UniProt ID | RAB10_HUMAN | |
---|---|---|
UniProt AC | P61026 | |
Protein Name | Ras-related protein Rab-10 | |
Gene Name | RAB10 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 200 | |
Subcellular Localization |
Cytoplasmic vesicle membrane Lipid-anchor Cytoplasmic side . Golgi apparatus membrane . Golgi apparatus, trans-Golgi network membrane . Endosome membrane . Recycling endosome membrane . Cytoplasmic vesicle, phagosome membrane . Cell projection, cilium |
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Protein Description | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. According to PubMed:23263280, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion.. | |
Protein Sequence | MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERMLLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKANINIEKAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Ubiquitination | -----MAKKTYDLLF -----CCHHHHHHHH | 44.33 | 33845483 | |
4 | Malonylation | ----MAKKTYDLLFK ----CCHHHHHHHHH | 42.66 | 26320211 | |
4 | Ubiquitination | ----MAKKTYDLLFK ----CCHHHHHHHHH | 42.66 | 33845483 | |
5 | Phosphorylation | ---MAKKTYDLLFKL ---CCHHHHHHHHHH | 22.89 | 28796482 | |
6 | Phosphorylation | --MAKKTYDLLFKLL --CCHHHHHHHHHHH | 17.30 | 25159151 | |
18 | Phosphorylation | KLLLIGDSGVGKTCV HHHHHCCCCCCCEEE | 30.11 | 23911959 | |
22 | Ubiquitination | IGDSGVGKTCVLFRF HCCCCCCCEEEEEEE | 36.02 | 33845483 | |
24 | S-palmitoylation | DSGVGKTCVLFRFSD CCCCCCEEEEEEECC | 2.59 | 29575903 | |
41 | Phosphorylation | FNTTFISTIGIDFKI CCCEEEEEEEECEEE | 20.57 | - | |
49 | Ubiquitination | IGIDFKIKTVELQGK EEECEEEEEEEECCE | 47.29 | 29901268 | |
50 | Phosphorylation | GIDFKIKTVELQGKK EECEEEEEEEECCEE | 23.76 | 22985185 | |
56 | Ubiquitination | KTVELQGKKIKLQIW EEEEECCEEEEEEEE | 38.06 | 33845483 | |
65 | Phosphorylation | IKLQIWDTAGQERFH EEEEEECCCCCCCEE | 20.07 | 28857561 | |
73 | Phosphorylation | AGQERFHTITTSYYR CCCCCEEEEECHHCC | 19.80 | 23401153 | |
75 | Phosphorylation | QERFHTITTSYYRGA CCCEEEEECHHCCCC | 15.73 | 28152594 | |
76 | Phosphorylation | ERFHTITTSYYRGAM CCEEEEECHHCCCCC | 15.75 | 28152594 | |
77 | Phosphorylation | RFHTITTSYYRGAMG CEEEEECHHCCCCCE | 16.12 | 28152594 | |
78 | Phosphorylation | FHTITTSYYRGAMGI EEEEECHHCCCCCEE | 8.62 | 28152594 | |
79 | Phosphorylation | HTITTSYYRGAMGIM EEEECHHCCCCCEEE | 11.44 | 28152594 | |
102 | Acetylation | KSFENISKWLRNIDE CCHHHHHHHHHCHHH | 46.58 | 19608861 | |
102 | Ubiquitination | KSFENISKWLRNIDE CCHHHHHHHHHCHHH | 46.58 | 23000965 | |
123 | Ubiquitination | ERMLLGNKCDMDDKR HHHHHCCCCCCCCCC | 29.79 | 33845483 | |
129 | Ubiquitination | NKCDMDDKRVVPKGK CCCCCCCCCCCCCCC | 42.71 | 24816145 | |
136 | Ubiquitination | KRVVPKGKGEQIARE CCCCCCCCHHHHHHH | 66.46 | 33845483 | |
147 | Methylation | IAREHGIRFFETSAK HHHHHCCEEEECCCC | 34.49 | - | |
154 | Ubiquitination | RFFETSAKANINIEK EEEECCCCCCCCHHH | 41.56 | 21906983 | |
161 | Ubiquitination | KANINIEKAFLTLAE CCCCCHHHHHHHHHH | 40.41 | 33845483 | |
165 | Phosphorylation | NIEKAFLTLAEDILR CHHHHHHHHHHHHHH | 19.91 | - | |
173 | Ubiquitination | LAEDILRKTPVKEPN HHHHHHHHCCCCCCC | 54.45 | 22817900 | |
174 | Phosphorylation | AEDILRKTPVKEPNS HHHHHHHCCCCCCCC | 27.21 | 25850435 | |
177 | Ubiquitination | ILRKTPVKEPNSENV HHHHCCCCCCCCCCC | 69.52 | 21906983 | |
181 | Phosphorylation | TPVKEPNSENVDISS CCCCCCCCCCCCCCC | 41.06 | 22167270 | |
187 | Phosphorylation | NSENVDISSGGGVTG CCCCCCCCCCCCCCC | 20.61 | 22167270 | |
188 | Phosphorylation | SENVDISSGGGVTGW CCCCCCCCCCCCCCC | 41.62 | 22167270 | |
193 | Phosphorylation | ISSGGGVTGWKSKCC CCCCCCCCCCCCCCC | 40.37 | 22167270 | |
196 | Acetylation | GGGVTGWKSKCC--- CCCCCCCCCCCC--- | 41.19 | 24847221 | |
199 | Geranylgeranylation | VTGWKSKCC------ CCCCCCCCC------ | 4.26 | - | |
200 | Geranylgeranylation | TGWKSKCC------- CCCCCCCC------- | 7.79 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
73 | T | Phosphorylation | Kinase | LRRK2 | Q5S007 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
73 | T | Phosphorylation |
| 26824392 |
* 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 RAB10_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RAB8A_HUMAN | RAB8A | physical | 17353931 | |
AP1S1_HUMAN | AP1S1 | physical | 17353931 | |
ENOPH_HUMAN | ENOPH1 | physical | 21900206 | |
MICA1_HUMAN | MICAL1 | physical | 21900206 | |
CXCL7_HUMAN | PPBP | physical | 21900206 | |
A4_HUMAN | APP | physical | 21832049 | |
BICL2_MOUSE | Ccdc64b | physical | 20360680 | |
COF1_HUMAN | CFL1 | physical | 26344197 | |
GDIB_HUMAN | GDI2 | physical | 26344197 | |
G6PI_HUMAN | GPI | physical | 26344197 | |
LEG1_HUMAN | LGALS1 | physical | 26344197 | |
PPIA_HUMAN | PPIA | physical | 26344197 | |
RAB5C_HUMAN | RAB5C | physical | 26344197 | |
RAB7A_HUMAN | RAB7A | physical | 26344197 | |
TIAR_HUMAN | TIAL1 | physical | 26344197 | |
QCR2_HUMAN | UQCRC2 | physical | 26344197 | |
MSS4_HUMAN | RABIF | physical | 28894007 |
Kegg Disease | ||||||
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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. |
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Acetylation | |
Reference | PubMed |
"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-102, AND MASS SPECTROMETRY. |