dbPTM

RFIP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RFIP3_HUMAN
UniProt AC	O75154
Protein Name	Rab11 family-interacting protein 3
Gene Name	RAB11FIP3
Organism	Homo sapiens (Human).
Sequence Length	756
Subcellular Localization	Recycling endosome membrane Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cleavage furrow . Midbody . In early mitosis remains diffuse and distributed through the cell. The onset of anaphase seque
Protein Description	Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis. Also required for the structural integrity of the endosomal recycling compartment during interphase. May play a role in breast cancer cell motility by regulating actin cytoskeleton. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). [PubMed: 25035494]
Protein Sequence	MASAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPESAPFRLQGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAVFDALDGDGDGFVRIEDFIQFATVYGAEQVKDLTKYLDPSGLGVISFEDFYQGITAIRNGDPDGQCYGGVASAQDEEPLACPDEFDDFVTYEANEVTDSAYMGSESTYSECETFTDEDTSTLVHPELQPEGDADSAGGSAVPSECLDAMEEPDHGALLLLPGRPHPHGQSVITVIGGEEHFEDYGEGSEAELSPETLCNGQLGCSDPAFLTPSPTKRLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MASAPPASPPGSEPP CCCCCCCCCCCCCCC	37.08	28348404
12	Phosphorylation	PPASPPGSEPPGPDP CCCCCCCCCCCCCCC	53.34	28348404
52	Phosphorylation	VGGPDPQSPGLDEPA CCCCCCCCCCCCCCC	26.73	21815630
102	Phosphorylation	GPRGQLASPDAPGPG CCCCCCCCCCCCCCC	31.72	24670416
185	Phosphorylation	PGSPPQPSDLSQTHP CCCCCCCCCCCCCCC	46.03	22468782
188	Phosphorylation	PPQPSDLSQTHPLPS CCCCCCCCCCCCCCC	37.71	22468782
281	Phosphorylation	QCYGGVASAQDEEPL CCCCCCCCCCCCCCC	24.85	22401586
348	Phosphorylation	DADSAGGSAVPSECL CCCCCCCCCCCHHHH	25.77	22401586
451	Phosphorylation	MEALEDPSPELMEGP HHHHCCCCHHHHCCC	43.24	22401586
467 (in isoform 3)	Phosphorylation	-	5.81	25627689
469 (in isoform 3)	Phosphorylation	-	3.19	25850435
480	Phosphorylation	VLELEKDTAATGEQH HHHHHHHHHCCCHHH	29.29	-
488	Phosphorylation	AATGEQHSRLRQENL HCCCHHHHHHHHHHH	32.48	22401586
538	Phosphorylation	CKMEREKSIEIENLQ HHHHHHHHHHHHHHH	22.24	28450419
560	Phosphorylation	EENSELRSCTPCLKA HHCHHHHHCHHHHHH	34.66	26699800
562	Phosphorylation	NSELRSCTPCLKANI CHHHHHCHHHHHHHH	20.48	26699800
585	Phosphorylation	KLLDEIESLTLRLSE HHHHHHHHHHHHCCH	32.11	-
646	Phosphorylation	AEQRRGRSSSMGLQE HHHHHCCCCHHHHHH	29.59	28450419
647	Phosphorylation	EQRRGRSSSMGLQEY HHHHCCCCHHHHHHH	24.00	28450419
648	Phosphorylation	QRRGRSSSMGLQEYH HHHCCCCHHHHHHHH	20.37	28450419
656	Phosphorylation	MGLQEYHSRARESEL HHHHHHHHHHHHHHH	27.08	-

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
102	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
102	S	Phosphorylation		22401586
Phosphorylated at Ser-102 by CDK1 during metaphase, and dephosphorylated as cells enter telophase.

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 RFIP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB11A_HUMAN	RAB11A	physical	11495908
TS101_HUMAN	TSG101	physical	22348143
TRPV1_MOUSE	Trpv1	physical	15883036
ASAP1_HUMAN	ASAP1	physical	18685082
ARF5_HUMAN	ARF5	physical	18685082
ARF6_HUMAN	ARF6	physical	18685082
RB11A_HUMAN	RAB11A	physical	18685082

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 RFIP3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Rab11-FIP3 is a cell cycle-regulated phosphoprotein."; Collins L.L., Simon G., Matheson J., Wu C., Miller M.C., Otani T.,Yu X., Hayashi S., Prekeris R., Gould G.W.; BMC Cell Biol. 13:4-4(2012). Cited for: PHOSPHORYLATION AT SER-102; SER-281; SER-348; SER-488; SER-538;SER-647 AND SER-648.	22401586 [Abstract]

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