RAB3I_HUMAN - dbPTM
RAB3I_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB3I_HUMAN
UniProt AC Q96QF0
Protein Name Rab-3A-interacting protein
Gene Name RAB3IP {ECO:0000312|EMBL:CAC59836.1}
Organism Homo sapiens (Human).
Sequence Length 476
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Predominantly cytoplasmic but a small proportion colocalizes with SSX2 in the nucleus. Activation of protein kinase C results in redistribution to the periphery of lamellipo
Protein Description Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. Together with RAB11A, 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..
Protein Sequence MGLKKMKGLSYDEAFAMANDPLEGFHEVNLASPTSPDLLGVYESGTQEQTTSPSVIYRPHPSALSSVPIQANALDVSELPTQPVYSSPRRLNCAEISSISFHVTDPAPCSTSGVTAGLTKLTTRKDNYNAEREFLQGATITEACDGSDDIFGLSTDSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKTLVLSSSPTSPTQEPLPGGKTPFKKGHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVLEAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQQGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKEEL
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
41 (in isoform 8)Phosphorylation-4.90-
43 (in isoform 8)Phosphorylation-40.04-
44 (in isoform 8)Phosphorylation-29.47-
44PhosphorylationDLLGVYESGTQEQTT
HHHCEECCCCCCCCC		29.4720068231
46 (in isoform 8)Phosphorylation-37.91-
46PhosphorylationLGVYESGTQEQTTSP
HCEECCCCCCCCCCC		37.9119413330
66 (in isoform 8)Phosphorylation-32.53-
66PhosphorylationPHPSALSSVPIQANA
CCCHHHCCCCCCCCC		32.5320068231
74PhosphorylationVPIQANALDVSELPT
CCCCCCCCCHHHCCC		7.2033259812
77PhosphorylationQANALDVSELPTQPV
CCCCCCHHHCCCCCC		32.8426074081
81PhosphorylationLDVSELPTQPVYSSP
CCHHHCCCCCCCCCC		59.1226074081
85PhosphorylationELPTQPVYSSPRRLN
HCCCCCCCCCCCCCC		15.3226074081
86PhosphorylationLPTQPVYSSPRRLNC
CCCCCCCCCCCCCCC		33.8226074081
87PhosphorylationPTQPVYSSPRRLNCA
CCCCCCCCCCCCCCE		12.5327050516
89UbiquitinationQPVYSSPRRLNCAEI
CCCCCCCCCCCCEEC		58.6332015554
115PhosphorylationPCSTSGVTAGLTKLT
CCCCCCCCCCCEECC		20.66-
139PhosphorylationREFLQGATITEACDG
HHHHCCCCHHHCCCC		34.9428102081
141PhosphorylationFLQGATITEACDGSD
HHCCCCHHHCCCCCC		17.1128102081
147 (in isoform 1)Phosphorylation-20.89-
147 (in isoform 2)Phosphorylation-20.89-
147PhosphorylationITEACDGSDDIFGLS
HHHCCCCCCCCCCCC		20.8920068231
147 (in isoform 3)Phosphorylation-20.89-
154PhosphorylationSDDIFGLSTDSLSRL
CCCCCCCCHHHHHHC		30.4628102081
155PhosphorylationDDIFGLSTDSLSRLR
CCCCCCCHHHHHHCC		34.3528102081
157PhosphorylationIFGLSTDSLSRLRSP
CCCCCHHHHHHCCCC		28.4730278072
159PhosphorylationGLSTDSLSRLRSPSV
CCCHHHHHHCCCCCH		32.9730278072
161UbiquitinationSTDSLSRLRSPSVLE
CHHHHHHCCCCCHHH		5.9729967540
163 (in isoform 4)Phosphorylation-26.56-
163PhosphorylationDSLSRLRSPSVLEVR
HHHHHCCCCCHHHHH		26.5625159151
163 (in isoform 6)Phosphorylation-26.56-
165PhosphorylationLSRLRSPSVLEVREK
HHHCCCCCHHHHHHH		40.3529978859
167UbiquitinationRLRSPSVLEVREKGY
HCCCCCHHHHHHHHH		6.2124816145
183UbiquitinationRLKEELAKAQRELKL
HHHHHHHHHHHHHCC		58.6424816145
217UbiquitinationEELTASLFEEAHKMV
HHHHHHHHHHHHHHH		8.0524816145
247 (in isoform 3)Phosphorylation-4.93-
247 (in isoform 2)Phosphorylation-4.93-
247 (in isoform 1)Phosphorylation-4.93-
249 (in isoform 2)Phosphorylation-35.01-
249 (in isoform 3)Phosphorylation-35.01-
249 (in isoform 1)Phosphorylation-35.01-
250 (in isoform 1)Phosphorylation-14.74-
250 (in isoform 2)Phosphorylation-14.74-
250 (in isoform 3)Phosphorylation-14.74-
250PhosphorylationGKIDVLQAEVAALKT
CCHHHHHHHHHHHHH		14.7432142685
252 (in isoform 1)Phosphorylation-4.18-
252 (in isoform 2)Phosphorylation-4.18-
252 (in isoform 3)Phosphorylation-4.18-
257PhosphorylationAEVAALKTLVLSSSP
HHHHHHHHHHHCCCC		23.9722199227
261PhosphorylationALKTLVLSSSPTSPT
HHHHHHHCCCCCCCC		22.6925159151
262PhosphorylationLKTLVLSSSPTSPTQ
HHHHHHCCCCCCCCC		35.8525159151
263 (in isoform 4)Phosphorylation-28.90-
263 (in isoform 6)Phosphorylation-28.90-
263PhosphorylationKTLVLSSSPTSPTQE
HHHHHCCCCCCCCCC		28.9025159151
265 (in isoform 4)Phosphorylation-49.65-
265 (in isoform 6)Phosphorylation-49.65-
265PhosphorylationLVLSSSPTSPTQEPL
HHHCCCCCCCCCCCC		49.6525159151
266 (in isoform 4)Phosphorylation-29.36-
266 (in isoform 6)Phosphorylation-29.36-
266PhosphorylationVLSSSPTSPTQEPLP
HHCCCCCCCCCCCCC		29.3628355574
268 (in isoform 4)Phosphorylation-45.38-
268PhosphorylationSSSPTSPTQEPLPGG
CCCCCCCCCCCCCCC		45.3825159151
268 (in isoform 6)Phosphorylation-45.38-
272 (in isoform 3)Phosphorylation-6.39-
272 (in isoform 1)Phosphorylation-6.39-
272 (in isoform 2)Phosphorylation-6.39-
272PhosphorylationTSPTQEPLPGGKTPF
CCCCCCCCCCCCCCC		6.3932645325
277PhosphorylationEPLPGGKTPFKKGHT
CCCCCCCCCCCCCCC		36.9126055452
280PhosphorylationPGGKTPFKKGHTRNK
CCCCCCCCCCCCCCC		60.0833259812
284PhosphorylationTPFKKGHTRNKSTSS
CCCCCCCCCCCCCCC		44.6028290473
288PhosphorylationKGHTRNKSTSSAMSG
CCCCCCCCCCCCCCC		36.7523927012
288 (in isoform 6)Phosphorylation-36.75-
288 (in isoform 4)Phosphorylation-36.75-
289PhosphorylationGHTRNKSTSSAMSGS
CCCCCCCCCCCCCCC		28.4525159151
290PhosphorylationHTRNKSTSSAMSGSH
CCCCCCCCCCCCCCC		24.1623927012
291PhosphorylationTRNKSTSSAMSGSHQ
CCCCCCCCCCCCCCC		28.2523927012
294PhosphorylationKSTSSAMSGSHQDLS
CCCCCCCCCCCCCHH		36.5423927012
295UbiquitinationSTSSAMSGSHQDLSV
CCCCCCCCCCCCHHH		18.9632015554
296PhosphorylationTSSAMSGSHQDLSVI
CCCCCCCCCCCHHHH		15.6323927012
301PhosphorylationSGSHQDLSVIQPIVK
CCCCCCHHHHHHHHC		26.0123927012
311UbiquitinationQPIVKDCKEADLSLY
HHHHCCHHHCCCHHH		67.1032015554
318PhosphorylationKEADLSLYNEFRLWK
HHCCCHHHHHHHHCC		14.8527642862
325UbiquitinationYNEFRLWKDEPTMDR
HHHHHHCCCCCCCCC		57.73-
329PhosphorylationRLWKDEPTMDRTCPF
HHCCCCCCCCCCCCH		29.65-
367UbiquitinationVLEAVENNTLSIEPV
HHHHHHCCCCCEEEC		28.9729967540
383UbiquitinationLQPIRFVKASAVECG
CCCEEEEEEEEEECC		33.6329967540
383AcetylationLQPIRFVKASAVECG
CCCEEEEEEEEEECC		33.6320167786
416PhosphorylationKLGDSSNYYYISPFC
EECCCCCEEEECCCC		10.2920090780
462MethylationWEVMQLRKEMSLAKL
HHHHHHHHHHHHHHH		67.38-
471PhosphorylationMSLAKLGYFKEEL--
HHHHHHCCCHHCC--		23.1619664994
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
288SPhosphorylationKinaseSTK38LQ9Y2H1
GPS
288SPhosphorylationKinaseSTK38Q15208
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB3I_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 RAB3I_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
R3GEF_HUMANRAB3IL1physical
19060904
SUV92_HUMANSUV39H2physical
23455924
K1C40_HUMANKRT40physical
25416956
F124A_HUMANFAM124Aphysical
25416956
TXND5_HUMANTXNDC5physical
21516116
PLOD3_HUMANPLOD3physical
21516116
1433E_HUMANYWHAEphysical
27173435
TPC2L_HUMANTRAPPC2Lphysical
27173435
TM102_HUMANTMEM102physical
27173435
PDLI7_HUMANPDLIM7physical
27173435
TPC10_HUMANTRAPPC10physical
27173435
M21D2_HUMANMB21D2physical
27173435
TBC25_HUMANTBC1D25physical
27173435
F110A_HUMANFAM110Aphysical
27173435
EPN2_HUMANEPN2physical
27173435
CCYL1_HUMANCCNYL1physical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
FA53C_HUMANFAM53Cphysical
27173435
UBP21_HUMANUSP21physical
27173435
F110B_HUMANFAM110Bphysical
27173435
AGAP1_HUMANAGAP1physical
27173435
SYDE1_HUMANSYDE1physical
27173435
SH3B4_HUMANSH3BP4physical
27173435
SRS12_HUMANSRSF12physical
27173435
AFAD_HUMANMLLT4physical
27173435
DCLK1_HUMANDCLK1physical
27173435
TESK2_HUMANTESK2physical
27173435
MAGI1_HUMANMAGI1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
KLC3_HUMANKLC3physical
27173435
PDZ11_HUMANPDZD11physical
27173435
DEP1B_HUMANDEPDC1Bphysical
27173435
M3K2_HUMANMAP3K2physical
27173435
PKHA5_HUMANPLEKHA5physical
27173435
UBP8_HUMANUSP8physical
27173435
ARAF_HUMANARAFphysical
27173435
NUMBL_HUMANNUMBLphysical
27173435
PI4KB_HUMANPI4KBphysical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
REEP4_HUMANREEP4physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
AKTS1_HUMANAKT1S1physical
27173435
BAIP2_HUMANBAIAP2physical
27173435
MELK_HUMANMELKphysical
27173435
RAB8A_HUMANRAB8Aphysical
27173435
CBY1_HUMANCBY1physical
27173435
CE170_HUMANCEP170physical
27173435
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 RAB3I_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265; SER-266 ANDTHR-268, AND MASS SPECTROMETRY.
"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-163, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND MASSSPECTROMETRY.

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