RAB1A_RAT - dbPTM
RAB1A_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB1A_RAT
UniProt AC Q6NYB7
Protein Name Ras-related protein Rab-1A
Gene Name Rab1A
Organism Rattus norvegicus (Rat).
Sequence Length 205
Subcellular Localization Golgi apparatus . Endoplasmic reticulum . Early endosome . Cytoplasm, cytosol . Membrane . Melanosome . Alternates between membrane-associated and cytosolic forms.
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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in anterograde melanosome transport (By similarity). Plays a role in microtubule-dependent protein transport by early endosomes..
Protein Sequence MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC
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
2Acetylation------MSSMNPEYD
------CCCCCHHHH
37.99-
2Phosphorylation------MSSMNPEYD
------CCCCCHHHH
37.9922673903
3Phosphorylation-----MSSMNPEYDY
-----CCCCCHHHHH
22.6823984901
8PhosphorylationMSSMNPEYDYLFKLL
CCCCCHHHHHHHHHH
15.9022673903
10PhosphorylationSMNPEYDYLFKLLLI
CCCHHHHHHHHHHHH
17.09-
35PhosphorylationLLRFADDTYTESYIS
EEEECCCCCCHHHHH
32.6522276854
36PhosphorylationLRFADDTYTESYIST
EEECCCCCCHHHHHE
18.5922276854
39PhosphorylationADDTYTESYISTIGV
CCCCCCHHHHHEEEC
21.7022276854
40PhosphorylationDDTYTESYISTIGVD
CCCCCHHHHHEEECC
7.8322276854
58AcetylationRTIELDGKTIKLQIW
EEEEECCEEEEEEEE
46.9054411765
61UbiquitinationELDGKTIKLQIWDTA
EECCEEEEEEEECCC
39.30-
61AcetylationELDGKTIKLQIWDTA
EECCEEEEEEEECCC
39.3066736229
75PhosphorylationAGQERFRTITSSYYR
CCHHHHHHHHHHHHC
26.3728432305
77PhosphorylationQERFRTITSSYYRGA
HHHHHHHHHHHHCCC
15.8228432305
78PhosphorylationERFRTITSSYYRGAH
HHHHHHHHHHHCCCC
16.7028432305
79OtherRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE
19.96-
79O-(2-cholinephosphoryl)serineRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE
19.96-
79PhosphorylationRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE
19.9628432305
112PhosphorylationWLQEIDRYASENVNK
HHHHHHHHHCCCHHH
15.6728551015
114PhosphorylationQEIDRYASENVNKLL
HHHHHHHCCCHHHHH
22.2928432305
132AcetylationKCDLTTKKVVDYTTA
CCCCCCCCCCCHHHH
45.4522902405
132SuccinylationKCDLTTKKVVDYTTA
CCCCCCCCCCCHHHH
45.4526843850
136PhosphorylationTTKKVVDYTTAKEFA
CCCCCCCHHHHHHHH
8.38-
140AcetylationVVDYTTAKEFADSLG
CCCHHHHHHHHHHHC
51.8022902405
173AcetylationMTMAAEIKKRMGPGA
HHHHHHHHHHHCCCC
26.3272592355
188PhosphorylationTAGGAEKSNVKIQST
CCCCCCCCCCEEECC
38.0628432305
194PhosphorylationKSNVKIQSTPVKQSG
CCCCEEECCCCCCCC
37.8528432305
195PhosphorylationSNVKIQSTPVKQSGG
CCCEEECCCCCCCCC
18.7428432305
204GeranylgeranylationVKQSGGGCC------
CCCCCCCCC------
2.55-
205GeranylgeranylationKQSGGGCC-------
CCCCCCCC-------
7.65-

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
194SPhosphorylationKinaseCDK1P39951
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB1A_RAT !!

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 RAB1A_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RAB1A_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAB1A_RAT

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Related Literatures of Post-Translational Modification

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