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O75154

- RFIP3_HUMAN

UniProt

O75154 - RFIP3_HUMAN

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Protein

Rab11 family-interacting protein 3

Gene
RAB11FIP3, ARFO1, KIAA0665
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 226121 Reviewed predictionAdd
BLAST
Calcium bindingi247 – 258122 Reviewed predictionAdd
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
Complete GO annotation...

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
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.7 Publications

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
Complete GO annotation...

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 1 Publication, it specifically interacts with ARF6 but not ARF5. Interacts with ARF6; according to 1 Publication but not 1 Publication. 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.

Miscellaneous databases

EvolutionaryTraceiO75154.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini202 – 23736EF-hand 1Add
BLAST
Domaini234 – 26936EF-hand 2Add
BLAST
Domaini694 – 75663FIP-RBDAdd
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 – 694210 Reviewed predictionAdd
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.
Contains 1 FIP-RBD domain.

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. VSP_038664Add
BLAST
Alternative sequencei297 – 3015FVTYE → MPFLK in isoform 2. VSP_038665
Alternative sequencei421 – 4211P → PSTDPLAAKLHSILTDEAFE FYCSQCHKQINRLEDLSARL SDLEMN in isoform 3. VSP_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]
ENST00000457159; ENSP00000398730; ENSG00000090565. [O75154-3]
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 ]
ENST00000457159 ; ENSP00000398730 ; ENSG00000090565 . [O75154-3 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 126 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

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