HDAC7_HUMAN - dbPTM
HDAC7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC7_HUMAN
UniProt AC Q8WUI4
Protein Name Histone deacetylase 7
Gene Name HDAC7
Organism Homo sapiens (Human).
Sequence Length 952
Subcellular Localization Nucleus. Cytoplasm. In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. Treatment with EDN1 results in shuttling from the nucleus to the perinuclear region. The export to cytopla
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 factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3. [PubMed: 17360565]
Protein Sequence MDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVGPQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPLETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEALLGQRLRLQETSVAPFALPTVSLLPAITLGLPAPARADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEPEAGGTLPSRLQPILLLDPSGSHAPLLTVPGLGPLPFHFAQSLMTTERLSGSGLHWPLSRTRSEPLPPSATAPPPPGPMQPRLEQLKTHVQVIKRSAKPSEKPRLRQIPSAEDLETDGGGPGQVVDDGLEHRELGHGQPEARGPAPLQQHPQVLLWEQQRLAGRLPRGSTGDTVLLPLAQGGHRPLSRAQSSPAAPASLSAPEPASQARVLSSSETPARTLPFTTGLIYDSVMLKHQCSCGDNSRHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQSKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNRVDPLSEEGWKQKPNLNAIRSLEAVIRVHSKYWGCMQRLASCPDSWVPRVPGADKEEVEAVTALASLSVGILAEDRPSEQLVEEEEPMNL
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
3 (in isoform 5)Phosphorylation-4.6427732954
3 (in isoform 7)Phosphorylation-4.6427732954
9 (in isoform 5)Phosphorylation-29.4227732954
9 (in isoform 7)Phosphorylation-29.4227732954
11 (in isoform 2)Phosphorylation-22.3424043423
12 (in isoform 5)Phosphorylation-58.8427732954
12 (in isoform 7)Phosphorylation-58.8427732954
15 (in isoform 2)Phosphorylation-71.5524043423
17 (in isoform 5)Phosphorylation-33.8327732954
17 (in isoform 7)Phosphorylation-33.8327732954
19 (in isoform 5)Phosphorylation-3.7427732954
19 (in isoform 7)Phosphorylation-3.7427732954
21 (in isoform 5)Phosphorylation-12.5427732954
21 (in isoform 7)Phosphorylation-12.5427732954
27 (in isoform 2)Phosphorylation-38.3824043423
42PhosphorylationAGLQQQRSVEPMRLS
HHHHHHCCCCCCCCC		26.8824719451
49PhosphorylationSVEPMRLSMDTPMPE
CCCCCCCCCCCCCCC		12.30-
52PhosphorylationPMRLSMDTPMPELQV
CCCCCCCCCCCCCCC		16.9128348404
76 (in isoform 9)Ubiquitination-56.9921890473
81 (in isoform 5)Phosphorylation-8.8724719451
82PhosphorylationSKRSAVASSVVKQKL
HHHHHHHHHHHHHHH		19.6426074081
83PhosphorylationKRSAVASSVVKQKLA
HHHHHHHHHHHHHHH		22.6126074081
104PhosphorylationQQAALERTVHPNSPG
HHHHHHCCCCCCCCC		17.5030183078
108UbiquitinationLERTVHPNSPGIPYR
HHCCCCCCCCCCCCC		46.0629967540
109PhosphorylationERTVHPNSPGIPYRT
HCCCCCCCCCCCCCC		29.0225159151
109 (in isoform 3)Phosphorylation-29.02-
114PhosphorylationPNSPGIPYRTLEPLE
CCCCCCCCCCCCCCC		17.8221712546
116PhosphorylationSPGIPYRTLEPLETE
CCCCCCCCCCCCCCC		29.6328555341
118UbiquitinationGIPYRTLEPLETEGA
CCCCCCCCCCCCCCH		47.4229967540
125UbiquitinationEPLETEGATRSMLSS
CCCCCCCHHHHHHHH		8.1329967540
128PhosphorylationETEGATRSMLSSFLP
CCCCHHHHHHHHCCC		21.5228555341
131 (in isoform 2)Ubiquitination-15.4821890473
135UbiquitinationSMLSSFLPPVPSLPS
HHHHHCCCCCCCCCC		26.3229967540
148PhosphorylationPSDPPEHFPLRKTVS
CCCCCCCCCCCCCCC		6.0918669648
148 (in isoform 5)Phosphorylation-6.0924719451
148 (in isoform 7)Phosphorylation-6.09-
153PhosphorylationEHFPLRKTVSEPNLK
CCCCCCCCCCCCCCC		23.8830266825
153 (in isoform 5)Phosphorylation-23.8827642862
155PhosphorylationFPLRKTVSEPNLKLR
CCCCCCCCCCCCCCC		53.2025159151
155 (in isoform 3)Phosphorylation-53.2021406692
160SumoylationTVSEPNLKLRYKPKK
CCCCCCCCCCCCCHH		37.24-
181PhosphorylationNPLLRKESAPPSLRR
CCCCCCCCCCHHHHC		49.4626846344
181 (in isoform 3)Phosphorylation-49.4621406692
182UbiquitinationPLLRKESAPPSLRRR
CCCCCCCCCHHHHCC		22.5529967540
185PhosphorylationRKESAPPSLRRRPAE
CCCCCCHHHHCCCCH		33.1930266825
194PhosphorylationRRRPAETLGDSSPSS
HCCCCHHHCCCCCCC		5.5918767875
194 (in isoform 5)Phosphorylation-5.5924719451
194 (in isoform 7)Phosphorylation-5.59-
197PhosphorylationPAETLGDSSPSSSST
CCHHHCCCCCCCCCC		42.2124247654
197 (in isoform 3)Phosphorylation-42.2123663014
198 (in isoform 3)Phosphorylation-33.2823663014
199UbiquitinationETLGDSSPSSSSTPA
HHHCCCCCCCCCCCC		42.0329967540
200 (in isoform 3)Phosphorylation-44.8123663014
201 (in isoform 3)Phosphorylation-31.5223663014
202 (in isoform 3)Phosphorylation-42.4423663014
203 (in isoform 3)Phosphorylation-40.1223663014
204 (in isoform 3)Phosphorylation-25.4823663014
207PhosphorylationSSSSTPASGCSSPND
CCCCCCCCCCCCCCC		41.3523663014
207 (in isoform 3)Phosphorylation-41.3523663014
210 (in isoform 3)Phosphorylation-52.9723663014
211 (in isoform 3)Phosphorylation-31.6223663014
215 (in isoform 3)Phosphorylation-37.8323663014
220PhosphorylationNDSEHGPNPILGSEA
CCCCCCCCCCCCCHH		40.6215738054
220 (in isoform 5)Phosphorylation-40.6224719451
220 (in isoform 7)Phosphorylation-40.62-
236 (in isoform 7)Phosphorylation-45.5523663014
237 (in isoform 7)Phosphorylation-47.8723663014
239 (in isoform 7)Phosphorylation-18.6123663014
240 (in isoform 7)Phosphorylation-11.6423663014
241 (in isoform 7)Phosphorylation-8.0223663014
242 (in isoform 7)Phosphorylation-16.9423663014
243 (in isoform 7)Phosphorylation-8.6523663014
246 (in isoform 3)Phosphorylation-27.59-
246 (in isoform 7)Phosphorylation-27.5923663014
247PhosphorylationVAPFALPTVSLLPAI
CCCCCCCHHHHCHHH		24.47-
249 (in isoform 3)Phosphorylation-27.02-
249 (in isoform 7)Phosphorylation-27.0223663014
250 (in isoform 7)Phosphorylation-6.0423663014
254 (in isoform 7)Phosphorylation-2.8523663014
255PhosphorylationVSLLPAITLGLPAPA
HHHCHHHHCCCCCCC		19.51-
265 (in isoform 10)Ubiquitination-45.5821890473
277MethylationTHPTLGPRGPILGSP
CCCCCCCCCCCCCCC		62.82115478347
283PhosphorylationPRGPILGSPHTPLFL
CCCCCCCCCCCCCCC		15.2926055452
285 (in isoform 7)Phosphorylation-41.64-
286PhosphorylationPILGSPHTPLFLPHG
CCCCCCCCCCCCCCC		25.6826055452
288 (in isoform 7)Phosphorylation-7.86-
301PhosphorylationLEPEAGGTLPSRLQP
CCCCCCCCCCCCCCC		34.2822199227
304PhosphorylationEAGGTLPSRLQPILL
CCCCCCCCCCCCEEE		49.0527080861
319 (in isoform 3)Phosphorylation-9.72-
321 (in isoform 3)Phosphorylation-6.94-
322PhosphorylationSGSHAPLLTVPGLGP
CCCCCCCEECCCCCC		4.4020068231
322 (in isoform 5)Phosphorylation-4.4024719451
325PhosphorylationHAPLLTVPGLGPLPF
CCCCEECCCCCCCCH		27.3620068231
325 (in isoform 5)Phosphorylation-27.3624719451
340PhosphorylationHFAQSLMTTERLSGS
HHHHHHHHCCCCCCC		30.6928634298
341PhosphorylationFAQSLMTTERLSGSG
HHHHHHHCCCCCCCC		12.7328634298
345PhosphorylationLMTTERLSGSGLHWP
HHHCCCCCCCCCCCC		36.8128634298
347PhosphorylationTTERLSGSGLHWPLS
HCCCCCCCCCCCCCC		34.5028634298
354PhosphorylationSGLHWPLSRTRSEPL
CCCCCCCCCCCCCCC		27.7626074081
356PhosphorylationLHWPLSRTRSEPLPP
CCCCCCCCCCCCCCC		34.8623401153
358PhosphorylationWPLSRTRSEPLPPSA
CCCCCCCCCCCCCCC		42.8430266825
358 (in isoform 7)Phosphorylation-42.84-
360 (in isoform 7)Phosphorylation-51.95-
364PhosphorylationRSEPLPPSATAPPPP
CCCCCCCCCCCCCCC		35.9930266825
366PhosphorylationEPLPPSATAPPPPGP
CCCCCCCCCCCCCCC		43.9930266825
368 (in isoform 3)Phosphorylation-37.26-
382SumoylationQPRLEQLKTHVQVIK
CHHHHHHHHHHHHHH		35.96-
391PhosphorylationHVQVIKRSAKPSEKP
HHHHHHHCCCCCCCC		35.33-
395PhosphorylationIKRSAKPSEKPRLRQ
HHHCCCCCCCCCHHC		58.5118669648
395 (in isoform 5)Phosphorylation-58.5124719451
397PhosphorylationRSAKPSEKPRLRQIP
HCCCCCCCCCHHCCC		39.5116956611
397 (in isoform 5)Phosphorylation-39.5127251275
405PhosphorylationPRLRQIPSAEDLETD
CCHHCCCCHHHHCCC		46.0123401153
407 (in isoform 7)Phosphorylation-68.42-
411PhosphorylationPSAEDLETDGGGPGQ
CCHHHHCCCCCCCCC		47.4430266825
444PhosphorylationRGPAPLQQHPQVLLW
CCCCCHHHCCHHHHH		58.8919651622
444 (in isoform 5)Phosphorylation-58.8924719451
449 (in isoform 3)Phosphorylation-3.7621406692
450 (in isoform 3)Phosphorylation-5.0621406692
456 (in isoform 3)Phosphorylation-5.2821406692
464PhosphorylationAGRLPRGSTGDTVLL
HCCCCCCCCCCEEEE		30.4223401153
464 (in isoform 3)Phosphorylation-30.4221406692
465PhosphorylationGRLPRGSTGDTVLLP
CCCCCCCCCCEEEEE		41.7323403867
468PhosphorylationPRGSTGDTVLLPLAQ
CCCCCCCEEEEEHHC		17.8823403867
482PhosphorylationQGGHRPLSRAQSSPA
CCCCCCCCHHCCCCC		28.4023403867
486PhosphorylationRPLSRAQSSPAAPAS
CCCCHHCCCCCCCCC		36.9929255136
487PhosphorylationPLSRAQSSPAAPASL
CCCHHCCCCCCCCCC		13.3829255136
488PhosphorylationLSRAQSSPAAPASLS
CCHHCCCCCCCCCCC		37.3732645325
488 (in isoform 7)Phosphorylation-37.37-
489 (in isoform 7)Phosphorylation-28.20-
493PhosphorylationSSPAAPASLSAPEPA
CCCCCCCCCCCCCCH		23.0729255136
495PhosphorylationPAAPASLSAPEPASQ
CCCCCCCCCCCCHHH		39.0023927012
501PhosphorylationLSAPEPASQARVLSS
CCCCCCHHHCCCCCC		34.7823403867
503 (in isoform 5)Phosphorylation-10.8924719451
507PhosphorylationASQARVLSSSETPAR
HHHCCCCCCCCCCCC		29.0325106551
508PhosphorylationSQARVLSSSETPART
HHCCCCCCCCCCCCC		28.2133259812
509PhosphorylationQARVLSSSETPARTL
HCCCCCCCCCCCCCC		41.9626699800
511PhosphorylationRVLSSSETPARTLPF
CCCCCCCCCCCCCCC		24.9726699800
515PhosphorylationSSETPARTLPFTTGL
CCCCCCCCCCCCCCC		40.67-
521 (in isoform 5)Phosphorylation-13.6627251275
524PhosphorylationPFTTGLIYDSVMLKH
CCCCCCCCCHHHHHE		13.75-
525PhosphorylationFTTGLIYDSVMLKHQ
CCCCCCCCHHHHHEE		27.9719664995
525 (in isoform 5)Phosphorylation-27.9724719451
526PhosphorylationTTGLIYDSVMLKHQC
CCCCCCCHHHHHEEC		7.7720068231
526 (in isoform 5)Phosphorylation-7.77-
530MethylationIYDSVMLKHQCSCGD
CCCHHHHHEECCCCC		17.3424507061
530UbiquitinationIYDSVMLKHQCSCGD
CCCHHHHHEECCCCC		17.34-
534PhosphorylationVMLKHQCSCGDNSRH
HHHHEECCCCCCCCC		17.9827251275
539PhosphorylationQCSCGDNSRHPEHAG
ECCCCCCCCCHHHHH		36.3832645325
546 (in isoform 5)Phosphorylation-29.1824719451
550PhosphorylationEHAGRIQSIWSRLQE
HHHHHHHHHHHHHHH		24.5328857561
566 (in isoform 3)Ubiquitination-4.0621890473
573PhosphorylationCLRGRKASLEELQSV
HHHCCCCCHHHHHHH		39.0723401153
573 (in isoform 4)Ubiquitination-39.0721890473
573 (in isoform 5)Phosphorylation-39.0727251275
579PhosphorylationASLEELQSVHSERHV
CCHHHHHHHHCCCEE		34.1327732954
582PhosphorylationEELQSVHSERHVLLY
HHHHHHHCCCEEEEE		33.8827732954
589PhosphorylationSERHVLLYGTNPLSR
CCCEEEEEECCCCHH		20.1023663014
591PhosphorylationRHVLLYGTNPLSRLK
CEEEEEECCCCHHEE		21.8023663014
595PhosphorylationLYGTNPLSRLKLDNG
EEECCCCHHEECCCC		36.5022617229
598AcetylationTNPLSRLKLDNGKLA
CCCCHHEECCCCHHH		53.3225953088
598UbiquitinationTNPLSRLKLDNGKLA
CCCCHHEECCCCHHH		53.3223000965
600UbiquitinationPLSRLKLDNGKLAGL
CCHHEECCCCHHHHH		61.3223000965
603AcetylationRLKLDNGKLAGLLAQ
HEECCCCHHHHHHHH		41.2223954790
603UbiquitinationRLKLDNGKLAGLLAQ
HEECCCCHHHHHHHH		41.2223000965
603 (in isoform 1)Ubiquitination-41.2221890473
605UbiquitinationKLDNGKLAGLLAQRM
ECCCCHHHHHHHHHC		15.2921890473
605 (in isoform 7)Ubiquitination-15.2921890473
610 (in isoform 5)Ubiquitination-37.02-
612 (in isoform 5)Phosphorylation-1.6527251275
620UbiquitinationFVMLPCGGVGVDTDT
CCEEECCCCCCCHHH		21.5223000965
625UbiquitinationCGGVGVDTDTIWNEL
CCCCCCCHHHHHHHH		32.4121890473
625 (in isoform 6)Ubiquitination-32.4121890473
634 (in isoform 5)Phosphorylation-37.6024719451
637UbiquitinationNELHSSNAARWAAGS
HHHHCCCHHHHHHCC		10.6023000965
642UbiquitinationSNAARWAAGSVTDLA
CCHHHHHHCCHHHHH		12.1121890473
642 (in isoform 5)Ubiquitination-12.1121890473
644PhosphorylationAARWAAGSVTDLAFK
HHHHHHCCHHHHHHH		19.6727067055
644UbiquitinationAARWAAGSVTDLAFK
HHHHHHCCHHHHHHH		19.6723000965
649UbiquitinationAGSVTDLAFKVASRE
HCCHHHHHHHHHCHH		12.6721890473
656UbiquitinationAFKVASRELKNGFAV
HHHHHCHHHCCCEEE		62.6933845483
659 (in isoform 8)Ubiquitination-64.5421890473
664UbiquitinationLKNGFAVVRPPGHHA
HCCCEEEECCCCCCC		7.3423000965
669UbiquitinationAVVRPPGHHADHSTA
EEECCCCCCCCCCCC		20.8021890473
681UbiquitinationSTAMGFCFFNSVAIA
CCCHHHHHHHHHHHH		6.4023000965
686UbiquitinationFCFFNSVAIACRQLQ
HHHHHHHHHHHHHHH		5.4021890473
903PhosphorylationGCMQRLASCPDSWVP
HHHHHHHCCCCCCCC		30.67-
907PhosphorylationRLASCPDSWVPRVPG
HHHCCCCCCCCCCCC		18.34-
932 (in isoform 5)Ubiquitination-13.05-
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
155SPhosphorylationKinasePRKD1Q15139
Uniprot
155SPhosphorylationKinasePRKD1Q62101
PSP
155SPhosphorylationKinaseMAP3K7O43318
GPS
155SPhosphorylationKinaseMARK2Q7KZI7
Uniprot
155SPhosphorylationKinaseMARK3P27448
Uniprot
155SPhosphorylationKinasePKD1P98161
PhosphoELM
155SPhosphorylationKinaseMARK-SUBFAMILY-GPS
155SPhosphorylationKinaseMARK_GROUP-PhosphoELM
181SPhosphorylationKinasePRKD2Q9BZL6
Uniprot
358SPhosphorylationKinasePRKD1Q15139
Uniprot
358SPhosphorylationKinasePRKD1Q62101
PSP
486SPhosphorylationKinasePRKD1Q15139
PSP
486SPhosphorylationKinasePRKD1Q62101
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
155SPhosphorylation

16980613
155SPhosphorylation

16980613
181SPhosphorylation

16980613
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 HDAC7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAT5_HUMANKAT5physical
12551922
HDAC3_HUMANHDAC3physical
11466315
NCOR1_HUMANNCOR1physical
11466315
NCOR2_HUMANNCOR2physical
11466315
BCL6_HUMANBCL6physical
11929873
ZBT16_HUMANZBTB16physical
11929873
IKZF1_HUMANIKZF1physical
12015313
FOXP3_HUMANFOXP3physical
17360565
CTNB1_HUMANCTNNB1physical
20224040
1433E_HUMANYWHAEphysical
20224040
1433F_HUMANYWHAHphysical
20224040
1433Z_HUMANYWHAZphysical
20224040
ESR1_HUMANESR1physical
19917725
FOXA1_HUMANFOXA1physical
19917725
KPCD1_HUMANPRKD1physical
19029091
1433T_HUMANYWHAQphysical
16980613
MARK3_HUMANMARK3physical
16980613
MARK2_HUMANMARK2physical
16980613
ACTN4_HUMANACTN4physical
16980305
1433T_HUMANYWHAQphysical
16956611
NCOR2_HUMANNCOR2physical
16956611
MEF2A_HUMANMEF2Aphysical
16956611
ANDR_HUMANARphysical
16860317
UBC9_HUMANUBE2Iphysical
18625722
PML_HUMANPMLphysical
18463162
PP2AA_HUMANPPP2CAphysical
18339811
MEF2C_HUMANMEF2Cphysical
11279209
HDAC1_HUMANHDAC1physical
11279209
HDAC2_HUMANHDAC2physical
11279209
HDAC4_HUMANHDAC4physical
11279209
HDAC5_HUMANHDAC5physical
11279209
HDAC7_HUMANHDAC7physical
11279209
KPCD2_HUMANPRKD2physical
17962809
NR2E1_HUMANNR2E1physical
17873065
KLF4_HUMANKLF4physical
17827213
MYPT1_HUMANPPP1R12Aphysical
17369396
PP1B_HUMANPPP1CBphysical
17369396
1433T_HUMANYWHAQphysical
17369396
1433B_HUMANYWHABphysical
17369396
1433E_HUMANYWHAEphysical
17369396
KDM5B_HUMANKDM5Bphysical
17373667
HIF1A_HUMANHIF1Aphysical
21148070
1433B_HUMANYWHABphysical
23752268
1433E_HUMANYWHAEphysical
23752268
1433F_HUMANYWHAHphysical
23752268
1433G_HUMANYWHAGphysical
23752268
1433S_HUMANSFNphysical
23752268
1433T_HUMANYWHAQphysical
23752268
1433Z_HUMANYWHAZphysical
23752268
TBL1X_HUMANTBL1Xphysical
23752268
TBL1R_HUMANTBL1XR1physical
23752268
HDAC3_HUMANHDAC3physical
23752268
HDAC7_HUMANHDAC7physical
23752268
NCOR1_HUMANNCOR1physical
23752268
NCOR2_HUMANNCOR2physical
23752268
RIPP1_HUMANRIPPLY1physical
25416956
FWCH2_HUMANFLYWCH2physical
26186194
ZY11B_HUMANZYG11Bphysical
26186194
HINT1_HUMANHINT1physical
26186194
ZMYM6_HUMANZMYM6physical
26186194
TTF2_HUMANTTF2physical
26186194
GDS1_HUMANRAP1GDS1physical
26186194
MOCOS_HUMANMOCOSphysical
26186194
UGPA_HUMANUGP2physical
26186194
DCA10_HUMANDCAF10physical
26186194
ADNP_HUMANADNPphysical
26186194
WDR73_HUMANWDR73physical
26186194
TTF2_HUMANTTF2physical
28514442
MOCOS_HUMANMOCOSphysical
28514442
UGPA_HUMANUGP2physical
28514442
HINT1_HUMANHINT1physical
28514442
ZMYM6_HUMANZMYM6physical
28514442
DCA10_HUMANDCAF10physical
28514442
FWCH2_HUMANFLYWCH2physical
28514442
ZY11B_HUMANZYG11Bphysical
28514442
RHOA_HUMANRHOAphysical
28514442
WDR73_HUMANWDR73physical
28514442
ADNP_HUMANADNPphysical
28514442
CBWD6_HUMANCBWD6physical
28514442
CING_HUMANCGNphysical
27173435
MAGI1_HUMANMAGI1physical
27173435
HIF1A_HUMANHIF1Aphysical
15280364
EP300_HUMANEP300physical
15280364
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 HDAC7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-283; THR-286AND SER-486, AND MASS SPECTROMETRY.
"Phosphorylation at Ser244 by CK1 determines nuclear localization andsubstrate targeting of PKD2.";
von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A.,Auer A., Van Lint J., Adler G., Seufferlein T.;
EMBO J. 26:4619-4633(2007).
Cited for: PHOSPHORYLATION AT SER-181.
"New role for hPar-1 kinases EMK and C-TAK1 in regulating localizationand activity of class IIa histone deacetylases.";
Dequiedt F., Martin M., Von Blume J., Vertommen D., Lecomte E.,Mari N., Heinen M.F., Bachmann M., Twizere J.C., Huang M.C.,Rider M.H., Piwnica-Worms H., Seufferlein T., Kettmann R.;
Mol. Cell. Biol. 26:7086-7102(2006).
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-155 AND SER-181, ANDMUTAGENESIS OF LEU-150; SER-155; SER-181; SER-358 AND SER-486.
"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-487, AND MASSSPECTROMETRY.
"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 TYR-114, AND MASSSPECTROMETRY.

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