RABE2_HUMAN - dbPTM
RABE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RABE2_HUMAN
UniProt AC Q9H5N1
Protein Name Rab GTPase-binding effector protein 2
Gene Name RABEP2
Organism Homo sapiens (Human).
Sequence Length 569
Subcellular Localization Cytoplasm . Early endosome .
Protein Description Plays a role in membrane trafficking and in homotypic early endosome fusion..
Protein Sequence MAAAAPVAADDDERRRRPGAALEDSRSQEGANGEAESGELSRLRAELAGALAEMETMKAVAEVSESTKAEAVAAVQRQCQEEVASLQAILKDSISSYEAQITALKQERQQQQQDCEEKERELGRLKQLLSRAYPLDSLEKQMEKAHEDSEKLREIVLPMEKEIEELKAKLLRAEELIQEIQRRPRHAPSLHGSTELLPLSRDPSPPLEPLEELSGDGGPAAEAFAHNCDDSASISSFSLGGGVGSSSSLPQSRQGLSPEQEETASLVSTGTLVPEGIYLPPPGYQLVPDTQWEQLQTEGRQLQKDLESVSRERDELQEGLRRSNEDCAKQMQVLLAQVQNSEQLLRTLQGTVSQAQERVQLQMAELVTTHKCLHHEVKRLNEENQGLRAEQLPSSAPQGSQQEQGEEESLPSSVPELQQLLCCTRQEARARLQAQEHGAERLRIEIVTLREALEEETVARASLEGQLRVQREETEVLEASLCSLRTEMERVQQEQSKAQLPDLLSEQRAKVLRLQAELETSEQVQRDFVRLSQALQVRLERIRQAETLEQVRSIMDEAPLTDVRDIKDT
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------MAAAAPVAA
------CCCCCCCCC		13.0522814378
25PhosphorylationPGAALEDSRSQEGAN
CCCCHHCCCCCCCCC		25.1824719451
27PhosphorylationAALEDSRSQEGANGE
CCHHCCCCCCCCCCC		36.2121815630
56PhosphorylationGALAEMETMKAVAEV
HHHHHHHHHHHHHHH		23.7422210691
91UbiquitinationASLQAILKDSISSYE
HHHHHHHHHHHHHHH		43.2329967540
93PhosphorylationLQAILKDSISSYEAQ
HHHHHHHHHHHHHHH		23.8424719451
105 (in isoform 2)Ubiquitination-47.8821890473
105 (in isoform 1)Ubiquitination-47.8821890473
105UbiquitinationEAQITALKQERQQQQ
HHHHHHHHHHHHHHH		47.8823000965
126AcetylationERELGRLKQLLSRAY
HHHHHHHHHHHHHHC		37.2212650579
126UbiquitinationERELGRLKQLLSRAY
HHHHHHHHHHHHHHC		37.2229967540
161UbiquitinationEIVLPMEKEIEELKA
HHHHCCHHHHHHHHH		58.71-
189PhosphorylationRRPRHAPSLHGSTEL
HCCCCCCCCCCCCCC		33.5123401153
193PhosphorylationHAPSLHGSTELLPLS
CCCCCCCCCCCCCCC		14.1528176443
194PhosphorylationAPSLHGSTELLPLSR
CCCCCCCCCCCCCCC		34.9328176443
200PhosphorylationSTELLPLSRDPSPPL
CCCCCCCCCCCCCCC		32.4729255136
204PhosphorylationLPLSRDPSPPLEPLE
CCCCCCCCCCCCCHH		43.3626074081
214PhosphorylationLEPLEELSGDGGPAA
CCCHHHHCCCCCHHH		37.8128348404
231PhosphorylationFAHNCDDSASISSFS
HHHCCCCCCCCCEEE		15.6328348404
233PhosphorylationHNCDDSASISSFSLG
HCCCCCCCCCEEECC		27.2728348404
235PhosphorylationCDDSASISSFSLGGG
CCCCCCCCEEECCCC		23.8828348404
236PhosphorylationDDSASISSFSLGGGV
CCCCCCCEEECCCCC		19.7228348404
238PhosphorylationSASISSFSLGGGVGS
CCCCCEEECCCCCCC		28.2228348404
257PhosphorylationPQSRQGLSPEQEETA
CHHHCCCCHHHHHHH		32.9628348404
263PhosphorylationLSPEQEETASLVSTG
CCHHHHHHHHHHCCC		22.3128348404
265PhosphorylationPEQEETASLVSTGTL
HHHHHHHHHHCCCCC		36.4024275569
268PhosphorylationEETASLVSTGTLVPE
HHHHHHHCCCCCCCC		26.8124275569
271PhosphorylationASLVSTGTLVPEGIY
HHHHCCCCCCCCCEE		25.3524275569
400PhosphorylationPSSAPQGSQQEQGEE
CCCCCCCCCCCCCCC		24.3628348404
409PhosphorylationQEQGEEESLPSSVPE
CCCCCCCCCCCCCHH		49.1928348404
497UbiquitinationRVQQEQSKAQLPDLL
HHHHHHHHHCCCHHH		39.5924816145
532PhosphorylationQRDFVRLSQALQVRL
HHHHHHHHHHHHHHH		11.6622210691
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
200SPhosphorylationKinaseGSK3-ALPHAP49840
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RABE2_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 RABE2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRCC3_HUMANBRCC3physical
22863883
LARP7_HUMANLARP7physical
22863883
NOLC1_HUMANNOLC1physical
22863883
RPB2_HUMANPOLR2Bphysical
22863883
RPAB1_HUMANPOLR2Ephysical
22863883
WDHD1_HUMANWDHD1physical
22863883
EXOC1_HUMANEXOC1physical
27173435
EXOC4_HUMANEXOC4physical
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 RABE2_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, AND MASS SPECTROMETRY.

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