RAB1B_HUMAN - dbPTM
RAB1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB1B_HUMAN
UniProt AC Q9H0U4
Protein Name Ras-related protein Rab-1B
Gene Name RAB1B
Organism Homo sapiens (Human).
Sequence Length 201
Subcellular Localization Cytoplasm . Membrane
Lipid-anchor
Cytoplasmic side . Preautophagosomal structure membrane
Lipid-anchor
Cytoplasmic side . Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and
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. RAB1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum..
Protein Sequence MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPAGGGCC
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
1Acetylation-------MNPEYDYL
-------CCHHHHHH		19.94-
1Sulfoxidation-------MNPEYDYL
-------CCHHHHHH		19.9428183972
5Phosphorylation---MNPEYDYLFKLL
---CCHHHHHHHHHH		15.9025159151
7Phosphorylation-MNPEYDYLFKLLLI
-CCHHHHHHHHHHHH		17.0928152594
17PhosphorylationKLLLIGDSGVGKSCL
HHHHHCCCCCCCCCE		30.11-
21UbiquitinationIGDSGVGKSCLLLRF
HCCCCCCCCCEEEEE		35.2733845483
23S-palmitoylationDSGVGKSCLLLRFAD
CCCCCCCCEEEEECC		3.3729575903
32PhosphorylationLLRFADDTYTESYIS
EEEECCCCCCHHHHH		32.6520068231
33PhosphorylationLRFADDTYTESYIST
EEECCCCCCHHHHHH		18.5928796482
34PhosphorylationRFADDTYTESYISTI
EECCCCCCHHHHHHE		22.1328796482
36PhosphorylationADDTYTESYISTIGV
CCCCCCHHHHHHEEC		21.7028796482
37PhosphorylationDDTYTESYISTIGVD
CCCCCHHHHHHEECC		7.8328796482
39PhosphorylationTYTESYISTIGVDFK
CCCHHHHHHEECCEE		13.0228796482
40PhosphorylationYTESYISTIGVDFKI
CCHHHHHHEECCEEE		16.5228796482
49PhosphorylationGVDFKIRTIELDGKT
ECCEEEEEEEECCEE		23.4422985185
55MalonylationRTIELDGKTIKLQIW
EEEEECCEEEEEEEE		46.9026320211
55UbiquitinationRTIELDGKTIKLQIW
EEEEECCEEEEEEEE		46.9023000965
56PhosphorylationTIELDGKTIKLQIWD
EEEECCEEEEEEEEC		28.9526307563
58AcetylationELDGKTIKLQIWDTA
EECCEEEEEEEECCC		39.3066727657
58UbiquitinationELDGKTIKLQIWDTA
EECCEEEEEEEECCC		39.3023000965
58MalonylationELDGKTIKLQIWDTA
EECCEEEEEEEECCC		39.3026320211
64PhosphorylationIKLQIWDTAGQERFR
EEEEEECCCCHHHHH		20.0728857561
72PhosphorylationAGQERFRTITSSYYR
CCHHHHHHHHHHHHC		26.3722617229
74PhosphorylationQERFRTITSSYYRGA
HHHHHHHHHHHHCCC		15.8230108239
75PhosphorylationERFRTITSSYYRGAH
HHHHHHHHHHHCCCC		16.7021130716
76PhosphorylationRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE		19.9628348404
76O-(2-cholinephosphoryl)serineRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE		19.96-
76OtherRFRTITSSYYRGAHG
HHHHHHHHHHCCCCE		19.9622158903
77PhosphorylationFRTITSSYYRGAHGI
HHHHHHHHHCCCCEE		9.2823663014
77AMPylationFRTITSSYYRGAHGI
HHHHHHHHHCCCCEE		9.2820651120
77O-AMP-tyrosineFRTITSSYYRGAHGI
HHHHHHHHHCCCCEE		9.28-
78PhosphorylationRTITSSYYRGAHGII
HHHHHHHHCCCCEEE		12.4328060719
88PhosphorylationAHGIIVVYDVTDQES
CCEEEEEEECCCHHH		8.1928985074
91PhosphorylationIIVVYDVTDQESYAN
EEEEEECCCHHHHHC		29.12-
96PhosphorylationDVTDQESYANVKQWL
ECCCHHHHHCHHHHH		11.0518083107
100UbiquitinationQESYANVKQWLQEID
HHHHHCHHHHHHHHH		35.25-
108MethylationQWLQEIDRYASENVN
HHHHHHHHHHCCCHH		34.28-
109PhosphorylationWLQEIDRYASENVNK
HHHHHHHHHCCCHHH		15.6726657352
111PhosphorylationQEIDRYASENVNKLL
HHHHHHHCCCHHHHH		22.2925849741
116UbiquitinationYASENVNKLLVGNKS
HHCCCHHHHHCCCHH		38.6323000965
122UbiquitinationNKLLVGNKSDLTTKK
HHHHCCCHHHCCCCE		39.1423000965
128UbiquitinationNKSDLTTKKVVDNTT
CHHHCCCCEECCCCC		38.0333845483
142PhosphorylationTAKEFADSLGIPFLE
CHHHHHHHHCCCCCC		25.6824719451
150PhosphorylationLGIPFLETSAKNATN
HCCCCCCCCCCCCCC		35.8121712546
151PhosphorylationGIPFLETSAKNATNV
CCCCCCCCCCCCCCH		28.0621712546
163SulfoxidationTNVEQAFMTMAAEIK
CCHHHHHHHHHHHHH		2.5428465586
173SulfoxidationAAEIKKRMGPGAASG
HHHHHHHHCCCCCCC		11.8821406390
179PhosphorylationRMGPGAASGGERPNL
HHCCCCCCCCCCCCC		46.9625159151
187UbiquitinationGGERPNLKIDSTPVK
CCCCCCCEECCCCCC		51.6233845483
190PhosphorylationRPNLKIDSTPVKPAG
CCCCEECCCCCCCCC		37.7823909892
191PhosphorylationPNLKIDSTPVKPAGG
CCCEECCCCCCCCCC		28.4925159151
200GeranylgeranylationVKPAGGGCC------
CCCCCCCCC------		2.558836150
200GeranylgeranylationVKPAGGGCC------
CCCCCCCCC------		2.558836150
201GeranylgeranylationKPAGGGCC-------
CCCCCCCC-------		7.658836150
201MethylationKPAGGGCC-------
CCCCCCCC-------		7.65-
201GeranylgeranylationKPAGGGCC-------
CCCCCCCC-------		7.658836150
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 RAB1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB1B_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 RAB1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAE1_HUMANCHMphysical
9437002
GOGA2_HUMANGOLGA2physical
11306556
A4_HUMANAPPphysical
21832049
RB11B_HUMANRAB11Bphysical
22939629
RAB8A_HUMANRAB8Aphysical
22939629
RB11A_HUMANRAB11Aphysical
22939629
SMRC2_HUMANSMARCC2physical
21988832
TM40L_HUMANTOMM40Lphysical
21988832
CH60_HUMANHSPD1physical
22863883
RINI_HUMANRNH1physical
22863883
GDIA_HUMANGDI1physical
26186194
GDIB_HUMANGDI2physical
26186194
RAB1A_HUMANRAB1Aphysical
26186194
RAB8B_HUMANRAB8Bphysical
26186194
RAE2_HUMANCHMLphysical
26186194
RAE1_HUMANCHMphysical
26186194
BZW2_HUMANBZW2physical
26186194
PGTA_HUMANRABGGTAphysical
26186194
RB33B_HUMANRAB33Bphysical
26186194
GDS1_HUMANRAP1GDS1physical
26186194
AT1A1_HUMANATP1A1physical
26344197
AT1A3_HUMANATP1A3physical
26344197
CCD47_HUMANCCDC47physical
26344197
CY1_HUMANCYC1physical
26344197
DRS7B_HUMANDHRS7Bphysical
26344197
DNJA3_HUMANDNAJA3physical
26344197
ETFA_HUMANETFAphysical
26344197
GDIB_HUMANGDI2physical
26344197
KDSR_HUMANKDSRphysical
26344197
LDHA_HUMANLDHAphysical
26344197
LDHB_HUMANLDHBphysical
26344197
LDHC_HUMANLDHCphysical
26344197
COX2_HUMANCOX2physical
26344197
PDCD6_HUMANPDCD6physical
26344197
PHB_HUMANPHBphysical
26344197
RB11B_HUMANRAB11Bphysical
26344197
RAB2A_HUMANRAB2Aphysical
26344197
RAB6A_HUMANRAB6Aphysical
26344197
RAB6B_HUMANRAB6Bphysical
26344197
RAB7A_HUMANRAB7Aphysical
26344197
RDH13_HUMANRDH13physical
26344197
RPN1_HUMANRPN1physical
26344197
RPN2_HUMANRPN2physical
26344197
STX12_HUMANSTX12physical
26344197
STX7_HUMANSTX7physical
26344197
TMED2_HUMANTMED2physical
26344197
VAPA_HUMANVAPAphysical
26344197
RAB1A_HUMANRAB1Agenetic
26472760
RAB18_HUMANRAB18genetic
26472760
VPS52_HUMANVPS52genetic
26472760
TPC12_HUMANTRAPPC12genetic
26472760
RIC1_HUMANRIC1genetic
26472760
COG3_HUMANCOG3genetic
26472760
COG7_HUMANCOG7genetic
26472760
TPC13_HUMANTRAPPC13genetic
26472760
VPS54_HUMANVPS54genetic
26472760
GDIA_HUMANGDI1physical
28514442
RAB8B_HUMANRAB8Bphysical
28514442
RAE2_HUMANCHMLphysical
28514442
RAE1_HUMANCHMphysical
28514442
GDIB_HUMANGDI2physical
28514442
PGTA_HUMANRABGGTAphysical
28514442
MSS4_HUMANRABIFphysical
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 RAB1B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Prenylation
ReferencePubMed
"Membrane targeting of a Rab GTPase that fails to associate with Rabescort protein (REP) or guanine nucleotide dissociation inhibitor(GDI).";
Overmeyer J.H., Wilson A.L., Maltese W.A.;
J. Biol. Chem. 276:20379-20386(2001).
Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION, INTERACTION WITH GDI1 AND CHM,AND MUTAGENESIS OF TYR-78.
"Prenylation of a Rab1B mutant with altered GTPase activity isimpaired in cell-free systems but not in intact mammalian cells.";
Wilson A.L., Sheridan K.M., Erdman R.A., Maltese W.A.;
Biochem. J. 318:1007-1014(1996).
Cited for: ISOPRENYLATION AT CYS-200 AND CYS-201, INTERACTION WITH GDI1, ANDMUTAGENESIS OF GLN-67.

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