RFIP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RFIP2_MOUSE
• UniProt AC: G3XA57
• Protein Name: Rab11 family-interacting protein 2
• Gene Name: Rab11fip2
• Organism: Mus musculus (Mouse).
• 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: MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSRQIDSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHSFGRQSDPFTNVTASLPQKFATLPRKKNPFEESSEPWDSSMNLFSKPIEVRKESKREKREKVSLFERVTGKRDSRRPDKLNNGGSDSPCDLKSPSAFSENRQDYFEYESTNPFTAKFRASTIMPSSSFHVNPTSSEDLRKIPDNNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFTNS

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
148	Phosphorylation	QFMRNNMTASMFDLS EEHHCCCCHHHHCCC		25521595
150	Phosphorylation	MRNNMTASMFDLSMK HHCCCCHHHHCCCCC		25521595
155	Phosphorylation	TASMFDLSMKDKTRS CHHHHCCCCCCCCCC		26745281
162	Phosphorylation	SMKDKTRSPFAKLKD CCCCCCCCCCHHHHH		-
176	Phosphorylation	DKMKGRKSDGVFSDT HHHCCCCCCCCCCCC		29899451
184	Phosphorylation	DGVFSDTSSAIVPST CCCCCCCCCCCCCCC		25338131
185	Phosphorylation	GVFSDTSSAIVPSTH CCCCCCCCCCCCCCC		25338131
223	Phosphorylation	LLGPQRLSSAHSMSD CCCHHHCCCCCCHHH		26160508
224	Phosphorylation	LGPQRLSSAHSMSDL CCHHHCCCCCCHHHC		26239621
227	Phosphorylation	QRLSSAHSMSDLTGS HHCCCCCCHHHCCCC		26824392
229	Phosphorylation	LSSAHSMSDLTGSHL CCCCCCHHHCCCCCC		26239621
232	Phosphorylation	AHSMSDLTGSHLSSE CCCHHHCCCCCCCCH		25777480
234	Phosphorylation	SMSDLTGSHLSSEKL CHHHCCCCCCCCHHH		25777480
237	Phosphorylation	DLTGSHLSSEKLKSS HCCCCCCCCHHHHCC		25777480
238	Phosphorylation	LTGSHLSSEKLKSST CCCCCCCCHHHHCCC		25777480
244	O-linked_Glycosylation	SSEKLKSSTVGPTHL CCHHHHCCCCCHHHH		55413499
258	Phosphorylation	LLSRQIDSFGVVPES HHHHHHCCCCCCCCC		29899451
265	Phosphorylation	SFGVVPESGSLKSPH CCCCCCCCCCCCCCC		29899451
267	Phosphorylation	GVVPESGSLKSPHRR CCCCCCCCCCCCCCC		29899451
270	Phosphorylation	PESGSLKSPHRRTLS CCCCCCCCCCCCEEC		29899451
275	Phosphorylation	LKSPHRRTLSFDTSK CCCCCCCEECCCHHH		28833060
277	Phosphorylation	SPHRRTLSFDTSKLN CCCCCEECCCHHHCC		25521595
280	Phosphorylation	RRTLSFDTSKLNQPG CCEECCCHHHCCCCC		28833060
281	Phosphorylation	RTLSFDTSKLNQPGS CEECCCHHHCCCCCC		28833060
288	Phosphorylation	SKLNQPGSIVDEGEH HHCCCCCCCCCCCCC		29899451
310	Phosphorylation	PFTNVTASLPQKFAT CCCCCCCCCCHHHCC		24719451
317	Phosphorylation	SLPQKFATLPRKKNP CCCHHHCCCCCCCCC		21454597
334	Phosphorylation	ESSEPWDSSMNLFSK CCCCCCCCCCCCCCC		29899451
380	Phosphorylation	DKLNNGGSDSPCDLK CCCCCCCCCCCCCCC		22324799
382	Phosphorylation	LNNGGSDSPCDLKSP CCCCCCCCCCCCCCC		29899451
388	Phosphorylation	DSPCDLKSPSAFSEN CCCCCCCCCCCCCCC		28973931
399	Phosphorylation	FSENRQDYFEYESTN CCCCCCCCCEECCCC		29899451
402	Phosphorylation	NRQDYFEYESTNPFT CCCCCCEECCCCCCC		29899451
420	Phosphorylation	RASTIMPSSSFHVNP ECCEECCCCCEECCC		25293948
421	Phosphorylation	ASTIMPSSSFHVNPT CCEECCCCCEECCCC		25293948
422	Phosphorylation	STIMPSSSFHVNPTS CEECCCCCEECCCCC		25293948
428	Phosphorylation	SSFHVNPTSSEDLRK CCEECCCCCHHHHHC		26643407
429	Phosphorylation	SFHVNPTSSEDLRKI CEECCCCCHHHHHCC		26643407
430	Phosphorylation	FHVNPTSSEDLRKIP EECCCCCHHHHHCCC		26824392
462	Ubiquitination	EVLQELVKHKELLRR HHHHHHHHCHHHHHC		22790023
462	Ubiquitination	EVLQELVKHKELLRR HHHHHHHHCHHHHHC		-

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
227	S	Phosphorylation	Kinase	MARK2	Q05512	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
227	S	Phosphorylation	Phosphorylation at Ser-227 by MARK2 regulates epithelial cell polarity.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RFIP2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.