RB11B_HUMAN - dbPTM
RB11B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB11B_HUMAN
UniProt AC Q15907
Protein Name Ras-related protein Rab-11B
Gene Name RAB11B
Organism Homo sapiens (Human).
Sequence Length 218
Subcellular Localization Recycling endosome membrane
Lipid-anchor
Cytoplasmic side. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
Lipid-anchor
Cytoplasmic side. Cytoplasmic vesicle, phagosome membrane
Lipid-anchor
Cytoplasmic side . Recruited to p
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 plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis..
Protein Sequence MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL
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
------CCCCHHHCC		29.47-
3Phosphorylation-----MGTRDDEYDY
-----CCCCHHHCCE		29.6228355574
4Citrullination----MGTRDDEYDYL
----CCCCHHHCCEE		43.59-
4Citrullination----MGTRDDEYDYL
----CCCCHHHCCEE		43.59-
8PhosphorylationMGTRDDEYDYLFKVV
CCCCHHHCCEEEEEE		19.5128796482
10PhosphorylationTRDDEYDYLFKVVLI
CCHHHCCEEEEEEEE		17.0928258704
20PhosphorylationKVVLIGDSGVGKSNL
EEEEECCCCCCHHHH		30.1121815630
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4921890473
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4921890473
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4921890473
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4921890473
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4921890473
24MethylationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4944500677
24UbiquitinationIGDSGVGKSNLLSRF
ECCCCCCHHHHHHHH		33.4923000965
40PhosphorylationRNEFNLESKSTIGVE
CCCCCCCCCCEEEEE		34.7630108239
41UbiquitinationNEFNLESKSTIGVEF
CCCCCCCCCEEEEEE		42.0933845483
42PhosphorylationEFNLESKSTIGVEFA
CCCCCCCCEEEEEEE		34.2429255136
43PhosphorylationFNLESKSTIGVEFAT
CCCCCCCEEEEEEEE		26.0330266825
50PhosphorylationTIGVEFATRSIQVDG
EEEEEEEEEEEEECC		30.2120068231
52PhosphorylationGVEFATRSIQVDGKT
EEEEEEEEEEECCEE		17.0224719451
58MalonylationRSIQVDGKTIKAQIW
EEEEECCEEEEEEEE		42.4826320211
58UbiquitinationRSIQVDGKTIKAQIW
EEEEECCEEEEEEEE		42.4823000965
61UbiquitinationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2021890473
61UbiquitinationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2021890473
61UbiquitinationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2021890473
61UbiquitinationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2021890473
61UbiquitinationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2021890473
61UbiquitinationQVDGKTIKAQIWDTA
EECCEEEEEEEECCC		39.2023000965
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-
95UbiquitinationLLVYDIAKHLTYENV
HHHHHHHHHCCHHHH		39.21-
98PhosphorylationYDIAKHLTYENVERW
HHHHHHCCHHHHHHH		28.6328152594
99PhosphorylationDIAKHLTYENVERWL
HHHHHCCHHHHHHHH		16.3328152594
104MethylationLTYENVERWLKELRD
CCHHHHHHHHHHHHH		39.48-
107UbiquitinationENVERWLKELRDHAD
HHHHHHHHHHHHCCC		47.98-
107UbiquitinationENVERWLKELRDHAD
HHHHHHHHHHHHCCC		47.98-
115PhosphorylationELRDHADSNIVIMLV
HHHHCCCCCEEEEEE		29.2830108239
126PhosphorylationIMLVGNKSDLRHLRA
EEEECCHHHHHHHCC		45.9728634298
132MethylationKSDLRHLRAVPTDEA
HHHHHHHCCCCHHHH		27.67-
136PhosphorylationRHLRAVPTDEARAFA
HHHCCCCHHHHHHHH		39.6121406692
145UbiquitinationEARAFAEKNNLSFIE
HHHHHHHHCCCCEEE		47.9421906983
145UbiquitinationEARAFAEKNNLSFIE
HHHHHHHHCCCCEEE		47.94-
170PhosphorylationEAFKNILTEIYRIVS
HHHHHHHHHHHHHHC		19.2820068231
173PhosphorylationKNILTEIYRIVSQKQ
HHHHHHHHHHHCHHH		6.5120068231
177PhosphorylationTEIYRIVSQKQIADR
HHHHHHHCHHHHHHH		29.3227067055
179UbiquitinationIYRIVSQKQIADRAA
HHHHHCHHHHHHHHC		35.8421890473
179UbiquitinationIYRIVSQKQIADRAA
HHHHHCHHHHHHHHC		35.8421890473
179UbiquitinationIYRIVSQKQIADRAA
HHHHHCHHHHHHHHC		35.8423000965
179AcetylationIYRIVSQKQIADRAA
HHHHHCHHHHHHHHC		35.8425953088
179UbiquitinationIYRIVSQKQIADRAA
HHHHHCHHHHHHHHC		35.8421890473
1792-HydroxyisobutyrylationIYRIVSQKQIADRAA
HHHHHCHHHHHHHHC		35.84-
179UbiquitinationIYRIVSQKQIADRAA
HHHHHCHHHHHHHHC		35.8421890473
190PhosphorylationDRAAHDESPGNNVVD
HHHCCCCCCCCCEEE		44.1327732954
214GeranylgeranylationQKPNKLQCCQNL---
CCCCCCCCCCCC---		3.6024023390
214GeranylgeranylationQKPNKLQCCQNL---
CCCCCCCCCCCC---		3.6024023390
215MethylationKPNKLQCCQNL----
CCCCCCCCCCC----		1.62-
215GeranylgeranylationKPNKLQCCQNL----
CCCCCCCCCCC----		1.6224023390
215GeranylgeranylationKPNKLQCCQNL----
CCCCCCCCCCC----		1.6224023390
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 RB11B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB11B_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 RB11B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFIP1_HUMANRAB11FIP1physical
11495908
RFIP2_HUMANRAB11FIP2physical
11495908
RFIP3_HUMANRAB11FIP3physical
11495908
RFIP5_HUMANRAB11FIP5physical
11495908
A4_HUMANAPPphysical
21832049
VATH_HUMANATP6V1Hphysical
22939629
BICL1_MOUSECcdc64physical
20360680
OPTN_HUMANOPTNphysical
24056041
RFIP1_HUMANRAB11FIP1physical
26186194
RFIP2_HUMANRAB11FIP2physical
26186194
WDR44_HUMANWDR44physical
26186194
RAE2_HUMANCHMLphysical
26186194
RAE1_HUMANCHMphysical
26186194
3BP5L_HUMANSH3BP5Lphysical
26186194
RAB25_HUMANRAB25physical
26186194
3BP5_HUMANSH3BP5physical
26186194
S10A3_HUMANS100A3physical
26186194
SPB5_HUMANSERPINB5physical
26186194
SBP1_HUMANSELENBP1physical
26186194
RFIP5_HUMANRAB11FIP5physical
26186194
LYG2_HUMANLYG2physical
26186194
LRC15_HUMANLRRC15physical
26186194
DNPEP_HUMANDNPEPphysical
26186194
HPHL1_HUMANHEPHL1physical
26186194
LEG3_HUMANLGALS3physical
26186194
DSG4_HUMANDSG4physical
26186194
CALL3_HUMANCALML3physical
26186194
DUS14_HUMANDUSP14physical
26186194
PLCD1_HUMANPLCD1physical
26186194
PADI3_HUMANPADI3physical
26186194
FA26D_HUMANFAM26Dphysical
26186194
TRI27_HUMANTRIM27physical
26186194
EPCR_HUMANPROCRphysical
26186194
DUT_HUMANDUTphysical
26344197
GNAI3_HUMANGNAI3physical
26344197
NTF2_HUMANNUTF2physical
26344197
PHB2_HUMANPHB2physical
26344197
RAB5B_HUMANRAB5Bphysical
26344197
RAB5C_HUMANRAB5Cphysical
26344197
RAB7A_HUMANRAB7Aphysical
26344197
RFIP2_HUMANRAB11FIP2physical
28514442
RFIP5_HUMANRAB11FIP5physical
28514442
RFIP1_HUMANRAB11FIP1physical
28514442
3BP5_HUMANSH3BP5physical
28514442
RAB25_HUMANRAB25physical
28514442
DNPEP_HUMANDNPEPphysical
28514442
LYG2_HUMANLYG2physical
28514442
RAE2_HUMANCHMLphysical
28514442
DSG4_HUMANDSG4physical
28514442
RAE1_HUMANCHMphysical
28514442
3BP5L_HUMANSH3BP5Lphysical
28514442
PLCD1_HUMANPLCD1physical
28514442
FA26D_HUMANFAM26Dphysical
28514442
HPHL1_HUMANHEPHL1physical
28514442
PADI3_HUMANPADI3physical
28514442
SBP1_HUMANSELENBP1physical
28514442
LRC15_HUMANLRRC15physical
28514442
DUS14_HUMANDUSP14physical
28514442
S10A3_HUMANS100A3physical
28514442
BSPRY_HUMANBSPRYphysical
28514442
WDR44_HUMANWDR44physical
28514442
CALL3_HUMANCALML3physical
28514442
SPB5_HUMANSERPINB5physical
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 RB11B_HUMAN

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Related Literatures of Post-Translational Modification

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