KAT2A_HUMAN - dbPTM
KAT2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAT2A_HUMAN
UniProt AC Q92830
Protein Name Histone acetyltransferase KAT2A
Gene Name KAT2A {ECO:0000312|HGNC:HGNC:4201}
Organism Homo sapiens (Human).
Sequence Length 837
Subcellular Localization Nucleus . Chromosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Mainly localizes to the nucleus. Also localizes to centrosomes in late G1 and around the G1/S transition, coinciding with the onset of centriole formation.
Protein Description Protein lysine acyltransferase that can act both as a acetyltransferase and succinyltransferase, depending on the context. [PubMed: 29211711 Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes]
Protein Sequence MAEPSQAPTPAPAAQPRPLQSPAPAPTPTPAPSPASAPIPTPTPAPAPAPAAAPAGSTGTGGPGVGSGGAGSGGDPARPGLSQQQRASQRKAQVRGLPRAKKLEKLGVFSACKANETCKCNGWKNPKPPTAPRMDLQQPAANLSELCRSCEHPLADHVSHLENVSEDEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMTRPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPRERQTMFELSKMFLLCLNYWKLETPAQFRQRSQAEDVATYKVNYTRWLCYCHVPQSCDSLPRYETTHVFGRSLLRSIFTVTRRQLLEKFRVEKDKLVPEKRTLILTHFPKFLSMLEEEIYGANSPIWESGFTMPPSEGTQLVPRPASVSAAVVPSTPIFSPSMGGGSNSSLSLDSAGAEPMPGEKRTLPENLTLEDAKRLRVMGDIPMELVNEVMLTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLTPKANRRVLLWLVGLQNVFSHQLPRMPKEYIARLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHNILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPYTELSHIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIPVESVPGIRETGWKPLGKEKGKELKDPDQLYTTLKNLLAQIKSHPSAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTERLRSRYYVTRKLFVADLQRVIANCREYNPPDSEYCRCASALEKFFYFKLKEGGLIDK
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------MAEPSQAPT
------CCCCCCCCC		37.0922814378
5 (in isoform 2)Phosphorylation-30.4029116813
9PhosphorylationAEPSQAPTPAPAAQP
CCCCCCCCCCCCCCC		34.7929507054
13 (in isoform 2)Phosphorylation-22.3429116813
33PhosphorylationPTPTPAPSPASAPIP
CCCCCCCCCCCCCCC		34.89-
36PhosphorylationTPAPSPASAPIPTPT
CCCCCCCCCCCCCCC		37.65-
82PhosphorylationDPARPGLSQQQRASQ
CCCCCCCCHHHHHHH		31.6825106551
194PhosphorylationHKEEDTDTKQVYFYL
CCCCCCCHHHHHHHH		26.0120860994
228SumoylationLGSPPFEKPNIEQGV
CCCCCCCCCCHHHHH		43.68-
272PhosphorylationLNYWKLETPAQFRQR
HHHHHCCCHHHHHHH		34.07-
289 (in isoform 1)Ubiquitination-21.4621890473
289UbiquitinationAEDVATYKVNYTRWL
HHHCCCCEECEEEEE		21.4622817900
307PhosphorylationHVPQSCDSLPRYETT
CCCCCCCCCCCCCCH		44.60-
372PhosphorylationEEIYGANSPIWESGF
HHHHCCCCCCHHCCC		19.75-
415PhosphorylationSPSMGGGSNSSLSLD
CCCCCCCCCCCCCCC		36.4930631047
446UbiquitinationNLTLEDAKRLRVMGD
CCCHHHHHHHHEECC		65.3729967540
549AcetylationLVFDPKHKTLALIKD
HHCCCCCCEEEEEEC		51.8954843203
555UbiquitinationHKTLALIKDGRVIGG
CCEEEEEECCEEEEE		55.79-
669UbiquitinationTELSHIIKKQKEIIK
HHHHHHHHHHHHHHH		48.8529967540
676MethylationKKQKEIIKKLIERKQ
HHHHHHHHHHHHHHH		47.3819351588
677MethylationKQKEIIKKLIERKQA
HHHHHHHHHHHHHHH		44.2619351588
688UbiquitinationRKQAQIRKVYPGLSC
HHHHHHHHHCCCCHH		47.9933845483
690PhosphorylationQAQIRKVYPGLSCFK
HHHHHHHCCCCHHHH		8.4629496907
697UbiquitinationYPGLSCFKEGVRQIP
CCCCHHHHHCCCCCC		58.8633845483
707PhosphorylationVRQIPVESVPGIRET
CCCCCHHCCCCCCCC		33.5722210691
714PhosphorylationSVPGIRETGWKPLGK
CCCCCCCCCCCCCCH		38.1922210691
717AcetylationGIRETGWKPLGKEKG
CCCCCCCCCCCHHCC		31.5426051181
721AcetylationTGWKPLGKEKGKELK
CCCCCCCHHCCCCCC		65.037304083
721UbiquitinationTGWKPLGKEKGKELK
CCCCCCCHHCCCCCC		65.0329967540
725UbiquitinationPLGKEKGKELKDPDQ
CCCHHCCCCCCCHHH		71.5829967540
725AcetylationPLGKEKGKELKDPDQ
CCCHHCCCCCCCHHH		71.5826051181
728UbiquitinationKEKGKELKDPDQLYT
HHCCCCCCCHHHHHH		69.2029967540
728SumoylationKEKGKELKDPDQLYT
HHCCCCCCCHHHHHH		69.2028112733
734PhosphorylationLKDPDQLYTTLKNLL
CCCHHHHHHHHHHHH		7.6425159151
735PhosphorylationKDPDQLYTTLKNLLA
CCHHHHHHHHHHHHH		33.9625884760
736PhosphorylationDPDQLYTTLKNLLAQ
CHHHHHHHHHHHHHH		23.3728152594
759UbiquitinationPFMEPVKKSEAPDYY
CCCCCCCCCCCCCCH		54.4833845483
759SumoylationPFMEPVKKSEAPDYY
CCCCCCCCCCCCCCH		54.4828112733
776UbiquitinationIRFPIDLKTMTERLR
EEEECCHHHHHHHHH		32.28-
787PhosphorylationERLRSRYYVTRKLFV
HHHHHHHHHHHHHHH		8.34-
791UbiquitinationSRYYVTRKLFVADLQ
HHHHHHHHHHHHHHH		36.59-
791SumoylationSRYYVTRKLFVADLQ
HHHHHHHHHHHHHHH		36.5928112733
830AcetylationKFFYFKLKEGGLIDK
HHHHEEHHHCCCCCC		55.7026051181
830UbiquitinationKFFYFKLKEGGLIDK
HHHHEEHHHCCCCCC		55.7033845483
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
272TPhosphorylationKinaseCDK4P11802
PSP
372SPhosphorylationKinaseCDK4P11802
PSP
-KUbiquitinationE3 ubiquitin ligaseDTLQ9NZJ0
PMID:21987584
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAT2A_HUMAN !!
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 KAT2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRRAP_HUMANTRRAPphysical
10611234
NOTC1_MOUSENotch1physical
10747963
XRCC6_HUMANXRCC6physical
9488450
XRCC5_HUMANXRCC5physical
9488450
TAD2A_HUMANTADA2Aphysical
8972232
ADA2_YEASTADA2physical
8972232
H31_HUMANHIST1H3Aphysical
16287840
MYC_HUMANMYCphysical
16287840
DHI2_HUMANHSD11B2physical
12878208
GATA2_HUMANGATA2physical
15001660
MED16_HUMANMED16physical
17967894
MED1_HUMANMED1physical
17967894
MED17_HUMANMED17physical
17967894
TAF9_HUMANTAF9physical
17967894
SUPT3_HUMANSUPT3Hphysical
17967894
ST65G_HUMANSUPT7Lphysical
17967894
CEBPB_HUMANCEBPBphysical
17301242
MED1_HUMANMED1physical
20508642
TRRAP_HUMANTRRAPphysical
20946988
TAF5L_HUMANTAF5Lphysical
20946988
ADAT3_HUMANADAT3physical
20946988
TAF6_HUMANTAF6physical
20946988
TADA1_HUMANTADA1physical
20946988
K22E_HUMANKRT2physical
20946988
RAE1L_HUMANRAE1physical
20946988
SUPT3_HUMANSUPT3Hphysical
20946988
TAF9_HUMANTAF9physical
20946988
PCBP2_HUMANPCBP2physical
20946988
SF3B3_HUMANSF3B3physical
20946988
JIP3_HUMANMAPK8IP3physical
20946988
LDHA_HUMANLDHAphysical
20946988
HDGF_HUMANHDGFphysical
20946988
COMD1_HUMANCOMMD1physical
19339690
TF65_HUMANRELAphysical
19339690
CUL2_HUMANCUL2physical
19339690
DTL_HUMANDTLphysical
21987584
CUL4A_HUMANCUL4Aphysical
21987584
DDB1_HUMANDDB1physical
21987584
WDHD1_HUMANWDHD1physical
21987584
CDK2_HUMANCDK2physical
19773423
TACC2_HUMANTACC2physical
14767476
WDHD1_HUMANWDHD1physical
21725360
ATX7_HUMANATXN7physical
19843541
SGF29_HUMANCCDC101physical
21746879
AT7L3_HUMANATXN7L3physical
21746879
UBP22_HUMANUSP22physical
21746879
NC2B_HUMANDR1physical
18838386
YETS2_HUMANYEATS2physical
18838386
H2A2C_HUMANHIST2H2ACphysical
16096645
H2B2E_HUMANHIST2H2BEphysical
16096645
H32_HUMANHIST2H3Cphysical
16096645
UBP22_HUMANUSP22physical
23382074
TIRAP_HUMANTIRAPphysical
23382074
H15_HUMANHIST1H1Bphysical
10373431
TEBP_HUMANPTGES3physical
23022381
UBP22_HUMANUSP22physical
18206973
H31T_HUMANHIST3H3physical
8684459
H2B2E_HUMANHIST2H2BEphysical
8684459
H2A2C_HUMANHIST2H2ACphysical
8684459
PTF1A_HUMANPTF1Aphysical
18834332
H31_HUMANHIST1H3Aphysical
14752096
MYB_HUMANMYBphysical
10656693
POL_HV1H2gag-polphysical
20226045
H31_HUMANHIST1H3Aphysical
19103755
KAT2A_HUMANKAT2Aphysical
21157427
TAF9_HUMANTAF9physical
12660246
SUPT3_HUMANSUPT3Hphysical
12660246
TAF5L_HUMANTAF5Lphysical
12660246
TRRAP_HUMANTRRAPphysical
12660246
ZZZ3_HUMANZZZ3physical
18838386
UBP2L_HUMANUBAP2Lphysical
18838386
CSR2B_HUMANCSRP2BPphysical
18838386
M3K7_HUMANMAP3K7physical
18838386
TADA3_HUMANTADA3physical
18838386
TAD2A_HUMANTADA2Aphysical
18838386
MBIP1_HUMANMBIPphysical
18838386
WDR5_HUMANWDR5physical
18838386
SGF29_HUMANCCDC101physical
18838386
SP20H_HUMANSUPT20Hphysical
18838386
UBP22_HUMANUSP22physical
18838386
H31_HUMANHIST1H3Aphysical
18838386
XBP1_HUMANXBP1physical
25426559
NDKA_HUMANNME1physical
25582197
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 KAT2A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-734, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-734, AND MASSSPECTROMETRY.

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