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Q9BXF6 (RFIP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rab11 family-interacting protein 5

Short name=Rab11-FIP5
Alternative name(s):
Gamma-SNAP-associated factor 1
Short name=Gaf-1
Phosphoprotein pp75
Rab11-interacting protein Rip11
Gene names
Name:RAB11FIP5
Synonyms:GAF1, KIAA0857, RIP11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. Ref.1 Ref.12

Subunit structure

Forms a heterooligomeric complex with RAB11FIP4. Binds NAPG and TROVE2. Binds RAB11A that has been activated by GTP binding. Ref.6

Subcellular location

Cytoplasm. Recycling endosome membrane; Peripheral membrane protein. Early endosome membrane; Peripheral membrane protein By similarity. Golgi apparatus membrane; Peripheral membrane protein By similarity. Cytoplasmic vesiclesecretory vesicle membrane; Peripheral membrane protein By similarity. Mitochondrion membrane; Peripheral membrane protein Ref.1 Ref.5.

Tissue specificity

Detected at low levels in heart, brain, placenta, lung, liver, adipocytes, kidney, spleen, skeletal muscle and pancreas. Ref.4 Ref.5

Domain

Binds to vesicles enriched in neutral phospholipids via its C2 domain. The interaction is favored by Mg2+ rather than Ca2+.

Post-translational modification

Phosphorylated on serine and threonine residues. Phosphorylation at Ser-357 is PKA-dependent. Ref.4

Miscellaneous

Antibodies against RIP11 are found in sera from patients with autoimmune diseases such as systemic lupus erythematosus (SLE) or Sjoegren syndrome (SS). It is also found in the sera from mothers of children with neonatal lupus erythematosus (NLE).

Sequence similarities

Contains 1 C2 domain.

Contains 1 FIP-RBD domain.

Sequence caution

The sequence BAA74880.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Cytoplasmic vesicle
Endosome
Golgi apparatus
Membrane
Mitochondrion
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to acidity

Inferred from direct assay Ref.12. Source: UniProtKB

insulin secretion involved in cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulated secretory pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein localization to cell surface

Inferred from mutant phenotype Ref.12. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

microtubule organizing center

Inferred from direct assay. Source: HPA

mitochondrial outer membrane

Inferred from direct assay Ref.5. Source: UniProtKB

recycling endosome

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiongamma-tubulin binding

Inferred from direct assay Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 653653Rab11 family-interacting protein 5
PRO_0000097307

Regions

Domain6 – 128123C2
Domain586 – 64863FIP-RBD

Amino acid modifications

Modified residue1761Phosphoserine Ref.11
Modified residue3071Phosphoserine Ref.8 Ref.11
Modified residue3571Phosphoserine By similarity
Modified residue4941Phosphoserine Ref.11
Modified residue5381Phosphoserine Ref.8 Ref.11
Modified residue5471Phosphoserine By similarity
Modified residue5531Phosphoserine By similarity

Experimental info

Sequence conflict1761Missing in AAH35013. Ref.3
Sequence conflict5031E → G in AAH35013. Ref.3
Sequence conflict5991H → N in AAH35013. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9BXF6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 716725537AA9D86E

FASTA65370,415
        10         20         30         40         50         60 
MALVRGAEPA AGPSRWLPTH VQVTVLRARG LRGKSSGAGS TSDAYTVIQV GREKYSTSVV 

        70         80         90        100        110        120 
EKTHGCPEWR EECSFELPPG ALDGLLRAQE ADAGPAPWAA SSAAACELVL TTMHRSLIGV 

       130        140        150        160        170        180 
DKFLGQATVA LDEVFGAGRA QHTQWYKLHS KPGKKEKERG EIEVTIQFTR NNLSASMFDL 

       190        200        210        220        230        240 
SMKDKPRSPF SKIRDKMKGK KKYDLESASA ILPSSAIEDP DLGSLGKMGK AKGFFLRNKL 

       250        260        270        280        290        300 
RKSSLTQSNT SLGSDSTLSS ASGSLAYQGP GAELLTRSPS RSSWLSTEGG RDSAQSPKLF 

       310        320        330        340        350        360 
THKRTYSDEA NQMRVAPPRA LLDLQGHLDA ASRSSLCVNG SHIYNEEPQG PVRHRSSISG 

       370        380        390        400        410        420 
SLPSSGSLQA VSSRFSEEGP RSTDDTWPRG SRSNSSSEAV LGQEELSAQA KVLAPGASHP 

       430        440        450        460        470        480 
GEEEGARLPE GKPVQVATPI VASSEAVAEK EGARKEERKP RMGLFHHHHQ GLSRSELGRR 

       490        500        510        520        530        540 
SSLGEKGGPI LGASPHHSSS GEEKAKSSWF GLREAKDPTQ KPSPHPVKPL SAAPVEGSPD 

       550        560        570        580        590        600 
RKQSRSSLSI ALSSGLEKLK TVTSGSIQPV TQAPQAGQMV DTKRLKDSAV LDQSAKYYHL 

       610        620        630        640        650 
THDELISLLL QRERELSQRD EHVQELESYI DRLLVRIMET SPTLLQIPPG PPK 

« Hide

References

« Hide 'large scale' references
[1]"A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes."
Prekeris R., Klumperman J., Scheller R.H.
Mol. Cell 6:1437-1448(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAB11A, SUBCELLULAR LOCATION.
[2]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"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].
Tissue: Testis.
[4]"Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and identification of distinct human autoantibodies."
Wang D., Buyon J.P., Zhu W., Chan E.K.L.
J. Clin. Invest. 104:1265-1275(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-653, INTERACTION WITH TROVE2, IDENTIFICATION AS ANTIGEN IN AUTOIMMUNE DISEASES, TISSUE SPECIFICITY, PHOSPHORYLATION.
Tissue: Keratinocyte.
[5]"Gaf-1, a gamma-SNAP-binding protein associated with the mitochondria."
Chen D., Xu W., He P., Medrano E.E., Whiteheart S.W.
J. Biol. Chem. 276:13127-13135(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAPG, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[6]"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: SUBUNIT.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-307; SER-494 AND SER-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts."
Oehlke O., Martin H.W., Osterberg N., Roussa E.
J. Cell. Physiol. 226:638-651(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF334812 mRNA. Translation: AAK20892.1.
AB020664 mRNA. Translation: BAA74880.1. Different initiation.
BC035013 mRNA. Translation: AAH35013.1.
AF153085 mRNA. Translation: AAF34356.1.
CCDSCCDS1923.1.
PIRT17312.
RefSeqNP_056285.1. NM_015470.2.
UniGeneHs.24557.

3D structure databases

ProteinModelPortalQ9BXF6.
SMRQ9BXF6. Positions 21-169, 600-651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117518. 15 interactions.
IntActQ9BXF6. 7 interactions.
STRING9606.ENSP00000258098.

PTM databases

PhosphoSiteQ9BXF6.

Polymorphism databases

DMDM34223002.

Proteomic databases

MaxQBQ9BXF6.
PaxDbQ9BXF6.
PRIDEQ9BXF6.

Protocols and materials databases

DNASU26056.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258098; ENSP00000258098; ENSG00000135631.
GeneID26056.
KEGGhsa:26056.
UCSCuc002sit.4. human.

Organism-specific databases

CTD26056.
GeneCardsGC02M073212.
HGNCHGNC:24845. RAB11FIP5.
HPAHPA036406.
HPA036407.
MIM605536. gene.
neXtProtNX_Q9BXF6.
PharmGKBPA134971129.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG84049.
HOGENOMHOG000234700.
HOVERGENHBG079127.
KOK12484.
OMAVEKTHGC.
OrthoDBEOG7WQ7SB.
PhylomeDBQ9BXF6.
TreeFamTF326172.

Gene expression databases

ArrayExpressQ9BXF6.
BgeeQ9BXF6.
CleanExHS_RAB11FIP5.
GenevestigatorQ9BXF6.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAB11FIP5.
GenomeRNAi26056.
NextBio47930.
PROQ9BXF6.
SOURCESearch...

Entry information

Entry nameRFIP5_HUMAN
AccessionPrimary (citable) accession number: Q9BXF6
Secondary accession number(s): O94939, Q9P0M1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 114 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

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM