P62491 (RB11A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-11A
Short name=Rab-11

Alternative name(s):
YL8

Gene names

Name:	RAB11A
Synonyms:	RAB11

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	216 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.20 Ref.21 Ref.23 Ref.26 Ref.27 Ref.30
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.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.30 Ref.32 Ref.36 Ref.37
Subcellular location	Cell membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Cleavage furrow. Cytoplasmic vesicle › phagosome. Cytoplasmic vesicle › phagosome 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.14 Ref.17 Ref.18 Ref.20 Ref.27 Ref.31
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Cell cycle Protein transport Transport
Cellular component	Cell membrane Cytoplasmic vesicle Endosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from mutant phenotype Ref.20. Source: UniProtKB melanosome transport Inferred from sequence or structural similarity. Source: UniProtKB neuron projection development Inferred from mutant phenotype Ref.22. Source: UniProtKB plasma membrane to endosome transport Non-traceable author statement PubMed 11163216. Source: UniProtKB protein localization to plasma membrane Inferred from direct assay Ref.22. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of long-term neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara regulation of protein transport Inferred from electronic annotation. Source: Compara small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro transmembrane transport Traceable author statement. Source: Reactome water transport Traceable author statement. Source: Reactome
Cellular_component	cleavage furrow Inferred from direct assay Ref.20. Source: UniProtKB cytoplasmic vesicle membrane Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara phagocytic vesicle Inferred from direct assay Ref.31. 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.23. 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: Compara
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay Ref.34Ref.37Ref.35Ref.36. Source: UniProtKB syntaxin binding Non-traceable author statement PubMed 12145319. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAB11FIP2	Q7L804	2	EBI-745098,EBI-1049676
ZFYVE27	Q5T4F4	4	EBI-745098,EBI-3892947

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 213

212

Ras-related protein Rab-11A

PRO_0000121151

Propeptide

214 – 216

3

Removed in mature form Potential

PRO_0000370807

Regions

Nucleotide binding

18 – 26

9

GTP

Nucleotide binding

66 – 70

5

GTP

Nucleotide binding

124 – 127

4

GTP

Nucleotide binding

154 – 156

3

GTP

Motif

40 – 48

9

Effector region By similarity

Amino acid modifications

Modified residue

2

1

N-acetylglycine Ref.10

Modified residue

213

1

Cysteine methyl ester Potential

Lipidation

212

1

S-geranylgeranyl cysteine By similarity

Lipidation

213

1

S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis

25

1

S → 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.20 Ref.21 Ref.26

Mutagenesis

70

1

Q → 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.21 Ref.34 Ref.35 Ref.36 Ref.37

Secondary structure

1

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216

Helix Strand Turn

Details...

Beta strand

9 – 18

10

Helix

24 – 33

10

Beta strand

45 – 55

11

Beta strand

58 – 67

10

Beta strand

72 – 74

3

Helix

78 – 81

4

Beta strand

86 – 92

7

Helix

96 – 100

5

Helix

102 – 112

11

Beta strand

118 – 124

7

Helix

126 – 131

6

Helix

136 – 145

10

Beta strand

149 – 152

4

Turn

155 – 157

3

Helix

161 – 172

12

Sequences

	Sequence		Length	Mass (Da)
	P62491 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 76FC1E113A29B269	FASTA	216	24,394
	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

References

	« Hide 'large scale' referencesShow '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].
[2]	Zahraoui A., Joberty G., Tavitian A. Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[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]. 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].
[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].
[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. , 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]. Tissue: Brain.
[8]	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. , 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].
[9]	"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.
[10]	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, MASS SPECTROMETRY. Tissue: B-cell lymphoma and Platelet.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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. , 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.
[29]	"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].
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
AK311770 mRNA. Translation: BAG34713.1.
CH471082 Genomic DNA. Translation: EAW77752.1.
BC013348 mRNA. Translation: AAH13348.1.

IPI

IPI00429190.

PIR

S47169.

RefSeq

NP_001193765.1. NM_001206836.1.
NP_004654.1. NM_004663.4.

UniGene

Hs.321541.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OIV	X-ray	1.98	A/B	1-173	[»]
1OIW	X-ray	2.05	A	1-173	[»]
1OIX	X-ray	1.70	A	1-173	[»]
1YZK	X-ray	2.00	A	8-175	[»]
2D7C	X-ray	1.75	A/B	7-173	[»]
2GZD	X-ray	2.44	A/B	2-172	[»]
2GZH	X-ray	2.47	A	2-172	[»]
2HV8	X-ray	1.86	A/B/C	6-174	[»]

ProteinModelPortal

P62491.

ModBase

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Protein-protein interaction databases

DIP

DIP-29138N.

IntAct

P62491. 14 interactions.

MINT

MINT-1434585.

STRING

9606.ENSP00000261890.

PTM databases

PhosphoSite

P62491.

Polymorphism databases

DMDM

50402542.

2D gel databases

OGP

P62491.

Proteomic databases

PaxDb

P62491.

PRIDE

P62491.

Protocols and materials databases

DNASU

8766.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000261890; ENSP00000261890; ENSG00000103769.

GeneID

8766.

KEGG

hsa:8766.

UCSC

uc002apk.3. human.

Organism-specific databases

CTD

8766.

GeneCards

GC15P066018.

HGNC

HGNC:9760. RAB11A.

HPA

CAB013097.

MIM

605570. gene.

neXtProt

NX_P62491.

PharmGKB

PA34101.

GenAtlas

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Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

P62491.

KO

K07904.

OMA

AMGTRDD.

OrthoDB

EOG4RR6J7.

PhylomeDB

P62491.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6downstreampathway. Arf6 downstream pathway.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_15518. Transmembrane transport of small molecules.

SignaLink

P62491.

Gene expression databases

ArrayExpress

P62491.

Bgee

P62491.

CleanEx

HS_RAB11A.

Genevestigator

P62491.

GermOnline

ENSG00000103769. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P62491.

GenomeRNAi

8766.

NextBio

32876.

SOURCE

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Entry information

Entry name

RB11A_HUMAN

Accession

Primary (citable) accession number: P62491
Secondary accession number(s): B2R4B6 , P24410, Q5TZN9, Q9JLX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.