KAT6B_HUMAN - dbPTM
KAT6B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAT6B_HUMAN
UniProt AC Q8WYB5
Protein Name Histone acetyltransferase KAT6B
Gene Name KAT6B
Organism Homo sapiens (Human).
Sequence Length 2073
Subcellular Localization Nucleus .
Protein Description Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity..
Protein Sequence MVKLANPLYTEWILEAIQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSVLKVTNKGLASYKDPDNPGRFSSVKPGTFPKSAKGSRGSCNDLRNVDWNKLLRRAIEGLEEPNGSSLKNIEKYLRSQSDLTSTTNNPAFQQRLRLGAKRAVNNGRLLKDGPQYRVNYGSLDGKGAPQYPSAFPSSLPPVSLLPHEKDQPRADPIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTTNVKALRWQCIECKTCSACRVQGRNADNMLFCDSCDRGFHMECCDPPLSRMPKGMWICQVCRPKKKGRKLLHEKAAQIKRRYAKPIGRPKNKLKQRLLSVTSDEGSMNAFTGRGSPGRGQKTKVCTTPSSGHAASGKDSSSRLAVTDPTRPGATTKITTTSTYISASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLATGTTQKLKPPPSSLPPPTPISGQSPSSQKSSTATSSPSPQSSSSQCSVPSLSSLTTNSQLKALFDGLSHIYTTQGQSRKKGHPSYAPPKRMRRKTELSSTAKSKAHFFGKRDIRSRFISHSSSSSWGMARGSIFKAIAHFKRTTFLKKHRMLGRLKYKVTPQMGTPSPGKGSLTDGRIKPDQDDDTEIKINIKQESADVNVIGNKDVVTEEDLDVFKQAQELSWEKIECESGVEDCGRYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYHHHERHISIKAISRATGMCPHDIATTLQHLHMIDKRDGRFVIIRREKLILSHMEKLKTCSRANELDPDSLRWTPILISNAAVSEEEREAEKEAERLMEQASCWEKEEQEILSTRANSRQSPAKVQSKNKYLHSPESRPVTGERGQLLELSKESSEEEEEEEDEEEEEEEEEEEEDEEEEEEEEEEEEEENIQSSPPRLTKPQSVAIKRKRPFVLKKKRGRKRRRINSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIEVEEDGRKPVLRKAFQHQPGKKRQTEEEEGKDNHCFKNADPCRNNMNDDSSNLKEGSKDNPEPLKCKQVWPKGTKRGLSKWRQNKERKTGFKLNLYTPPETPMEPDEQVTVEEQKETSEGKTSPSPIRIEEEVKETGEALLPQEENRREETCAPVSPNTSPGEKPEDDLIKPEEEEEEEEEEEEEEEEEEGEEEEGGGNVEKDPDGAKSQEKEEPEISTEKEDSARLDDHEEEEEEDEEPSHNEDHDADDEDDSHMESAEVEKEELPRESFKEVLENQETFLDLNVQPGHSNPEVLMDCGVDLTASCNSEPKELAGDPEAVPESDEEPPPGEQAQKQDQKNSKEVDTEFKEGNPATMEIDSETVQAVQSLTQESSEQDDTFQDCAETQEACRSLQNYTRADQSPQIATTLDDCQQSDHSSPVSSVHSHPGQSVRSVNSPSVPALENSYAQISPDQSAISVPSLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNGSSQNSCSYSNLTSSSLTQSSCAVTQQMSNISGSCSMLQQTSISSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLAEIPETSNANIGLYERMGQSDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQLSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASKGHISMRTKSASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVNSVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGTQPYAQQPMQTPPHGNMMYTAPGHHGYMNTGMSKQSLNGSYMRR
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
84AcetylationPGRFSSVKPGTFPKS
CCCCCCCCCCCCCCC
39.4125953088
127UbiquitinationEPNGSSLKNIEKYLR
CCCCHHHHHHHHHHH
58.80-
182AcetylationNYGSLDGKGAPQYPS
ECCCCCCCCCCCCCC
52.1226051181
217PhosphorylationADPIPICSFCLGTKE
CCCCCCCHHHCCCCC
21.51-
222PhosphorylationICSFCLGTKESNREK
CCHHHCCCCCCCCCC
20.77-
223AcetylationCSFCLGTKESNREKK
CHHHCCCCCCCCCCC
58.3023749302
242PhosphorylationLSCADCGSSGHPSCL
HCCCCCCCCCCHHHH
39.2030631047
243PhosphorylationSCADCGSSGHPSCLK
CCCCCCCCCCHHHHH
26.8030631047
260AcetylationPELTTNVKALRWQCI
HHHCCCCCCEEEEEE
43.7225953088
270AcetylationRWQCIECKTCSACRV
EEEEEECCCCCCCCC
39.5125953088
355PhosphorylationKLKQRLLSVTSDEGS
HHHHHHHCCCCCCCC
28.1330108239
357PhosphorylationKQRLLSVTSDEGSMN
HHHHHCCCCCCCCCC
27.3830576142
358PhosphorylationQRLLSVTSDEGSMNA
HHHHCCCCCCCCCCC
31.3525849741
362PhosphorylationSVTSDEGSMNAFTGR
CCCCCCCCCCCCCCC
13.5530108239
367PhosphorylationEGSMNAFTGRGSPGR
CCCCCCCCCCCCCCC
24.4530108239
367 (in isoform 3)Phosphorylation-24.4528348404
371PhosphorylationNAFTGRGSPGRGQKT
CCCCCCCCCCCCCCC
23.8725849741
371 (in isoform 3)Phosphorylation-23.8726657352
374DimethylationTGRGSPGRGQKTKVC
CCCCCCCCCCCCEEE
47.99-
374MethylationTGRGSPGRGQKTKVC
CCCCCCCCCCCCEEE
47.9924379935
379AcetylationPGRGQKTKVCTTPSS
CCCCCCCEEEECCCC
42.2023749302
382PhosphorylationGQKTKVCTTPSSGHA
CCCCEEEECCCCCCC
44.7428348404
383PhosphorylationQKTKVCTTPSSGHAA
CCCEEEECCCCCCCC
18.9525159151
391PhosphorylationPSSGHAASGKDSSSR
CCCCCCCCCCCCCCC
47.35-
393AcetylationSGHAASGKDSSSRLA
CCCCCCCCCCCCCEE
52.5223749302
402PhosphorylationSSSRLAVTDPTRPGA
CCCCEEECCCCCCCC
30.5620068231
412AcetylationTRPGATTKITTTSTY
CCCCCEEEEEECCCE
33.4325953088
414PhosphorylationPGATTKITTTSTYIS
CCCEEEEEECCCEEE
26.1025404012
415PhosphorylationGATTKITTTSTYISA
CCEEEEEECCCEEEC
23.4025404012
416PhosphorylationATTKITTTSTYISAS
CEEEEEECCCEEECC
15.4925404012
417PhosphorylationTTKITTTSTYISAST
EEEEEECCCEEECCE
19.6825404012
418PhosphorylationTKITTTSTYISASTL
EEEEECCCEEECCEE
23.8425404012
419PhosphorylationKITTTSTYISASTLK
EEEECCCEEECCEEE
7.8222496350
421PhosphorylationTTTSTYISASTLKVN
EECCCEEECCEEECC
13.0225404012
423PhosphorylationTSTYISASTLKVNKK
CCCEEECCEEECCCC
27.7325404012
424PhosphorylationSTYISASTLKVNKKT
CCEEECCEEECCCCC
30.2528555341
432AcetylationLKVNKKTKGLIDGLT
EECCCCCCCCCCHHH
61.6826051181
440AcetylationGLIDGLTKFFTPSPD
CCCCHHHHCCCCCCC
43.4523236377
440UbiquitinationGLIDGLTKFFTPSPD
CCCCHHHHCCCCCCC
43.4521890473
440 (in isoform 1)Ubiquitination-43.4521890473
440 (in isoform 2)Ubiquitination-43.4521890473
443PhosphorylationDGLTKFFTPSPDGRR
CHHHHCCCCCCCCCC
26.4530266825
445PhosphorylationLTKFFTPSPDGRRSR
HHHCCCCCCCCCCCC
32.3430266825
451PhosphorylationPSPDGRRSRGEIIDF
CCCCCCCCCCCCCCC
43.1925159151
471AcetylationPRKKVSQKQSCTSHV
CCCCCCCCCCCCCCE
36.3525953088
493 (in isoform 3)Ubiquitination-51.1521890473
504PhosphorylationPTPISGQSPSSQKSS
CCCCCCCCCCCCCCC
30.2128985074
548PhosphorylationKALFDGLSHIYTTQG
HHHHHHCCCEEECCC
17.2321552520
553PhosphorylationGLSHIYTTQGQSRKK
HCCCEEECCCCCCCC
17.4621552520
557PhosphorylationIYTTQGQSRKKGHPS
EEECCCCCCCCCCCC
53.5521552520
582AcetylationTELSSTAKSKAHFFG
HHCCHHHHHHHHHHC
53.2125953088
584AcetylationLSSTAKSKAHFFGKR
CCHHHHHHHHHHCCH
45.2125953088
590AcetylationSKAHFFGKRDIRSRF
HHHHHHCCHHHHHHH
41.5623749302
599PhosphorylationDIRSRFISHSSSSSW
HHHHHHHCCCCCCHH
18.0127732954
601PhosphorylationRSRFISHSSSSSWGM
HHHHHCCCCCCHHHC
25.7327732954
602PhosphorylationSRFISHSSSSSWGMA
HHHHCCCCCCHHHCH
28.9027732954
602 (in isoform 2)Ubiquitination-28.9021890473
603PhosphorylationRFISHSSSSSWGMAR
HHHCCCCCCHHHCHH
31.2627732954
604PhosphorylationFISHSSSSSWGMARG
HHCCCCCCHHHCHHH
31.8727732954
605PhosphorylationISHSSSSSWGMARGS
HCCCCCCHHHCHHHH
29.6027732954
612PhosphorylationSWGMARGSIFKAIAH
HHHCHHHHHHHHHHH
21.2124719451
615AcetylationMARGSIFKAIAHFKR
CHHHHHHHHHHHHHH
36.897481477
621AcetylationFKAIAHFKRTTFLKK
HHHHHHHHHHHHHHH
38.6825953088
638AcetylationMLGRLKYKVTPQMGT
HHCCCEEEECCCCCC
37.7423236377
640PhosphorylationGRLKYKVTPQMGTPS
CCCEEEECCCCCCCC
12.0321712546
645PhosphorylationKVTPQMGTPSPGKGS
EECCCCCCCCCCCCC
18.4325159151
647PhosphorylationTPQMGTPSPGKGSLT
CCCCCCCCCCCCCCC
46.2325849741
650AcetylationMGTPSPGKGSLTDGR
CCCCCCCCCCCCCCC
49.0323236377
652PhosphorylationTPSPGKGSLTDGRIK
CCCCCCCCCCCCCCC
31.4221712546
654PhosphorylationSPGKGSLTDGRIKPD
CCCCCCCCCCCCCCC
37.80-
673SumoylationTEIKINIKQESADVN
CEEEEEEEEECCCEE
43.45-
673SumoylationTEIKINIKQESADVN
CEEEEEEEEECCCEE
43.4528112733
728PhosphorylationSVIEFGKYEIQTWYS
CCEEECCEEEEECCC
20.74-
734PhosphorylationKYEIQTWYSSPYPQE
CEEEEECCCCCCHHH
11.5822817900
738PhosphorylationQTWYSSPYPQEYARL
EECCCCCCHHHHHHC
21.3522817900
757PhosphorylationLCEFCLKYMKSKNIL
HHHHHHHHHHHCCEE
9.2319664994
785UbiquitinationANEIYRRKDLSVFEV
HHHHHHCCCCEEEEE
54.7621890473
785 (in isoform 1)Ubiquitination-54.7621890473
815AcetylationAKLFLDHKTLYYDVE
HHHHCCCCCEECCCH
39.633751055
878PhosphorylationRFLIDFSYLLSRREG
HHHHHHHHHHHCCCC
16.2019702290
889PhosphorylationRREGQAGSPEKPLSD
CCCCCCCCCCCCHHH
32.6630266825
892AcetylationGQAGSPEKPLSDLGR
CCCCCCCCCHHHHHH
55.4325953088
895PhosphorylationGSPEKPLSDLGRLSY
CCCCCCHHHHHHHHH
39.0430266825
923PhosphorylationHHHERHISIKAISRA
HHCHHCCCHHHHHHH
16.3524719451
970UbiquitinationLILSHMEKLKTCSRA
HHHHHHHHHHCCCCC
47.94-
993PhosphorylationRWTPILISNAAVSEE
CCCEEEEECCCCCHH
19.5728102081
998PhosphorylationLISNAAVSEEEREAE
EEECCCCCHHHHHHH
46.4830108239
1027PhosphorylationKEEQEILSTRANSRQ
HHHHHHHHHHCCCCC
22.8528985074
1035PhosphorylationTRANSRQSPAKVQSK
HHCCCCCCCHHHHCC
26.2224719451
1038AcetylationNSRQSPAKVQSKNKY
CCCCCCHHHHCCCCC
44.1619608861
1042AcetylationSPAKVQSKNKYLHSP
CCHHHHCCCCCCCCC
40.1319608861
1044AcetylationAKVQSKNKYLHSPES
HHHHCCCCCCCCCCC
53.5819608861
1045PhosphorylationKVQSKNKYLHSPESR
HHHCCCCCCCCCCCC
21.0226657352
1048PhosphorylationSKNKYLHSPESRPVT
CCCCCCCCCCCCCCC
27.9730266825
1051PhosphorylationKYLHSPESRPVTGER
CCCCCCCCCCCCCCH
45.3123403867
1055PhosphorylationSPESRPVTGERGQLL
CCCCCCCCCCHHHHH
35.6923403867
1065PhosphorylationRGQLLELSKESSEEE
HHHHHHHHHCCCHHH
25.6321815630
1114PhosphorylationQSSPPRLTKPQSVAI
HCCCCCCCCCCEEEE
41.79-
1115AcetylationSSPPRLTKPQSVAIK
CCCCCCCCCCEEEEC
45.7323749302
1122AcetylationKPQSVAIKRKRPFVL
CCCEEEECCCCCCEE
41.9725953088
1199AcetylationAFQHQPGKKRQTEEE
HHHCCCCCCCCCCCC
52.0125953088
1228PhosphorylationRNNMNDDSSNLKEGS
CCCCCCCCCCCCCCC
24.8029052541
1229PhosphorylationNNMNDDSSNLKEGSK
CCCCCCCCCCCCCCC
53.8529052541
1236AcetylationSNLKEGSKDNPEPLK
CCCCCCCCCCCCCCC
72.8326051181
1245AcetylationNPEPLKCKQVWPKGT
CCCCCCCCCCCCCCC
46.4223749302
1265MethylationKWRQNKERKTGFKLN
HHHHCCCCCCCCEEE
43.3712018083
1267PhosphorylationRQNKERKTGFKLNLY
HHCCCCCCCCEEEEE
54.8123403867
1274PhosphorylationTGFKLNLYTPPETPM
CCCEEEEECCCCCCC
19.0027732954
1275PhosphorylationGFKLNLYTPPETPME
CCEEEEECCCCCCCC
35.2227732954
1279PhosphorylationNLYTPPETPMEPDEQ
EEECCCCCCCCCCCC
33.4427732954
1295PhosphorylationTVEEQKETSEGKTSP
CHHHHHHCCCCCCCC
38.8323312004
1296PhosphorylationVEEQKETSEGKTSPS
HHHHHHCCCCCCCCC
45.5030576142
1300PhosphorylationKETSEGKTSPSPIRI
HHCCCCCCCCCCCCC
57.6425849741
1301PhosphorylationETSEGKTSPSPIRIE
HCCCCCCCCCCCCCC
27.2030266825
1303PhosphorylationSEGKTSPSPIRIEEE
CCCCCCCCCCCCCHH
32.5030266825
1502PhosphorylationDPEAVPESDEEPPPG
CCCCCCCCCCCCCCC
44.2325159151
1520PhosphorylationQKQDQKNSKEVDTEF
HHHHHCCCHHCCCHH
36.9126074081
1525PhosphorylationKNSKEVDTEFKEGNP
CCCHHCCCHHHCCCC
48.8026074081
1571PhosphorylationETQEACRSLQNYTRA
HHHHHHHHHHHHCCC
33.9024719451
1581PhosphorylationNYTRADQSPQIATTL
HHCCCCCCCCCCCCH
21.2221082442
1586PhosphorylationDQSPQIATTLDDCQQ
CCCCCCCCCHHHHHH
29.5330108239
1587PhosphorylationQSPQIATTLDDCQQS
CCCCCCCCHHHHHHC
21.1130108239
1594PhosphorylationTLDDCQQSDHSSPVS
CHHHHHHCCCCCCCC
16.0630576142
1597PhosphorylationDCQQSDHSSPVSSVH
HHHHCCCCCCCCCCC
41.1330108239
1598PhosphorylationCQQSDHSSPVSSVHS
HHHCCCCCCCCCCCC
26.3830108239
1601PhosphorylationSDHSSPVSSVHSHPG
CCCCCCCCCCCCCCC
29.9930108239
1602PhosphorylationDHSSPVSSVHSHPGQ
CCCCCCCCCCCCCCC
24.8830108239
1605PhosphorylationSPVSSVHSHPGQSVR
CCCCCCCCCCCCCCC
29.2630108239
1610PhosphorylationVHSHPGQSVRSVNSP
CCCCCCCCCCCCCCC
25.9730108239
1750PhosphorylationPPTCSVKSPQGCVVE
CCCCCCCCCCCCEEE
21.9428348404
1903PhosphorylationLQRNMAASNIGISHS
HHHHHHHHHCCCCHH
21.31-
1915PhosphorylationSHSQRLQTQIASKGH
CHHHHHHHHHHHCCC
26.9122817900
1924PhosphorylationIASKGHISMRTKSAS
HHHCCCEEEEECCCC
9.13-
1928AcetylationGHISMRTKSASLSPA
CCEEEEECCCCCCHH
33.3926051181
1929PhosphorylationHISMRTKSASLSPAA
CEEEEECCCCCCHHH
23.6028555341
1933PhosphorylationRTKSASLSPAAATHQ
EECCCCCCHHHHHCH
15.2527251275
1938PhosphorylationSLSPAAATHQSQIYG
CCCHHHHHCHHHHHC
18.7430631047
1941PhosphorylationPAAATHQSQIYGRSQ
HHHHHCHHHHHCCCC
15.7930631047
1947PhosphorylationQSQIYGRSQTVAMQG
HHHHHCCCCEEEECC
26.32-
2065PhosphorylationNTGMSKQSLNGSYMR
CCCCCCCCCCCCCCC
27.7820068231
2069PhosphorylationSKQSLNGSYMRR---
CCCCCCCCCCCC---
18.0620068231
2070PhosphorylationKQSLNGSYMRR----
CCCCCCCCCCC----
8.9520068231

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

Oops, there are no upstream regulatory protein records of KAT6B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
815KAcetylation

10497217

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 KAT6B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUNX2_HUMANRUNX2physical
11965546
RUNX1_HUMANRUNX1physical
11965546
H31T_HUMANHIST3H3physical
23063713

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=A chromosomal aberration involving KAT6B may be a cause acute myeloid leukemias. Translocation t(10
16)(q22
p13) with CREBBP.
603736
606170Genitopatellar syndrome (GTPTS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KAT6B_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-440; LYS-1038; LYS-1042 ANDLYS-1044, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, 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 THR-1915, AND MASSSPECTROMETRY.

TOP