Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ras-related protein Rab-11B

Gene

RAB11B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269GTP
Nucleotide bindingi66 – 705GTP
Nucleotide bindingi124 – 1274GTP
Nucleotide bindingi154 – 1563GTP

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • myosin V binding Source: UniProtKB

GO - Biological processi

  • cellular response to acidic pH Source: UniProtKB
  • constitutive secretory pathway Source: UniProtKB
  • establishment of protein localization to membrane Source: UniProtKB
  • insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • intracellular protein transport Source: GO_Central
  • melanosome transport Source: UniProtKB
  • Rab protein signal transduction Source: GO_Central
  • receptor recycling Source: UniProtKB
  • regulated secretory pathway Source: UniProtKB
  • regulation of anion transport Source: UniProtKB
  • regulation of endocytic recycling Source: UniProtKB
  • regulation of protein localization to cell surface Source: UniProtKB
  • retrograde transport, endosome to plasma membrane Source: UniProtKB
  • transferrin transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-11B
Alternative name(s):
GTP-binding protein YPT3
Gene namesi
Name:RAB11B
Synonyms:YPT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9761. RAB11B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Endosome, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251S → N: Dominant negative mutant locked in the inactive GDP-bound form; alters apical recycling. 1 Publication
Mutagenesisi70 – 701Q → L: Constitutively active mutant locked in the active GTP-bound form; alters apical recycling. 1 Publication

Organism-specific databases

PharmGKBiPA34102.

Polymorphism and mutation databases

BioMutaiRAB11B.
DMDMi38258938.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 215214Ras-related protein Rab-11BPRO_0000121158Add
BLAST
Propeptidei216 – 2183Removed in mature formSequence AnalysisPRO_0000370815

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Modified residuei4 – 41CitrullineBy similarity
Lipidationi214 – 2141S-geranylgeranyl cysteine1 Publication
Modified residuei215 – 2151Cysteine methyl esterSequence Analysis
Lipidationi215 – 2151S-geranylgeranyl cysteine1 Publication

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ15907.
PaxDbiQ15907.
PeptideAtlasiQ15907.
PRIDEiQ15907.

PTM databases

PhosphoSiteiQ15907.

Expressioni

Inductioni

Up-regulated by extracellular acidosis and down-regulated by alkalosis (at protein level).1 Publication

Gene expression databases

BgeeiQ15907.
CleanExiHS_RAB11B.
ExpressionAtlasiQ15907. baseline and differential.
GenevisibleiQ15907. HS.

Interactioni

Subunit structurei

Interacts with KCNMA1 (By similarity). Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. May interact with TBC1D14. Interacts with ATP6V1E1.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TBC1D14Q9P2M42EBI-722234,EBI-2797718

Protein-protein interaction databases

BioGridi114661. 52 interactions.
DIPiDIP-50898N.
IntActiQ15907. 6 interactions.
STRINGi9606.ENSP00000333547.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 1911Combined sources
Helixi24 – 3310Combined sources
Beta strandi47 – 559Combined sources
Beta strandi58 – 669Combined sources
Helixi70 – 723Combined sources
Helixi74 – 763Combined sources
Helixi78 – 814Combined sources
Beta strandi85 – 928Combined sources
Helixi96 – 1005Combined sources
Helixi102 – 11211Combined sources
Beta strandi118 – 1247Combined sources
Helixi129 – 1313Combined sources
Helixi136 – 14510Combined sources
Beta strandi149 – 1524Combined sources
Turni155 – 1573Combined sources
Helixi161 – 17717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9LX-ray1.55A8-205[»]
2F9MX-ray1.95A8-205[»]
4OJKX-ray2.66A/B8-205[»]
ProteinModelPortaliQ15907.
SMRiQ15907. Positions 8-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15907.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi40 – 489Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ15907.
KOiK07905.
OMAiETKQGCC.
PhylomeDBiQ15907.
TreeFamiTF300099.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15907-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT
60 70 80 90 100
RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE
110 120 130 140 150
NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNNLSF
160 170 180 190 200
IETSALDSTN VEEAFKNILT EIYRIVSQKQ IADRAAHDES PGNNVVDISV
210
PPTTDGQKPN KLQCCQNL
Length:218
Mass (Da):24,489
Last modified:January 23, 2007 - v4
Checksum:i8DF146BA39EBD9FF
GO
Isoform 2 (identifier: Q15907-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     171-218: EIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL → GGRGPDGCG

Note: No experimental confirmation available.
Show »
Length:179
Mass (Da):19,971
Checksum:i9D14388D83279277
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751A → R in CAA56176 (PubMed:7811277).Curated
Sequence conflicti116 – 1161N → D in AAV38342 (Ref. 5) Curated
Sequence conflicti154 – 1541S → A in CAG38733 (Ref. 6) Curated
Sequence conflicti184 – 1841R → C in CAG46492 (Ref. 6) Curated
Sequence conflicti216 – 2161Q → R in ABQ59034 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei171 – 21848EIYRI…CCQNL → GGRGPDGCG in isoform 2. 1 PublicationVSP_055832Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79780 mRNA. Translation: CAA56176.1.
EF560724 mRNA. Translation: ABQ59034.1.
AF498947 mRNA. Translation: AAM21095.1.
AK297498 mRNA. Translation: BAG59912.1.
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.
AC136469 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68927.1.
BC110081 mRNA. Translation: AAI10082.1.
CCDSiCCDS12201.1. [Q15907-1]
PIRiJC2487.
RefSeqiNP_004209.2. NM_004218.3. [Q15907-1]
UniGeneiHs.626404.

Genome annotation databases

EnsembliENST00000328024; ENSP00000333547; ENSG00000185236.
ENST00000594216; ENSP00000471148; ENSG00000185236. [Q15907-2]
GeneIDi9230.
KEGGihsa:9230.
UCSCiuc002mju.4. human. [Q15907-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79780 mRNA. Translation: CAA56176.1.
EF560724 mRNA. Translation: ABQ59034.1.
AF498947 mRNA. Translation: AAM21095.1.
AK297498 mRNA. Translation: BAG59912.1.
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.
AC136469 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68927.1.
BC110081 mRNA. Translation: AAI10082.1.
CCDSiCCDS12201.1. [Q15907-1]
PIRiJC2487.
RefSeqiNP_004209.2. NM_004218.3. [Q15907-1]
UniGeneiHs.626404.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9LX-ray1.55A8-205[»]
2F9MX-ray1.95A8-205[»]
4OJKX-ray2.66A/B8-205[»]
ProteinModelPortaliQ15907.
SMRiQ15907. Positions 8-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114661. 52 interactions.
DIPiDIP-50898N.
IntActiQ15907. 6 interactions.
STRINGi9606.ENSP00000333547.

PTM databases

PhosphoSiteiQ15907.

Polymorphism and mutation databases

BioMutaiRAB11B.
DMDMi38258938.

Proteomic databases

MaxQBiQ15907.
PaxDbiQ15907.
PeptideAtlasiQ15907.
PRIDEiQ15907.

Protocols and materials databases

DNASUi9230.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328024; ENSP00000333547; ENSG00000185236.
ENST00000594216; ENSP00000471148; ENSG00000185236. [Q15907-2]
GeneIDi9230.
KEGGihsa:9230.
UCSCiuc002mju.4. human. [Q15907-1]

Organism-specific databases

CTDi9230.
GeneCardsiGC19P008455.
HGNCiHGNC:9761. RAB11B.
MIMi604198. gene.
neXtProtiNX_Q15907.
PharmGKBiPA34102.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ15907.
KOiK07905.
OMAiETKQGCC.
PhylomeDBiQ15907.
TreeFamiTF300099.

Miscellaneous databases

ChiTaRSiRAB11B. human.
EvolutionaryTraceiQ15907.
GeneWikiiRAB11B.
GenomeRNAii9230.
NextBioi34597.
PROiQ15907.
SOURCEiSearch...

Gene expression databases

BgeeiQ15907.
CleanExiHS_RAB11B.
ExpressionAtlasiQ15907. baseline and differential.
GenevisibleiQ15907. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    Tissue: Muscle.
  2. Schupp I.
    Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
    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.
    , 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 and 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] (ISOFORM 1).
  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] (ISOFORM 1).
  7. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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] (ISOFORM 1).
  10. 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.
  11. Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.

Entry informationi

Entry nameiRB11B_HUMAN
AccessioniPrimary (citable) accession number: Q15907
Secondary accession number(s): A5YM50
, B2R7I4, B4DMK0, D6W671, Q2YDT2, Q5U0I1, Q6FHR0, Q6FI42, Q8NI07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 156 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.