Full text data of RAB11B
RAB11B
(YPT3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ras-related protein Rab-11B (GTP-binding protein YPT3; Flags: Precursor)
Ras-related protein Rab-11B (GTP-binding protein YPT3; Flags: Precursor)
UniProt
Q15907
ID RB11B_HUMAN Reviewed; 218 AA.
AC Q15907; A5YM50; B2R7I4; D6W671; Q2YDT2; Q5U0I1; Q6FHR0; Q6FI42;
read moreAC Q8NI07;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Ras-related protein Rab-11B;
DE AltName: Full=GTP-binding protein YPT3;
DE Flags: Precursor;
GN Name=RAB11B; Synonyms=YPT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=7811277; DOI=10.1006/bbrc.1994.2889;
RA Zhu A.X., Zhao Y., Flier J.S.;
RT "Molecular cloning of two small GTP-binding proteins from human
RT skeletal muscle.";
RL Biochem. Biophys. Res. Commun. 205:1875-1882(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Schupp I.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-13; 34-51; 62-72; 83-95; 111-125 AND 167-174,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [10]
RP INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
RX PubMed=11495908; DOI=10.1074/jbc.M104831200;
RA Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D.,
RA Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.;
RT "Identification and characterization of a family of Rab11-interacting
RT proteins.";
RL J. Biol. Chem. 276:39067-39075(2001).
RN [11]
RP FUNCTION IN EXOCYTOSIS.
RX PubMed=14627637;
RA Khvotchev M.V., Ren M., Takamori S., Jahn R., Suedhof T.C.;
RT "Divergent functions of neuronal Rab11b in Ca2+-regulated versus
RT constitutive exocytosis.";
RL J. Neurosci. 23:10531-10539(2003).
RN [12]
RP FUNCTION.
RX PubMed=19029296; DOI=10.1074/jbc.M807289200;
RA Delisle B.P., Underkofler H.A., Moungey B.M., Slind J.K., Kilby J.A.,
RA Best J.M., Foell J.D., Balijepalli R.C., Kamp T.J., January C.T.;
RT "Small GTPase determinants for the Golgi processing and plasmalemmal
RT expression of human ether-a-go-go related (hERG) K+ channels.";
RL J. Biol. Chem. 284:2844-2853(2009).
RN [13]
RP FUNCTION IN APICAL RECYCLING, AND MUTAGENESIS OF SER-25 AND GLN-70.
RX PubMed=19244346; DOI=10.1091/mbc.E08-01-0084;
RA Silvis M.R., Bertrand C.A., Ameen N., Golin-Bisello F.,
RA Butterworth M.B., Frizzell R.A., Bradbury N.A.;
RT "Rab11b regulates the apical recycling of the cystic fibrosis
RT transmembrane conductance regulator in polarized intestinal epithelial
RT cells.";
RL Mol. Biol. Cell 20:2337-2350(2009).
RN [14]
RP FUNCTION.
RX PubMed=21248079; DOI=10.1152/ajpcell.00288.2010;
RA Best J.M., Foell J.D., Buss C.R., Delisle B.P., Balijepalli R.C.,
RA January C.T., Kamp T.J.;
RT "Small GTPase Rab11b regulates degradation of surface membrane L-type
RT Cav1.2 channels.";
RL Am. J. Physiol. 300:C1023-C1033(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION IN V-ATPASE TRANSPORT, INTERACTION WITH ATP6V1E1, AND
RP INDUCTION.
RX PubMed=20717956; DOI=10.1002/jcp.22388;
RA Oehlke O., Martin H.W., Osterberg N., Roussa E.;
RT "Rab11b and its effector Rip11 regulate the acidosis-induced traffic
RT of V-ATPase in salivary ducts.";
RL J. Cell. Physiol. 226:638-651(2011).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially
RT recruited to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [18]
RP FUNCTION.
RX PubMed=22129970; DOI=10.1152/ajprenal.00304.2011;
RA Butterworth M.B., Edinger R.S., Silvis M.R., Gallo L.I., Liang X.,
RA Apodaca G., Frizzell R.A., Fizzell R.A., Johnson J.P.;
RT "Rab11b regulates the trafficking and recycling of the epithelial
RT sodium channel (ENaC).";
RL Am. J. Physiol. 302:F581-F590(2012).
RN [19]
RP INTERACTION WITH TBC1D14.
RX PubMed=22613832; DOI=10.1083/jcb.201111079;
RA Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.;
RT "TBC1D14 regulates autophagosome formation via Rab11- and ULK1-
RT positive recycling endosomes.";
RL J. Cell Biol. 197:659-675(2012).
RN [20]
RP ISOPRENYLATION AT CYS-214 AND CYS-215, AND MASS SPECTROMETRY.
RX PubMed=24023390; DOI=10.1074/mcp.M113.030114;
RA Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T.,
RA Tran J.C., Thomas P.M., Kelleher N.L.;
RT "Large-scale top down proteomics of the human proteome: membrane
RT proteins, mitochondria, and senescence.";
RL Mol. Cell. Proteomics 0:0-0(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-205 IN COMPLEX WITH GTP
RP ANALOG AND GDP.
RX PubMed=16545962; DOI=10.1016/j.jsb.2006.01.007;
RA Scapin S.M., Carneiro F.R., Alves A.C., Medrano F.J., Guimaraes B.G.,
RA Zanchin N.I.;
RT "The crystal structure of the small GTPase Rab11b reveals critical
RT differences relative to the Rab11a isoform.";
RL J. Struct. Biol. 154:260-268(2006).
CC -!- FUNCTION: The small GTPases Rab are key regulators of
CC intracellular membrane trafficking, from the formation of
CC transport vesicles to their fusion with membranes. Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different set of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab plays a role in endocytic
CC recycling, regulating apical recycling of several transmembrane
CC proteins including cystic fibrosis transmembrane conductance
CC regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-
CC gated channel, and voltage-dependent L-type calcium channel. May
CC also regulate constitutive and regulated secretion, like insulin
CC granule exocytosis. Required for melanosome transport and release
CC from melanocytes. Also regulates V-ATPase intracellular transport
CC in response to extracellular acidosis.
CC -!- SUBUNIT: Interacts with KCNMA1 (By similarity). Interacts with
CC RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. May interact with
CC TBC1D14. Interacts with ATP6V1E1.
CC -!- INTERACTION:
CC Q9P2M4:TBC1D14; NbExp=2; IntAct=EBI-722234, EBI-2797718;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor;
CC Cytoplasmic side (By similarity). Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane; Lipid-anchor; Cytoplasmic side
CC (By similarity). Cytoplasmic vesicle, phagosome membrane; Lipid-
CC anchor; Cytoplasmic side (Probable). Note=Recruited to phagosomes
CC containing S.aureus.
CC -!- INDUCTION: Up-regulated by extracellular acidosis and down-
CC regulated by alkalosis (at protein level).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; X79780; CAA56176.1; -; mRNA.
DR EMBL; EF560724; ABQ59034.1; -; mRNA.
DR EMBL; AF498947; AAM21095.1; -; mRNA.
DR EMBL; AK312994; BAG35831.1; -; mRNA.
DR EMBL; BT019535; AAV38342.1; -; mRNA.
DR EMBL; BT019536; AAV38343.1; -; mRNA.
DR EMBL; CR536494; CAG38733.1; -; mRNA.
DR EMBL; CR541691; CAG46492.1; -; mRNA.
DR EMBL; CH471139; EAW68927.1; -; Genomic_DNA.
DR EMBL; BC110081; AAI10082.1; -; mRNA.
DR PIR; JC2487; JC2487.
DR RefSeq; NP_004209.2; NM_004218.3.
DR UniGene; Hs.626404; -.
DR PDB; 2F9L; X-ray; 1.55 A; A=8-205.
DR PDB; 2F9M; X-ray; 1.95 A; A=8-205.
DR PDBsum; 2F9L; -.
DR PDBsum; 2F9M; -.
DR ProteinModelPortal; Q15907; -.
DR SMR; Q15907; 8-188.
DR IntAct; Q15907; 6.
DR STRING; 9606.ENSP00000333547; -.
DR PhosphoSite; Q15907; -.
DR DMDM; 38258938; -.
DR PaxDb; Q15907; -.
DR PeptideAtlas; Q15907; -.
DR PRIDE; Q15907; -.
DR DNASU; 9230; -.
DR Ensembl; ENST00000328024; ENSP00000333547; ENSG00000185236.
DR GeneID; 9230; -.
DR KEGG; hsa:9230; -.
DR UCSC; uc002mju.4; human.
DR CTD; 9230; -.
DR GeneCards; GC19P008455; -.
DR HGNC; HGNC:9761; RAB11B.
DR MIM; 604198; gene.
DR neXtProt; NX_Q15907; -.
DR PharmGKB; PA34102; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q15907; -.
DR KO; K07905; -.
DR OMA; IQVDAKT; -.
DR PhylomeDB; Q15907; -.
DR ChiTaRS; RAB11B; human.
DR EvolutionaryTrace; Q15907; -.
DR GeneWiki; RAB11B; -.
DR GenomeRNAi; 9230; -.
DR NextBio; 34597; -.
DR PRO; PR:Q15907; -.
DR ArrayExpress; Q15907; -.
DR Bgee; Q15907; -.
DR CleanEx; HS_RAB11B; -.
DR Genevestigator; Q15907; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0071468; P:cellular response to acidity; IDA:UniProtKB.
DR GO; GO:0045054; P:constitutive secretory pathway; IMP:UniProtKB.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated secretory pathway; ISS:UniProtKB.
DR GO; GO:0044070; P:regulation of anion transport; IMP:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:1990126; P:retrograde transport, endosome to plasma membrane; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0033572; P:transferrin transport; ISS:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Complete proteome;
KW Cytoplasmic vesicle; Direct protein sequencing; Endosome; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Synapse; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Ras-related protein Rab-11B.
FT /FTId=PRO_0000121158.
FT PROPEP 216 218 Removed in mature form (Potential).
FT /FTId=PRO_0000370815.
FT NP_BIND 18 26 GTP.
FT NP_BIND 66 70 GTP.
FT NP_BIND 124 127 GTP.
FT NP_BIND 154 156 GTP.
FT MOTIF 40 48 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylglycine.
FT MOD_RES 215 215 Cysteine methyl ester (Potential).
FT LIPID 214 214 S-geranylgeranyl cysteine.
FT LIPID 215 215 S-geranylgeranyl cysteine.
FT MUTAGEN 25 25 S->N: Dominant negative mutant locked in
FT the inactive GDP-bound form; alters
FT apical recycling.
FT MUTAGEN 70 70 Q->L: Constitutively active mutant locked
FT in the active GTP-bound form; alters
FT apical recycling.
FT CONFLICT 75 75 A -> R (in Ref. 1; CAA56176).
FT CONFLICT 116 116 N -> D (in Ref. 5; AAV38342).
FT CONFLICT 154 154 S -> A (in Ref. 6; CAG38733).
FT CONFLICT 184 184 R -> C (in Ref. 6; CAG46492).
FT CONFLICT 216 216 Q -> R (in Ref. 2; ABQ59034).
FT STRAND 9 19
FT HELIX 24 33
FT STRAND 47 55
FT STRAND 58 66
FT HELIX 70 72
FT HELIX 78 81
FT STRAND 85 92
FT HELIX 96 100
FT HELIX 102 112
FT STRAND 118 124
FT HELIX 129 131
FT HELIX 136 145
FT STRAND 149 152
FT TURN 155 157
FT HELIX 161 177
SQ SEQUENCE 218 AA; 24489 MW; 8DF146BA39EBD9FF CRC64;
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM
LVGNKSDLRH LRAVPTDEAR AFAEKNNLSF IETSALDSTN VEEAFKNILT EIYRIVSQKQ
IADRAAHDES PGNNVVDISV PPTTDGQKPN KLQCCQNL
//
ID RB11B_HUMAN Reviewed; 218 AA.
AC Q15907; A5YM50; B2R7I4; D6W671; Q2YDT2; Q5U0I1; Q6FHR0; Q6FI42;
read moreAC Q8NI07;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Ras-related protein Rab-11B;
DE AltName: Full=GTP-binding protein YPT3;
DE Flags: Precursor;
GN Name=RAB11B; Synonyms=YPT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=7811277; DOI=10.1006/bbrc.1994.2889;
RA Zhu A.X., Zhao Y., Flier J.S.;
RT "Molecular cloning of two small GTP-binding proteins from human
RT skeletal muscle.";
RL Biochem. Biophys. Res. Commun. 205:1875-1882(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Schupp I.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-13; 34-51; 62-72; 83-95; 111-125 AND 167-174,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [10]
RP INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
RX PubMed=11495908; DOI=10.1074/jbc.M104831200;
RA Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D.,
RA Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.;
RT "Identification and characterization of a family of Rab11-interacting
RT proteins.";
RL J. Biol. Chem. 276:39067-39075(2001).
RN [11]
RP FUNCTION IN EXOCYTOSIS.
RX PubMed=14627637;
RA Khvotchev M.V., Ren M., Takamori S., Jahn R., Suedhof T.C.;
RT "Divergent functions of neuronal Rab11b in Ca2+-regulated versus
RT constitutive exocytosis.";
RL J. Neurosci. 23:10531-10539(2003).
RN [12]
RP FUNCTION.
RX PubMed=19029296; DOI=10.1074/jbc.M807289200;
RA Delisle B.P., Underkofler H.A., Moungey B.M., Slind J.K., Kilby J.A.,
RA Best J.M., Foell J.D., Balijepalli R.C., Kamp T.J., January C.T.;
RT "Small GTPase determinants for the Golgi processing and plasmalemmal
RT expression of human ether-a-go-go related (hERG) K+ channels.";
RL J. Biol. Chem. 284:2844-2853(2009).
RN [13]
RP FUNCTION IN APICAL RECYCLING, AND MUTAGENESIS OF SER-25 AND GLN-70.
RX PubMed=19244346; DOI=10.1091/mbc.E08-01-0084;
RA Silvis M.R., Bertrand C.A., Ameen N., Golin-Bisello F.,
RA Butterworth M.B., Frizzell R.A., Bradbury N.A.;
RT "Rab11b regulates the apical recycling of the cystic fibrosis
RT transmembrane conductance regulator in polarized intestinal epithelial
RT cells.";
RL Mol. Biol. Cell 20:2337-2350(2009).
RN [14]
RP FUNCTION.
RX PubMed=21248079; DOI=10.1152/ajpcell.00288.2010;
RA Best J.M., Foell J.D., Buss C.R., Delisle B.P., Balijepalli R.C.,
RA January C.T., Kamp T.J.;
RT "Small GTPase Rab11b regulates degradation of surface membrane L-type
RT Cav1.2 channels.";
RL Am. J. Physiol. 300:C1023-C1033(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION IN V-ATPASE TRANSPORT, INTERACTION WITH ATP6V1E1, AND
RP INDUCTION.
RX PubMed=20717956; DOI=10.1002/jcp.22388;
RA Oehlke O., Martin H.W., Osterberg N., Roussa E.;
RT "Rab11b and its effector Rip11 regulate the acidosis-induced traffic
RT of V-ATPase in salivary ducts.";
RL J. Cell. Physiol. 226:638-651(2011).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially
RT recruited to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [18]
RP FUNCTION.
RX PubMed=22129970; DOI=10.1152/ajprenal.00304.2011;
RA Butterworth M.B., Edinger R.S., Silvis M.R., Gallo L.I., Liang X.,
RA Apodaca G., Frizzell R.A., Fizzell R.A., Johnson J.P.;
RT "Rab11b regulates the trafficking and recycling of the epithelial
RT sodium channel (ENaC).";
RL Am. J. Physiol. 302:F581-F590(2012).
RN [19]
RP INTERACTION WITH TBC1D14.
RX PubMed=22613832; DOI=10.1083/jcb.201111079;
RA Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.;
RT "TBC1D14 regulates autophagosome formation via Rab11- and ULK1-
RT positive recycling endosomes.";
RL J. Cell Biol. 197:659-675(2012).
RN [20]
RP ISOPRENYLATION AT CYS-214 AND CYS-215, AND MASS SPECTROMETRY.
RX PubMed=24023390; DOI=10.1074/mcp.M113.030114;
RA Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T.,
RA Tran J.C., Thomas P.M., Kelleher N.L.;
RT "Large-scale top down proteomics of the human proteome: membrane
RT proteins, mitochondria, and senescence.";
RL Mol. Cell. Proteomics 0:0-0(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-205 IN COMPLEX WITH GTP
RP ANALOG AND GDP.
RX PubMed=16545962; DOI=10.1016/j.jsb.2006.01.007;
RA Scapin S.M., Carneiro F.R., Alves A.C., Medrano F.J., Guimaraes B.G.,
RA Zanchin N.I.;
RT "The crystal structure of the small GTPase Rab11b reveals critical
RT differences relative to the Rab11a isoform.";
RL J. Struct. Biol. 154:260-268(2006).
CC -!- FUNCTION: The small GTPases Rab are key regulators of
CC intracellular membrane trafficking, from the formation of
CC transport vesicles to their fusion with membranes. Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different set of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab plays a role in endocytic
CC recycling, regulating apical recycling of several transmembrane
CC proteins including cystic fibrosis transmembrane conductance
CC regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-
CC gated channel, and voltage-dependent L-type calcium channel. May
CC also regulate constitutive and regulated secretion, like insulin
CC granule exocytosis. Required for melanosome transport and release
CC from melanocytes. Also regulates V-ATPase intracellular transport
CC in response to extracellular acidosis.
CC -!- SUBUNIT: Interacts with KCNMA1 (By similarity). Interacts with
CC RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. May interact with
CC TBC1D14. Interacts with ATP6V1E1.
CC -!- INTERACTION:
CC Q9P2M4:TBC1D14; NbExp=2; IntAct=EBI-722234, EBI-2797718;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor;
CC Cytoplasmic side (By similarity). Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane; Lipid-anchor; Cytoplasmic side
CC (By similarity). Cytoplasmic vesicle, phagosome membrane; Lipid-
CC anchor; Cytoplasmic side (Probable). Note=Recruited to phagosomes
CC containing S.aureus.
CC -!- INDUCTION: Up-regulated by extracellular acidosis and down-
CC regulated by alkalosis (at protein level).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; X79780; CAA56176.1; -; mRNA.
DR EMBL; EF560724; ABQ59034.1; -; mRNA.
DR EMBL; AF498947; AAM21095.1; -; mRNA.
DR EMBL; AK312994; BAG35831.1; -; mRNA.
DR EMBL; BT019535; AAV38342.1; -; mRNA.
DR EMBL; BT019536; AAV38343.1; -; mRNA.
DR EMBL; CR536494; CAG38733.1; -; mRNA.
DR EMBL; CR541691; CAG46492.1; -; mRNA.
DR EMBL; CH471139; EAW68927.1; -; Genomic_DNA.
DR EMBL; BC110081; AAI10082.1; -; mRNA.
DR PIR; JC2487; JC2487.
DR RefSeq; NP_004209.2; NM_004218.3.
DR UniGene; Hs.626404; -.
DR PDB; 2F9L; X-ray; 1.55 A; A=8-205.
DR PDB; 2F9M; X-ray; 1.95 A; A=8-205.
DR PDBsum; 2F9L; -.
DR PDBsum; 2F9M; -.
DR ProteinModelPortal; Q15907; -.
DR SMR; Q15907; 8-188.
DR IntAct; Q15907; 6.
DR STRING; 9606.ENSP00000333547; -.
DR PhosphoSite; Q15907; -.
DR DMDM; 38258938; -.
DR PaxDb; Q15907; -.
DR PeptideAtlas; Q15907; -.
DR PRIDE; Q15907; -.
DR DNASU; 9230; -.
DR Ensembl; ENST00000328024; ENSP00000333547; ENSG00000185236.
DR GeneID; 9230; -.
DR KEGG; hsa:9230; -.
DR UCSC; uc002mju.4; human.
DR CTD; 9230; -.
DR GeneCards; GC19P008455; -.
DR HGNC; HGNC:9761; RAB11B.
DR MIM; 604198; gene.
DR neXtProt; NX_Q15907; -.
DR PharmGKB; PA34102; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q15907; -.
DR KO; K07905; -.
DR OMA; IQVDAKT; -.
DR PhylomeDB; Q15907; -.
DR ChiTaRS; RAB11B; human.
DR EvolutionaryTrace; Q15907; -.
DR GeneWiki; RAB11B; -.
DR GenomeRNAi; 9230; -.
DR NextBio; 34597; -.
DR PRO; PR:Q15907; -.
DR ArrayExpress; Q15907; -.
DR Bgee; Q15907; -.
DR CleanEx; HS_RAB11B; -.
DR Genevestigator; Q15907; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0071468; P:cellular response to acidity; IDA:UniProtKB.
DR GO; GO:0045054; P:constitutive secretory pathway; IMP:UniProtKB.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated secretory pathway; ISS:UniProtKB.
DR GO; GO:0044070; P:regulation of anion transport; IMP:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:1990126; P:retrograde transport, endosome to plasma membrane; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0033572; P:transferrin transport; ISS:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Complete proteome;
KW Cytoplasmic vesicle; Direct protein sequencing; Endosome; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Synapse; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Ras-related protein Rab-11B.
FT /FTId=PRO_0000121158.
FT PROPEP 216 218 Removed in mature form (Potential).
FT /FTId=PRO_0000370815.
FT NP_BIND 18 26 GTP.
FT NP_BIND 66 70 GTP.
FT NP_BIND 124 127 GTP.
FT NP_BIND 154 156 GTP.
FT MOTIF 40 48 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylglycine.
FT MOD_RES 215 215 Cysteine methyl ester (Potential).
FT LIPID 214 214 S-geranylgeranyl cysteine.
FT LIPID 215 215 S-geranylgeranyl cysteine.
FT MUTAGEN 25 25 S->N: Dominant negative mutant locked in
FT the inactive GDP-bound form; alters
FT apical recycling.
FT MUTAGEN 70 70 Q->L: Constitutively active mutant locked
FT in the active GTP-bound form; alters
FT apical recycling.
FT CONFLICT 75 75 A -> R (in Ref. 1; CAA56176).
FT CONFLICT 116 116 N -> D (in Ref. 5; AAV38342).
FT CONFLICT 154 154 S -> A (in Ref. 6; CAG38733).
FT CONFLICT 184 184 R -> C (in Ref. 6; CAG46492).
FT CONFLICT 216 216 Q -> R (in Ref. 2; ABQ59034).
FT STRAND 9 19
FT HELIX 24 33
FT STRAND 47 55
FT STRAND 58 66
FT HELIX 70 72
FT HELIX 78 81
FT STRAND 85 92
FT HELIX 96 100
FT HELIX 102 112
FT STRAND 118 124
FT HELIX 129 131
FT HELIX 136 145
FT STRAND 149 152
FT TURN 155 157
FT HELIX 161 177
SQ SEQUENCE 218 AA; 24489 MW; 8DF146BA39EBD9FF CRC64;
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM
LVGNKSDLRH LRAVPTDEAR AFAEKNNLSF IETSALDSTN VEEAFKNILT EIYRIVSQKQ
IADRAAHDES PGNNVVDISV PPTTDGQKPN KLQCCQNL
//
MIM
604198
*RECORD*
*FIELD* NO
604198
*FIELD* TI
*604198 RAS-ASSOCIATED PROTEIN RAB11B; RAB11B
*FIELD* TX
DESCRIPTION
The Ras superfamily of small GTP-binding proteins, which includes the
read moreRas (see 190020), Ral (see 179550), Rho (see 165390), Rap (see 179520),
and Rab (see 179508) families, is involved in controlling a diverse set
of essential cellular functions. The Rab family, including RAB11B,
appears to play a critical role in regulating exocytotic and endocytotic
pathways (summary by Zhu et al., 1994).
CLONING
By PCR using degenerate oligonucleotides based on the RAB3D (604350)
amino acid sequence, followed by screening of a human fetal skeletal
muscle cDNA library with the PCR product, Zhu et al. (1994) isolated
cDNAs encoding RAB11B, which they called YPT3, and RAB35 (604199). The
deduced 218-amino acid RAB11B protein is similar to yeast Ypt3, 99%
identical to mouse Ypt3, and 91% identical to human RAB11A (605570).
RAB11B contains the 4 conserved domains important for GTP binding. The C
terminus sequence of RAB11B is similar to that of RAB11A; in Rab
proteins, this region is thought to be involved in membrane association.
Recombinant RAB11B expressed in bacteria had GTP-binding activity.
Northern blot analysis detected a 1.3-kb RAB11B transcript in all human
tissues examined.
*FIELD* RF
1. Zhu, A. X.; Zhao, Y.; Flier, J. S.: Molecular cloning of two small
GTP-binding proteins from human skeletal muscle. Biochem. Biophys.
Res. Commun. 205: 1875-1882, 1994.
*FIELD* CD
Patti M. Sherman: 9/29/1999
*FIELD* ED
wwang: 11/24/2010
carol: 3/14/2006
mgross: 1/22/2001
alopez: 12/13/1999
mgross: 9/29/1999
psherman: 9/29/1999
*RECORD*
*FIELD* NO
604198
*FIELD* TI
*604198 RAS-ASSOCIATED PROTEIN RAB11B; RAB11B
*FIELD* TX
DESCRIPTION
The Ras superfamily of small GTP-binding proteins, which includes the
read moreRas (see 190020), Ral (see 179550), Rho (see 165390), Rap (see 179520),
and Rab (see 179508) families, is involved in controlling a diverse set
of essential cellular functions. The Rab family, including RAB11B,
appears to play a critical role in regulating exocytotic and endocytotic
pathways (summary by Zhu et al., 1994).
CLONING
By PCR using degenerate oligonucleotides based on the RAB3D (604350)
amino acid sequence, followed by screening of a human fetal skeletal
muscle cDNA library with the PCR product, Zhu et al. (1994) isolated
cDNAs encoding RAB11B, which they called YPT3, and RAB35 (604199). The
deduced 218-amino acid RAB11B protein is similar to yeast Ypt3, 99%
identical to mouse Ypt3, and 91% identical to human RAB11A (605570).
RAB11B contains the 4 conserved domains important for GTP binding. The C
terminus sequence of RAB11B is similar to that of RAB11A; in Rab
proteins, this region is thought to be involved in membrane association.
Recombinant RAB11B expressed in bacteria had GTP-binding activity.
Northern blot analysis detected a 1.3-kb RAB11B transcript in all human
tissues examined.
*FIELD* RF
1. Zhu, A. X.; Zhao, Y.; Flier, J. S.: Molecular cloning of two small
GTP-binding proteins from human skeletal muscle. Biochem. Biophys.
Res. Commun. 205: 1875-1882, 1994.
*FIELD* CD
Patti M. Sherman: 9/29/1999
*FIELD* ED
wwang: 11/24/2010
carol: 3/14/2006
mgross: 1/22/2001
alopez: 12/13/1999
mgross: 9/29/1999
psherman: 9/29/1999