RB11A_MOUSE - dbPTM
RB11A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB11A_MOUSE
UniProt AC P62492
Protein Name Ras-related protein Rab-11A
Gene Name Rab11a
Organism Mus musculus (Mouse).
Sequence Length 216
Subcellular Localization Cell membrane
Lipid-anchor . Recycling endosome membrane
Lipid-anchor . Cleavage furrow . Cytoplasmic vesicle, phagosome . Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Localize
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. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes (By similarity). May also play a role in melanosome transport and release from melanocytes..
Protein Sequence MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQMSDRRENDMSPSNNVVPIHVPPTTENKPKVQCCQNI
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------MGTRDDEYD
------CCCCHHHHC
29.47-
3Phosphorylation-----MGTRDDEYDY
-----CCCCHHHHCE
29.6222499769
8PhosphorylationMGTRDDEYDYLFKVV
CCCCHHHHCEEEEEE
19.5122499769
10PhosphorylationTRDDEYDYLFKVVLI
CCHHHHCEEEEEEEE
17.0928066266
20PhosphorylationKVVLIGDSGVGKSNL
EEEEECCCCCCHHHH
30.1125338131
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH
33.49-
40PhosphorylationRNEFNLESKSTIGVE
CCCCCCCCCCEEEEE
34.76-
42PhosphorylationEFNLESKSTIGVEFA
CCCCCCCCEEEEEEE
34.2426824392
43PhosphorylationFNLESKSTIGVEFAT
CCCCCCCEEEEEEEE
26.0319060867
52PhosphorylationGVEFATRSIQVDGKT
EEEEEEEEEEECCEE
17.02-
73PhosphorylationDTAGQERYRAITSAY
CCCCHHHHHHHHHHH
12.0229514104
77PhosphorylationQERYRAITSAYYRGA
HHHHHHHHHHHHHHH
13.3026745281
78PhosphorylationERYRAITSAYYRGAV
HHHHHHHHHHHHHHH
14.2526824392
80PhosphorylationYRAITSAYYRGAVGA
HHHHHHHHHHHHHHH
8.0828066266
115PhosphorylationELRDHADSNIVIMLV
HHHHCCCCCEEEEEE
29.2822817900
145UbiquitinationEARAFAEKNGLSFIE
HHHHHHHHHCCCEEE
53.54-
167PhosphorylationNVEAAFQTILTEIYR
CHHHHHHHHHHHHHH
16.11-
170PhosphorylationAAFQTILTEIYRIVS
HHHHHHHHHHHHHHC
19.24-
173PhosphorylationQTILTEIYRIVSQKQ
HHHHHHHHHHHCHHH
6.51-
179UbiquitinationIYRIVSQKQMSDRRE
HHHHHCHHHHCCCCC
40.2222790023
182PhosphorylationIVSQKQMSDRRENDM
HHCHHHHCCCCCCCC
26.0223375375
190PhosphorylationDRRENDMSPSNNVVP
CCCCCCCCCCCCEEC
28.2125521595
192PhosphorylationRENDMSPSNNVVPIH
CCCCCCCCCCEECCC
33.4625521595
203PhosphorylationVPIHVPPTTENKPKV
ECCCCCCCCCCCCCC
40.4420415495
204PhosphorylationPIHVPPTTENKPKVQ
CCCCCCCCCCCCCCE
43.2525521595
212GeranylgeranylationENKPKVQCCQNI---
CCCCCCEECCCC---
2.63-
213MethylationNKPKVQCCQNI----
CCCCCEECCCC----
1.62-
213GeranylgeranylationNKPKVQCCQNI----
CCCCCEECCCC----
1.62-

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 RB11A_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB11A_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 RB11A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OPTN_MOUSEOptnphysical
22465952
RB11A_MOUSERab11aphysical
22465952
ADT2_HUMANSLC25A5physical
26496610
PHB_HUMANPHBphysical
26496610
EVI5_HUMANEVI5physical
26496610
RB11B_HUMANRAB11Bphysical
26496610
CHK2_HUMANCHEK2physical
26496610
PHB2_HUMANPHB2physical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
WDR44_HUMANWDR44physical
26496610
RFIP1_HUMANRAB11FIP1physical
26496610
EVI5L_HUMANEVI5Lphysical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RB11A_MOUSE

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Related Literatures of Post-Translational Modification

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