Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O75154 (RFIP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rab11 family-interacting protein 3

Short name=FIP3-Rab11
Short name=Rab11-FIP3
Alternative name(s):
Arfophilin-1
EF hands-containing Rab-interacting protein
Short name=Eferin
MU-MB-17.148
Gene names
Name:RAB11FIP3
Synonyms:ARFO1, KIAA0665
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.15 Ref.17

Subunit structure

Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and ARF6. Interacts with RAB11A; the interaction is direct. Interacts with RAB11B, RAB25 and RAB11FIP4. Interacts with ARF6; according to Ref.11, it specifically interacts with ARF6 but not ARF5. Interacts with ARF6; according to Ref.20 but not Ref.11. Interacts with RACGAP1/MgcRacGAP; interaction takes place during late stage of cytokinesis and is required for recruitment to the midbody. Interacts with ASAP1 and EXOC7. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.19 Ref.20

Subcellular location

Recycling endosome membrane; Peripheral membrane protein. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cleavage furrow. Midbody. Note: In early mitosis remains diffuse and distributed through the cell. The onset of anaphase sequesters these vesicles to the centrosomes at the opposite poles of the cell. During telophase these vesicles move from the centrosomes, to the furrow, and then to the midbody to aid in abscission. Interaction with Rab11 mediates localization to endosomes. Interaction with ARF6 mediates localization to the midbody. Ref.8 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.19

Domain

The RBD-FIP domain mediates the interaction with Rab11 (RAB11A or RAB11B). Ref.20

Post-translational modification

Phosphorylated at Ser-102 by CDK1 during metaphase, and dephosphorylated as cells enter telophase. Ref.18

Sequence similarities

Contains 2 EF-hand domains.

Contains 1 FIP-RBD domain.

Sequence caution

The sequence BAA31640.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAG57098.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAQ09358.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAQ09642.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAQ11003.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Transport
   Cellular componentCytoplasm
Cytoskeleton
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   LigandCalcium
Metal-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis

Inferred from mutant phenotype Ref.12Ref.11. Source: UniProtKB

endocytic recycling

Inferred from direct assay Ref.15. Source: UniProtKB

vesicle-mediated transport

Traceable author statement Ref.11. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay Ref.12. Source: UniProtKB

cleavage furrow

Inferred from direct assay Ref.12Ref.11Ref.16. Source: UniProtKB

endosome

Inferred from direct assay Ref.12Ref.11. Source: UniProtKB

intercellular bridge

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

microtubule organizing center

Inferred from direct assay. Source: HPA

midbody

Inferred from direct assay Ref.12Ref.11Ref.16. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

recycling endosome

Inferred from direct assay Ref.15. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionADP-ribosylation factor binding

Inferred from physical interaction Ref.11Ref.20Ref.16. Source: UniProtKB

Rab GTPase binding

Inferred from physical interaction Ref.12Ref.11Ref.20Ref.16. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

protein homodimerization activity

Inferred from direct assay Ref.20Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RACGAP1Q9H0H57EBI-7942186,EBI-717233

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75154-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75154-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-296: Missing.
     297-301: FVTYE → MPFLK
Note: No experimental confirmation available.
Isoform 3 (identifier: O75154-3)

The sequence of this isoform differs from the canonical sequence as follows:
     421-421: P → PSTDPLAAKLHSILTDEAFEFYCSQCHKQINRLEDLSARLSDLEMN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 756756Rab11 family-interacting protein 3
PRO_0000073879

Regions

Domain202 – 23736EF-hand 1
Domain234 – 26936EF-hand 2
Domain694 – 75663FIP-RBD
Calcium binding215 – 226121 Potential
Calcium binding247 – 258122 Potential
Region484 – 588105ARF-binding domain (ABD)
Coiled coil485 – 694210 Potential
Compositional bias5 – 197193Pro-rich
Compositional bias148 – 1514Poly-Ser
Compositional bias366 – 3694Poly-Leu

Amino acid modifications

Modified residue1021Phosphoserine; by CDK1 Ref.18
Modified residue2811Phosphoserine Ref.18
Modified residue3481Phosphoserine Ref.18
Modified residue4881Phosphoserine Ref.18
Modified residue5381Phosphoserine Ref.18
Modified residue6471Phosphoserine Ref.18
Modified residue6481Phosphoserine Ref.18

Natural variations

Alternative sequence1 – 296296Missing in isoform 2.
VSP_038664
Alternative sequence297 – 3015FVTYE → MPFLK in isoform 2.
VSP_038665
Alternative sequence4211P → PSTDPLAAKLHSILTDEAFE FYCSQCHKQINRLEDLSARL SDLEMN in isoform 3.
VSP_038666

Experimental info

Mutagenesis7371Y → S: Abolishes Rab11-binding. Ref.20
Mutagenesis7381I → E: Abolishes Rab11-binding. Ref.11 Ref.12
Mutagenesis7391D → A: Abolishes Rab11-binding. Ref.20
Mutagenesis7461M → S: Abolishes Rab11-binding. Ref.20
Mutagenesis7471E → A: Abolishes Rab11-binding. Ref.20

Secondary structure

....... 756
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 264CEC399F28AFB9

FASTA75682,440
        10         20         30         40         50         60 
MASAPPASPP GSEPPGPDPE PGGPDGPGAA QLAPGPAELR LGAPVGGPDP QSPGLDEPAP 

        70         80         90        100        110        120 
GAAADGGARW SAGPAPGLEG GPRDPGPSAP PPRSGPRGQL ASPDAPGPGP RSEAPLPELD 

       130        140        150        160        170        180 
PLFSWTEEPE ECGPASCPES APFRLQGSSS SHRARGEVDV FSPFPAPTAG ELALEQGPGS 

       190        200        210        220        230        240 
PPQPSDLSQT HPLPSEPVGS QEDGPRLRAV FDALDGDGDG FVRIEDFIQF ATVYGAEQVK 

       250        260        270        280        290        300 
DLTKYLDPSG LGVISFEDFY QGITAIRNGD PDGQCYGGVA SAQDEEPLAC PDEFDDFVTY 

       310        320        330        340        350        360 
EANEVTDSAY MGSESTYSEC ETFTDEDTST LVHPELQPEG DADSAGGSAV PSECLDAMEE 

       370        380        390        400        410        420 
PDHGALLLLP GRPHPHGQSV ITVIGGEEHF EDYGEGSEAE LSPETLCNGQ LGCSDPAFLT 

       430        440        450        460        470        480 
PSPTKRLSSK KVARYLHQSG ALTMEALEDP SPELMEGPEE DIADKVVFLE RRVLELEKDT 

       490        500        510        520        530        540 
AATGEQHSRL RQENLQLVHR ANALEEQLKE QELRACEMVL EETRRQKELL CKMEREKSIE 

       550        560        570        580        590        600 
IENLQTRLQQ LDEENSELRS CTPCLKANIE RLEEEKQKLL DEIESLTLRL SEEQENKRRM 

       610        620        630        640        650        660 
GDRLSHERHQ FQRDKEATQE LIEDLRKQLE HLQLLKLEAE QRRGRSSSMG LQEYHSRARE 

       670        680        690        700        710        720 
SELEQEVRRL KQDNRNLKEQ NEELNGQIIT LSIQGAKSLF STAFSESLAA EISSVSRDEL 

       730        740        750 
MEAIQKQEEI NFRLQDYIDR IIVAIMETNP SILEVK 

« Hide

Isoform 2 [UniParc].

Checksum: 574FC0A764FCA199
Show »

FASTA46052,451
Isoform 3 [UniParc].

Checksum: 4B4D2E7E868CF67B
Show »

FASTA80187,577

References

« Hide 'large scale' references
[1]"Identification of a novel Rab11/25 binding domain present in eferin and rip proteins."
Prekeris R., Davies J.M., Scheller R.H.
J. Biol. Chem. 276:38966-38970(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-756 (ISOFORM 3).
Tissue: Cerebellum and Testis.
[4]"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Ovary.
[7]"Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries."
Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A., Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S., Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F., Asmuss H.-P., Bise K., Mautner J.
Int. J. Cancer 106:244-251(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 532-756.
[8]"Identification and characterization of a family of Rab11-interacting proteins."
Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.
J. Biol. Chem. 276:39067-39075(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11A; RAB11B AND RAB25, SUBCELLULAR LOCATION.
[9]"Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells."
Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.
Biochem. Biophys. Res. Commun. 299:770-779(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP4.
[10]"Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis."
Horgan C.P., Walsh M., Zurawski T.H., McCaffrey M.W.
Biochem. Biophys. Res. Commun. 319:83-94(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane traffic in cytokinesis."
Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.
EMBO J. 24:3389-3399(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EXOC7; RAB11A AND ARF6, MUTAGENESIS OF ILE-738.
[12]"The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis."
Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.
Mol. Biol. Cell 16:849-860(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11A, MUTAGENESIS OF ILE-738.
[13]"Molecular characterization of Rab11-FIP3 binding to ARF GTPases."
Schonteich E., Pilli M., Simon G.C., Matern H.T., Junutula J.R., Sentz D., Holmes R.K., Prekeris R.
Eur. J. Cell Biol. 86:417-431(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11A AND ARF6.
[14]"Identification of Rab11 as a small GTPase binding protein for the Evi5 oncogene."
Westlake C.J., Junutula J.R., Simon G.C., Pilli M., Prekeris R., Scheller R.H., Jackson P.K., Eldridge A.G.
Proc. Natl. Acad. Sci. U.S.A. 104:1236-1241(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11A.
[15]"Rab11-FIP3 is critical for the structural integrity of the endosomal recycling compartment."
Horgan C.P., Oleksy A., Zhdanov A.V., Lall P.Y., White I.J., Khan A.R., Futter C.E., McCaffrey J.G., McCaffrey M.W.
Traffic 8:414-430(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]"Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis."
Simon G.C., Schonteich E., Wu C.C., Piekny A., Ekiert D., Yu X., Gould G.W., Glotzer M., Prekeris R.
EMBO J. 27:1791-1803(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RACGAP1.
[17]"Rab11-FIP3 is a Rab11-binding protein that regulates breast cancer cell motility by modulating the actin cytoskeleton."
Jing J., Tarbutton E., Wilson G., Prekeris R.
Eur. J. Cell Biol. 88:325-341(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-102; SER-281; SER-348; SER-488; SER-538; SER-647 AND SER-648.
[19]"Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes."
Eathiraj S., Mishra A., Prekeris R., Lambright D.G.
J. Mol. Biol. 364:121-135(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 695-756 IN COMPLEX WITH RAB11A, SUBCELLULAR LOCATION, HOMODIMERIZATION.
[20]"Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1."
Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S.
Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 715-756 IN COMPLEX WITH RAB11A, DOMAIN RBD-FIP, HOMODIMERIZATION, INTERACTION WITH RAB11A; ARF5 AND ARF6, MUTAGENESIS OF TYR-737; ASP-739; MET-746 AND GLU-747.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF395731 mRNA. Translation: AAL12940.1.
AB014565 mRNA. Translation: BAA31640.2. Different initiation.
AK293644 mRNA. Translation: BAG57098.1. Different initiation.
AK303061 mRNA. Translation: BAG64178.1.
AE006463 Genomic DNA. Translation: AAK61232.1.
AL023881, AL049542, Z98882 Genomic DNA. Translation: CAI95593.1.
AL049542, AL023881, Z98882 Genomic DNA. Translation: CAI95788.1.
AL023881, AL049542, Z98882 Genomic DNA. Translation: CAQ11003.1. Sequence problems.
AL049542, AL023881, Z98882 Genomic DNA. Translation: CAQ09358.1. Sequence problems.
Z98882, AL023881, AL049542 Genomic DNA. Translation: CAQ09642.1. Sequence problems.
Z98882, AL023881, AL049542 Genomic DNA. Translation: CAI95591.1.
BC051360 mRNA. Translation: AAH51360.1.
AY130007 mRNA. Translation: AAN05091.1.
PIRT00367.
RefSeqNP_001135744.1. NM_001142272.1.
NP_055515.1. NM_014700.3.
XP_005255770.1. XM_005255713.1.
XP_005255772.1. XM_005255715.2.
UniGeneHs.531642.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D7CX-ray1.75C/D715-756[»]
2HV8X-ray1.86D/E/F695-756[»]
ProteinModelPortalO75154.
SMRO75154. Positions 199-265, 466-509, 702-756.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115076. 10 interactions.
IntActO75154. 4 interactions.
MINTMINT-6799564.
STRING9606.ENSP00000262305.

PTM databases

PhosphoSiteO75154.

Proteomic databases

PaxDbO75154.
PRIDEO75154.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262305; ENSP00000262305; ENSG00000090565. [O75154-1]
ENST00000450428; ENSP00000415919; ENSG00000090565. [O75154-2]
ENST00000457159; ENSP00000398730; ENSG00000090565. [O75154-3]
GeneID9727.
KEGGhsa:9727.
UCSCuc002chf.3. human. [O75154-1]
uc010uuf.2. human. [O75154-2]
uc010uug.2. human. [O75154-3]

Organism-specific databases

CTD9727.
GeneCardsGC16P000475.
HGNCHGNC:17224. RAB11FIP3.
HPAHPA028088.
HPA028631.
HPA030086.
MIM608738. gene.
neXtProtNX_O75154.
PharmGKBPA134950896.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259959.
HOVERGENHBG054059.
InParanoidO75154.
KOK12485.
OMADFGESNT.
OrthoDBEOG793B75.
PhylomeDBO75154.
TreeFamTF327221.

Gene expression databases

ArrayExpressO75154.
BgeeO75154.
CleanExHS_RAB11FIP3.
GenevestigatorO75154.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 2 hits.
PS51511. FIP_RBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB11FIP3. human.
EvolutionaryTraceO75154.
GeneWikiRAB11FIP3.
GenomeRNAi9727.
NextBio36593.
PROO75154.
SOURCESearch...

Entry information

Entry nameRFIP3_HUMAN
AccessionPrimary (citable) accession number: O75154
Secondary accession number(s): B0QYI8 expand/collapse secondary AC list , B0QYT8, B1AHQ0, B4DEI7, B4DZR6, Q4VXV7, Q7Z5E9, Q9H155, Q9H1G0, Q9NUI0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM