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Q9D620

- RFIP1_MOUSE

UniProt

Q9D620 - RFIP1_MOUSE

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Protein

Rab11 family-interacting protein 1

Gene
Rab11fip1, Rcp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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.

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
Complete GO annotation...

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.

GO - Cellular componenti

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

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 – 2041Phosphoserine By similarity
Modified residuei301 – 3011Phosphoserine By similarity
Modified residuei340 – 3401Phosphoserine1 Publication
Modified residuei344 – 3441Phosphoserine1 Publication
Modified residuei346 – 3461Phosphoserine1 Publication
Modified residuei358 – 3581Phosphoserine1 Publication
Modified residuei434 – 4341Phosphoserine By 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.

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 110106C2Add
BLAST
Domaini573 – 63563FIP-RBDAdd
BLAST

Region

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

Compositional bias

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

Sequence similaritiesi

Contains 1 C2 domain.
Contains 1 FIP-RBD domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601S → T in BAB29507. 1 Publication
Sequence conflicti207 – 2071E → K in BAE30042. 1 Publication
Sequence conflicti256 – 2561Q → H in BAE30042. 1 Publication
Sequence conflicti283 – 2831T → A in BAE30042. 1 Publication

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: July 9, 2014
This is version 98 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

Similar proteinsi