RAB10_HUMAN - dbPTM
RAB10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
3Ubiquitination-----MAKKTYDLLF
-----CCHHHHHHHH
44.3333845483
4Malonylation----MAKKTYDLLFK
----CCHHHHHHHHH
42.6626320211
4Ubiquitination----MAKKTYDLLFK
----CCHHHHHHHHH
42.6633845483
5Phosphorylation---MAKKTYDLLFKL
---CCHHHHHHHHHH
22.8928796482
6Phosphorylation--MAKKTYDLLFKLL
--CCHHHHHHHHHHH
17.3025159151
18PhosphorylationKLLLIGDSGVGKTCV
HHHHHCCCCCCCEEE
30.1123911959
22UbiquitinationIGDSGVGKTCVLFRF
HCCCCCCCEEEEEEE
36.0233845483
24S-palmitoylationDSGVGKTCVLFRFSD
CCCCCCEEEEEEECC
2.5929575903
41PhosphorylationFNTTFISTIGIDFKI
CCCEEEEEEEECEEE
20.57-
49UbiquitinationIGIDFKIKTVELQGK
EEECEEEEEEEECCE
47.2929901268
50PhosphorylationGIDFKIKTVELQGKK
EECEEEEEEEECCEE
23.7622985185
56UbiquitinationKTVELQGKKIKLQIW
EEEEECCEEEEEEEE
38.0633845483
65PhosphorylationIKLQIWDTAGQERFH
EEEEEECCCCCCCEE
20.0728857561
73PhosphorylationAGQERFHTITTSYYR
CCCCCEEEEECHHCC
19.8023401153
75PhosphorylationQERFHTITTSYYRGA
CCCEEEEECHHCCCC
15.7328152594
76PhosphorylationERFHTITTSYYRGAM
CCEEEEECHHCCCCC
15.7528152594
77PhosphorylationRFHTITTSYYRGAMG
CEEEEECHHCCCCCE
16.1228152594
78PhosphorylationFHTITTSYYRGAMGI
EEEEECHHCCCCCEE
8.6228152594
79PhosphorylationHTITTSYYRGAMGIM
EEEECHHCCCCCEEE
11.4428152594
102AcetylationKSFENISKWLRNIDE
CCHHHHHHHHHCHHH
46.5819608861
102UbiquitinationKSFENISKWLRNIDE
CCHHHHHHHHHCHHH
46.5823000965
123UbiquitinationERMLLGNKCDMDDKR
HHHHHCCCCCCCCCC
29.7933845483
129UbiquitinationNKCDMDDKRVVPKGK
CCCCCCCCCCCCCCC
42.7124816145
136UbiquitinationKRVVPKGKGEQIARE
CCCCCCCCHHHHHHH
66.4633845483
147MethylationIAREHGIRFFETSAK
HHHHHCCEEEECCCC
34.49-
154UbiquitinationRFFETSAKANINIEK
EEEECCCCCCCCHHH
41.5621906983
161UbiquitinationKANINIEKAFLTLAE
CCCCCHHHHHHHHHH
40.4133845483
165PhosphorylationNIEKAFLTLAEDILR
CHHHHHHHHHHHHHH
19.91-
173UbiquitinationLAEDILRKTPVKEPN
HHHHHHHHCCCCCCC
54.4522817900
174PhosphorylationAEDILRKTPVKEPNS
HHHHHHHCCCCCCCC
27.2125850435
177UbiquitinationILRKTPVKEPNSENV
HHHHCCCCCCCCCCC
69.5221906983
181PhosphorylationTPVKEPNSENVDISS
CCCCCCCCCCCCCCC
41.0622167270
187PhosphorylationNSENVDISSGGGVTG
CCCCCCCCCCCCCCC
20.6122167270
188PhosphorylationSENVDISSGGGVTGW
CCCCCCCCCCCCCCC
41.6222167270
193PhosphorylationISSGGGVTGWKSKCC
CCCCCCCCCCCCCCC
40.3722167270
196AcetylationGGGVTGWKSKCC---
CCCCCCCCCCCC---
41.1924847221
199GeranylgeranylationVTGWKSKCC------
CCCCCCCCC------
4.26-
200GeranylgeranylationTGWKSKCC-------
CCCCCCCC-------
7.79-

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
73TPhosphorylationKinaseLRRK2Q5S007
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
73TPhosphorylation

26824392

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 RAB10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB8A_HUMANRAB8Aphysical
17353931
AP1S1_HUMANAP1S1physical
17353931
ENOPH_HUMANENOPH1physical
21900206
MICA1_HUMANMICAL1physical
21900206
CXCL7_HUMANPPBPphysical
21900206
A4_HUMANAPPphysical
21832049
BICL2_MOUSECcdc64bphysical
20360680
COF1_HUMANCFL1physical
26344197
GDIB_HUMANGDI2physical
26344197
G6PI_HUMANGPIphysical
26344197
LEG1_HUMANLGALS1physical
26344197
PPIA_HUMANPPIAphysical
26344197
RAB5C_HUMANRAB5Cphysical
26344197
RAB7A_HUMANRAB7Aphysical
26344197
TIAR_HUMANTIAL1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
MSS4_HUMANRABIFphysical
28894007

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 RAB10_HUMAN

loading...

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-102, AND MASS SPECTROMETRY.

TOP