RB11B_HUMAN
ID RB11B_HUMAN Reviewed; 218 AA.
AC Q15907; A5YM50; B2R7I4; B4DMK0; D6W671; Q2YDT2; Q5U0I1; Q6FHR0; Q6FI42;
AC Q8NI07;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Ras-related protein Rab-11B;
DE EC=3.6.5.2 {ECO:0000269|PubMed:16545962};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 skeletal
RT muscle.";
RL Biochem. Biophys. Res. Commun. 205:1875-1882(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Schupp I.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT 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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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] (ISOFORM 1).
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 vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
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 IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [11]
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., Kumar R.,
RA 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 [12]
RP FUNCTION IN EXOCYTOSIS.
RX PubMed=14627637; DOI=10.1523/jneurosci.23-33-10531.2003;
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 [13]
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 [14]
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., Butterworth M.B.,
RA Frizzell R.A., Bradbury N.A.;
RT "Rab11b regulates the apical recycling of the cystic fibrosis transmembrane
RT conductance regulator in polarized intestinal epithelial cells.";
RL Mol. Biol. Cell 20:2337-2350(2009).
RN [15]
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 [16]
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., Buerckstuemmer T.,
RA 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 [17]
RP FUNCTION IN V-ATPASE TRANSPORT, INTERACTION WITH ATP6V1E1, AND 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 of V-
RT ATPase in salivary ducts.";
RL J. Cell. Physiol. 226:638-651(2011).
RN [18]
RP INTERACTION WITH ZFYVE27 AND KIF5A, AND MUTAGENESIS OF GLN-70.
RX PubMed=21976701; DOI=10.1091/mbc.e11-01-0068;
RA Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.;
RT "Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes
RT in vesicular transport during process formation.";
RL Mol. Biol. Cell 22:4602-4620(2011).
RN [19]
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 recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [20]
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 sodium
RT channel (ENaC).";
RL Am. J. Physiol. 302:F581-F590(2012).
RN [21]
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-positive
RT recycling endosomes.";
RL J. Cell Biol. 197:659-675(2012).
RN [22]
RP INTERACTION WITH PI4KB.
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
RN [23]
RP ISOPRENYLATION AT CYS-214 AND CYS-215, AND IDENTIFICATION BY MASS
RP 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 proteins,
RT mitochondria, and senescence.";
RL Mol. Cell. Proteomics 12:3465-3473(2013).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [25]
RP INVOLVEMENT IN NDAGSCW, AND VARIANTS NDAGSCW MET-22 AND THR-68.
RX PubMed=29106825; DOI=10.1016/j.ajhg.2017.09.015;
RG DDD Study;
RA Lamers I.J.C., Reijnders M.R.F., Venselaar H., Kraus A., Jansen S.,
RA de Vries B.B.A., Houge G., Gradek G.A., Seo J., Choi M., Chae J.H.,
RA van der Burgt I., Pfundt R., Letteboer S.J.F., van Beersum S.E.C.,
RA Dusseljee S., Brunner H.G., Doherty D., Kleefstra T., Roepman R.;
RT "Recurrent de novo mutations disturbing the GTP/GDP binding pocket of
RT RAB11B cause intellectual disability and a distinctive brain phenotype.";
RL Am. J. Hum. Genet. 101:824-832(2017).
RN [26]
RP INTERACTION WITH TBC1D8B.
RX PubMed=30661770; DOI=10.1016/j.ajhg.2018.12.016;
RA Dorval G., Kuzmuk V., Gribouval O., Welsh G.I., Bierzynska A., Schmitt A.,
RA Miserey-Lenkei S., Koziell A., Haq S., Benmerah A., Mollet G., Boyer O.,
RA Saleem M.A., Antignac C.;
RT "TBC1D8B Loss-of-Function Mutations Lead to X-Linked Nephrotic Syndrome via
RT Defective Trafficking Pathways.";
RL Am. J. Hum. Genet. 104:348-355(2019).
RN [27]
RP GLYCOSYLATION (MICROBIAL INFECTION).
RX PubMed=32974215; DOI=10.3389/fcimb.2020.00419;
RA Gan J., Scott N.E., Newson J.P.M., Wibawa R.R., Wong Fok Lung T.,
RA Pollock G.L., Ng G.Z., van Driel I., Pearson J.S., Hartland E.L.,
RA Giogha C.;
RT "The Salmonella effector SseK3 targets small Rab GTPases.";
RL Front. Cell. Infect. Microbiol. 10:419-419(2020).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-205 IN COMPLEX WITH GTP ANALOG
RP AND GDP, GTP-BINDING, AND CATALYTIC ACTIVITY.
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 intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. The small Rab GTPase RAB11B
CC plays a role in endocytic recycling, regulating apical recycling of
CC several transmembrane proteins including cystic fibrosis transmembrane
CC conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium
CC voltage-gated channel, and voltage-dependent L-type calcium channel.
CC May also regulate constitutive and regulated secretion, like insulin
CC granule exocytosis. Required for melanosome transport and release from
CC melanocytes. Also regulates V-ATPase intracellular transport in
CC response to extracellular acidosis. {ECO:0000269|PubMed:14627637,
CC ECO:0000269|PubMed:19029296, ECO:0000269|PubMed:19244346,
CC ECO:0000269|PubMed:20717956, ECO:0000269|PubMed:21248079,
CC ECO:0000269|PubMed:22129970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:16545962};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:16545962};
CC -!- SUBUNIT: Interacts with KCNMA1 (By similarity). Interacts with
CC RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4 (PubMed:11495908). May
CC interact with TBC1D14 (PubMed:22613832). Interacts with ATP6V1E1
CC (PubMed:20717956). Interacts with PI4KB (PubMed:23572552). Interacts
CC (GDP-bound form) with ZFYVE27 (PubMed:21976701). Interacts (GDP-bound
CC form) with KIF5A in a ZFYVE27-dependent manner (PubMed:21976701).
CC Interacts with RELCH (By similarity). Interacts (in GTP-bound form)
CC with TBC1D8B (via domain Rab-GAP TBC) (PubMed:30661770).
CC {ECO:0000250|UniProtKB:P46638, ECO:0000269|PubMed:11495908,
CC ECO:0000269|PubMed:20717956, ECO:0000269|PubMed:21976701,
CC ECO:0000269|PubMed:22613832, ECO:0000269|PubMed:23572552,
CC ECO:0000269|PubMed:30661770}.
CC -!- INTERACTION:
CC Q15907; P01100: FOS; NbExp=3; IntAct=EBI-722234, EBI-852851;
CC Q15907; P62993: GRB2; NbExp=3; IntAct=EBI-722234, EBI-401755;
CC Q15907; P42261: GRIA1; NbExp=3; IntAct=EBI-722234, EBI-6980805;
CC Q15907; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-722234, EBI-16439278;
CC Q15907; Q9ULV0-2: MYO5B; NbExp=3; IntAct=EBI-722234, EBI-14093244;
CC Q15907; Q7L804: RAB11FIP2; NbExp=4; IntAct=EBI-722234, EBI-1049676;
CC Q15907; Q7L8J4: SH3BP5L; NbExp=4; IntAct=EBI-722234, EBI-747389;
CC Q15907; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-722234, EBI-5235340;
CC Q15907; P12931: SRC; NbExp=3; IntAct=EBI-722234, EBI-621482;
CC Q15907; Q9P2M4: TBC1D14; NbExp=2; IntAct=EBI-722234, EBI-2797718;
CC Q15907; Q86WV8: TSC1; NbExp=3; IntAct=EBI-722234, EBI-12806590;
CC Q15907; O76024: WFS1; NbExp=3; IntAct=EBI-722234, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P46638}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P46638}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P46638}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:O35509}; Lipid-anchor
CC {ECO:0000250|UniProtKB:O35509}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O35509}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000305|PubMed:21255211}; Lipid-anchor
CC {ECO:0000305|PubMed:21255211}; Cytoplasmic side
CC {ECO:0000305|PubMed:21255211}. Note=Recruited to phagosomes containing
CC S.aureus. {ECO:0000305|PubMed:21255211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15907-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15907-2; Sequence=VSP_055832;
CC -!- INDUCTION: Up-regulated by extracellular acidosis and down-regulated by
CC alkalosis (at protein level). {ECO:0000269|PubMed:20717956}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P46638}.
CC -!- PTM: (Microbial infection) Glycosylated on arginine residues by
CC S.typhimurium protein Ssek3. {ECO:0000269|PubMed:32974215}.
CC -!- DISEASE: Neurodevelopmental disorder with ataxic gait, absent speech,
CC and decreased cortical white matter (NDAGSCW) [MIM:617807]: An
CC autosomal dominant neurodevelopmental disorder apparent in infancy and
CC characterized by severe intellectual disability with absent speech,
CC epilepsy, and hypotonia. Additionally, visual problems, musculoskeletal
CC abnormalities, and microcephaly can be present. Brain imaging shows
CC decreased cortical white matter, often with decreased cerebellar white
CC matter, thin corpus callosum, and thin brainstem.
CC {ECO:0000269|PubMed:29106825}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X79780; CAA56176.1; -; mRNA.
DR EMBL; EF560724; ABQ59034.1; -; mRNA.
DR EMBL; AF498947; AAM21095.1; -; mRNA.
DR EMBL; AK297498; BAG59912.1; -; 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; AC136469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW68927.1; -; Genomic_DNA.
DR EMBL; BC110081; AAI10082.1; -; mRNA.
DR CCDS; CCDS12201.1; -. [Q15907-1]
DR PIR; JC2487; JC2487.
DR RefSeq; NP_004209.2; NM_004218.3. [Q15907-1]
DR PDB; 2F9L; X-ray; 1.55 A; A=8-205.
DR PDB; 2F9M; X-ray; 1.95 A; A=8-205.
DR PDB; 4OJK; X-ray; 2.66 A; A/B=8-205.
DR PDBsum; 2F9L; -.
DR PDBsum; 2F9M; -.
DR PDBsum; 4OJK; -.
DR AlphaFoldDB; Q15907; -.
DR SMR; Q15907; -.
DR BioGRID; 114661; 131.
DR CORUM; Q15907; -.
DR DIP; DIP-50898N; -.
DR IntAct; Q15907; 75.
DR MINT; Q15907; -.
DR STRING; 9606.ENSP00000333547; -.
DR iPTMnet; Q15907; -.
DR PhosphoSitePlus; Q15907; -.
DR SwissPalm; Q15907; -.
DR BioMuta; RAB11B; -.
DR DMDM; 38258938; -.
DR EPD; Q15907; -.
DR jPOST; Q15907; -.
DR MassIVE; Q15907; -.
DR MaxQB; Q15907; -.
DR PaxDb; Q15907; -.
DR PeptideAtlas; Q15907; -.
DR PRIDE; Q15907; -.
DR ProteomicsDB; 60808; -. [Q15907-1]
DR TopDownProteomics; Q15907-1; -. [Q15907-1]
DR Antibodypedia; 24871; 189 antibodies from 30 providers.
DR DNASU; 9230; -.
DR Ensembl; ENST00000328024.11; ENSP00000333547.5; ENSG00000185236.12. [Q15907-1]
DR Ensembl; ENST00000594216.1; ENSP00000471148.1; ENSG00000185236.12. [Q15907-2]
DR GeneID; 9230; -.
DR KEGG; hsa:9230; -.
DR MANE-Select; ENST00000328024.11; ENSP00000333547.5; NM_004218.4; NP_004209.2.
DR UCSC; uc002mju.5; human. [Q15907-1]
DR CTD; 9230; -.
DR DisGeNET; 9230; -.
DR GeneCards; RAB11B; -.
DR HGNC; HGNC:9761; RAB11B.
DR HPA; ENSG00000185236; Low tissue specificity.
DR MalaCards; RAB11B; -.
DR MIM; 604198; gene.
DR MIM; 617807; phenotype.
DR neXtProt; NX_Q15907; -.
DR OpenTargets; ENSG00000185236; -.
DR PharmGKB; PA34102; -.
DR VEuPathDB; HostDB:ENSG00000185236; -.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000161659; -.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; Q15907; -.
DR OMA; PSSYENC; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; Q15907; -.
DR TreeFam; TF300099; -.
DR PathwayCommons; Q15907; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q15907; -.
DR BioGRID-ORCS; 9230; 7 hits in 1084 CRISPR screens.
DR ChiTaRS; RAB11B; human.
DR EvolutionaryTrace; Q15907; -.
DR GeneWiki; RAB11B; -.
DR GenomeRNAi; 9230; -.
DR Pharos; Q15907; Tbio.
DR PRO; PR:Q15907; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q15907; protein.
DR Bgee; ENSG00000185236; Expressed in right lobe of thyroid gland and 144 other tissues.
DR ExpressionAtlas; Q15907; baseline and differential.
DR Genevisible; Q15907; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; TAS:Reactome.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
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:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IGI:ARUK-UCL.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0045054; P:constitutive secretory pathway; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
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 exocytosis; 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:0033572; P:transferrin transport; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 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; Alternative splicing; Citrullination;
KW Cytoplasmic vesicle; Direct protein sequencing; Disease variant; Endosome;
KW Glycoprotein; GTP-binding; Hydrolase; Intellectual disability; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.10"
FT CHAIN 2..215
FT /note="Ras-related protein Rab-11B"
FT /id="PRO_0000121158"
FT PROPEP 216..218
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT /id="PRO_0000370815"
FT REGION 184..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 196..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16545962"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16545962"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16545962"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16545962"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 4
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P46638"
FT MOD_RES 215
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:24023390"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:24023390"
FT VAR_SEQ 171..218
FT /note="EIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL ->
FT GGRGPDGCG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055832"
FT VARIANT 22
FT /note="V -> M (in NDAGSCW; dbSNP:rs1555690779)"
FT /evidence="ECO:0000269|PubMed:29106825"
FT /id="VAR_080598"
FT VARIANT 68
FT /note="A -> T (in NDAGSCW; dbSNP:rs1555690804)"
FT /evidence="ECO:0000269|PubMed:29106825"
FT /id="VAR_080599"
FT MUTAGEN 25
FT /note="S->N: Dominant negative mutant locked in the
FT inactive GDP-bound form; alters apical recycling. Does not
FT interact with ZFYV2E and KIF5A."
FT /evidence="ECO:0000269|PubMed:19244346,
FT ECO:0000269|PubMed:21976701"
FT MUTAGEN 70
FT /note="Q->L: Constitutively active mutant locked in the
FT active GTP-bound form; alters apical recycling."
FT /evidence="ECO:0000269|PubMed:19244346"
FT CONFLICT 75
FT /note="A -> R (in Ref. 1; CAA56176)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="N -> D (in Ref. 5; AAV38342)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> A (in Ref. 6; CAG38733)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="R -> C (in Ref. 6; CAG46492)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="Q -> R (in Ref. 2; ABQ59034)"
FT /evidence="ECO:0000305"
FT STRAND 9..19
FT /evidence="ECO:0007829|PDB:2F9L"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:2F9L"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:2F9L"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:2F9L"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2F9L"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4OJK"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2F9L"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:2F9L"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:2F9L"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:2F9L"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:2F9L"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2F9L"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:2F9L"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2F9L"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2F9L"
FT HELIX 161..177
FT /evidence="ECO:0007829|PDB:2F9L"
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
