UniProt ID | HDAC5_HUMAN | |
---|---|---|
UniProt AC | Q9UQL6 | |
Protein Name | Histone deacetylase 5 | |
Gene Name | HDAC5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1122 | |
Subcellular Localization | Nucleus. Cytoplasm. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its p | |
Protein Description | Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.. | |
Protein Sequence | MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL | |
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 |
---|---|---|---|---|---|
3 (in isoform 3) | Phosphorylation | - | 40.75 | 22210691 | |
3 | Phosphorylation | -----MNSPNESDGM -----CCCCCCCCCC | 40.75 | 21081666 | |
7 (in isoform 3) | Phosphorylation | - | 46.21 | 24043423 | |
7 | Phosphorylation | -MNSPNESDGMSGRE -CCCCCCCCCCCCCC | 46.21 | 21081666 | |
12 (in isoform 3) | Phosphorylation | - | 29.13 | 24043423 | |
16 | Phosphorylation | GMSGREPSLEILPRT CCCCCCCCCEECCCC | 33.60 | 22210691 | |
23 | Phosphorylation | SLEILPRTSLHSIPV CCEECCCCCCCCCCE | 33.43 | 27251275 | |
24 | Phosphorylation | LEILPRTSLHSIPVT CEECCCCCCCCCCEE | 25.93 | 28555341 | |
25 | Phosphorylation | EILPRTSLHSIPVTV EECCCCCCCCCCEEE | 3.48 | 27251275 | |
32 (in isoform 3) | Phosphorylation | - | 8.95 | 22210691 | |
35 | Sumoylation | IPVTVEVKPVLPRAM CCEEEEEECCCCCCC | 18.86 | 28112733 | |
35 | Sumoylation | IPVTVEVKPVLPRAM CCEEEEEECCCCCCC | 18.86 | - | |
44 | Phosphorylation | VLPRAMPSSMGGGGG CCCCCCCCCCCCCCC | 21.63 | 29214152 | |
45 | Phosphorylation | LPRAMPSSMGGGGGG CCCCCCCCCCCCCCC | 18.64 | 24043423 | |
53 | Phosphorylation | MGGGGGGSPSPVELR CCCCCCCCCCCHHHH | 26.02 | 25850435 | |
54 | Phosphorylation | GGGGGGSPSPVELRG CCCCCCCCCCHHHHH | 46.02 | 24719451 | |
55 | Phosphorylation | GGGGGSPSPVELRGA CCCCCCCCCHHHHHH | 43.18 | 25850435 | |
56 | Phosphorylation | GGGGSPSPVELRGAL CCCCCCCCHHHHHHH | 27.30 | 27251275 | |
66 | Phosphorylation | LRGALVGSVDPTLRE HHHHHHCCCCHHHHH | 18.83 | 21081666 | |
70 | Phosphorylation | LVGSVDPTLREQQLQ HHCCCCHHHHHHHHH | 33.70 | - | |
84 | Ubiquitination | QQELLALKQQQQLQK HHHHHHHHHHHHHHH | 40.22 | 29967540 | |
85 | Ubiquitination | QELLALKQQQQLQKQ HHHHHHHHHHHHHHH | 47.36 | 29967540 | |
115 | Ubiquitination | QHEVQLQKHLKQQQE HHHHHHHHHHHHHHH | 60.54 | 29967540 | |
116 | Ubiquitination | HEVQLQKHLKQQQEM HHHHHHHHHHHHHHH | 25.87 | 29967540 | |
136 | Ubiquitination | QQEMLAAKRQQELEQ HHHHHHHHHHHHHHH | 45.17 | 29967540 | |
137 | Ubiquitination | QEMLAAKRQQELEQQ HHHHHHHHHHHHHHH | 38.39 | 29967540 | |
180 | Phosphorylation | SKESAIASTEVKLRL CHHHHHCHHHHHHHH | 20.98 | - | |
181 | Phosphorylation | KESAIASTEVKLRLQ HHHHHCHHHHHHHHH | 35.46 | - | |
199 | Phosphorylation | LSKSKEPTPGGLNHS HHCCCCCCCCCCCCC | 35.34 | 28787133 | |
206 | Phosphorylation | TPGGLNHSLPQHPKC CCCCCCCCCCCCCCC | 40.44 | 21081666 | |
220 | Phosphorylation | CWGAHHASLDQSSPP CCCCCCCCCCCCCCC | 28.28 | 27080861 | |
221 | Phosphorylation | WGAHHASLDQSSPPQ CCCCCCCCCCCCCCC | 7.83 | 27251275 | |
224 | Phosphorylation | HHASLDQSSPPQSGP CCCCCCCCCCCCCCC | 44.47 | 27080861 | |
225 | Phosphorylation | HASLDQSSPPQSGPP CCCCCCCCCCCCCCC | 34.66 | 27080861 | |
229 | Phosphorylation | DQSSPPQSGPPGTPP CCCCCCCCCCCCCCC | 60.07 | 27080861 | |
234 | Phosphorylation | PQSGPPGTPPSYKLP CCCCCCCCCCCCCCC | 37.49 | 27251275 | |
256 | Ubiquitination | RDDFPLRKTASEPNL CCCCCCCCCCCCCCH | 57.01 | - | |
257 | Phosphorylation | DDFPLRKTASEPNLK CCCCCCCCCCCCCHH | 29.05 | 30183078 | |
259 | Phosphorylation | FPLRKTASEPNLKVR CCCCCCCCCCCHHHH | 59.84 | 25159151 | |
260 | Phosphorylation | PLRKTASEPNLKVRS CCCCCCCCCCHHHHH | 35.43 | 24719451 | |
278 | Phosphorylation | QKVAERRSSPLLRRK HHHHHHCCCCCHHCC | 42.39 | 25159151 | |
279 | Phosphorylation | KVAERRSSPLLRRKD HHHHHCCCCCHHCCC | 20.11 | 26846344 | |
288 | Phosphorylation | LLRRKDGTVISTFKK CHHCCCCCEEECCCC | 25.46 | - | |
291 | Phosphorylation | RKDGTVISTFKKRAV CCCCCEEECCCCCEE | 24.37 | - | |
292 | Phosphorylation | KDGTVISTFKKRAVE CCCCEEECCCCCEEE | 28.49 | 20188095 | |
368 | Phosphorylation | FSLYTSPSLPNISLG EEEEECCCCCCCEEE | 57.11 | 21081666 | |
458 | Phosphorylation | LEQARQQSTLIAVPL HHHHHHCCCEEEEEC | 19.49 | 24043423 | |
459 | Phosphorylation | EQARQQSTLIAVPLH HHHHHCCCEEEEECC | 20.18 | 24043423 | |
469 | Phosphorylation | AVPLHGQSPLVTGER EEECCCCCCCCCCCH | 25.46 | 21712546 | |
473 | Phosphorylation | HGQSPLVTGERVATS CCCCCCCCCCHHHCC | 40.79 | 24043423 | |
479 | Phosphorylation | VTGERVATSMRTVGK CCCCHHHCCCCCCCC | 21.87 | 24043423 | |
480 | Phosphorylation | TGERVATSMRTVGKL CCCHHHCCCCCCCCC | 9.13 | 24043423 | |
496 | Phosphorylation | RHRPLSRTQSSPLPQ CCCCCCCCCCCCCCC | 29.44 | 30266825 | |
498 | Phosphorylation | RPLSRTQSSPLPQSP CCCCCCCCCCCCCCH | 33.05 | 30266825 | |
499 | Phosphorylation | PLSRTQSSPLPQSPQ CCCCCCCCCCCCCHH | 22.19 | 30266825 | |
500 | Phosphorylation | LSRTQSSPLPQSPQA CCCCCCCCCCCCHHH | 53.99 | 27251275 | |
504 | Phosphorylation | QSSPLPQSPQALQQL CCCCCCCCHHHHHHH | 19.62 | 30266825 | |
533 | Sumoylation | QQQLQLGKILTKTGE HHHHHHHHHHHHCCC | 43.04 | - | |
533 | Acetylation | QQQLQLGKILTKTGE HHHHHHHHHHHHCCC | 43.04 | 19608861 | |
533 | Sumoylation | QQQLQLGKILTKTGE HHHHHHHHHHHHCCC | 43.04 | 19608861 | |
534 | Acetylation | QQLQLGKILTKTGEL HHHHHHHHHHHCCCC | 5.84 | 19608861 | |
537 | Ubiquitination | QLGKILTKTGELPRQ HHHHHHHHCCCCCCC | 51.60 | 29967540 | |
538 | Ubiquitination | LGKILTKTGELPRQP HHHHHHHCCCCCCCC | 30.56 | 29967540 | |
546 | Phosphorylation | GELPRQPTTHPEETE CCCCCCCCCCHHHCH | 29.42 | 20736484 | |
547 | Phosphorylation | ELPRQPTTHPEETEE CCCCCCCCCHHHCHH | 41.96 | - | |
605 | Sumoylation | EEDCIQVKDEEGESG HHCCEEEECCCCCCC | 42.94 | - | |
611 | Phosphorylation | VKDEEGESGAEEGPD EECCCCCCCCCCCCC | 54.91 | 23927012 | |
612 | Phosphorylation | KDEEGESGAEEGPDL ECCCCCCCCCCCCCC | 32.48 | 24719451 | |
650 | Phosphorylation | QAPLSLATVPHQALG ECCCCCCCCCHHHCC | 39.60 | 29514088 | |
659 | Phosphorylation | PHQALGRTQSSPAAP CHHHCCCCCCCCCCC | 30.88 | 22115753 | |
661 | Phosphorylation | QALGRTQSSPAAPGG HHCCCCCCCCCCCCC | 37.36 | 23401153 | |
662 | Phosphorylation | ALGRTQSSPAAPGGM HCCCCCCCCCCCCCC | 14.56 | 22115753 | |
671 | Phosphorylation | AAPGGMKSPPDQPVK CCCCCCCCCCCCCCC | 32.54 | 28985074 | |
713 | Phosphorylation | EHAGRIQSIWSRLQE HHHHHHHHHHHHHHH | 24.53 | 28857561 | |
725 | Phosphorylation | LQETGLLSKCERIRG HHHHCCHHHHHHHCC | 40.06 | 24719451 | |
755 | Phosphorylation | HTLLYGTSPLNRQKL HHHHHCCCCCCHHHC | 24.03 | 21081666 | |
776 | Phosphorylation | GPISQKMYAVLPCGG HCHHHCEEEEEECCC | 10.70 | - | |
798 | Phosphorylation | VWNEMHSSSAVRMAV HHHHHCCHHHHHHHH | 13.98 | - | |
799 | Phosphorylation | WNEMHSSSAVRMAVG HHHHCCHHHHHHHHH | 33.52 | - | |
1046 | Phosphorylation | PNINAVATLEKVIEI CCCCCEEEHHHHHHH | 28.93 | 24719451 | |
1071 | Phosphorylation | FAAGLGRSLREAQAG HHHHHCHHHHHHHCC | 29.94 | - | |
1108 | Phosphorylation | AAAAREHSPRPAEEP HHHHHHCCCCCCCCC | 20.18 | 23401153 | |
1109 | Phosphorylation | AAAREHSPRPAEEPM HHHHHCCCCCCCCCC | 48.45 | 24719451 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
259 | S | Phosphorylation | Kinase | AMPK-FAMILY | - | GPS |
259 | S | Phosphorylation | Kinase | MAP3K7 | O43318 | GPS |
259 | S | Phosphorylation | Kinase | MARK2 | Q7KZI7 | PSP |
259 | S | Phosphorylation | Kinase | PRKD1 | Q15139 | Uniprot |
259 | S | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
259 | S | Phosphorylation | Kinase | SIK1 | P57059 | Uniprot |
259 | S | Phosphorylation | Kinase | KKCC1 | Q8N5S9 | PhosphoELM |
259 | S | Phosphorylation | Kinase | CAMK4 | Q16566 | PSP |
259 | S | Phosphorylation | Kinase | QIK | Q9H0K1 | PSP |
259 | S | Phosphorylation | Kinase | CAMK2A | Q9UQM7 | PSP |
259 | S | Phosphorylation | Kinase | CAMK1A | Q14012 | PSP |
259 | S | Phosphorylation | Kinase | CAMK1-FAMILY | - | GPS |
259 | S | Phosphorylation | Kinase | PRKAA2 | P54646 | GPS |
259 | S | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
259 | S | Phosphorylation | Kinase | AMPK | Q9Y478 | Uniprot |
278 | S | Phosphorylation | Kinase | AURKB | Q96GD4 | GPS |
279 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
279 | S | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
279 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
292 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
292 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
292 | T | Phosphorylation | Kinase | PKN1 | Q16512 | PSP |
498 | S | Phosphorylation | Kinase | PRKD3 | O94806 | PSP |
498 | S | Phosphorylation | Kinase | PRKD2 | Q9BZL6 | PSP |
498 | S | Phosphorylation | Kinase | PRKD1 | Q15139 | Uniprot |
498 | S | Phosphorylation | Kinase | KKCC1 | Q8N5S9 | PhosphoELM |
498 | S | Phosphorylation | Kinase | SIK1 | P57059 | Uniprot |
498 | S | Phosphorylation | Kinase | CAMK4 | Q16566 | PSP |
498 | S | Phosphorylation | Kinase | CAMK2A | Q9UQM7 | PSP |
498 | S | Phosphorylation | Kinase | AMPK-FAMILY | - | GPS |
498 | S | Phosphorylation | Kinase | CAMK1-FAMILY | - | GPS |
498 | S | Phosphorylation | Kinase | CAMK1A | Q14012 | PSP |
498 | S | Phosphorylation | Kinase | PRKAA2 | P54646 | GPS |
498 | S | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
498 | S | Phosphorylation | Kinase | AMPK | Q9Y478 | Uniprot |
* 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 HDAC5_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-533, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, AND MASSSPECTROMETRY. | |
"Protein kinase D-dependent phosphorylation and nuclear export ofhistone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis."; Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K.,McKinsey T.A., Olson E.N., Jin Z.G.; J. Biol. Chem. 283:14590-14599(2008). Cited for: PHOSPHORYLATION AT SER-259 AND SER-498. | |
"AMP-activated protein kinase regulates GLUT4 transcription byphosphorylating histone deacetylase 5."; McGee S.L., van Denderen B.J., Howlett K.F., Mollica J.,Schertzer J.D., Kemp B.E., Hargreaves M.; Diabetes 57:860-867(2008). Cited for: PHOSPHORYLATION AT SER-259 AND SER-498, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-259 AND SER-498. | |
"Activation of the myocyte enhancer factor-2 transcription factor bycalcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5."; McKinsey T.A., Zhang C.-L., Olson E.N.; Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000). Cited for: INTERACTION WITH 14-3-3, AND PHOSPHORYLATION AT SER-259 AND SER-498. | |
"Protein kinase C-related kinase targets nuclear localization signalsin a subset of class IIa histone deacetylases."; Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,McKinsey T.A.; FEBS Lett. 584:1103-1110(2010). Cited for: PHOSPHORYLATION AT THR-292, AND MUTAGENESIS OF SER-259; SER-291 ANDTHR-292. |