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Q9D620

- RFIP1_MOUSE

UniProt

Q9D620 - RFIP1_MOUSE

Protein

Rab11 family-interacting protein 1

Gene

Rab11fip1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and phagocytosis By similarity.By similarity

    GO - Biological processi

    1. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rab11 family-interacting protein 1
    Short name:
    Rab11-FIP1
    Alternative name(s):
    Rab-coupling protein
    Gene namesi
    Name:Rab11fip1
    Synonyms:Rcp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1923017. Rab11fip1.

    Subcellular locationi

    Recycling endosome By similarity. Cytoplasmic vesiclephagosome membrane By similarity
    Note: Membrane-bound. RAB11A rather than RAB4A mediates RAB11FIP1 localization in the endocytic recycling compartment (ERC). Colocalizes with RAB11A at phagosomes By similarity.By similarity

    GO - Cellular componenti

    1. phagocytic vesicle membrane Source: UniProtKB-SubCell
    2. recycling endosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 645645Rab11 family-interacting protein 1PRO_0000097305Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei204 – 2041PhosphoserineBy similarity
    Modified residuei301 – 3011PhosphoserineBy similarity
    Modified residuei340 – 3401Phosphoserine1 Publication
    Modified residuei344 – 3441Phosphoserine1 Publication
    Modified residuei346 – 3461Phosphoserine1 Publication
    Modified residuei358 – 3581Phosphoserine1 Publication
    Modified residuei434 – 4341PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9D620.
    PaxDbiQ9D620.
    PRIDEiQ9D620.

    PTM databases

    PhosphoSiteiQ9D620.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9D620.
    BgeeiQ9D620.
    CleanExiMM_RAB11FIP1.
    GenevestigatoriQ9D620.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with RAB4A, RAB11A, RAB11B and RAB25 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9D620. 1 interaction.
    MINTiMINT-4127168.
    STRINGi10090.ENSMUSP00000058042.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D620.
    SMRiQ9D620. Positions 19-152, 605-637.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 110106C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini573 – 63563FIP-RBDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni581 – 64565Necessary for interaction with RAB4A and RAB11A, subcellular location and endosomal recyclingBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi211 – 22010Poly-Lys

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG85521.
    GeneTreeiENSGT00530000063203.
    HOGENOMiHOG000234700.
    HOVERGENiHBG079127.
    KOiK12484.
    OrthoDBiEOG7WQ7SB.

    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.

    Q9D620-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLAASAGRG PGTMWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE    50
    KYATSVSERS LGAPVWREEA TFELPPLLSS GAAPAAAATL QLTVLHRALL 100
    GLDKFLGRAE VDLRELHRDQ GRRKKQWYTL KSKPGKKDKE RGEIEVDIQF 150
    MRNNMTASMF DLSMKDKSRN PFGKLKDKIK GKNKDSASDT ASAIVPSVTP 200
    SVDSDDESFS KDKKKKSKIK TLFSKSSLQK TPLSQSMSVL PTSKSDKVLL 250
    RAGDFQSQWD DDAHEDESSS ASDVMSHKRT SSTDQQPNQS NFSLPKKEGL 300
    SFLGGLRSKN DSLSRSTVCI NGNHVYMEQP EARSEIRESS PSNSPSPQGF 350
    RRKHLFSSTE NLAARSPKEP GEGGGTSSDR RLSDSSTKDS MKSMSLPSYR 400
    PLTSGDNRES MSPANVEAAR ETKDSKKQES KKSSLLSLVT GKRDAAAKGS 450
    ESEPLPTVSE KEKERKGALV EAQLREEDLM RRPEKDALPV ASQWGSSLNP 500
    FEDVQISDPG ATTESRSEPK PPVPAARVPQ TKAVKPRPHP VKPMNTTATK 550
    IANSSLGTAT IITENLISEA LMKKYQPSDP AFAYAQLTHD ELIQLVLKQK 600
    ETISKKEFQV RELEDYIDNL LVRVMEETPN ILRVPAQMGK KAGKM 645
    Length:645
    Mass (Da):70,684
    Last modified:July 27, 2011 - v2
    Checksum:i667E0D12EC5FBD3B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601S → T in BAB29507. (PubMed:16141072)Curated
    Sequence conflicti207 – 2071E → K in BAE30042. (PubMed:16141072)Curated
    Sequence conflicti256 – 2561Q → H in BAE30042. (PubMed:16141072)Curated
    Sequence conflicti283 – 2831T → A in BAE30042. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014696 mRNA. Translation: BAB29507.1.
    AK151024 mRNA. Translation: BAE30042.1.
    CH466580 Genomic DNA. Translation: EDL32793.1.
    BC125400 mRNA. Translation: AAI25401.1.
    BC132094 mRNA. Translation: AAI32095.1.
    CCDSiCCDS52534.1.
    RefSeqiNP_083699.2. NM_029423.2.
    UniGeneiMm.205335.

    Genome annotation databases

    EnsembliENSMUST00000033878; ENSMUSP00000033878; ENSMUSG00000031488.
    GeneIDi75767.
    KEGGimmu:75767.
    UCSCiuc009lia.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014696 mRNA. Translation: BAB29507.1 .
    AK151024 mRNA. Translation: BAE30042.1 .
    CH466580 Genomic DNA. Translation: EDL32793.1 .
    BC125400 mRNA. Translation: AAI25401.1 .
    BC132094 mRNA. Translation: AAI32095.1 .
    CCDSi CCDS52534.1.
    RefSeqi NP_083699.2. NM_029423.2.
    UniGenei Mm.205335.

    3D structure databases

    ProteinModelPortali Q9D620.
    SMRi Q9D620. Positions 19-152, 605-637.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9D620. 1 interaction.
    MINTi MINT-4127168.
    STRINGi 10090.ENSMUSP00000058042.

    PTM databases

    PhosphoSitei Q9D620.

    Proteomic databases

    MaxQBi Q9D620.
    PaxDbi Q9D620.
    PRIDEi Q9D620.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033878 ; ENSMUSP00000033878 ; ENSMUSG00000031488 .
    GeneIDi 75767.
    KEGGi mmu:75767.
    UCSCi uc009lia.2. mouse.

    Organism-specific databases

    CTDi 80223.
    MGIi MGI:1923017. Rab11fip1.

    Phylogenomic databases

    eggNOGi NOG85521.
    GeneTreei ENSGT00530000063203.
    HOGENOMi HOG000234700.
    HOVERGENi HBG079127.
    KOi K12484.
    OrthoDBi EOG7WQ7SB.

    Miscellaneous databases

    NextBioi 343894.
    PROi Q9D620.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D620.
    Bgeei Q9D620.
    CleanExi MM_RAB11FIP1.
    Genevestigatori Q9D620.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow and Head.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Brain.
    4. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; SER-344 AND SER-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiRFIP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9D620
    Secondary accession number(s): Q05A58, Q3UBC2, Q8BN24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3