RARG_HUMAN - dbPTM
RARG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RARG_HUMAN
UniProt AC P13631
Protein Name Retinoic acid receptor gamma
Gene Name RARG
Organism Homo sapiens (Human).
Sequence Length 454
Subcellular Localization Nucleus.
Protein Description Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function (By similarity)..
Protein Sequence MATNKERLFAAGALGPGSGYPGAGFPFAFPGALRGSPPFEMLSPSFRGLGQPDLPKEMASLSVETQSTSSEEMVPSSPSPPPPPRVYKPCFVCNDKSSGYHYGVSSCEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKEAVRNDRNKKKKEVKEEGSPDSYELSPQLEELITKVSKAHQETFPSLCQLGKYTTNSSADHRVQLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLSIADQITLLKAACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFAGQLLPLEMDDTETGLLSAICLICGDRMDLEEPEKVDKLQEPLLEALRLYARRRRPSQPYMFPRMLMKITDLRGISTKGAERAITLKMEIPGPMPPLIREMLENPEMFEDDSSQPGPHPNASSEDEVPGGQGKGGLKSPA
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
5 (in isoform 3)Phosphorylation-39.6027135362
7 (in isoform 3)Phosphorylation-36.3927135362
34MethylationFAFPGALRGSPPFEM
CCCCCHHCCCCCHHH
42.90-
36PhosphorylationFPGALRGSPPFEMLS
CCCHHCCCCCHHHCC
23.9830266825
43PhosphorylationSPPFEMLSPSFRGLG
CCCHHHCCHHHCCCC
19.7225106551
76PhosphorylationSSEEMVPSSPSPPPP
CCCCCCCCCCCCCCC
43.3923663014
77PhosphorylationSEEMVPSSPSPPPPP
CCCCCCCCCCCCCCC
24.2723663014
79PhosphorylationEMVPSSPSPPPPPRV
CCCCCCCCCCCCCCC
52.5723663014
120UbiquitinationFFRRSIQKNMVYTCH
HHHHHHHHCCEEEEC
45.39-
172SumoylationNKKKKEVKEEGSPDS
HHHHHHHHHCCCCCH
51.65-
172SumoylationNKKKKEVKEEGSPDS
HHHHHHHHHCCCCCH
51.6528112733
176PhosphorylationKEVKEEGSPDSYELS
HHHHHCCCCCHHHCC
28.9030624053
179PhosphorylationKEEGSPDSYELSPQL
HHCCCCCHHHCCHHH
24.7230624053
180PhosphorylationEEGSPDSYELSPQLE
HCCCCCHHHCCHHHH
28.4127732954
192UbiquitinationQLEELITKVSKAHQE
HHHHHHHHHHHHHHH
37.20-
371PhosphorylationYARRRRPSQPYMFPR
HHHHHCCCCCCCHHH
41.8125219547
374PhosphorylationRRRPSQPYMFPRMLM
HHCCCCCCCHHHHHH
12.0725219547
384PhosphorylationPRMLMKITDLRGIST
HHHHHHHHHCCCCCC
24.3823532336
390PhosphorylationITDLRGISTKGAERA
HHHCCCCCCCCCHHE
27.22-
401SumoylationAERAITLKMEIPGPM
CHHEEEEEEECCCCC
26.3228112733
426PhosphorylationPEMFEDDSSQPGPHP
HHHCCCCCCCCCCCC
43.1027251275
427PhosphorylationEMFEDDSSQPGPHPN
HHCCCCCCCCCCCCC
47.6027251275
436PhosphorylationPGPHPNASSEDEVPG
CCCCCCCCCCCCCCC
40.6827251275
437PhosphorylationGPHPNASSEDEVPGG
CCCCCCCCCCCCCCC
46.8127251275
452PhosphorylationQGKGGLKSPA-----
CCCCCCCCCC-----
30.9724719451

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
77SPhosphorylationKinaseCDK7P50613
PSP
77SPhosphorylationKinaseGTF2F1P35269
PSP
79SPhosphorylationKinaseCDK7P50613
PSP
79SPhosphorylationKinaseMAPK3P27361
GPS
79SPhosphorylationKinaseGTF2F1P35269
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RARG_HUMAN !!

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 RARG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOR1_HUMANNCOR1physical
10336495
NR2F6_HUMANNR2F6physical
10318855
SUZ12_HUMANSUZ12physical
20857416
H2AZ_HUMANH2AFZphysical
20857416
RXRA_HUMANRXRAphysical
15604093
PNRC1_HUMANPNRC1physical
15604093
RXRG_HUMANRXRGphysical
15604093
PNRC2_HUMANPNRC2physical
15604093
NR0B2_HUMANNR0B2physical
15604093
RXRB_HUMANRXRBphysical
15604093
MAP6_HUMANMAP6physical
15604093
ITBP2_HUMANITGB1BP2physical
15604093
NCOA1_HUMANNCOA1physical
15604093
HACE1_HUMANHACE1physical
19350571
SPHK1_HUMANSPHK1physical
21988832
ZN576_HUMANZNF576physical
21988832
RHPN2_HUMANRHPN2physical
21988832
PRS8_HUMANPSMC5physical
15604093
RARA_HUMANRARAphysical
28514442
PNM8A_HUMANPNMAL1physical
28514442
RXRB_HUMANRXRBphysical
28514442
ZPLD1_HUMANZPLD1physical
28514442
KCNJ6_HUMANKCNJ6physical
28514442
RBL2_HUMANRBL2physical
28514442

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
DB00459Acitretin
DB00210Adapalene
DB00523Alitretinoin
DB00799Tazarotene
DB00755Tretinoin
Regulatory Network of RARG_HUMAN

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Related Literatures of Post-Translational Modification

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