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Q86YS3

- RFIP4_HUMAN

UniProt

Q86YS3 - RFIP4_HUMAN

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Protein

Rab11 family-interacting protein 4

Gene
RAB11FIP4, ARFO2, KIAA1821
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. In case of infection by HCMV (human cytomegalovirus), may participate in egress of the virus out of nucleus; this function is independent of ARF6.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi62 – 7312 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. transport Source: UniProtKB-KW
  3. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transport

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Rab11 family-interacting protein 4
Short name:
FIP4-Rab11
Short name:
Rab11-FIP4
Alternative name(s):
Arfophilin-2
Gene namesi
Synonyms:ARFO2, KIAA1821
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:30267. RAB11FIP4.

Subcellular locationi

Recycling endosome membrane; Peripheral membrane protein. Cleavage furrow. Midbody. Cytoplasmic vesicle
Note: Recruited to the cleavage furrow and the midbody during cytokinesis.4 Publications

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB
  2. endocytic vesicle Source: UniProtKB
  3. endosome Source: UniProtKB
  4. extracellular space Source: UniProt
  5. midbody Source: UniProtKB
  6. recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi627 – 6271D → A: Abolishes Rab11-binding. 1 Publication

Organism-specific databases

PharmGKBiPA134978007.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Rab11 family-interacting protein 4PRO_0000073880Add
BLAST

Proteomic databases

MaxQBiQ86YS3.
PaxDbiQ86YS3.
PRIDEiQ86YS3.

PTM databases

PhosphoSiteiQ86YS3.

Expressioni

Tissue specificityi

Present at high level in testis (at protein level). Weakly expressed in other tissues.1 Publication

Gene expression databases

ArrayExpressiQ86YS3.
BgeeiQ86YS3.
CleanExiHS_RAB11FIP4.
GenevestigatoriQ86YS3.

Organism-specific databases

HPAiHPA021595.

Interactioni

Subunit structurei

Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and ARF6. Interacts with RAB11A; the interaction is direct. Forms a heterooligomeric complex with RAB11FIP2, RAB11FIP3 and RAB11FIP5. Interacts with HCMV (human cytomegalovirus) gM/UL100. Interacts with ECM29.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arf6P623312EBI-949727,EBI-988682From a different organism.

Protein-protein interaction databases

BioGridi124079. 10 interactions.
IntActiQ86YS3. 3 interactions.
MINTiMINT-2877094.
STRINGi9606.ENSP00000312837.

Structurei

3D structure databases

ProteinModelPortaliQ86YS3.
SMRiQ86YS3. Positions 17-81, 596-636.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 8436EF-handAdd
BLAST
Domaini574 – 63663FIP-RBDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 637556Necessary for interaction with RAB11A, subcellular location, homo- or heterooligomerizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili280 – 617338 Reviewed predictionAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 EF-hand domain.
Contains 1 FIP-RBD domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG259959.
HOGENOMiHOG000063670.
HOVERGENiHBG054059.
InParanoidiQ86YS3.
KOiK12485.
OMAiGRQLMHS.
OrthoDBiEOG793B75.
PhylomeDBiQ86YS3.
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]
PfamiPF09457. RBD-FIP. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86YS3-1) [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

MAGGAGWSGA PAALLRSVRR LREVFEVCGR DPDGFLRVER VAALGLRFGQ    50
GEEVEKLVKY LDPNDLGRIN FKDFCRGVFA MKGCEELLKD VLSVESAGTL 100
PCAPEIPDCV EQGSEVTGPT FADGELIPRE PGFFPEDEEE AMTLAPPEGP 150
QELYTDSPME STQSLEGSVG SPAEKDGGLG GLFLPEDKSL VHTPSMTTSD 200
LSTHSTTSLI SNEEQFEDYG EGDDVDCAPS SPCPDDETRT NVYSDLGSSV 250
SSSAGQTPRK MRHVYNSELL DVYCSQCCKK INLLNDLEAR LKNLKANSPN 300
RKISSTAFGR QLMHSSNFSS SNGSTEDLFR DSIDSCDNDI TEKVSFLEKK 350
VTELENDSLT NGDLKSKLKQ ENTQLVHRVH ELEEMVKDQE TTAEQALEEE 400
ARRHREAYGK LEREKATEVE LLNARVQQLE EENTELRTTV TRLKSQTEKL 450
DEERQRMSDR LEDTSLRLKD EMDLYKRMMD KLRQNRLEFQ KEREATQELI 500
EDLRKELEHL QMYKLDCERP GRGRSASSGL GEFNARAREV ELEHEVKRLK 550
QENYKLRDQN DDLNGQILSL SLYEAKNLFA AQTKAQSLAA EIDTASRDEL 600
MEALKEQEEI NFRLRQYMDK IILAILDHNP SILEIKH 637
Length:637
Mass (Da):71,928
Last modified:June 1, 2003 - v1
Checksum:i8A5CDB9799383342
GO
Isoform 2 (identifier: Q86YS3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.
     103-111: APEIPDCVE → MRTPPALGS

Show »
Length:535
Mass (Da):60,771
Checksum:i7ECB4806726B7D5D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 102102Missing in isoform 2. VSP_013724Add
BLAST
Alternative sequencei103 – 1119APEIPDCVE → MRTPPALGS in isoform 2. VSP_013725

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti417 – 4171T → I in BAC05045. 1 Publication
Sequence conflicti518 – 5181E → G in BAC05045. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY169244 mRNA. Translation: AAO21970.1.
AK097424 mRNA. Translation: BAC05045.1.
BC093914 mRNA. Translation: AAH93914.1.
BC101517 mRNA. Translation: AAI01518.1.
AJ314646 mRNA. Translation: CAC44535.1.
AB058724 mRNA. Translation: BAB47450.1.
AL831830 mRNA. Translation: CAD38543.1.
CCDSiCCDS11267.1. [Q86YS3-1]
RefSeqiNP_116321.2. NM_032932.3. [Q86YS3-1]
UniGeneiHs.406788.

Genome annotation databases

EnsembliENST00000325874; ENSP00000312837; ENSG00000131242. [Q86YS3-1]
ENST00000394744; ENSP00000378227; ENSG00000131242. [Q86YS3-2]
GeneIDi84440.
KEGGihsa:84440.
UCSCiuc002hgn.1. human. [Q86YS3-1]
uc002hgo.2. human. [Q86YS3-2]

Polymorphism databases

DMDMi67472134.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY169244 mRNA. Translation: AAO21970.1 .
AK097424 mRNA. Translation: BAC05045.1 .
BC093914 mRNA. Translation: AAH93914.1 .
BC101517 mRNA. Translation: AAI01518.1 .
AJ314646 mRNA. Translation: CAC44535.1 .
AB058724 mRNA. Translation: BAB47450.1 .
AL831830 mRNA. Translation: CAD38543.1 .
CCDSi CCDS11267.1. [Q86YS3-1 ]
RefSeqi NP_116321.2. NM_032932.3. [Q86YS3-1 ]
UniGenei Hs.406788.

3D structure databases

ProteinModelPortali Q86YS3.
SMRi Q86YS3. Positions 17-81, 596-636.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124079. 10 interactions.
IntActi Q86YS3. 3 interactions.
MINTi MINT-2877094.
STRINGi 9606.ENSP00000312837.

PTM databases

PhosphoSitei Q86YS3.

Polymorphism databases

DMDMi 67472134.

Proteomic databases

MaxQBi Q86YS3.
PaxDbi Q86YS3.
PRIDEi Q86YS3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325874 ; ENSP00000312837 ; ENSG00000131242 . [Q86YS3-1 ]
ENST00000394744 ; ENSP00000378227 ; ENSG00000131242 . [Q86YS3-2 ]
GeneIDi 84440.
KEGGi hsa:84440.
UCSCi uc002hgn.1. human. [Q86YS3-1 ]
uc002hgo.2. human. [Q86YS3-2 ]

Organism-specific databases

CTDi 84440.
GeneCardsi GC17P029718.
HGNCi HGNC:30267. RAB11FIP4.
HPAi HPA021595.
MIMi 611999. gene.
neXtProti NX_Q86YS3.
PharmGKBi PA134978007.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259959.
HOGENOMi HOG000063670.
HOVERGENi HBG054059.
InParanoidi Q86YS3.
KOi K12485.
OMAi GRQLMHS.
OrthoDBi EOG793B75.
PhylomeDBi Q86YS3.
TreeFami TF327221.

Miscellaneous databases

ChiTaRSi RAB11FIP4. human.
GeneWikii RAB11FIP4.
GenomeRNAii 84440.
NextBioi 74191.
PROi Q86YS3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q86YS3.
Bgeei Q86YS3.
CleanExi HS_RAB11FIP4.
Genevestigatori Q86YS3.

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 PF09457. RBD-FIP. 1 hit.
[Graphical view ]
PROSITEi PS50222. EF_HAND_2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN ENDOSOMAL TRAFFICKING, SUBUNIT, INTERACTION WITH RAB11A.
  2. "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).
    Tissue: Testis.
  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] (ISOFORM 1).
    Tissue: Brain.
  4. "Complete physical map and gene content of the human NF1 tumor suppressor region in human and mouse."
    Jenne D.E., Tinschert S., Dorschner M.O., Hameister H., Stephens K., Kehrer-Sawatzki H.
    Genes Chromosomes Cancer 37:111-120(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-637 (ISOFORM 1).
  5. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-637 (ISOFORM 1).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-637 (ISOFORM 1).
    Tissue: Brain.
  7. "The novel Rab11-FIP/Rip/RCP family of proteins displays extensive homo- and hetero-interacting abilities."
    Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.
    Biochem. Biophys. Res. Commun. 292:909-915(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling endosome distribution and are related to Drosophila nuclear fallout."
    Hickson G.R., Matheson J., Riggs B., Maier V.H., Fielding A.B., Prekeris R., Sullivan W., Barr F.A., Gould G.W.
    Mol. Biol. Cell 14:2908-2920(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "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 RAB11A AND ARF6, MUTAGENESIS OF ASP-627.
  10. "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: SUBCELLULAR LOCATION, INTERACTION WITH RAB11A.
  11. "HCMV-encoded glycoprotein M (UL100) interacts with Rab11 effector protein FIP4."
    Krzyzaniak M.A., Mach M., Britt W.J.
    Traffic 10:1439-1457(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCMV RAB11FIP4.
  12. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
    Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
    J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.

Entry informationi

Entry nameiRFIP4_HUMAN
AccessioniPrimary (citable) accession number: Q86YS3
Secondary accession number(s): Q52LI1
, Q8N829, Q8NDT7, Q969D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 99 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

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