Reviewed, UniProtKB/Swiss-Prot P62491 (RB11A_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Modulates endosomal trafficking By similarity.
Subunit structure	Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. Binds RIP11 and STXBP6. Interacts with SGSM1, SGSM2 and SGSM3 By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Note: Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Ref.13 Ref.16 Ref.17
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Endosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	plasma membrane to endosome transport Non-traceable author statement. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network Inferred from direct assay. Source: MGI
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Non-traceable author statement. Source: UniProtKB syntaxin binding Non-traceable author statement. Source: UniProtKB transporter activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAB11FIP1	Q6WKZ4	1	EBI-745098,EBI-1043591

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

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 – 25

8

GTP By similarity

Nucleotide binding

66 – 70

5

GTP By similarity

Nucleotide binding

124 – 127

4

GTP By similarity

Motif

40 – 48

9

Effector region By similarity

Amino acid modifications

Modified residue

2

1

N-acetylglycine Ref.9

Modified residue

213

1

Cysteine methyl ester Potential

Lipidation

212

1

S-geranylgeranyl cysteine By similarity

Lipidation

213

1

S-geranylgeranyl cysteine By similarity

Secondary structure

1

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216

Helix Strand Turn

Details...

Beta strand

9 – 19

11

Helix

24 – 33

10

Beta strand

44 – 55

12

Beta strand

58 – 67

10

Helix

74 – 81

8

Beta strand

84 – 92

9

Helix

96 – 100

5

Helix

102 – 112

11

Beta strand

118 – 124

7

Helix

129 – 131

3

Helix

136 – 146

11

Beta strand

149 – 152

4

Turn

155 – 157

3

Helix

161 – 172

12

Sequences

	Sequence		Length	Mass (Da)
	P62491-1 [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: 1704119] [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: 9662449] [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 (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"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].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[9]	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.
[10]	"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: 11495908] [Abstract] Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
[11]	"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: 12470645] [Abstract] Cited for: INTERACTION WITH RAB11A.
[12]	"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: 11786538] [Abstract] Cited for: INTERACTION WITH RAB11FIP4. Tissue: Cervix carcinoma.
[13]	"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: 11994279] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"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: 15280022] [Abstract] Cited for: INTERACTION WITH RAB11FIP1.
[15]	"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: 15173169] [Abstract] Cited for: INTERACTION WITH RAB11FIP2.
[16]	"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: 15304524] [Abstract] Cited for: SUBCELLULAR LOCATION.
[17]	"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: 15181150] [Abstract] Cited for: INTERACTION WITH RAB11FIP1, SUBCELLULAR LOCATION.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC013348 mRNA. Translation: AAH13348.1.

IPI

IPI00429190.

PIR

S47169.

RefSeq

NP_004654.1.

UniGene

Hs.321541

3D structure databases

PDBPDBe

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	[»]

SMR

P62491. Positions 7-187, 8-188.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29138N.

IntAct

P62491. 10 interactions.

PTM databases

PhosphoSite

P62491.

2-D gel databases

OGP

P62491.

Proteomic databases

PRIDE

P62491.

Genome annotation databases

Ensembl

ENSG00000103769. Homo sapiens. [Contig view]

GeneID

8766.

KEGG

hsa:8766.

Organism-specific databases

GeneCards

GC15P063948.

H-InvDB

HIX0012357.

HGNC

HGNC:9760. RAB11A.

HPA

CAB013097.

MIM

605570. gene.

PharmGKB

PA34101.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P62491.

HOVERGEN

P62491.

OMA

P62491. SALERTN.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Gene expression databases

ArrayExpress

P62491.

Bgee

P62491.

CleanEx

HS_RAB11A.

GermOnline

ENSG00000103769. Homo sapiens.

Family and domain databases

InterPro

IPR003579. GTPase_Rab.
IPR015595. Rab11.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]

PANTHER

PTHR11708:SF213. Rab11. 1 hit.

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

32876.

SOURCE

Search...

Entry information

Entry name

RB11A_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 69 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)