RAB1A_MOUSE - dbPTM
RAB1A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB1A_MOUSE
UniProt AC P62821
Protein Name Ras-related protein Rab-1A
Gene Name Rab1A
Organism Mus musculus (Mouse).
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 (By similarity). Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport..
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
2Phosphorylation------MSSMNPEYD
------CCCCCHHHH
37.9926643407
2Acetylation------MSSMNPEYD
------CCCCCHHHH
37.99-
3Phosphorylation-----MSSMNPEYDY
-----CCCCCHHHHH
22.6829472430
8PhosphorylationMSSMNPEYDYLFKLL
CCCCCHHHHHHHHHH
15.9022499769
10PhosphorylationSMNPEYDYLFKLLLI
CCCHHHHHHHHHHHH
17.0922499769
20PhosphorylationKLLLIGDSGVGKSCL
HHHHHCCCCCCCCCE
30.1122817900
24AcetylationIGDSGVGKSCLLLRF
HCCCCCCCCCEEEEE
35.2722826441
26S-nitrosocysteineDSGVGKSCLLLRFAD
CCCCCCCCEEEEECC
3.37-
26S-nitrosylationDSGVGKSCLLLRFAD
CCCCCCCCEEEEECC
3.3721278135
39PhosphorylationADDTYTESYISTIGV
CCCCCCHHHHHEEEC
21.7025159016
40PhosphorylationDDTYTESYISTIGVD
CCCCCHHHHHEEECC
7.8325159016
42PhosphorylationTYTESYISTIGVDFK
CCCHHHHHEEECCEE
13.0225159016
58UbiquitinationRTIELDGKTIKLQIW
EEEEECCEEEEEEEE
46.90-
58MalonylationRTIELDGKTIKLQIW
EEEEECCEEEEEEEE
46.9026320211
58AcetylationRTIELDGKTIKLQIW
EEEEECCEEEEEEEE
46.9023236377
61UbiquitinationELDGKTIKLQIWDTA
EECCEEEEEEEECCC
39.30-
61MalonylationELDGKTIKLQIWDTA
EECCEEEEEEEECCC
39.3026320211
61AcetylationELDGKTIKLQIWDTA
EECCEEEEEEEECCC
39.3023806337
75PhosphorylationAGQERFRTITSSYYR
CCHHHHHHHHHHHHC
26.3726239621
77PhosphorylationQERFRTITSSYYRGA
HHHHHHHHHHHHCCC
15.8226745281
78PhosphorylationERFRTITSSYYRGAH
HHHHHHHHHHHCCCC
16.7024453211
79O-(2-cholinephosphoryl)serineRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE
19.96-
79OtherRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE
19.96-
79PhosphorylationRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE
19.9626745281
80PhosphorylationFRTITSSYYRGAHGI
HHHHHHHHHCCCCEE
9.2829472430
103UbiquitinationQESFNNVKQWLQEID
HHHHHHHHHHHHHHH
37.57-
112PhosphorylationWLQEIDRYASENVNK
HHHHHHHHHCCCHHH
15.6722499769
114PhosphorylationQEIDRYASENVNKLL
HHHHHHHCCCHHHHH
22.2922499769
119AcetylationYASENVNKLLVGNKC
HHCCCHHHHHCCCCC
38.6322826441
119UbiquitinationYASENVNKLLVGNKC
HHCCCHHHHHCCCCC
38.6322790023
125UbiquitinationNKLLVGNKCDLTTKK
HHHHCCCCCCCCCCC
24.1722790023
126S-nitrosylationKLLVGNKCDLTTKKV
HHHCCCCCCCCCCCC
6.3420925432
126S-nitrosocysteineKLLVGNKCDLTTKKV
HHHCCCCCCCCCCCC
6.34-
126GlutathionylationKLLVGNKCDLTTKKV
HHHCCCCCCCCCCCC
6.3424333276
131UbiquitinationNKCDLTTKKVVDYTT
CCCCCCCCCCCCHHH
38.0322790023
136PhosphorylationTTKKVVDYTTAKEFA
CCCCCCCHHHHHHHH
8.3825195567
137PhosphorylationTKKVVDYTTAKEFAD
CCCCCCHHHHHHHHH
18.8025367039
138PhosphorylationKKVVDYTTAKEFADS
CCCCCHHHHHHHHHH
29.5125367039
145PhosphorylationTAKEFADSLGIPFLE
HHHHHHHHHCCCCCC
25.6823984901
187SuccinylationATAGGAEKSNVKIQS
CCCCCCCCCCCEEEC
46.96-
187MalonylationATAGGAEKSNVKIQS
CCCCCCCCCCCEEEC
46.9626320211
187AcetylationATAGGAEKSNVKIQS
CCCCCCCCCCCEEEC
46.9623806337
187UbiquitinationATAGGAEKSNVKIQS
CCCCCCCCCCCEEEC
46.96-
191MalonylationGAEKSNVKIQSTPVK
CCCCCCCEEECCCCC
39.0026320211
191UbiquitinationGAEKSNVKIQSTPVK
CCCCCCCEEECCCCC
39.00-
194PhosphorylationKSNVKIQSTPVKQSG
CCCCEEECCCCCCCC
37.8525521595
195PhosphorylationSNVKIQSTPVKQSGG
CCCEEECCCCCCCCC
18.7425521595
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
194SPhosphorylationKinaseCDK1P11440
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB1A_MOUSE !!

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_MOUSE !!

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

Oops, there are no PPI records of RAB1A_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAB1A_MOUSE

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Related Literatures of Post-Translational Modification

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