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O75154

- RFIP3_HUMAN

UniProt

O75154 - RFIP3_HUMAN

Protein

Rab11 family-interacting protein 3

Gene

RAB11FIP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi215 – 226121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi247 – 258122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ADP-ribosylation factor binding Source: UniProtKB
    2. calcium ion binding Source: InterPro
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. Rab GTPase binding Source: UniProtKB

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. endocytic recycling Source: UniProtKB
    3. vesicle-mediated transport Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:RAB11FIP3
    Synonyms:ARFO1, KIAA0665
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:17224. RAB11FIP3.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cleavage furrow Source: UniProtKB
    3. endosome Source: UniProtKB
    4. intercellular bridge Source: HPA
    5. intracellular membrane-bounded organelle Source: HPA
    6. microtubule organizing center Source: HPA
    7. midbody Source: UniProtKB
    8. nucleus Source: HPA
    9. recycling endosome Source: UniProtKB
    10. recycling endosome membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi737 – 7371Y → S: Abolishes Rab11-binding. 1 Publication
    Mutagenesisi738 – 7381I → E: Abolishes Rab11-binding. 2 Publications
    Mutagenesisi739 – 7391D → A: Abolishes Rab11-binding. 1 Publication
    Mutagenesisi746 – 7461M → S: Abolishes Rab11-binding. 1 Publication
    Mutagenesisi747 – 7471E → A: Abolishes Rab11-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134950896.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 756756Rab11 family-interacting protein 3PRO_0000073879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei102 – 1021Phosphoserine; by CDK11 Publication
    Modified residuei281 – 2811Phosphoserine1 Publication
    Modified residuei348 – 3481Phosphoserine1 Publication
    Modified residuei488 – 4881Phosphoserine1 Publication
    Modified residuei538 – 5381Phosphoserine1 Publication
    Modified residuei647 – 6471Phosphoserine1 Publication
    Modified residuei648 – 6481Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated at Ser-102 by CDK1 during metaphase, and dephosphorylated as cells enter telophase.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75154.
    PaxDbiO75154.
    PRIDEiO75154.

    PTM databases

    PhosphoSiteiO75154.

    Expressioni

    Gene expression databases

    ArrayExpressiO75154.
    BgeeiO75154.
    CleanExiHS_RAB11FIP3.
    GenevestigatoriO75154.

    Organism-specific databases

    HPAiHPA028088.
    HPA028631.
    HPA030086.

    Interactioni

    Subunit structurei

    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 PubMed:16148947, it specifically interacts with ARF6 but not ARF5. Interacts with ARF6; according to PubMed:17030804 but not PubMed:16148947. Interacts with RACGAP1/MgcRacGAP; interaction takes place during late stage of cytokinesis and is required for recruitment to the midbody. Interacts with ASAP1 and EXOC7.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RACGAP1Q9H0H57EBI-7942186,EBI-717233

    Protein-protein interaction databases

    BioGridi115076. 10 interactions.
    IntActiO75154. 4 interactions.
    MINTiMINT-6799564.
    STRINGi9606.ENSP00000262305.

    Structurei

    Secondary structure

    1
    756
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi704 – 7096
    Helixi717 – 74630
    Helixi750 – 7534

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D7CX-ray1.75C/D715-756[»]
    2HV8X-ray1.86D/E/F695-756[»]
    4D0MX-ray6.00E/F/K/L/U/V/a/b/e/f/i/j713-756[»]
    ProteinModelPortaliO75154.
    SMRiO75154. Positions 206-263, 702-756.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75154.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini202 – 23736EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini234 – 26936EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini694 – 75663FIP-RBDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni484 – 588105ARF-binding domain (ABD)Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili485 – 694210Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 197193Pro-richAdd
    BLAST
    Compositional biasi148 – 1514Poly-Ser
    Compositional biasi366 – 3694Poly-Leu

    Domaini

    The RBD-FIP domain mediates the interaction with Rab11 (RAB11A or RAB11B).1 Publication

    Sequence similaritiesi

    Contains 2 EF-hand domains.PROSITE-ProRule annotation
    Contains 1 FIP-RBD domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG259959.
    HOVERGENiHBG054059.
    InParanoidiO75154.
    KOiK12485.
    OMAiDFGESNT.
    OrthoDBiEOG793B75.
    PhylomeDBiO75154.
    TreeFamiTF327221.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR002048. EF_hand_dom.
    IPR019018. Rab-bd_FIP-RBD.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 1 hit.
    PF09457. RBD-FIP. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 2 hits.
    [Graphical view]
    PROSITEiPS50222. EF_HAND_2. 2 hits.
    PS51511. FIP_RBD. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75154-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MASAPPASPP GSEPPGPDPE PGGPDGPGAA QLAPGPAELR LGAPVGGPDP    50
    QSPGLDEPAP GAAADGGARW SAGPAPGLEG GPRDPGPSAP PPRSGPRGQL 100
    ASPDAPGPGP RSEAPLPELD PLFSWTEEPE ECGPASCPES APFRLQGSSS 150
    SHRARGEVDV FSPFPAPTAG ELALEQGPGS PPQPSDLSQT HPLPSEPVGS 200
    QEDGPRLRAV FDALDGDGDG FVRIEDFIQF ATVYGAEQVK DLTKYLDPSG 250
    LGVISFEDFY QGITAIRNGD PDGQCYGGVA SAQDEEPLAC PDEFDDFVTY 300
    EANEVTDSAY MGSESTYSEC ETFTDEDTST LVHPELQPEG DADSAGGSAV 350
    PSECLDAMEE PDHGALLLLP GRPHPHGQSV ITVIGGEEHF EDYGEGSEAE 400
    LSPETLCNGQ LGCSDPAFLT PSPTKRLSSK KVARYLHQSG ALTMEALEDP 450
    SPELMEGPEE DIADKVVFLE RRVLELEKDT AATGEQHSRL RQENLQLVHR 500
    ANALEEQLKE QELRACEMVL EETRRQKELL CKMEREKSIE IENLQTRLQQ 550
    LDEENSELRS CTPCLKANIE RLEEEKQKLL DEIESLTLRL SEEQENKRRM 600
    GDRLSHERHQ FQRDKEATQE LIEDLRKQLE HLQLLKLEAE QRRGRSSSMG 650
    LQEYHSRARE SELEQEVRRL KQDNRNLKEQ NEELNGQIIT LSIQGAKSLF 700
    STAFSESLAA EISSVSRDEL MEAIQKQEEI NFRLQDYIDR IIVAIMETNP 750
    SILEVK 756
    Length:756
    Mass (Da):82,440
    Last modified:November 1, 1998 - v1
    Checksum:i264CEC399F28AFB9
    GO
    Isoform 2 (identifier: O75154-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-296: Missing.
         297-301: FVTYE → MPFLK

    Note: No experimental confirmation available.

    Show »
    Length:460
    Mass (Da):52,451
    Checksum:i574FC0A764FCA199
    GO
    Isoform 3 (identifier: O75154-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         421-421: P → PSTDPLAAKLHSILTDEAFEFYCSQCHKQINRLEDLSARLSDLEMN

    Note: No experimental confirmation available.

    Show »
    Length:801
    Mass (Da):87,577
    Checksum:i4B4D2E7E868CF67B
    GO

    Sequence cautioni

    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.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 296296Missing in isoform 2. 1 PublicationVSP_038664Add
    BLAST
    Alternative sequencei297 – 3015FVTYE → MPFLK in isoform 2. 1 PublicationVSP_038665
    Alternative sequencei421 – 4211P → PSTDPLAAKLHSILTDEAFE FYCSQCHKQINRLEDLSARL SDLEMN in isoform 3. 1 PublicationVSP_038666

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS32351.1. [O75154-1]
    CCDS45364.1. [O75154-2]
    PIRiT00367.
    RefSeqiNP_001135744.1. NM_001142272.1. [O75154-2]
    NP_055515.1. NM_014700.3. [O75154-1]
    XP_005255770.1. XM_005255713.1. [O75154-3]
    XP_005255772.1. XM_005255715.2.
    XP_006725305.1. XM_006725242.1. [O75154-3]
    XP_006725309.1. XM_006725246.1.
    UniGeneiHs.531642.

    Genome annotation databases

    EnsembliENST00000262305; ENSP00000262305; ENSG00000090565. [O75154-1]
    ENST00000450428; ENSP00000415919; ENSG00000090565. [O75154-2]
    GeneIDi9727.
    KEGGihsa:9727.
    UCSCiuc002chf.3. human. [O75154-1]
    uc010uuf.2. human. [O75154-2]
    uc010uug.2. human. [O75154-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS32351.1. [O75154-1 ]
    CCDS45364.1. [O75154-2 ]
    PIRi T00367.
    RefSeqi NP_001135744.1. NM_001142272.1. [O75154-2 ]
    NP_055515.1. NM_014700.3. [O75154-1 ]
    XP_005255770.1. XM_005255713.1. [O75154-3 ]
    XP_005255772.1. XM_005255715.2.
    XP_006725305.1. XM_006725242.1. [O75154-3 ]
    XP_006725309.1. XM_006725246.1.
    UniGenei Hs.531642.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D7C X-ray 1.75 C/D 715-756 [» ]
    2HV8 X-ray 1.86 D/E/F 695-756 [» ]
    4D0M X-ray 6.00 E/F/K/L/U/V/a/b/e/f/i/j 713-756 [» ]
    ProteinModelPortali O75154.
    SMRi O75154. Positions 206-263, 702-756.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115076. 10 interactions.
    IntActi O75154. 4 interactions.
    MINTi MINT-6799564.
    STRINGi 9606.ENSP00000262305.

    PTM databases

    PhosphoSitei O75154.

    Proteomic databases

    MaxQBi O75154.
    PaxDbi O75154.
    PRIDEi O75154.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262305 ; ENSP00000262305 ; ENSG00000090565 . [O75154-1 ]
    ENST00000450428 ; ENSP00000415919 ; ENSG00000090565 . [O75154-2 ]
    GeneIDi 9727.
    KEGGi hsa:9727.
    UCSCi uc002chf.3. human. [O75154-1 ]
    uc010uuf.2. human. [O75154-2 ]
    uc010uug.2. human. [O75154-3 ]

    Organism-specific databases

    CTDi 9727.
    GeneCardsi GC16P000475.
    HGNCi HGNC:17224. RAB11FIP3.
    HPAi HPA028088.
    HPA028631.
    HPA030086.
    MIMi 608738. gene.
    neXtProti NX_O75154.
    PharmGKBi PA134950896.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259959.
    HOVERGENi HBG054059.
    InParanoidi O75154.
    KOi K12485.
    OMAi DFGESNT.
    OrthoDBi EOG793B75.
    PhylomeDBi O75154.
    TreeFami TF327221.

    Miscellaneous databases

    ChiTaRSi RAB11FIP3. human.
    EvolutionaryTracei O75154.
    GeneWikii RAB11FIP3.
    GenomeRNAii 9727.
    NextBioi 36593.
    PROi O75154.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75154.
    Bgeei O75154.
    CleanExi HS_RAB11FIP3.
    Genevestigatori O75154.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR002048. EF_hand_dom.
    IPR019018. Rab-bd_FIP-RBD.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 1 hit.
    PF09457. RBD-FIP. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 2 hits.
    [Graphical view ]
    PROSITEi PS50222. EF_HAND_2. 2 hits.
    PS51511. FIP_RBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 532-756.
    8. 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. Cited for: INTERACTION WITH RAB11A AND ARF6.
    14. 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. 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.

    Entry informationi

    Entry nameiRFIP3_HUMAN
    AccessioniPrimary (citable) accession number: O75154
    Secondary accession number(s): B0QYI8
    , B0QYT8, B1AHQ0, B4DEI7, B4DZR6, Q4VXV7, Q7Z5E9, Q9H155, Q9H1G0, Q9NUI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 127 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3