HDAC7_MOUSE - dbPTM
HDAC7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC7_MOUSE
UniProt AC Q8C2B3
Protein Name Histone deacetylase 7
Gene Name Hdac7
Organism Mus musculus (Mouse).
Sequence Length 938
Subcellular Localization Nucleus. Cytoplasm. In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm de
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. Positively regulates the transcriptional repressor activity of FOXP3 (By similarity)..
Protein Sequence MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLLDPSVSHAPLWTVPGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYWGCMQRLASCPDSWLPRVPGADAEVEAVTALASLSVGILAEDRPSERLVEEEEPMNL
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
3Phosphorylation-----MHSPGAGCPA
-----CCCCCCCCCC		24.5926643407
127PhosphorylationQQAALERTVHPSSPS
HHHHHHCCCCCCCCC		17.5026239621
131PhosphorylationLERTVHPSSPSIPYR
HHCCCCCCCCCCCCC		39.7526239621
132PhosphorylationERTVHPSSPSIPYRT
HCCCCCCCCCCCCCC		27.4126239621
134PhosphorylationTVHPSSPSIPYRTLE
CCCCCCCCCCCCCCC		37.8426239621
137PhosphorylationPSSPSIPYRTLEPLD
CCCCCCCCCCCCCCC		17.9823984901
139PhosphorylationSPSIPYRTLEPLDTE
CCCCCCCCCCCCCCH		29.6323984901
162PhosphorylationSFLPPVPSLPTEPPE
HHCCCCCCCCCCCCC		47.4125367039
165PhosphorylationPPVPSLPTEPPEHFP
CCCCCCCCCCCCCCC		67.4325367039
176PhosphorylationEHFPLRKTVSEPNLK
CCCCCCCCCCCCCCC		23.8828833060
178PhosphorylationFPLRKTVSEPNLKLR
CCCCCCCCCCCCCCC		53.2027087446
191PhosphorylationLRYKPKKSLERRKNP
CCCCCHHHHHHHCCC		41.4025338131
196 (in isoform 4)Phosphorylation-69.9625338131
198 (in isoform 3)Phosphorylation-35.4925338131
198 (in isoform 2)Phosphorylation-35.4925338131
200 (in isoform 4)Phosphorylation-8.5125338131
202 (in isoform 4)Phosphorylation-56.8625338131
202 (in isoform 3)Phosphorylation-56.8625338131
202 (in isoform 2)Phosphorylation-56.8625338131
204 (in isoform 2)Phosphorylation-49.4625338131
204 (in isoform 3)Phosphorylation-49.4625338131
204PhosphorylationNPLLRKESAPPSLRR
CCCCCCCCCCHHHHC		49.4626824392
206 (in isoform 4)Phosphorylation-28.4325338131
208 (in isoform 2)Phosphorylation-33.1925338131
208 (in isoform 3)Phosphorylation-33.1925338131
208PhosphorylationRKESAPPSLRRRPAE
CCCCCCHHHHCCCCH		33.1928833060
209 (in isoform 4)Phosphorylation-6.4325338131
211 (in isoform 2)Phosphorylation-54.9825338131
211 (in isoform 3)Phosphorylation-54.9825338131
216PhosphorylationLRRRPAETLGDSSPS
HHCCCCHHHCCCCCC		37.8421183079
220PhosphorylationPAETLGDSSPSSSST
CCHHHCCCCCCCCCC		42.2125338131
221PhosphorylationAETLGDSSPSSSSTP
CHHHCCCCCCCCCCC		33.2825338131
223PhosphorylationTLGDSSPSSSSTPAS
HHCCCCCCCCCCCCC		44.8125338131
224PhosphorylationLGDSSPSSSSTPASG
HCCCCCCCCCCCCCC		31.5221183079
227PhosphorylationSSPSSSSTPASGCSS
CCCCCCCCCCCCCCC		25.4825338131
230PhosphorylationSSSSTPASGCSSPND
CCCCCCCCCCCCCCC		41.3521183079
233PhosphorylationSTPASGCSSPNDSEH
CCCCCCCCCCCCCCC		52.9725338131
234PhosphorylationTPASGCSSPNDSEHG
CCCCCCCCCCCCCCC		31.6225338131
238PhosphorylationGCSSPNDSEHGPNPA
CCCCCCCCCCCCCCC		37.8321183079
287PhosphorylationLEPEAGGTLPSRLQP
CCCCCCCCCCCCCCE		34.2829514104
342PhosphorylationLHRPLNRTRSEPLPP
CCCCCCCCCCCCCCC		37.1627087446
344PhosphorylationRPLNRTRSEPLPPSA
CCCCCCCCCCCCCCC		42.8427087446
350PhosphorylationRSEPLPPSATASPLL
CCCCCCCCCCCCCCC		35.9921082442
352PhosphorylationEPLPPSATASPLLAP
CCCCCCCCCCCCCCC		31.8225619855
354PhosphorylationLPPSATASPLLAPLQ
CCCCCCCCCCCCCCC		16.2425619855
379PhosphorylationQLIKPAISPPQRPAK
EEECCCCCCCCCCCC		32.4126824392
398PhosphorylationPRLRQIPSAEDLETD
CCHHCCCCHHHHCCC		46.0125521595
404PhosphorylationPSAEDLETDGGGVGP
CCHHHHCCCCCCCCC		47.4425619855
432PhosphorylationGPPEGRGSISLQQHQ
CCCCCCCCCCCCCCC		13.9821183079
434PhosphorylationPEGRGSISLQQHQQV
CCCCCCCCCCCCCCC		23.0921183079
454PhosphorylationQHLAGRLSQGSPGDS
HHHHHHCCCCCCCCC		31.0026643407
457PhosphorylationAGRLSQGSPGDSVLI
HHHCCCCCCCCCEEE		20.3326824392
461PhosphorylationSQGSPGDSVLIPLAQ
CCCCCCCCEEEEHHH		25.4126643407
475PhosphorylationQVGHRPLSRTQSSPA
HCCCCCCCCCCCCCC		35.6426643407
477PhosphorylationGHRPLSRTQSSPAAP
CCCCCCCCCCCCCCC		29.4426643407
479PhosphorylationRPLSRTQSSPAAPVS
CCCCCCCCCCCCCCC		37.3626643407
480PhosphorylationPLSRTQSSPAAPVSL
CCCCCCCCCCCCCCC		14.5626643407
486PhosphorylationSSPAAPVSLLSPEPT
CCCCCCCCCCCCCCC		23.6423649490
489PhosphorylationAAPVSLLSPEPTCQT
CCCCCCCCCCCCCCE		32.2925777480
493PhosphorylationSLLSPEPTCQTQVLN
CCCCCCCCCCEEECC		18.6525777480
496PhosphorylationSPEPTCQTQVLNSSE
CCCCCCCEEECCCCC		23.8525777480
501PhosphorylationCQTQVLNSSETPATG
CCEEECCCCCCCCCC		25.9525777480
502PhosphorylationQTQVLNSSETPATGL
CEEECCCCCCCCCCE		44.4025777480
504PhosphorylationQVLNSSETPATGLVY
EECCCCCCCCCCEEE		21.8525777480
507PhosphorylationNSSETPATGLVYDSV
CCCCCCCCCEEEEHH		32.0525777480
511PhosphorylationTPATGLVYDSVMLKH
CCCCCEEEEHHHHEE		13.9325777480
513PhosphorylationATGLVYDSVMLKHQC
CCCEEEEHHHHEEEC		7.5525777480
560PhosphorylationCLRGRKASLEELQSV
HHHCCCCCHHHHHHH		39.0728833060
578PhosphorylationRHVLLYGTNPLSRLK
CEEEEEECCCCHHEE		21.8026824392
582PhosphorylationLYGTNPLSRLKLDNG
EEECCCCHHEECCCC		36.5026824392
590AcetylationRLKLDNGKLTGLLAQ
HEECCCCCCCHHHCC		49.4823236377
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
178SPhosphorylationKinaseCAMK1Q14012
GPS
178SPhosphorylationKinasePRKD1Q62101
Uniprot
178SPhosphorylationKinaseMARK2Q05512
Uniprot
178SPhosphorylationKinaseMARK3Q03141
Uniprot
204SPhosphorylationKinasePRKD2Q8BZ03
Uniprot
344SPhosphorylationKinaseCAMK1Q14012
GPS
344SPhosphorylationKinasePRKD1Q62101
Uniprot
479SPhosphorylationKinaseCAMK1Q14012
GPS
479SPhosphorylationKinasePRKD1Q62101
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
178SPhosphorylation

11585834
178SPhosphorylation

11585834
204SPhosphorylation

-
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN3A_HUMANSIN3Aphysical
10640276
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HDAC7_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Control of endothelial cell proliferation and migration by VEGFsignaling to histone deacetylase 7.";
Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.;
Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008).
Cited for: PHOSPHORYLATION AT SER-178; SER-344 AND SER-479.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASSSPECTROMETRY.

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