RB22A_HUMAN - dbPTM
RB22A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB22A_HUMAN
UniProt AC Q9UL26
Protein Name Ras-related protein Rab-22A
Gene Name RAB22A
Organism Homo sapiens (Human).
Sequence Length 194
Subcellular Localization Endosome membrane
Lipid-anchor . Cell membrane
Lipid-anchor . Early endosome . Late endosome . Cell projection, ruffle . Cytoplasmic vesicle . Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane
Lipid-anchor
Cytoplasmic side .
Protein Description Plays a role in endocytosis and intracellular protein transport. Mediates trafficking of TF from early endosomes to recycling endosomes. [PubMed: 16537905 Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth]
Protein Sequence MALRELKVCLLGDTGVGKSSIVWRFVEDSFDPNINPTIGASFMTKTVQYQNELHKFLIWDTAGQERFRALAPMYYRGSAAAIIVYDITKEETFSTLKNWVKELRQHGPPNIVVAIAGNKCDLIDVREVMERDAKDYADSIHAIFVETSAKNAININELFIEISRRIPSTDANLPSGGKGFKLRRQPSEPKRSCC
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
7Ubiquitination-MALRELKVCLLGDT
-CCCCCEEEEEECCC
26.58-
14PhosphorylationKVCLLGDTGVGKSSI
EEEEECCCCCCCHHH
31.78-
19PhosphorylationGDTGVGKSSIVWRFV
CCCCCCCHHHHHHHH
21.26-
20PhosphorylationDTGVGKSSIVWRFVE
CCCCCCHHHHHHHHC
25.33-
94PhosphorylationITKEETFSTLKNWVK
CCCHHHHHHHHHHHH
40.0022210691
95PhosphorylationTKEETFSTLKNWVKE
CCHHHHHHHHHHHHH
37.2422210691
101AcetylationSTLKNWVKELRQHGP
HHHHHHHHHHHHHCC
42.52-
101UbiquitinationSTLKNWVKELRQHGP
HHHHHHHHHHHHHCC
42.52-
147PhosphorylationIHAIFVETSAKNAIN
EEEEEEECCCCCCCC
28.7827251275
148PhosphorylationHAIFVETSAKNAINI
EEEEEECCCCCCCCH
24.6027251275
163PhosphorylationNELFIEISRRIPSTD
HHHHHHHHCCCCCCC
11.6127251275
175PhosphorylationSTDANLPSGGKGFKL
CCCCCCCCCCCCCCC
64.4421815630
178UbiquitinationANLPSGGKGFKLRRQ
CCCCCCCCCCCCCCC
65.7833845483
181UbiquitinationPSGGKGFKLRRQPSE
CCCCCCCCCCCCCCC
50.15-
187PhosphorylationFKLRRQPSEPKRSCC
CCCCCCCCCCCCCCC
59.1829691806
190UbiquitinationRRQPSEPKRSCC---
CCCCCCCCCCCC---
53.5524816145
193GeranylgeranylationPSEPKRSCC------
CCCCCCCCC------
3.56-
194GeranylgeranylationSEPKRSCC-------
CCCCCCCC-------
7.05-

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

Oops, there are no upstream regulatory protein records of RB22A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB22A_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 RB22A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EEA1_HUMANEEA1physical
11870209
RABX5_HUMANRABGEF1physical
19759177
RAB5A_HUMANRAB5Aphysical
19759177

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 RB22A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND MASS SPECTROMETRY.

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