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P62491 (RB11A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-11A

Short name=Rab-11
Alternative name(s):
YL8
Gene names
Name:RAB11A
Synonyms:RAB11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes. Ref.21 Ref.22 Ref.24 Ref.27 Ref.28 Ref.31

Subunit structure

Interacts with RIP11 and STXBP6. Interacts with SGSM1, SGSM2 and SGSM3 By similarity. Interacts with EXOC6 in a GTP-dependent manner By similarity. Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4. Interacts with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and compete for binding RAB11A. Interacts with VIPAS39. Interacts with MYO5B. Found in a complex with MYO5B and CFTR. Interacts with NPC1L1. Interacts (GDP-bound form) with ZFYVE27. Interacts with BIRC6/bruce. May interact with TBC1D14. Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.31 Ref.33 Ref.38 Ref.39

Subcellular location

Cell membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Cleavage furrow. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Localizes to the cleavage furrow. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.15 Ref.18 Ref.19 Ref.21 Ref.28 Ref.32

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processCell cycle
Protein transport
Transport
   Cellular componentCell membrane
Cytoplasmic vesicle
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis

Inferred from mutant phenotype Ref.21. Source: UniProtKB

melanosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection development

Inferred from mutant phenotype Ref.23. Source: UniProtKB

plasma membrane to endosome transport

Non-traceable author statement PubMed 11163216. Source: UniProtKB

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

protein localization to plasma membrane

Inferred from direct assay Ref.23. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of protein transport

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

transmembrane transport

Traceable author statement. Source: Reactome

vesicle-mediated transport

Inferred from direct assay Ref.24Ref.27. Source: UniProtKB

water transport

Traceable author statement. Source: Reactome

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cleavage furrow

Inferred from direct assay Ref.21. Source: UniProtKB

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

phagocytic vesicle

Inferred from direct assay Ref.32. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay Ref.24. Source: UniProtKB

recycling endosome

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from direct assay PubMed 15229288. Source: MGI

transport vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay Ref.36Ref.39Ref.37Ref.38. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13Ref.21Ref.20Ref.39Ref.37Ref.38Ref.24Ref.26PubMed 18511905Ref.27PubMed 23535298. Source: UniProtKB

syntaxin binding

Non-traceable author statement PubMed 12145319. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAB11FIP2Q7L8042EBI-745098,EBI-1049676
ZFYVE27Q5T4F44EBI-745098,EBI-3892947

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62491-1)

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.
Isoform 2 (identifier: P62491-2)

The sequence of this isoform differs from the canonical sequence as follows:
     147-216: GLSFIETSAL...KPKVQCCQNI → EANVRQTRK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 213212Ras-related protein Rab-11A
PRO_0000121151
Propeptide214 – 2163Removed in mature form Potential
PRO_0000370807

Regions

Nucleotide binding18 – 269GTP
Nucleotide binding66 – 705GTP
Nucleotide binding124 – 1274GTP
Nucleotide binding154 – 1563GTP
Motif40 – 489Effector region By similarity

Amino acid modifications

Modified residue21N-acetylglycine Ref.11
Modified residue2131Cysteine methyl ester Potential
Lipidation2121S-geranylgeranyl cysteine Ref.34
Lipidation2131S-geranylgeranyl cysteine Ref.34

Natural variations

Alternative sequence147 – 21670GLSFI…CCQNI → EANVRQTRK in isoform 2.
VSP_046755

Experimental info

Mutagenesis251S → N: Dominant-negative mutant. Induces increased number of binucleated cells, indicating defects in cytokinesis. Inhibits the transport of NPC1L1 to the plama membrane. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. Ref.21 Ref.22 Ref.27
Mutagenesis701Q → L: Constitutively active mutant. Decreases GTPase activity. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. Ref.22 Ref.36 Ref.37 Ref.38 Ref.39

Secondary structure

............................... 216
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 76FC1E113A29B269

FASTA21624,394
        10         20         30         40         50         60 
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI 

        70         80         90        100        110        120 
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM 

       130        140        150        160        170        180 
LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ 

       190        200        210 
MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI 

« Hide

Isoform 2 [UniParc].

Checksum: 70C3A0F378C9893A
Show »

FASTA15517,659

References

« Hide 'large scale' references
[1]"Identification and characterization of a human homolog of the Schizosaccharomyces pombe ras-like gene YPT-3."
Drivas G.T., Shih A., Coutavas E.E., D'Eustachio P., Rush M.G.
Oncogene 6:3-9(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Zahraoui A., Joberty G., Tavitian A.
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Human rab11a: transcription, chromosome mapping and effect on the expression levels of host GTP-binding proteins."
Gromov P.S., Celis J.E., Hansen C., Tommerup N., Gromova I., Madsen P.
FEBS Lett. 429:359-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Brain.
[8]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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.
[11]Bienvenut W.V.
Submitted (OCT-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-24; 34-58; 62-72; 75-95 AND 133-140, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Platelet.
[12]"Identification and characterization of a family of Rab11-interacting proteins."
Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.
J. Biol. Chem. 276:39067-39075(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
[13]"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.
[14]"Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein."
Lindsay A.J., Hendrick A.G., Cantalupo G., Senic-Matuglia F., Goud B., Bucci C., McCaffrey M.W.
J. Biol. Chem. 277:12190-12199(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP4.
Tissue: Cervix carcinoma.
[15]"Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain."
Lindsay A.J., McCaffrey M.W.
J. Biol. Chem. 277:27193-27199(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis."
Lindsay A.J., McCaffrey M.W.
FEBS Lett. 571:86-92(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP1.
[17]"Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins."
Junutula J.R., Schonteich E., Wilson G.M., Peden A.A., Scheller R.H., Prekeris R.
J. Biol. Chem. 279:33430-33437(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP2.
[18]"The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane."
Lindsay A.J., McCaffrey M.W.
J. Cell Sci. 117:4365-4375(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[19]"The RCP-Rab11 complex regulates endocytic protein sorting."
Peden A.A., Schonteich E., Chun J., Junutula J.R., Scheller R.H., Prekeris R.
Mol. Biol. Cell 15:3530-3541(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP1, SUBCELLULAR LOCATION.
[20]"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: INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
[21]"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 RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF SER-25.
[22]"Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin."
Lock J.G., Stow J.L.
Mol. Biol. Cell 16:1744-1755(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-25 AND GLN-70.
[23]"Protrudin induces neurite formation by directional membrane trafficking."
Shirane M., Nakayama K.I.
Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFYVE27.
[24]"Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells."
Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S., Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E., Langford G.M., Fukuda M., Stanton B.A.
J. Biol. Chem. 282:23725-23736(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYO5B, IDENTIFICATION IN A COMPLEX WITH MYO5B AND CFTR.
[25]"Identification of Rab11 as a small GTPase binding protein for the Evi5 oncogene."
Westlake C.J., Junutula J.R., Simon G.C., Pilli M., Prekeris R., Scheller R.H., Jackson P.K., Eldridge A.G.
Proc. Natl. Acad. Sci. U.S.A. 104:1236-1241(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP3 AND EVI5.
[26]"Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
Pohl C., Jentsch S.
Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIRC6/BRUCE.
[27]"Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface."
Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L.
J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NPC1L1, MUTAGENESIS OF SER-25.
[28]"A molecular network for de novo generation of the apical surface and lumen."
Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E.
Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[29]"Mutations in VIPAR cause an arthrogryposis, renal dysfunction and cholestasis syndrome phenotype with defects in epithelial polarization."
Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y., Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B., Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P., Thomas S.G., Rappoport J.Z. expand/collapse author list , Arias I.M., Wolburg H., Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P.
Nat. Genet. 42:303-312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VIPAS39.
[30]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization."
Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.
Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYO5B.
[32]"Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
Seto S., Tsujimura K., Koide Y.
Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[33]"TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes."
Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.
J. Cell Biol. 197:659-675(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBC1D14.
[34]"Large-scale top down proteomics of the human proteome: membrane proteins, mitochondria, and senescence."
Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T., Tran J.C., Thomas P.M., Kelleher N.L.
Mol. Cell. Proteomics 12:3465-3473(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-212 AND CYS-213, IDENTIFICATION BY MASS SPECTROMETRY.
[35]"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
Eathiraj S., Pan X., Ritacco C., Lambright D.G.
Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-175 IN COMPLEX WITH GTP ANALOG.
[36]"Crystallographic evidence for substrate-assisted GTP hydrolysis by a small GTP binding protein."
Pasqualato S., Cherfils J.
Structure 13:533-540(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP ANALOG AND GDP, MUTAGENESIS OF GLN-70.
[37]"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 6-175 IN COMPLEX WITH GTP AND RAB11FIP3, MUTAGENESIS OF GLN-70.
[38]"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 7-173 IN COMPLEX WITH GTP, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF GLN-70.
[39]"Crystal structure of rab11 in complex with rab11 family interacting protein 2."
Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.
Structure 14:1273-1283(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP, INTERACTION WITH RAB11FIP2, MUTAGENESIS OF GLN-70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53143 mRNA. Translation: CAA37300.1.
X56740 mRNA. Translation: CAA40064.1.
AF000231 mRNA. Translation: AAC32887.1.
AF498946 mRNA. Translation: AAM21094.1.
CR407669 mRNA. Translation: CAG28597.1.
CR536493 mRNA. Translation: CAG38732.1.
BT020151 mRNA. Translation: AAV38953.1.
BT020154 mRNA. Translation: AAV38956.1.
AK300008 mRNA. Translation: BAG61825.1.
AK311770 mRNA. Translation: BAG34713.1.
AC011939 Genomic DNA. No translation available.
AC084854 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77752.1.
BC013348 mRNA. Translation: AAH13348.1.
CCDSCCDS10212.1. [P62491-1]
CCDS58373.1. [P62491-2]
PIRS47169.
RefSeqNP_001193765.1. NM_001206836.1. [P62491-2]
NP_004654.1. NM_004663.4. [P62491-1]
UniGeneHs.321541.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OIVX-ray1.98A/B1-173[»]
1OIWX-ray2.05A1-173[»]
1OIXX-ray1.70A1-173[»]
1YZKX-ray2.00A8-175[»]
2D7CX-ray1.75A/B7-173[»]
2GZDX-ray2.44A/B2-173[»]
2GZHX-ray2.47A2-173[»]
2HV8X-ray1.86A/B/C6-175[»]
4C4PX-ray2.00A1-173[»]
4LWZX-ray2.55A/C1-177[»]
4LX0X-ray2.19A/C1-177[»]
ProteinModelPortalP62491.
SMRP62491. Positions 6-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114299. 48 interactions.
DIPDIP-29138N.
IntActP62491. 20 interactions.
MINTMINT-1434585.
STRING9606.ENSP00000261890.

PTM databases

PhosphoSiteP62491.

Polymorphism databases

DMDM50402542.

2D gel databases

OGPP62491.

Proteomic databases

MaxQBP62491.
PaxDbP62491.
PRIDEP62491.

Protocols and materials databases

DNASU8766.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261890; ENSP00000261890; ENSG00000103769. [P62491-1]
ENST00000569896; ENSP00000456420; ENSG00000103769. [P62491-2]
GeneID8766.
KEGGhsa:8766.
UCSCuc002apk.3. human. [P62491-1]

Organism-specific databases

CTD8766.
GeneCardsGC15P066018.
HGNCHGNC:9760. RAB11A.
HPACAB013097.
MIM605570. gene.
neXtProtNX_P62491.
PharmGKBPA34101.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP62491.
KOK07904.
OMAAMGTRDD.
PhylomeDBP62491.
TreeFamTF300099.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
SignaLinkP62491.

Gene expression databases

ArrayExpressP62491.
BgeeP62491.
CleanExHS_RAB11A.
GenevestigatorP62491.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62491.
GeneWikiRAB11A.
GenomeRNAi8766.
NextBio32876.
PROP62491.
SOURCESearch...

Entry information

Entry nameRB11A_HUMAN
AccessionPrimary (citable) accession number: P62491
Secondary accession number(s): B2R4B6 expand/collapse secondary AC list , B4DT13, P24410, Q5TZN9, Q9JLX1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM