RAB31_HUMAN - dbPTM
RAB31_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB31_HUMAN
UniProt AC Q13636
Protein Name Ras-related protein Rab-31
Gene Name RAB31
Organism Homo sapiens (Human).
Sequence Length 194
Subcellular Localization Golgi apparatus, trans-Golgi network . Golgi apparatus, trans-Golgi network membrane
Lipid-anchor
Cytoplasmic side . Early endosome . Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane
Lipid-anchor
Cytoplasmic side . Rap
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. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis..
Protein Sequence MAIRELKVCLLGDTGVGKSSIVCRFVQDHFDHNISPTIGASFMTKTVPCGNELHKFLIWDTAGQERFHSLAPMYYRGSAAAVIVYDITKQDSFYTLKKWVKELKEHGPENIVMAIAGNKCDLSDIREVPLKDAKEYAESIGAIVVETSAKNAINIEELFQGISRQIPPLDPHENGNNGTIKVEKPTMQASRRCC
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
8UbiquitinationMAIRELKVCLLGDTG
CCCCEEEEEEECCCC		4.3229967540
14PhosphorylationKVCLLGDTGVGKSSI
EEEEECCCCCCCHHH		31.78-
19PhosphorylationGDTGVGKSSIVCRFV
CCCCCCCHHHHHHHH		21.26-
20PhosphorylationDTGVGKSSIVCRFVQ
CCCCCCHHHHHHHHH		23.64-
35PhosphorylationDHFDHNISPTIGASF
HHCCCCCCCCCCCCE		22.7011784320
36PhosphorylationHFDHNISPTIGASFM
HCCCCCCCCCCCCEE		25.0020230923
37PhosphorylationFDHNISPTIGASFMT
CCCCCCCCCCCCEEC		25.8330266825
41PhosphorylationISPTIGASFMTKTVP
CCCCCCCCEECCCCC		15.4423403867
44PhosphorylationTIGASFMTKTVPCGN
CCCCCEECCCCCCCC		22.8923403867
61PhosphorylationHKFLIWDTAGQERFH
EEEEEEECCCCHHHH		20.0726074081
69PhosphorylationAGQERFHSLAPMYYR
CCCHHHHHHCCCCCC		24.4226074081
74PhosphorylationFHSLAPMYYRGSAAA
HHHHCCCCCCCCCEE		6.7526074081
75PhosphorylationHSLAPMYYRGSAAAV
HHHCCCCCCCCCEEE		11.4026074081
78PhosphorylationAPMYYRGSAAAVIVY
CCCCCCCCCEEEEEE		13.0226074081
85PhosphorylationSAAAVIVYDITKQDS
CCEEEEEEECCCCCC		7.1826074081
88PhosphorylationAVIVYDITKQDSFYT
EEEEEECCCCCCHHH		21.5426074081
98UbiquitinationDSFYTLKKWVKELKE
CCHHHHHHHHHHHHH		61.4029967540
123PhosphorylationAGNKCDLSDIREVPL
ECCCCCHHHHCCCCH		20.1026091039
136PhosphorylationPLKDAKEYAESIGAI
CHHHHHHHHHHHCEE		18.2419835603
137PhosphorylationLKDAKEYAESIGAIV
HHHHHHHHHHHCEEE		12.73-
139PhosphorylationDAKEYAESIGAIVVE
HHHHHHHHHCEEEEE		20.3919835603
140PhosphorylationAKEYAESIGAIVVET
HHHHHHHHCEEEEEC		3.04-
147PhosphorylationIGAIVVETSAKNAIN
HCEEEEECCCCCCCC		23.5226126808
148PhosphorylationGAIVVETSAKNAINI
CEEEEECCCCCCCCH		24.6026126808
163PhosphorylationEELFQGISRQIPPLD
HHHHHHHHCCCCCCC		25.5921712546
164PhosphorylationELFQGISRQIPPLDP
HHHHHHHCCCCCCCC		36.21-
179PhosphorylationHENGNNGTIKVEKPT
CCCCCCCCEEECCCC		21.5424719451
180PhosphorylationENGNNGTIKVEKPTM
CCCCCCCEEECCCCC		5.0824719451
190PhosphorylationEKPTMQASRRCC---
CCCCCHHHHCCC---		11.9024114839
193GeranylgeranylationTMQASRRCC------
CCHHHHCCC------		2.91-
194GeranylgeranylationMQASRRCC-------
CHHHHCCC-------		6.23-
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 RAB31_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB31_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 RAB31_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB8A_HUMANRAB8Aphysical
22939629
STX7_HUMANSTX7physical
22939629
RAE2_HUMANCHMLphysical
26186194
RAE1_HUMANCHMphysical
26186194
RB22A_HUMANRAB22Aphysical
26186194
GDIB_HUMANGDI2physical
26186194
GDS1_HUMANRAP1GDS1physical
26186194
PGTB2_HUMANRABGGTBphysical
26186194
PGTA_HUMANRABGGTAphysical
26186194
TRIM4_HUMANTRIM4physical
26186194
RAB5A_HUMANRAB5Aphysical
26186194
RAE2_HUMANCHMLphysical
28514442
RAE1_HUMANCHMphysical
28514442
GDIA_HUMANGDI1physical
28514442
TRIM4_HUMANTRIM4physical
28514442
RB22A_HUMANRAB22Aphysical
28514442
PGTA_HUMANRABGGTAphysical
28514442
PGTB2_HUMANRABGGTBphysical
28514442
GDIB_HUMANGDI2physical
28514442
EGFR_HUMANEGFRphysical
19725050
EEA1_HUMANEEA1physical
19725050
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 RAB31_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.

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