Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9BXF6

- RFIP5_HUMAN

UniProt

Q9BXF6 - RFIP5_HUMAN

Protein

Rab11 family-interacting protein 5

Gene

RAB11FIP5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.2 Publications

    GO - Molecular functioni

    1. gamma-tubulin binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to acidic pH Source: UniProtKB
    2. insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    3. protein transport Source: UniProtKB-KW
    4. regulated secretory pathway Source: UniProtKB
    5. regulation of protein localization to cell surface Source: UniProtKB

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:RAB11FIP5
    Synonyms:GAF1, KIAA0857, RIP11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:24845. RAB11FIP5.

    Subcellular locationi

    GO - Cellular componenti

    1. early endosome Source: UniProtKB
    2. early endosome membrane Source: UniProtKB-SubCell
    3. Golgi apparatus Source: UniProtKB
    4. Golgi membrane Source: UniProtKB-SubCell
    5. intracellular membrane-bounded organelle Source: HPA
    6. microtubule organizing center Source: HPA
    7. mitochondrial outer membrane Source: UniProtKB
    8. recycling endosome Source: UniProtKB
    9. recycling endosome membrane Source: UniProtKB-SubCell
    10. secretory granule Source: UniProtKB
    11. transport vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134971129.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 653653Rab11 family-interacting protein 5PRO_0000097307Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei176 – 1761Phosphoserine2 Publications
    Modified residuei307 – 3071Phosphoserine3 Publications
    Modified residuei357 – 3571PhosphoserineBy similarity
    Modified residuei494 – 4941Phosphoserine2 Publications
    Modified residuei538 – 5381Phosphoserine3 Publications
    Modified residuei547 – 5471PhosphoserineBy similarity
    Modified residuei553 – 5531PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on serine and threonine residues. Phosphorylation at Ser-357 is PKA-dependent.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BXF6.
    PaxDbiQ9BXF6.
    PRIDEiQ9BXF6.

    PTM databases

    PhosphoSiteiQ9BXF6.

    Expressioni

    Tissue specificityi

    Detected at low levels in heart, brain, placenta, lung, liver, adipocytes, kidney, spleen, skeletal muscle and pancreas.2 Publications

    Gene expression databases

    ArrayExpressiQ9BXF6.
    BgeeiQ9BXF6.
    CleanExiHS_RAB11FIP5.
    GenevestigatoriQ9BXF6.

    Organism-specific databases

    HPAiHPA036406.
    HPA036407.

    Interactioni

    Subunit structurei

    Forms a heterooligomeric complex with RAB11FIP4. Binds NAPG and TROVE2. Binds RAB11A that has been activated by GTP binding.1 Publication

    Protein-protein interaction databases

    BioGridi117518. 15 interactions.
    IntActiQ9BXF6. 7 interactions.
    STRINGi9606.ENSP00000258098.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BXF6.
    SMRiQ9BXF6. Positions 21-169, 600-651.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 128123C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini586 – 64863FIP-RBDPROSITE-ProRule annotationAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 FIP-RBD domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG84049.
    HOGENOMiHOG000234700.
    HOVERGENiHBG079127.
    KOiK12484.
    OMAiVEKTHGC.
    OrthoDBiEOG7WQ7SB.
    PhylomeDBiQ9BXF6.
    TreeFamiTF326172.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR019018. Rab-bd_FIP-RBD.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF09457. RBD-FIP. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS51511. FIP_RBD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BXF6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALVRGAEPA AGPSRWLPTH VQVTVLRARG LRGKSSGAGS TSDAYTVIQV    50
    GREKYSTSVV EKTHGCPEWR EECSFELPPG ALDGLLRAQE ADAGPAPWAA 100
    SSAAACELVL TTMHRSLIGV DKFLGQATVA LDEVFGAGRA QHTQWYKLHS 150
    KPGKKEKERG EIEVTIQFTR NNLSASMFDL SMKDKPRSPF SKIRDKMKGK 200
    KKYDLESASA ILPSSAIEDP DLGSLGKMGK AKGFFLRNKL RKSSLTQSNT 250
    SLGSDSTLSS ASGSLAYQGP GAELLTRSPS RSSWLSTEGG RDSAQSPKLF 300
    THKRTYSDEA NQMRVAPPRA LLDLQGHLDA ASRSSLCVNG SHIYNEEPQG 350
    PVRHRSSISG SLPSSGSLQA VSSRFSEEGP RSTDDTWPRG SRSNSSSEAV 400
    LGQEELSAQA KVLAPGASHP GEEEGARLPE GKPVQVATPI VASSEAVAEK 450
    EGARKEERKP RMGLFHHHHQ GLSRSELGRR SSLGEKGGPI LGASPHHSSS 500
    GEEKAKSSWF GLREAKDPTQ KPSPHPVKPL SAAPVEGSPD RKQSRSSLSI 550
    ALSSGLEKLK TVTSGSIQPV TQAPQAGQMV DTKRLKDSAV LDQSAKYYHL 600
    THDELISLLL QRERELSQRD EHVQELESYI DRLLVRIMET SPTLLQIPPG 650
    PPK 653
    Length:653
    Mass (Da):70,415
    Last modified:June 1, 2001 - v1
    Checksum:i716725537AA9D86E
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761Missing in AAH35013. (PubMed:15489334)Curated
    Sequence conflicti503 – 5031E → G in AAH35013. (PubMed:15489334)Curated
    Sequence conflicti599 – 5991H → N in AAH35013. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF334812 mRNA. Translation: AAK20892.1.
    AB020664 mRNA. Translation: BAA74880.1. Different initiation.
    BC035013 mRNA. Translation: AAH35013.1.
    AF153085 mRNA. Translation: AAF34356.1.
    CCDSiCCDS1923.1.
    PIRiT17312.
    RefSeqiNP_056285.1. NM_015470.2.
    UniGeneiHs.24557.

    Genome annotation databases

    EnsembliENST00000258098; ENSP00000258098; ENSG00000135631.
    GeneIDi26056.
    KEGGihsa:26056.
    UCSCiuc002sit.4. human.

    Polymorphism databases

    DMDMi34223002.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF334812 mRNA. Translation: AAK20892.1 .
    AB020664 mRNA. Translation: BAA74880.1 . Different initiation.
    BC035013 mRNA. Translation: AAH35013.1 .
    AF153085 mRNA. Translation: AAF34356.1 .
    CCDSi CCDS1923.1.
    PIRi T17312.
    RefSeqi NP_056285.1. NM_015470.2.
    UniGenei Hs.24557.

    3D structure databases

    ProteinModelPortali Q9BXF6.
    SMRi Q9BXF6. Positions 21-169, 600-651.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117518. 15 interactions.
    IntActi Q9BXF6. 7 interactions.
    STRINGi 9606.ENSP00000258098.

    PTM databases

    PhosphoSitei Q9BXF6.

    Polymorphism databases

    DMDMi 34223002.

    Proteomic databases

    MaxQBi Q9BXF6.
    PaxDbi Q9BXF6.
    PRIDEi Q9BXF6.

    Protocols and materials databases

    DNASUi 26056.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258098 ; ENSP00000258098 ; ENSG00000135631 .
    GeneIDi 26056.
    KEGGi hsa:26056.
    UCSCi uc002sit.4. human.

    Organism-specific databases

    CTDi 26056.
    GeneCardsi GC02M073212.
    HGNCi HGNC:24845. RAB11FIP5.
    HPAi HPA036406.
    HPA036407.
    MIMi 605536. gene.
    neXtProti NX_Q9BXF6.
    PharmGKBi PA134971129.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG84049.
    HOGENOMi HOG000234700.
    HOVERGENi HBG079127.
    KOi K12484.
    OMAi VEKTHGC.
    OrthoDBi EOG7WQ7SB.
    PhylomeDBi Q9BXF6.
    TreeFami TF326172.

    Miscellaneous databases

    GeneWikii RAB11FIP5.
    GenomeRNAii 26056.
    NextBioi 47930.
    PROi Q9BXF6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BXF6.
    Bgeei Q9BXF6.
    CleanExi HS_RAB11FIP5.
    Genevestigatori Q9BXF6.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR019018. Rab-bd_FIP-RBD.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF09457. RBD-FIP. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS51511. FIP_RBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiRFIP5_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXF6
    Secondary accession number(s): O94939, Q9P0M1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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).

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3