RB11A_HUMAN - dbPTM
RB11A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB11A_HUMAN
UniProt AC P62491
Protein Name Ras-related protein Rab-11A
Gene Name RAB11A
Organism Homo sapiens (Human).
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 (PubMed:1
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. 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		29.6228355574
8PhosphorylationMGTRDDEYDYLFKVV
CCCCHHHHCEEEEEE		19.5128796482
10PhosphorylationTRDDEYDYLFKVVLI
CCHHHHCEEEEEEEE		17.0928258704
20PhosphorylationKVVLIGDSGVGKSNL
EEEEECCCCCCHHHH		30.1121815630
24MethylationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4944500665
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4921906983
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4921890473
24AcetylationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4927452117
40PhosphorylationRNEFNLESKSTIGVE
CCCCCCCCCCEEEEE		34.7630108239
42PhosphorylationEFNLESKSTIGVEFA
CCCCCCCCEEEEEEE		34.2429255136
43PhosphorylationFNLESKSTIGVEFAT
CCCCCCCEEEEEEEE		26.0330266825
50PhosphorylationTIGVEFATRSIQVDG
EEEEEEEEEEEEECC		30.2120068231
52PhosphorylationGVEFATRSIQVDGKT
EEEEEEEEEEECCEE		17.0224719451
58MalonylationRSIQVDGKTIKAQIW
EEEEECCEEEEEEEE		42.4826320211
58UbiquitinationRSIQVDGKTIKAQIW
EEEEECCEEEEEEEE		42.48-
61AcetylationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2026822725
61UbiquitinationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2021890473
61UbiquitinationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2021906983
73PhosphorylationDTAGQERYRAITSAY
CCCCHHHHHHHHHHH		12.0228152594
74MethylationTAGQERYRAITSAYY
CCCHHHHHHHHHHHH		26.24-
77PhosphorylationQERYRAITSAYYRGA
HHHHHHHHHHHHHHH		13.3030266825
78PhosphorylationERYRAITSAYYRGAV
HHHHHHHHHHHHHHH		14.2530266825
80PhosphorylationYRAITSAYYRGAVGA
HHHHHHHHHHHHHHH		8.0823403867
81PhosphorylationRAITSAYYRGAVGAL
HHHHHHHHHHHHHHH		11.4228152594
91PhosphorylationAVGALLVYDIAKHLT
HHHHHHHHHHHHHCC		11.12-
95UbiquitinationLLVYDIAKHLTYENV
HHHHHHHHHCCHHHH		39.21-
98PhosphorylationYDIAKHLTYENVERW
HHHHHHCCHHHHHHH		28.6328152594
99PhosphorylationDIAKHLTYENVERWL
HHHHHCCHHHHHHHH		16.3328152594
104MethylationLTYENVERWLKELRD
CCHHHHHHHHHHHHH		39.48-
107UbiquitinationENVERWLKELRDHAD
HHHHHHHHHHHHCCC		47.98-
115PhosphorylationELRDHADSNIVIMLV
HHHHCCCCCEEEEEE		29.2830108239
126PhosphorylationIMLVGNKSDLRHLRA
EEEECCHHHHHHHCC		45.9728634298
132MethylationKSDLRHLRAVPTDEA
HHHHHHHCCCCHHHH		27.67-
136PhosphorylationRHLRAVPTDEARAFA
HHHCCCCHHHHHHHH		39.6121406692
145UbiquitinationEARAFAEKNGLSFIE
HHHHHHHHHCCCEEE		53.54-
177PhosphorylationTEIYRIVSQKQMSDR
HHHHHHHCHHHHCCC		29.3222188018
179AcetylationIYRIVSQKQMSDRRE
HHHHHCHHHHCCCCC		40.2226210075
179UbiquitinationIYRIVSQKQMSDRRE
HHHHHCHHHHCCCCC		40.2221906983
190PhosphorylationDRRENDMSPSNNVVP
CCCCCCCCCCCCEEC		28.2125159151
192PhosphorylationRENDMSPSNNVVPIH
CCCCCCCCCCEECCC		33.4625159151
203PhosphorylationVPIHVPPTTENKPKV
ECCCCCCCCCCCCCC		40.4420068231
204PhosphorylationPIHVPPTTENKPKVQ
CCCCCCCCCCCCCCE		43.2520068231
207UbiquitinationVPPTTENKPKVQCCQ
CCCCCCCCCCCEECC		39.7321906983
212GeranylgeranylationENKPKVQCCQNI---
CCCCCCEECCCC---		2.6324023390
212GeranylgeranylationENKPKVQCCQNI---
CCCCCCEECCCC---		2.6324023390
213GeranylgeranylationNKPKVQCCQNI----
CCCCCEECCCC----		1.6224023390
213GeranylgeranylationNKPKVQCCQNI----
CCCCCEECCCC----		1.6224023390
213MethylationNKPKVQCCQNI----
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
177SPhosphorylationKinasePRKCBP05771-2
GPS
177SPhosphorylationKinasePRKCEQ02156
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB11A_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFIP1_HUMANRAB11FIP1physical
17353931
RFIP5_HUMANRAB11FIP5physical
11163216
SEC13_HUMANSEC13physical
10747849
RFIP1_HUMANRAB11FIP1physical
11786538
RFIP2_HUMANRAB11FIP2physical
11495908
RFIP3_HUMANRAB11FIP3physical
11495908
RFIP5_HUMANRAB11FIP5physical
11495908
RFIP1_HUMANRAB11FIP1physical
11495908
RFIP5_HUMANRAB11FIP5physical
16148947
RFIP3_HUMANRAB11FIP3physical
16148947
RB11B_HUMANRAB11Bphysical
22939629
KCNH2_HUMANKCNH2physical
23589291
RFIP2_HUMANRAB11FIP2physical
16734419
OPTN_HUMANOPTNphysical
17626244
TYDP2_HUMANTDP2physical
21988832
1433G_HUMANYWHAGphysical
21988832
ZN363_HUMANRCHY1physical
21988832
OPTN_HUMANOPTNphysical
16905101
OPTN_HUMANOPTNphysical
24056041
RFIP2_HUMANRAB11FIP2physical
16473632
GDIR1_HUMANARHGDIAphysical
26344197
NTF2_HUMANNUTF2physical
26344197
RAB5A_HUMANRAB5Aphysical
26344197
RAB5B_HUMANRAB5Bphysical
26344197
RAB5C_HUMANRAB5Cphysical
26344197
RAB7A_HUMANRAB7Aphysical
26344197
RFIP3_HUMANRAB11FIP3physical
19327867
PHB_HUMANPHBphysical
26496610
SOAT1_HUMANSOAT1physical
26496610
EVI5_HUMANEVI5physical
26496610
EHD1_HUMANEHD1physical
26496610
PHB2_HUMANPHB2physical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
RFIP5_HUMANRAB11FIP5physical
26496610
WDR44_HUMANWDR44physical
26496610
GTPB2_HUMANGTPBP2physical
26496610
KDIS_HUMANKIDINS220physical
26496610
XPO5_HUMANXPO5physical
26496610
TMM43_HUMANTMEM43physical
26496610
RFIP1_HUMANRAB11FIP1physical
26496610
TB182_HUMANTNKS1BP1physical
26496610
EVI5L_HUMANEVI5Lphysical
26496610
EXOC6_HUMANEXOC6physical
26553929
SYTL4_HUMANSYTL4physical
26553929
RAB3B_HUMANRAB3Bphysical
26553929
STX3_HUMANSTX3physical
26553929
VAMP7_HUMANVAMP7physical
26553929
MTMR4_HUMANMTMR4physical
27432908
RFIP2_HUMANRAB11FIP2physical
28514442
RFIP5_HUMANRAB11FIP5physical
28514442
RFIP1_HUMANRAB11FIP1physical
28514442
RAB25_HUMANRAB25physical
28514442
RAE2_HUMANCHMLphysical
28514442
3BP5_HUMANSH3BP5physical
28514442
DNPEP_HUMANDNPEPphysical
28514442
RAE1_HUMANCHMphysical
28514442
3BP5L_HUMANSH3BP5Lphysical
28514442
PLCG1_HUMANPLCG1physical
28514442
WDR44_HUMANWDR44physical
28514442
GDIA_HUMANGDI1physical
28514442
CARM1_HUMANCARM1physical
28514442
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 RB11A_HUMAN

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