| UniProt ID | KAT2B_HUMAN | |
|---|---|---|
| UniProt AC | Q92831 | |
| Protein Name | Histone acetyltransferase KAT2B | |
| Gene Name | KAT2B {ECO:0000303|PubMed:27796307, ECO:0000312|HGNC:HGNC:8638} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 832 | |
| Subcellular Localization | Nucleus . 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 | Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY, PLK4 and TBX5. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5. [PubMed: 29174768 Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4] | |
| Protein Sequence | MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 49 | Phosphorylation | CAAAAGGSGACGPAT CCHHCCCCCCCCHHH | 23.46 | - | |
| 72 | Phosphorylation | EGPGGGGSARIAVKK CCCCCCHHHHHHHHH | 20.04 | - | |
| 78 | Methylation | GSARIAVKKAQLRSA HHHHHHHHHHHHHCC | 33.11 | 19351588 | |
| 78 | Acetylation | GSARIAVKKAQLRSA HHHHHHHHHHHHHCC | 33.11 | 20167786 | |
| 79 | Acetylation | SARIAVKKAQLRSAP HHHHHHHHHHHHCCC | 34.46 | 20167786 | |
| 89 | Methylation | LRSAPRAKKLEKLGV HHCCCCHHHHHHHCC | 60.20 | 19351588 | |
| 117 | Phosphorylation | GWKNPNPSPTPPRAD CCCCCCCCCCCCCCH | 48.31 | 25849741 | |
| 119 | Phosphorylation | KNPNPSPTPPRADLQ CCCCCCCCCCCCHHH | 50.71 | 25849741 | |
| 131 | Phosphorylation | DLQQIIVSLTESCRS HHHHHHHHHHHHHHH | 21.11 | 28122231 | |
| 197 | Phosphorylation | LFKLLRKSILQRGKP HHHHHHHHHHHCCCC | 23.30 | 23532336 | |
| 270 | Phosphorylation | PSQRRLRSPNDDISG CCHHCCCCCCCCCCC | 32.42 | - | |
| 276 | Phosphorylation | RSPNDDISGYKENYT CCCCCCCCCCHHHHH | 42.96 | - | |
| 301 | Phosphorylation | FCDSLPRYETTQVFG HHHCCCCCCHHHHHH | 18.71 | - | |
| 303 | Phosphorylation | DSLPRYETTQVFGRT HCCCCCCHHHHHHHH | 17.37 | 24719451 | |
| 310 | Phosphorylation | TTQVFGRTLLRSVFT HHHHHHHHHHHHHHH | 30.44 | 24719451 | |
| 314 | Phosphorylation | FGRTLLRSVFTVMRR HHHHHHHHHHHHHHH | 22.88 | - | |
| 317 | Phosphorylation | TLLRSVFTVMRRQLL HHHHHHHHHHHHHHH | 15.96 | - | |
| 416 | Acetylation | GSSSPACKASSGLEA CCCCCCHHHHCCCCC | 54.10 | 12888487 | |
| 428 | Acetylation | LEANPGEKRKMTDSH CCCCCCCCCCCCHHH | 64.33 | 12888487 | |
| 430 | Acetylation | ANPGEKRKMTDSHVL CCCCCCCCCCHHHHH | 58.16 | 12888487 | |
| 441 | Acetylation | SHVLEEAKKPRVMGD HHHHHHHCCCCCCCC | 67.59 | 12888487 | |
| 442 | Acetylation | HVLEEAKKPRVMGDI HHHHHHCCCCCCCCC | 45.14 | 12888487 | |
| 533 | Phosphorylation | LPRMPKEYITRLVFD CCCCCHHHHHHHHCC | 17.45 | 23312004 | |
| 535 | Phosphorylation | RMPKEYITRLVFDPK CCCHHHHHHHHCCCC | 19.63 | 23312004 | |
| 550 | Ubiquitination | HKTLALIKDGRVIGG CCEEEEEECCEEEEE | 55.79 | - | |
| 638 | Ubiquitination | TKYVGYIKDYEGATL CCEEEEEECCCCCEE | 45.86 | - | |
| 638 | Methylation | TKYVGYIKDYEGATL CCEEEEEECCCCCEE | 45.86 | 19351588 | |
| 671 | Methylation | KKQKEIIKKLIERKQ HHHHHHHHHHHHHHH | 47.38 | - | |
| 672 | Methylation | KQKEIIKKLIERKQA HHHHHHHHHHHHHHH | 44.26 | - | |
| 683 | Ubiquitination | RKQAQIRKVYPGLSC HHHHHHHHHCCCCCC | 47.99 | - | |
| 685 | Phosphorylation | QAQIRKVYPGLSCFK HHHHHHHCCCCCCCC | 8.46 | 29496907 | |
| 692 | Methylation | YPGLSCFKDGVRQIP CCCCCCCCCCCCCCC | 58.88 | 19351588 | |
| 729 | Phosphorylation | PRDPDQLYSTLKSIL CCCHHHHHHHHHHHH | 8.25 | 17360941 | |
| 730 | Phosphorylation | RDPDQLYSTLKSILQ CCHHHHHHHHHHHHH | 35.54 | 29978859 | |
| 731 | Phosphorylation | DPDQLYSTLKSILQQ CHHHHHHHHHHHHHH | 25.34 | 29978859 | |
| 733 | Acetylation | DQLYSTLKSILQQVK HHHHHHHHHHHHHHH | 35.22 | 19608861 | |
| 734 | Phosphorylation | QLYSTLKSILQQVKS HHHHHHHHHHHHHHH | 31.48 | 29978859 | |
| 753 | Acetylation | WPFMEPVKRTEAPGY CCCCCCCCCCCCCCC | 65.40 | 25953088 | |
| 781 | Phosphorylation | SERLKNRYYVSKKLF HHHHHHHHHHCHHHH | 20.01 | 23403867 | |
| 802 | Phosphorylation | VFTNCKEYNPPESEY HHHCCHHHCCCHHHH | 20.61 | - | |
| 807 | Phosphorylation | KEYNPPESEYYKCAN HHHCCCHHHHHHHHH | 36.35 | - | |
| 809 | Phosphorylation | YNPPESEYYKCANIL HCCCHHHHHHHHHHH | 19.94 | - | |
| 810 | Phosphorylation | NPPESEYYKCANILE CCCHHHHHHHHHHHH | 8.78 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KAT2B_HUMAN !! | ||||||
* 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 KAT2B_HUMAN !! | ||||||
| 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. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "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-733, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "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-729, AND MASSSPECTROMETRY. | |
