RARB_HUMAN - dbPTM
RARB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RARB_HUMAN
UniProt AC P10826
Protein Name Retinoic acid receptor beta
Gene Name RARB
Organism Homo sapiens (Human).
Sequence Length 455
Subcellular Localization Isoform Beta-1: Nucleus.
Isoform Beta-2: Nucleus.
Isoform Beta-4: Cytoplasm.
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 RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function..
Protein Sequence MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPATIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPSSSGNTAEHSPSISPSSVENSGVSQSPLVQ
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
22 (in isoform 2)Phosphorylation-17.65-
67 (in isoform 2)Phosphorylation-40.7925850435
70 (in isoform 2)Phosphorylation-57.9525850435
77PhosphorylationELVPSPPSPLPPPRV
CCCCCCCCCCCCCCC
42.312836738
96PhosphorylationFVCQDKSSGYHYGVS
EEEECCCCCCEEEEH
49.4616417524
122PhosphorylationSIQKNMIYTCHRDKN
HHHHCEEEEECCCCC
7.7929083192
123PhosphorylationIQKNMIYTCHRDKNC
HHHCEEEEECCCCCC
7.3029083192
250PhosphorylationAKRLPGFTGLTIADQ
HHHCCCCCCCCHHHH
36.88-
346PhosphorylationRQDLEEPTKVDKLQE
CCCCCCCCCCCCCHH
47.1624732914
369O-linked_GlycosylationYIRKRRPSKPHMFPK
HHHHCCCCCCCCCHH
57.9429351928
382PhosphorylationPKILMKITDLRSISA
HHHHHHHHCHHHCCC
24.3823532336
405PhosphorylationLKMEIPGSMPPLIQE
EEEECCCCCCHHHHH
23.82-

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
-KUbiquitinationE3 ubiquitin ligaseHACE1Q8IYU2
PMID:19350571

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RARB_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 RARB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RXRG_HUMANRXRGphysical
20211142
HAIR_HUMANHRphysical
20211142
RXRA_HUMANRXRAphysical
15528208
NCOA1_HUMANNCOA1physical
15604093
RXRB_HUMANRXRBphysical
15604093
RXRG_HUMANRXRGphysical
15604093
PNRC1_HUMANPNRC1physical
15604093
MAP6_HUMANMAP6physical
15604093
RXRB_HUMANRXRBphysical
25416956
RXRG_HUMANRXRGphysical
25416956
PRS8_HUMANPSMC5physical
15604093

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RARB_HUMAN

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Related Literatures of Post-Translational Modification

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