RFIP2_HUMAN - dbPTM
RFIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFIP2_HUMAN
UniProt AC Q7L804
Protein Name Rab11 family-interacting protein 2
Gene Name RAB11FIP2
Organism Homo sapiens (Human).
Sequence Length 512
Subcellular Localization Cell membrane
Peripheral membrane protein. Recycling endosome membrane
Peripheral membrane protein. Translocates with RAB11A from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane.
Protein Description A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity..
Protein Sequence MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLIQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKNDGTFSDTSSAIIPSTHMPDANSEFSSGEIQMKSKPKKPFLLGPQRLSSAHSMSDLSGSHMSSEKLKAGTIGQTHLLGHQLDSFGTVPESGSLKSPHRRTLSFDTSKMNQPDSIVDEGELCFGRQNDPFTNVTASLPQKFATLPRKKNPFEESSETWDSSMNLFSKPIEIRKENKREKREKVSLFERVTGKKDSRRSDKLNNGGSDSPCDLKSPNAFSENRQDYFDYESTNPFTAKFRASNIMPSSSFHMSPTSNEDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFSNS
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
4Phosphorylation----MMLSEQAQKWF
----CCCHHHHHHHC		15.1230576142
13PhosphorylationQAQKWFPTHVQVTVL
HHHHHCCCCEEEEEE		25.7924670416
46UbiquitinationIIQLGKEKYSTSVAE
EEECCCCCCCCCCCH		48.24-
65PhosphorylationPVWKEEASFELPGLL
CHHCCCCCCCCCCEE		23.6430619164
148PhosphorylationQFMRNNMTASMFDLS
EEHHCCCCHHHHCCC		20.0830266825
150PhosphorylationMRNNMTASMFDLSMK
HHCCCCHHHHCCCCC		15.7129255136
155PhosphorylationTASMFDLSMKDKTRS
CHHHHCCCCCCCCCC		26.1530266825
160PhosphorylationDLSMKDKTRSPFAKL
CCCCCCCCCCCCHHH		46.6524719451
162PhosphorylationSMKDKTRSPFAKLKD
CCCCCCCCCCHHHHH		29.6028674419
179PhosphorylationKGRKNDGTFSDTSSA
CCCCCCCCCCCCCCC		23.8828857561
181PhosphorylationRKNDGTFSDTSSAII
CCCCCCCCCCCCCEE		39.5628857561
184PhosphorylationDGTFSDTSSAIIPST
CCCCCCCCCCEECCC		23.8228348404
185PhosphorylationGTFSDTSSAIIPSTH
CCCCCCCCCEECCCC		26.1128348404
223PhosphorylationLLGPQRLSSAHSMSD
CCCCCCCCCCCCHHH		27.8923927012
224PhosphorylationLGPQRLSSAHSMSDL
CCCCCCCCCCCHHHC		34.2923927012
227PhosphorylationQRLSSAHSMSDLSGS
CCCCCCCCHHHCCCC		21.5023927012
229PhosphorylationLSSAHSMSDLSGSHM
CCCCCCHHHCCCCCC		38.1123927012
232PhosphorylationAHSMSDLSGSHMSSE
CCCHHHCCCCCCCCC		43.1523403867
234PhosphorylationSMSDLSGSHMSSEKL
CHHHCCCCCCCCCHH		16.7923403867
237PhosphorylationDLSGSHMSSEKLKAG
HCCCCCCCCCHHCCC		29.8923403867
238PhosphorylationLSGSHMSSEKLKAGT
CCCCCCCCCHHCCCC		31.0423403867
245PhosphorylationSEKLKAGTIGQTHLL
CCHHCCCCCCHHHHH		27.1323312004
249PhosphorylationKAGTIGQTHLLGHQL
CCCCCCHHHHHCCCC		14.8523312004
258PhosphorylationLLGHQLDSFGTVPES
HHCCCCCCCCCCCCC		33.8823312004
261PhosphorylationHQLDSFGTVPESGSL
CCCCCCCCCCCCCCC		30.7729255136
265PhosphorylationSFGTVPESGSLKSPH
CCCCCCCCCCCCCCC		27.8429255136
267PhosphorylationGTVPESGSLKSPHRR
CCCCCCCCCCCCCCC		41.7329255136
270PhosphorylationPESGSLKSPHRRTLS
CCCCCCCCCCCCEEC		31.0929255136
275PhosphorylationLKSPHRRTLSFDTSK
CCCCCCCEECCCHHH		27.0630266825
277PhosphorylationSPHRRTLSFDTSKMN
CCCCCEECCCHHHCC		22.0623401153
280PhosphorylationRRTLSFDTSKMNQPD
CCEECCCHHHCCCCC		28.3930266825
281PhosphorylationRTLSFDTSKMNQPDS
CEECCCHHHCCCCCC		31.5830266825
288PhosphorylationSKMNQPDSIVDEGEL
HHCCCCCCCCCCCCC		31.06-
310PhosphorylationPFTNVTASLPQKFAT
CCCCCEECCCHHHCC		31.0828555341
317PhosphorylationSLPQKFATLPRKKNP
CCCHHHCCCCCCCCC		40.1922617229
322UbiquitinationFATLPRKKNPFEESS
HCCCCCCCCCCCCCC		71.74-
340PhosphorylationDSSMNLFSKPIEIRK
HHHHHHHCCCEEHHH		40.4624719451
341UbiquitinationSSMNLFSKPIEIRKE
HHHHHHCCCEEHHHH		42.55-
350AcetylationIEIRKENKREKREKV
EEHHHHCHHHHHHHH		64.1318586721
380PhosphorylationDKLNNGGSDSPCDLK
CCCCCCCCCCCCCCC		35.9929978859
382PhosphorylationLNNGGSDSPCDLKSP
CCCCCCCCCCCCCCC		29.1721815630
387MethylationSDSPCDLKSPNAFSE
CCCCCCCCCCCCCCC		51.09115976021
388PhosphorylationDSPCDLKSPNAFSEN
CCCCCCCCCCCCCCC		30.5929255136
393PhosphorylationLKSPNAFSENRQDYF
CCCCCCCCCCCCCCC		31.3922199227
399PhosphorylationFSENRQDYFDYESTN
CCCCCCCCCCCCCCC		7.0422199227
415PhosphorylationFTAKFRASNIMPSSS
CCCEEEHHHCCCCCC		23.7223186163
420PhosphorylationRASNIMPSSSFHMSP
EHHHCCCCCCEECCC		22.6428857561
421PhosphorylationASNIMPSSSFHMSPT
HHHCCCCCCEECCCC		31.0225850435
422PhosphorylationSNIMPSSSFHMSPTS
HHCCCCCCEECCCCC		24.4125850435
426PhosphorylationPSSSFHMSPTSNEDL
CCCCEECCCCCHHHH		19.2225850435
428PhosphorylationSSFHMSPTSNEDLRK
CCEECCCCCHHHHHC		36.5625850435
429PhosphorylationSFHMSPTSNEDLRKI
CEECCCCCHHHHHCC		41.4229507054
448PhosphorylationPFDATAGYRSLTYEE
CCCCCCCCCCCCHHH		8.4528674419
480PhosphorylationHIRELEDYIDNLLVR
CHHHHHHHHHHHHHH		10.7829978859
494PhosphorylationRVMEETPSILRVPYE
HHHHHCCCCEECCCC		41.4918452278
500PhosphorylationPSILRVPYEPSRKAG
CCCEECCCCCCCCCC		37.3018452278
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
227SPhosphorylationKinaseMARK2Q7KZI7
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
227SPhosphorylation

16775013
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 RFIP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO5B_HUMANMYO5Bphysical
12393859
RFIP2_HUMANRAB11FIP2physical
12364336
RFIP5_HUMANRAB11FIP5physical
12364336
RB11A_HUMANRAB11Aphysical
11994279
RFIP2_HUMANRAB11FIP2physical
11994279
RB11A_HUMANRAB11Aphysical
11495908
RAB25_HUMANRAB25physical
11481332
RB11A_HUMANRAB11Aphysical
11481332
RFIP2_HUMANRAB11FIP2physical
16734419
RFIP2_HUMANRAB11FIP2physical
16473632
RB11A_HUMANRAB11Aphysical
17156409
ASAP1_HUMANASAP1physical
18685082
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
CING_HUMANCGNphysical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
RTKN_HUMANRTKNphysical
27173435
MAST3_HUMANMAST3physical
27173435
DEN1A_HUMANDENND1Aphysical
27173435
SPD2A_HUMANSH3PXD2Aphysical
27173435
SRGP2_HUMANSRGAP2physical
27173435
PPM1H_HUMANPPM1Hphysical
27173435
CBY1_HUMANCBY1physical
27173435
INP5E_HUMANINPP5Ephysical
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 RFIP2_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 SER-382, 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-150, AND MASSSPECTROMETRY.
"MARK2/EMK1/Par-1Balpha phosphorylation of Rab11-family interactingprotein 2 is necessary for the timely establishment of polarity inMadin-Darby canine kidney cells.";
Ducharme N.A., Hales C.M., Lapierre L.A., Ham A.J., Oztan A.,Apodaca G., Goldenring J.R.;
Mol. Biol. Cell 17:3625-3637(2006).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-227, AND MUTAGENESIS OF SER-223;SER-224; SER-227 AND SER-229.

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