Q15907 (RB11B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-11B

Alternative name(s):
GTP-binding protein YPT3

Gene names

Name:	RAB11B
Synonyms:	YPT3

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	218 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	GTPase that modulates endosomal trafficking. Acts as a major regulator of membrane delivery during cytokinesis By similarity.
Subunit structure	Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. May interact with TBC1D14. Ref.8 Ref.11
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Cytoplasmic vesicle › phagosome. Cytoplasmic vesicle › phagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.10
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 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 melanosome transport Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara phagocytic vesicle Inferred from direct assay Ref.10. Source: UniProtKB phagocytic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GDP binding Inferred from direct assay Ref.12. Source: UniProtKB GTP binding Inferred from direct assay Ref.12. Source: UniProtKB GTPase activity Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 215

214

Ras-related protein Rab-11B

PRO_0000121158

Propeptide

216 – 218

3

Removed in mature form Potential

PRO_0000370815

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.7

Modified residue

215

1

Cysteine methyl ester Potential

Lipidation

214

1

S-geranylgeranyl cysteine By similarity

Lipidation

215

1

S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict

75

1

A → R in CAA56176. Ref.1

Secondary structure

1

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218

Helix Strand Turn

Details...

Beta strand

9 – 19

11

Helix

24 – 33

10

Beta strand

47 – 55

9

Beta strand

58 – 66

9

Helix

70 – 72

3

Helix

78 – 81

4

Beta strand

85 – 92

8

Helix

96 – 100

5

Helix

102 – 112

11

Beta strand

118 – 124

7

Helix

129 – 131

3

Helix

136 – 145

10

Beta strand

149 – 152

4

Turn

155 – 157

3

Helix

161 – 177

17

Sequences

	Sequence		Length	Mass (Da)
	Q15907 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 8DF146BA39EBD9FF	FASTA	218	24,489
	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 AFAEKNNLSF IETSALDSTN VEEAFKNILT EIYRIVSQKQ 190 200 210 IADRAAHDES PGNNVVDISV PPTTDGQKPN KLQCCQNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of two small GTP-binding proteins from human skeletal muscle." Zhu A.X., Zhao Y., Flier J.S. Biochem. Biophys. Res. Commun. 205:1875-1882(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle.
[2]	"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.
[3]	"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: Cerebellum.
[4]	"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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].
[7]	Bienvenut W.V. Submitted (MAR-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 34-51; 62-72; 83-95; 111-125 AND 167-174, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[8]	"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.
[9]	"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].
[10]	"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.
[11]	"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.
[12]	"The crystal structure of the small GTPase Rab11b reveals critical differences relative to the Rab11a isoform." Scapin S.M., Carneiro F.R., Alves A.C., Medrano F.J., Guimaraes B.G., Zanchin N.I. J. Struct. Biol. 154:260-268(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-205 IN COMPLEX WITH GTP ANALOG AND GDP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X79780 mRNA. Translation: CAA56176.1.
AF498947 mRNA. Translation: AAM21095.1.
AK312994 mRNA. Translation: BAG35831.1.
BT019536 mRNA. Translation: AAV38343.1.
CH471139 Genomic DNA. Translation: EAW68927.1.
BC110081 mRNA. Translation: AAI10082.1.

IPI

IPI00020436.

PIR

JC2487.

RefSeq

NP_004209.2. NM_004218.3.

UniGene

Hs.626404.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F9L	X-ray	1.55	A	8-205	[»]
2F9M	X-ray	1.95	A	8-205	[»]

ProteinModelPortal

Q15907.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15907. 5 interactions.

STRING

9606.ENSP00000333547.

PTM databases

PhosphoSite

Q15907.

Polymorphism databases

DMDM

38258938.

Proteomic databases

PaxDb

Q15907.

PeptideAtlas

Q15907.

PRIDE

Q15907.

Protocols and materials databases

DNASU

9230.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000328024; ENSP00000333547; ENSG00000185236.

GeneID

9230.

KEGG

hsa:9230.

UCSC

uc002mju.4. human.

Organism-specific databases

CTD

9230.

GeneCards

GC19P008455.

HGNC

HGNC:9761. RAB11B.

MIM

604198. gene.

neXtProt

NX_Q15907.

PharmGKB

PA34102.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

Q15907.

KO

K07905.

OMA

ERSAHDE.

OrthoDB

EOG4RR6J7.

PhylomeDB

Q15907.

Gene expression databases

Bgee

Q15907.

CleanEx

HS_RAB11B.

Genevestigator

Q15907.

GermOnline

ENSG00000185236. Homo sapiens.

Family and domain databases

InterPro

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]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAB11B. human.

EvolutionaryTrace

Q15907.

GenomeRNAi

9230.

NextBio

34597.

SOURCE

Search...

Entry information

Entry name

RB11B_HUMAN

Accession

Primary (citable) accession number: Q15907
Secondary accession number(s): B2R7I4 , D6W671, Q2YDT2, Q8NI07

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 131 of the entry and version 4 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.