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Q15907 (RB11B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-11B
Alternative name(s):
GTP-binding protein YPT3
Gene names
Name:RAB11B
Synonyms:YPT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 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 plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis. Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18

Subunit structure

Interacts with KCNMA1 By similarity. Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. May interact with TBC1D14. Interacts with ATP6V1E1. Ref.10 Ref.16 Ref.19

Subcellular location

Recycling endosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Lipid-anchor; Cytoplasmic side By similarity. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side Probable. Note: Recruited to phagosomes containing S.aureus. Ref.17

Induction

Up-regulated by extracellular acidosis and down-regulated by alkalosis (at protein level). Ref.16

Post-translational modification

Citrullinated by PADI4 By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell junction
Cytoplasmic vesicle
Endosome
Membrane
Synapse
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Citrullination
Lipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.21. Source: GOC

cellular response to acidity

Inferred from direct assay Ref.16. Source: UniProtKB

constitutive secretory pathway

Inferred from mutant phenotype Ref.11. Source: UniProtKB

insulin secretion involved in cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

receptor recycling

Inferred from sequence or structural similarity. Source: UniProtKB

regulated secretory pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of anion transport

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of endocytic recycling

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein localization to cell surface

Inferred from mutant phenotype Ref.16. Source: UniProtKB

retrograde transport, endosome to plasma membrane

Inferred from mutant phenotype Ref.13. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

transferrin transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

phagocytic vesicle

Inferred from direct assay Ref.17. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synaptic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGDP binding

Inferred from direct assay Ref.21. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.21. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.21. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TBC1D14Q9P2M42EBI-722234,EBI-2797718

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 215214Ras-related protein Rab-11B
PRO_0000121158
Propeptide216 – 2183Removed in mature form Potential
PRO_0000370815

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.9
Modified residue41Citrulline By similarity
Modified residue2151Cysteine methyl ester Potential
Lipidation2141S-geranylgeranyl cysteine Ref.20
Lipidation2151S-geranylgeranyl cysteine Ref.20

Experimental info

Mutagenesis251S → N: Dominant negative mutant locked in the inactive GDP-bound form; alters apical recycling. Ref.13
Mutagenesis701Q → L: Constitutively active mutant locked in the active GTP-bound form; alters apical recycling. Ref.13
Sequence conflict751A → R in CAA56176. Ref.1
Sequence conflict1161N → D in AAV38342. Ref.5
Sequence conflict1541S → A in CAG38733. Ref.6
Sequence conflict1841R → C in CAG46492. Ref.6
Sequence conflict2161Q → R in ABQ59034. Ref.2

Secondary structure

............................... 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15907 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 8DF146BA39EBD9FF

FASTA21824,489
        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 

« Hide

References

« Hide '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]Schupp I.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"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.
[4]"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].
Tissue: Cerebellum.
[5]"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].
[6]"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].
[7]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
[11]"Divergent functions of neuronal Rab11b in Ca2+-regulated versus constitutive exocytosis."
Khvotchev M.V., Ren M., Takamori S., Jahn R., Suedhof T.C.
J. Neurosci. 23:10531-10539(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EXOCYTOSIS.
[12]"Small GTPase determinants for the Golgi processing and plasmalemmal expression of human ether-a-go-go related (hERG) K+ channels."
Delisle B.P., Underkofler H.A., Moungey B.M., Slind J.K., Kilby J.A., Best J.M., Foell J.D., Balijepalli R.C., Kamp T.J., January C.T.
J. Biol. Chem. 284:2844-2853(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Rab11b regulates the apical recycling of the cystic fibrosis transmembrane conductance regulator in polarized intestinal epithelial cells."
Silvis M.R., Bertrand C.A., Ameen N., Golin-Bisello F., Butterworth M.B., Frizzell R.A., Bradbury N.A.
Mol. Biol. Cell 20:2337-2350(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APICAL RECYCLING, MUTAGENESIS OF SER-25 AND GLN-70.
[14]"Small GTPase Rab11b regulates degradation of surface membrane L-type Cav1.2 channels."
Best J.M., Foell J.D., Buss C.R., Delisle B.P., Balijepalli R.C., January C.T., Kamp T.J.
Am. J. Physiol. 300:C1023-C1033(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"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].
[16]"Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts."
Oehlke O., Martin H.W., Osterberg N., Roussa E.
J. Cell. Physiol. 226:638-651(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN V-ATPASE TRANSPORT, INTERACTION WITH ATP6V1E1, INDUCTION.
[17]"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.
[18]"Rab11b regulates the trafficking and recycling of the epithelial sodium channel (ENaC)."
Butterworth M.B., Edinger R.S., Silvis M.R., Gallo L.I., Liang X., Apodaca G., Frizzell R.A., Fizzell R.A., Johnson J.P.
Am. J. Physiol. 302:F581-F590(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"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.
[20]"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-214 AND CYS-215, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"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.
EF560724 mRNA. Translation: ABQ59034.1.
AF498947 mRNA. Translation: AAM21095.1.
AK312994 mRNA. Translation: BAG35831.1.
BT019535 mRNA. Translation: AAV38342.1.
BT019536 mRNA. Translation: AAV38343.1.
CR536494 mRNA. Translation: CAG38733.1.
CR541691 mRNA. Translation: CAG46492.1.
CH471139 Genomic DNA. Translation: EAW68927.1.
BC110081 mRNA. Translation: AAI10082.1.
CCDSCCDS12201.1.
PIRJC2487.
RefSeqNP_004209.2. NM_004218.3.
UniGeneHs.626404.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9LX-ray1.55A8-205[»]
2F9MX-ray1.95A8-205[»]
ProteinModelPortalQ15907.
SMRQ15907. Positions 8-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114661. 29 interactions.
DIPDIP-50898N.
IntActQ15907. 6 interactions.
STRING9606.ENSP00000333547.

PTM databases

PhosphoSiteQ15907.

Polymorphism databases

DMDM38258938.

Proteomic databases

MaxQBQ15907.
PaxDbQ15907.
PeptideAtlasQ15907.
PRIDEQ15907.

Protocols and materials databases

DNASU9230.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328024; ENSP00000333547; ENSG00000185236.
GeneID9230.
KEGGhsa:9230.
UCSCuc002mju.4. human.

Organism-specific databases

CTD9230.
GeneCardsGC19P008455.
HGNCHGNC:9761. RAB11B.
MIM604198. gene.
neXtProtNX_Q15907.
PharmGKBPA34102.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ15907.
KOK07905.
OMAIQVDAKT.
PhylomeDBQ15907.
TreeFamTF300099.

Gene expression databases

ArrayExpressQ15907.
BgeeQ15907.
CleanExHS_RAB11B.
GenevestigatorQ15907.

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

ChiTaRSRAB11B. human.
EvolutionaryTraceQ15907.
GeneWikiRAB11B.
GenomeRNAi9230.
NextBio34597.
PROQ15907.
SOURCESearch...

Entry information

Entry nameRB11B_HUMAN
AccessionPrimary (citable) accession number: Q15907
Secondary accession number(s): A5YM50 expand/collapse secondary AC list , B2R7I4, D6W671, Q2YDT2, Q5U0I1, Q6FHR0, Q6FI42, Q8NI07
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 144 of the entry and version 4 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 19

Human chromosome 19: entries, gene names and cross-references to MIM