosphorylationDAEQYRSYRLDIKRR
HHHHHHHHHHHHHHH		13.2422817900
359UbiquitinationRLDIKRRLISPYKKK
HHHHHHHHCCCCHHH		5.4424816145
361PhosphorylationDIKRRLISPYKKKQR
HHHHHHCCCCHHHHH		27.1122167270
363PhosphorylationKRRLISPYKKKQRDL
HHHHCCCCHHHHHHH		28.7528152594
364AcetylationRRLISPYKKKQRDLA
HHHCCCCHHHHHHHH		57.8025953088
365UbiquitinationRLISPYKKKQRDLAK
HHCCCCHHHHHHHHH		48.5824816145
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
190SPhosphorylationKinaseAMPKA1Q13131
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
190SPhosphorylation

28143904
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 HAT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASF1B_HUMANASF1Bphysical
20953179
B2LA1_HUMANBCL2A1physical
22615379
THIK_HUMANACAA1physical
9427644
H2A2C_HUMANHIST2H2ACphysical
9427644
RBBP7_HUMANRBBP7physical
22939629
RBBP7_HUMANRBBP7physical
26186194
CE051_HUMANC5orf51physical
26344197
SNF8_HUMANSNF8physical
26344197
TLN2_HUMANTLN2physical
26344197
RBBP7_HUMANRBBP7physical
28514442
ASF1A_HUMANASF1Aphysical
28514442
RBBP7_HUMANRBBP7physical
28143904
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 HAT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-361, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASSSPECTROMETRY.

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