RABE1_HUMAN - dbPTM
RABE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RABE1_HUMAN
UniProt AC Q15276
Protein Name Rab GTPase-binding effector protein 1
Gene Name RABEP1
Organism Homo sapiens (Human).
Sequence Length 862
Subcellular Localization Cytoplasm. Early endosome. Recycling endosome. Cytoplasmic vesicle.
Protein Description Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. [PubMed: 22841712 Stimulates RABGEF1 mediated nucleotide exchange on RAB5A.]
Protein Sequence MAQPGPASQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERTQWAQYRESAEREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNKRKDHKKADVEEEIKIPVVCALTQEESSAQLSNEEEHLDSTRGSVHSLDAGLLLPSGDPFSKSDNDMFKDGLRRAQSTDSLGTSGSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTASLGSLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSETEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRELVLKYREDIINVRTAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQLPET
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------MAQPGPASQ
------CCCCCCCCC		25.0322814378
8PhosphorylationMAQPGPASQPDVSLQ
CCCCCCCCCCCCCHH		45.4320068231
13PhosphorylationPASQPDVSLQQRVAE
CCCCCCCCHHHHHHH		28.0420068231
23UbiquitinationQRVAELEKINAEFLR
HHHHHHHHHHHHHHH		54.61-
42UbiquitinationLEQEFNQKRAKFKEL
HHHHHHHHHHHHHHH		56.26-
47MalonylationNQKRAKFKELYLAKE
HHHHHHHHHHHHHCH		46.2126320211
99UbiquitinationATVSENTKQEAIDEV
EEECCHHHHHHHHHH		58.69-
107UbiquitinationQEAIDEVKRQWREEV
HHHHHHHHHHHHHHH		36.50-
107 (in isoform 2)Ubiquitination-36.50-
116PhosphorylationQWREEVASLQAVMKE
HHHHHHHHHHHHHHH		26.62-
162PhosphorylationADLRRRLSEGQEEEN
HHHHHHHHHCHHHHH		37.5629255136
174SulfoxidationEENLENEMKKAQEDA
HHHHHHHHHHHHHHH		8.9921406390
203PhosphorylationAALKDKLTEAEDKIK
HHHHHHHHHHHHHHH		38.60-
218UbiquitinationELEASKVKELNHYLE
HHHHHHHHHHHHHHH		61.29-
223PhosphorylationKVKELNHYLEAEKSC
HHHHHHHHHHHHHHC		12.7425159151
229PhosphorylationHYLEAEKSCRTDLEM
HHHHHHHHCCCCHHH		10.5928270605
232PhosphorylationEAEKSCRTDLEMYVA
HHHHHCCCCHHHHHH		49.6228270605
237PhosphorylationCRTDLEMYVAVLNTQ
CCCCHHHHHHHHHCC		3.9527642862
243PhosphorylationMYVAVLNTQKSVLQE
HHHHHHHCCHHHHHH		32.9628270605
246PhosphorylationAVLNTQKSVLQEDAE
HHHHCCHHHHHHHHH		20.4522985185
277UbiquitinationRQQHNQLKHTWQKAN
HHHHHHHHHHHHHHH		29.26-
282AcetylationQLKHTWQKANDQFLE
HHHHHHHHHHHHHHH		40.4919608861
282MalonylationQLKHTWQKANDQFLE
HHHHHHHHHHHHHHH		40.4926320211
282 (in isoform 2)Acetylation-40.49-
306PhosphorylationQRMEIVLTSEQLRQV
HHHHHHHCHHHHHHH		21.2328464451
307PhosphorylationRMEIVLTSEQLRQVE
HHHHHHCHHHHHHHH		21.1328464451
331UbiquitinationDEQQRLNKRKDHKKA
HHHHHHHHHHHHHCC		66.47-
353PhosphorylationIPVVCALTQEESSAQ
CCHHHCCCCCHHHCC		18.5328270605
357PhosphorylationCALTQEESSAQLSNE
HCCCCCHHHCCCCCC		30.1628270605
358PhosphorylationALTQEESSAQLSNEE
CCCCCHHHCCCCCCH		24.2628270605
362PhosphorylationEESSAQLSNEEEHLD
CHHHCCCCCCHHHHH		30.0728270605
370PhosphorylationNEEEHLDSTRGSVHS
CCHHHHHCCCCCCEE		26.7727362937
371PhosphorylationEEEHLDSTRGSVHSL
CHHHHHCCCCCCEEC		38.4228270605
374PhosphorylationHLDSTRGSVHSLDAG
HHHCCCCCCEECCCC		17.2330266825
377PhosphorylationSTRGSVHSLDAGLLL
CCCCCCEECCCCEEC		26.2829255136
386PhosphorylationDAGLLLPSGDPFSKS
CCCEECCCCCCCCCC		56.6623403867
391PhosphorylationLPSGDPFSKSDNDMF
CCCCCCCCCCCCCHH		36.3223403867
392UbiquitinationPSGDPFSKSDNDMFK
CCCCCCCCCCCCHHH		63.31-
393PhosphorylationSGDPFSKSDNDMFKD
CCCCCCCCCCCHHHH		40.2127732954
399UbiquitinationKSDNDMFKDGLRRAQ
CCCCCHHHHHHHHHH		44.22-
407PhosphorylationDGLRRAQSTDSLGTS
HHHHHHHCCCCCCCC		32.9519664994
407 (in isoform 2)Phosphorylation-32.95-
408PhosphorylationGLRRAQSTDSLGTSG
HHHHHHCCCCCCCCH		19.9629255136
408 (in isoform 2)Phosphorylation-19.96-
410PhosphorylationRRAQSTDSLGTSGSL
HHHHCCCCCCCCHHH		28.8729255136
410 (in isoform 2)Phosphorylation-28.87-
413PhosphorylationQSTDSLGTSGSLQSK
HCCCCCCCCHHHHHH		34.9029255136
413 (in isoform 2)Phosphorylation-34.90-
414PhosphorylationSTDSLGTSGSLQSKA
CCCCCCCCHHHHHHH		25.2930266825
414 (in isoform 2)Phosphorylation-25.29-
416PhosphorylationDSLGTSGSLQSKALG
CCCCCCHHHHHHHHC		24.0130266825
419PhosphorylationGTSGSLQSKALGYNY
CCCHHHHHHHHCCCC		25.7823927012
420UbiquitinationTSGSLQSKALGYNYK
CCHHHHHHHHCCCCC		34.37-
424PhosphorylationLQSKALGYNYKAKSA
HHHHHHCCCCCCCCC		19.0326074081
426PhosphorylationSKALGYNYKAKSAGN
HHHHCCCCCCCCCCC		12.1126074081
427UbiquitinationKALGYNYKAKSAGNL
HHHCCCCCCCCCCCC		45.78-
430PhosphorylationGYNYKAKSAGNLDES
CCCCCCCCCCCCCHH		46.3929507054
447PhosphorylationGPLVGADSVSENFDT
CCCCCCCCCCCCCCC		27.3225921289
449PhosphorylationLVGADSVSENFDTAS
CCCCCCCCCCCCCCC		30.6725921289
454PhosphorylationSVSENFDTASLGSLQ
CCCCCCCCCCCCCCC		17.6326074081
456PhosphorylationSENFDTASLGSLQMP
CCCCCCCCCCCCCCC		35.0426074081
459PhosphorylationFDTASLGSLQMPSGF
CCCCCCCCCCCCCCE		22.2626074081
464PhosphorylationLGSLQMPSGFMLTKD
CCCCCCCCCEEECCC		39.0426074081
469PhosphorylationMPSGFMLTKDQERAI
CCCCEEECCCHHHHH		22.3126074081
480PhosphorylationERAIKAMTPEQEETA
HHHHHHCCHHHHHHH		28.6528102081
480 (in isoform 2)Phosphorylation-28.65-
486PhosphorylationMTPEQEETASLLSSV
CCHHHHHHHHHHHHH		22.3122199227
488PhosphorylationPEQEETASLLSSVTQ
HHHHHHHHHHHHHHH		36.9422199227
491PhosphorylationEETASLLSSVTQGME
HHHHHHHHHHHHCHH		28.2320068231
492PhosphorylationETASLLSSVTQGMES
HHHHHHHHHHHCHHH		29.2026657352
494PhosphorylationASLLSSVTQGMESAY
HHHHHHHHHCHHHEE		22.7328464451
499PhosphorylationSVTQGMESAYVSPSG
HHHHCHHHEEECCCC		18.9222199227
501PhosphorylationTQGMESAYVSPSGYR
HHCHHHEEECCCCCE		15.6722199227
503PhosphorylationGMESAYVSPSGYRLV
CHHHEEECCCCCEEC		10.7322199227
503 (in isoform 2)Phosphorylation-10.73-
505PhosphorylationESAYVSPSGYRLVSE
HHEEECCCCCEECCH		40.7322199227
507PhosphorylationAYVSPSGYRLVSETE
EEECCCCCEECCHHH		12.7122199227
511PhosphorylationPSGYRLVSETEWNLL
CCCCEECCHHHHHHH		43.3128857561
520UbiquitinationTEWNLLQKEVHNAGN
HHHHHHHHHHHHHHH		62.7721890473
520UbiquitinationTEWNLLQKEVHNAGN
HHHHHHHHHHHHHHH		62.7721890473
520 (in isoform 1)Ubiquitination-62.7721890473
520 (in isoform 2)Ubiquitination-62.7721890473
528UbiquitinationEVHNAGNKLGRRCDM
HHHHHHHHHHHCCCC		51.94-
553PhosphorylationIQIQEAETRDQVKKL
CCCEECHHHHHHHHH		46.74-
559MalonylationETRDQVKKLQLMLRQ
HHHHHHHHHHHHHHH		42.4826320211
578UbiquitinationLEKTMKDKQELEDFI
HHHHHHHHHHHHHHH		39.90-
586UbiquitinationQELEDFIKQSSEDSS
HHHHHHHHHCCCCCH		44.09-
586 (in isoform 2)Ubiquitination-44.09-
634PhosphorylationQMAVLMQSREQVSEE
HHHHHHHCHHHHHHH		24.6628348404
647UbiquitinationEELVRLQKDNDSLQG
HHHHHHHCCCCCCCC		64.19-
651PhosphorylationRLQKDNDSLQGKHSL
HHHCCCCCCCCCCCE		28.9324719451
701UbiquitinationAADHVEEKLKAEILF
HHHHHHHHHHHHHHH		41.61-
742PhosphorylationKEEIASISSLKAELE
HHHHHHHHHHHHHHH		27.4224719451
745UbiquitinationIASISSLKAELERIK
HHHHHHHHHHHHHHH		41.59-
759 (in isoform 2)Phosphorylation-33.5120068231
765UbiquitinationLESTLREKSQQLESL
HHHHHHHHHHHHHHH		47.32-
766PhosphorylationESTLREKSQQLESLQ
HHHHHHHHHHHHHHH		20.5718452278
771PhosphorylationEKSQQLESLQEIKIS
HHHHHHHHHHHHHCC		43.9018452278
778PhosphorylationSLQEIKISLEEQLKK
HHHHHHCCHHHHHHH		25.4022985185
784UbiquitinationISLEEQLKKETAAKA
CCHHHHHHHHHHHHH		48.54-
792PhosphorylationKETAAKATVEQLMFE
HHHHHHHHHHHHHHH		24.7020068231
797SulfoxidationKATVEQLMFEEKNKA
HHHHHHHHHHHHHHH		3.8721406390
852UbiquitinationRAILNDTKLTDINQL
HHHHHCCCCCCHHHC		52.86-
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
407SPhosphorylationKinasePRKD1Q15139
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RABE1_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 RABE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB5A_HUMANRAB5Aphysical
9045618
HUNK_HUMANHUNKphysical
11129044
RABE1_HUMANRABEP1physical
9524117
RAB5A_HUMANRAB5Aphysical
9524117
RAB4A_HUMANRAB4Aphysical
9524117
GGA1_HUMANGGA1physical
12505986
GGA2_HUMANGGA2physical
12505986
EEA1_HUMANEEA1physical
10720461
RABE2_HUMANRABEP2physical
10720461
RABX5_HUMANRABGEF1physical
10720461
ECM29_HUMANKIAA0368physical
20682791
RABX5_HUMANRABGEF1physical
11452015
SMU1_HUMANSMU1physical
22939629
UACA_HUMANUACAphysical
22939629
TRI26_HUMANTRIM26physical
21988832
RGS17_HUMANRGS17physical
21988832
PLEC_HUMANPLECphysical
22863883
RABE1_HUMANRABEP1physical
15457209
RABX5_HUMANRABGEF1physical
9323142
AP1G2_HUMANAP1G2physical
14665628
AP1G1_HUMANAP1G1physical
14665628
GGA3_HUMANGGA3physical
14665628
GGA2_HUMANGGA2physical
14665628
GGA1_HUMANGGA1physical
14665628
RABX5_HUMANRABGEF1physical
26430212
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
YETS4_HUMANYEATS4physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
EXOC4_HUMANEXOC4physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
GRAP1_HUMANGRIPAP1physical
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 RABE1_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-407; THR-408 AND SER-410, AND MASSSPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-282, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.
"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-407; THR-408 AND SER-410, AND MASSSPECTROMETRY.
"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-407 AND SER-410, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-408 AND SER-410, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.

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