UniProt ID | HDAC6_HUMAN | |
---|---|---|
UniProt AC | Q9UBN7 | |
Protein Name | Histone deacetylase 6 | |
Gene Name | HDAC6 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1215 | |
Subcellular Localization | Nucleus. Cytoplasm. Perikaryon. Cell projection, dendrite. Cell projection, axon. It is mainly cytoplasmic, where it is associated with microtubules. | |
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 (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.; In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.. | |
Protein Sequence | MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
16 | Phosphorylation | TTTRQRRSRQNPQSP HHHHHHHHCCCCCCC | 40.17 | 23403867 | |
22 | Phosphorylation | RSRQNPQSPPQDSSV HHCCCCCCCCCCCCC | 39.54 | 29255136 | |
27 | Phosphorylation | PQSPPQDSSVTSKRN CCCCCCCCCCCCHHH | 22.81 | 30266825 | |
28 | Phosphorylation | QSPPQDSSVTSKRNI CCCCCCCCCCCHHHH | 37.39 | 30266825 | |
30 | Phosphorylation | PPQDSSVTSKRNIKK CCCCCCCCCHHHHCC | 30.40 | 30266825 | |
31 | Phosphorylation | PQDSSVTSKRNIKKG CCCCCCCCHHHHCCC | 27.71 | 30266825 | |
32 | Ubiquitination | QDSSVTSKRNIKKGA CCCCCCCHHHHCCCC | 39.85 | - | |
32 | Acetylation | QDSSVTSKRNIKKGA CCCCCCCHHHHCCCC | 39.85 | 22438583 | |
33 | Methylation | DSSVTSKRNIKKGAV CCCCCCHHHHCCCCC | 50.28 | - | |
36 | Acetylation | VTSKRNIKKGAVPRS CCCHHHHCCCCCCCC | 49.02 | 22438583 | |
37 | Acetylation | TSKRNIKKGAVPRSI CCHHHHCCCCCCCCC | 48.59 | 22438583 | |
43 | Phosphorylation | KKGAVPRSIPNLAEV CCCCCCCCCCCHHHH | 36.01 | 25159151 | |
51 | Acetylation | IPNLAEVKKKGKMKK CCCHHHHHHHCHHHH | 40.03 | 22438583 | |
51 | Ubiquitination | IPNLAEVKKKGKMKK CCCHHHHHHHCHHHH | 40.03 | - | |
52 | Acetylation | PNLAEVKKKGKMKKL CCHHHHHHHCHHHHH | 72.44 | 22438583 | |
53 | Acetylation | NLAEVKKKGKMKKLG CHHHHHHHCHHHHHH | 59.03 | 22438583 | |
55 | Acetylation | AEVKKKGKMKKLGQA HHHHHHCHHHHHHHH | 57.32 | 22438583 | |
57 | Acetylation | VKKKGKMKKLGQAME HHHHCHHHHHHHHHH | 48.62 | 22438583 | |
58 | Acetylation | KKKGKMKKLGQAMEE HHHCHHHHHHHHHHH | 55.11 | 22438583 | |
116 | Ubiquitination | PERLHAIKEQLIQEG HHHHHHHHHHHHHCC | 39.94 | 2190698 | |
130 | Ubiquitination | GLLDRCVSFQARFAE CCHHHHHHHHHHHCC | 18.44 | 21906983 | |
146 | Phosphorylation | EELMLVHSLEYIDLM HHHHHHEEHHHEEHH | 18.54 | - | |
381 | Phosphorylation | AGGKLILSLEGGYNL HCCEEEEEECCCCHH | 19.85 | 29083192 | |
386 | Phosphorylation | ILSLEGGYNLRALAE EEEECCCCHHHHHHH | 23.14 | 29083192 | |
412 | Phosphorylation | DPCPMLESPGAPCRS CCCCCCCCCCCCCCC | 25.36 | 28348404 | |
458 | Phosphorylation | EEDNVEESEEEGPWE CCCCCCCCCCCCCCC | 36.48 | 21486957 | |
525 | Phosphorylation | GLAGRCLTLTPRPAT CCCCEEEECCCCCCC | 32.01 | 28348404 | |
527 | Phosphorylation | AGRCLTLTPRPATEA CCEEEECCCCCCCHH | 16.41 | 24719451 | |
538 | Phosphorylation | ATEAELLTCHSAEYV CCHHHHHHCCCHHHH | 22.31 | 28796482 | |
541 | Phosphorylation | AELLTCHSAEYVGHL HHHHHCCCHHHHCHH | 25.58 | 28796482 | |
544 | Phosphorylation | LTCHSAEYVGHLRAT HHCCCHHHHCHHHHH | 16.08 | 28796482 | |
551 | Phosphorylation | YVGHLRATEKMKTRE HHCHHHHHHHCHHHH | 29.70 | 24719451 | |
553 | Acetylation | GHLRATEKMKTRELH CHHHHHHHCHHHHHH | 41.14 | 22438583 | |
555 | Acetylation | LRATEKMKTRELHRE HHHHHHCHHHHHHHH | 56.34 | 22438583 | |
556 | Phosphorylation | RATEKMKTRELHRES HHHHHCHHHHHHHHC | 26.36 | 22210691 | |
570 | Phosphorylation | SSNFDSIYICPSTFA CCCCCEEEECCHHHH | 10.62 | 20029029 | |
807 | Phosphorylation | GDPPPLLTLPRPPLS CCCCCCCCCCCCCCC | 42.26 | 24719451 | |
846 | Phosphorylation | VEDREGPSSSKLVTK EECCCCCCCCCCEEC | 59.09 | - | |
847 | Phosphorylation | EDREGPSSSKLVTKK ECCCCCCCCCCEECC | 34.33 | - | |
849 | Ubiquitination | REGPSSSKLVTKKAP CCCCCCCCCEECCCC | 49.26 | - | |
849 | Acetylation | REGPSSSKLVTKKAP CCCCCCCCCEECCCC | 49.26 | 25953088 | |
853 | Acetylation | SSSKLVTKKAPQPAK CCCCCEECCCCCCCC | 39.18 | 22438583 | |
854 | Ubiquitination | SSKLVTKKAPQPAKP CCCCEECCCCCCCCC | 56.80 | - | |
854 | Acetylation | SSKLVTKKAPQPAKP CCCCEECCCCCCCCC | 56.80 | 22438583 | |
860 | Ubiquitination | KKAPQPAKPRLAERM CCCCCCCCCHHHHHC | 37.04 | - | |
868 | Phosphorylation | PRLAERMTTREKKVL CHHHHHCCHHHHHHH | 28.99 | 30108239 | |
869 | Phosphorylation | RLAERMTTREKKVLE HHHHHCCHHHHHHHH | 27.73 | 30108239 | |
872 | Acetylation | ERMTTREKKVLEAGM HHCCHHHHHHHHHCC | 44.91 | 22438583 | |
873 | Acetylation | RMTTREKKVLEAGMG HCCHHHHHHHHHCCC | 47.50 | 22438583 | |
881 | Acetylation | VLEAGMGKVTSASFG HHHHCCCEEEEECCC | 33.19 | 22424773 | |
883 | Phosphorylation | EAGMGKVTSASFGEE HHCCCEEEEECCCCC | 23.28 | 24275569 | |
886 | Phosphorylation | MGKVTSASFGEESTP CCEEEEECCCCCCCC | 33.29 | 22468782 | |
915 | Phosphorylation | DQPSEAATGGATLAQ CCCCHHCCCCCHHHH | 43.10 | 24275569 | |
919 | Phosphorylation | EAATGGATLAQTISE HHCCCCCHHHHHHHH | 26.38 | 24275569 | |
923 | Phosphorylation | GGATLAQTISEAAIG CCCHHHHHHHHHHHC | 22.36 | 24275569 | |
925 | Phosphorylation | ATLAQTISEAAIGGA CHHHHHHHHHHHCCH | 25.27 | 24275569 | |
993 | Phosphorylation | GGATLAQTTSEAAME CCCCEEEHHHHHHHC | 27.04 | 24275569 | |
994 | Phosphorylation | GATLAQTTSEAAMEG CCCEEEHHHHHHHCC | 16.70 | 24275569 | |
995 | Phosphorylation | ATLAQTTSEAAMEGA CCEEEHHHHHHHCCC | 28.73 | 24275569 | |
1003 | Phosphorylation | EAAMEGATLDQTTSE HHHHCCCCCCCCCCC | 41.55 | 24275569 | |
1007 | Phosphorylation | EGATLDQTTSEEAPG CCCCCCCCCCCCCCC | 31.77 | 24275569 | |
1016 | Phosphorylation | SEEAPGGTELIQTPL CCCCCCCCEEEECCC | 33.27 | 24275569 | |
1021 | Phosphorylation | GGTELIQTPLASSTD CCCEEEECCCCCCCC | 17.18 | 24275569 | |
1025 | Phosphorylation | LIQTPLASSTDHQTP EEECCCCCCCCCCCC | 41.26 | 26074081 | |
1026 | Phosphorylation | IQTPLASSTDHQTPP EECCCCCCCCCCCCC | 32.04 | 26074081 | |
1027 | Phosphorylation | QTPLASSTDHQTPPT ECCCCCCCCCCCCCC | 34.70 | 26074081 | |
1031 | Phosphorylation | ASSTDHQTPPTSPVQ CCCCCCCCCCCCCCC | 28.02 | 26657352 | |
1034 | Phosphorylation | TDHQTPPTSPVQGTT CCCCCCCCCCCCCCC | 47.03 | 26657352 | |
1035 | Phosphorylation | DHQTPPTSPVQGTTP CCCCCCCCCCCCCCC | 28.93 | 26657352 | |
1040 | Phosphorylation | PTSPVQGTTPQISPS CCCCCCCCCCCCCHH | 20.43 | 12354939 | |
1041 | Phosphorylation | TSPVQGTTPQISPST CCCCCCCCCCCCHHH | 21.74 | 24275569 | |
1047 | Phosphorylation | TTPQISPSTLIGSLR CCCCCCHHHHHHHEE | 29.11 | 24275569 | |
1048 | Phosphorylation | TPQISPSTLIGSLRT CCCCCHHHHHHHEEE | 26.27 | 24275569 | |
1052 | Phosphorylation | SPSTLIGSLRTLELG CHHHHHHHEEEEECC | 14.00 | 24719451 | |
1055 | Phosphorylation | TLIGSLRTLELGSES HHHHHEEEEECCCCC | 29.85 | - | |
1062 | Phosphorylation | TLELGSESQGASESQ EEECCCCCCCCCCCC | 35.29 | 28348404 | |
1066 | Phosphorylation | GSESQGASESQAPGE CCCCCCCCCCCCCCC | 44.60 | 28348404 | |
1068 | Phosphorylation | ESQGASESQAPGEEN CCCCCCCCCCCCCCC | 29.19 | 28348404 | |
1206 | Ubiquitination | KNIAHQNKFGEDMPH HCHHHHCCCCCCCCC | 48.45 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
22 | S | Phosphorylation | Kinase | GRK5 | P34947 | PSP |
458 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
458 | S | Phosphorylation | Kinase | CK2A1 | Q60737 | PSP |
458 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
570 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
1031 | T | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
1031 | T | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
1035 | S | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | SPOP | O43791 | PMID:28599312 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HDAC6_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 HDAC6_HUMAN !! |
loading...
Phosphorylation | |
Reference | PubMed |
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, 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-22, AND MASSSPECTROMETRY. | |
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-30, AND MASSSPECTROMETRY. |