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Ras-related protein Rab-11A (Rab-11) (YL8)

 RB11A_HUMAN             Reviewed;         216 AA.
P62491; B2R4B6; B4DT13; P24410; Q5TZN9; Q9JLX1;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 162.
RecName: Full=Ras-related protein Rab-11A;
Short=Rab-11;
AltName: Full=YL8;
Flags: Precursor;
Name=RAB11A; Synonyms=RAB11;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1704119;
Drivas G.T., Shih A., Coutavas E.E., D'Eustachio P., Rush M.G.;
"Identification and characterization of a human homolog of the
Schizosaccharomyces pombe ras-like gene YPT-3.";
Oncogene 6:3-9(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Zahraoui A., Joberty G., Tavitian A.;
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9662449; DOI=10.1016/S0014-5793(98)00607-3;
Gromov P.S., Celis J.E., Hansen C., Tommerup N., Gromova I.,
Madsen P.;
"Human rab11a: transcription, chromosome mapping and effect on the
expression levels of host GTP-binding proteins.";
FEBS Lett. 429:359-364(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 2-24; 34-58; 62-72; 75-95 AND 133-140, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma, and Platelet;
Bienvenut W.V.;
Submitted (OCT-2005) to UniProtKB.
[12]
INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
PubMed=11495908; DOI=10.1074/jbc.M104831200;
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.;
"Identification and characterization of a family of Rab11-interacting
proteins.";
J. Biol. Chem. 276:39067-39075(2001).
[13]
INTERACTION WITH RAB11FIP4.
PubMed=12470645; DOI=10.1016/S0006-291X(02)02720-1;
Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.;
"Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its
overexpression condenses the Rab11 positive compartment in HeLa
cells.";
Biochem. Biophys. Res. Commun. 299:770-779(2002).
[14]
INTERACTION WITH RAB11FIP4.
TISSUE=Cervix carcinoma;
PubMed=11786538; DOI=10.1074/jbc.M108665200;
Lindsay A.J., Hendrick A.G., Cantalupo G., Senic-Matuglia F., Goud B.,
Bucci C., McCaffrey M.W.;
"Rab coupling protein (RCP), a novel Rab4 and Rab11 effector
protein.";
J. Biol. Chem. 277:12190-12199(2002).
[15]
SUBCELLULAR LOCATION.
PubMed=11994279; DOI=10.1074/jbc.M200757200;
Lindsay A.J., McCaffrey M.W.;
"Rab11-FIP2 functions in transferrin recycling and associates with
endosomal membranes via its COOH-terminal domain.";
J. Biol. Chem. 277:27193-27199(2002).
[16]
INTERACTION WITH RAB11FIP1.
PubMed=15280022; DOI=10.1016/j.febslet.2004.06.068;
Lindsay A.J., McCaffrey M.W.;
"Characterisation of the Rab binding properties of Rab coupling
protein (RCP) by site-directed mutagenesis.";
FEBS Lett. 571:86-92(2004).
[17]
INTERACTION WITH RAB11FIP2.
PubMed=15173169; DOI=10.1074/jbc.M404633200;
Junutula J.R., Schonteich E., Wilson G.M., Peden A.A., Scheller R.H.,
Prekeris R.;
"Molecular characterization of Rab11 interactions with members of the
family of Rab11-interacting proteins.";
J. Biol. Chem. 279:33430-33437(2004).
[18]
SUBCELLULAR LOCATION.
PubMed=15304524; DOI=10.1242/jcs.01280;
Lindsay A.J., McCaffrey M.W.;
"The C2 domains of the class I Rab11 family of interacting proteins
target recycling vesicles to the plasma membrane.";
J. Cell Sci. 117:4365-4375(2004).
[19]
INTERACTION WITH RAB11FIP1, AND SUBCELLULAR LOCATION.
PubMed=15181150; DOI=10.1091/mbc.E03-12-0918;
Peden A.A., Schonteich E., Chun J., Junutula J.R., Scheller R.H.,
Prekeris R.;
"The RCP-Rab11 complex regulates endocytic protein sorting.";
Mol. Biol. Cell 15:3530-3541(2004).
[20]
INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
PubMed=16148947; DOI=10.1038/sj.emboj.7600803;
Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X.,
Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.;
"Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control
membrane traffic in cytokinesis.";
EMBO J. 24:3389-3399(2005).
[21]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND
RAB11FIP4, AND MUTAGENESIS OF SER-25.
PubMed=15601896; DOI=10.1091/mbc.E04-10-0927;
Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D.,
Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.;
"The FIP3-Rab11 protein complex regulates recycling endosome targeting
to the cleavage furrow during late cytokinesis.";
Mol. Biol. Cell 16:849-860(2005).
[22]
FUNCTION, AND MUTAGENESIS OF SER-25 AND GLN-70.
PubMed=15689490; DOI=10.1091/mbc.E04-10-0867;
Lock J.G., Stow J.L.;
"Rab11 in recycling endosomes regulates the sorting and basolateral
transport of E-cadherin.";
Mol. Biol. Cell 16:1744-1755(2005).
[23]
INTERACTION WITH ZFYVE27.
PubMed=17082457; DOI=10.1126/science.1134027;
Shirane M., Nakayama K.I.;
"Protrudin induces neurite formation by directional membrane
trafficking.";
Science 314:818-821(2006).
[24]
FUNCTION, INTERACTION WITH MYO5B, AND IDENTIFICATION IN A COMPLEX WITH
MYO5B AND CFTR.
PubMed=17462998; DOI=10.1074/jbc.M608531200;
Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S.,
Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E.,
Langford G.M., Fukuda M., Stanton B.A.;
"Myosin Vb is required for trafficking of the cystic fibrosis
transmembrane conductance regulator in Rab11a-specific apical
recycling endosomes in polarized human airway epithelial cells.";
J. Biol. Chem. 282:23725-23736(2007).
[25]
INTERACTION WITH RAB11FIP3 AND EVI5.
PubMed=17229837; DOI=10.1073/pnas.0610500104;
Westlake C.J., Junutula J.R., Simon G.C., Pilli M., Prekeris R.,
Scheller R.H., Jackson P.K., Eldridge A.G.;
"Identification of Rab11 as a small GTPase binding protein for the
Evi5 oncogene.";
Proc. Natl. Acad. Sci. U.S.A. 104:1236-1241(2007).
[26]
INTERACTION WITH BIRC6/BRUCE.
PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
Pohl C., Jentsch S.;
"Final stages of cytokinesis and midbody ring formation are controlled
by BRUCE.";
Cell 132:832-845(2008).
[27]
FUNCTION, INTERACTION WITH NPC1L1, AND MUTAGENESIS OF SER-25.
PubMed=19542231; DOI=10.1074/jbc.M109.034355;
Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L.,
Song B.-L.;
"Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-
regulated translocation of NPC1L1 to the cell surface.";
J. Biol. Chem. 284:22481-22490(2009).
[28]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20890297; DOI=10.1038/ncb2106;
Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J.,
Martin-Belmonte F., Mostov K.E.;
"A molecular network for de novo generation of the apical surface and
lumen.";
Nat. Cell Biol. 12:1035-1045(2010).
[29]
INTERACTION WITH VIPAS39.
PubMed=20190753; DOI=10.1038/ng.538;
Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y.,
Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B.,
Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H.,
Matthews R.P., Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H.,
Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P.;
"Mutations in VIPAR cause an arthrogryposis, renal dysfunction and
cholestasis syndrome phenotype with defects in epithelial
polarization.";
Nat. Genet. 42:303-312(2010).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[31]
INTERACTION WITH ZFYVE27 AND KIF5A.
PubMed=21976701; DOI=10.1091/mbc.E11-01-0068;
Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.;
"Protrudin serves as an adaptor molecule that connects KIF5 and its
cargoes in vesicular transport during process formation.";
Mol. Biol. Cell 22:4602-4620(2011).
[32]
FUNCTION, AND INTERACTION WITH MYO5B.
PubMed=21282656; DOI=10.1073/pnas.1010754108;
Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E.,
Goldenring J.R.;
"Rab GTPase-Myo5B complexes control membrane recycling and epithelial
polarization.";
Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011).
[33]
SUBCELLULAR LOCATION.
PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
Seto S., Tsujimura K., Koide Y.;
"Rab GTPases regulating phagosome maturation are differentially
recruited to mycobacterial phagosomes.";
Traffic 12:407-420(2011).
[34]
INTERACTION WITH TBC1D14.
PubMed=22613832; DOI=10.1083/jcb.201111079;
Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.;
"TBC1D14 regulates autophagosome formation via Rab11- and ULK1-
positive recycling endosomes.";
J. Cell Biol. 197:659-675(2012).
[35]
INTERACTION WITH UNC119.
PubMed=23535298; DOI=10.4161/cc.24404;
Lee Y., Chung S., Baek I.K., Lee T.H., Paik S.Y., Lee J.;
"UNC119a bridges the transmission of Fyn signals to Rab11, leading to
the completion of cytokinesis.";
Cell Cycle 12:1303-1315(2013).
[36]
ISOPRENYLATION AT CYS-212 AND CYS-213, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=24023390; DOI=10.1074/mcp.M113.030114;
Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T.,
Tran J.C., Thomas P.M., Kelleher N.L.;
"Large-scale top down proteomics of the human proteome: membrane
proteins, mitochondria, and senescence.";
Mol. Cell. Proteomics 12:3465-3473(2013).
[37]
INTERACTION WITH SH3BP5.
PubMed=26506309; DOI=10.1016/j.devcel.2015.09.013;
Sakaguchi A., Sato M., Sato K., Gengyo-Ando K., Yorimitsu T.,
Nakai J., Hara T., Sato K., Sato K.;
"REI-1 is a guanine nucleotide exchange factor regulating RAB-11
localization and function in C. elegans embryos.";
Dev. Cell 35:211-221(2015).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[39]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-175 IN COMPLEX WITH GTP
ANALOG.
PubMed=16034420; DOI=10.1038/nature03798;
Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
"Structural basis of family-wide Rab GTPase recognition by rabenosyn-
5.";
Nature 436:415-419(2005).
[40]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP
ANALOG AND GDP, AND MUTAGENESIS OF GLN-70.
PubMed=15837192; DOI=10.1016/j.str.2005.01.014;
Pasqualato S., Cherfils J.;
"Crystallographic evidence for substrate-assisted GTP hydrolysis by a
small GTP binding protein.";
Structure 13:533-540(2005).
[41]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 6-175 IN COMPLEX WITH GTP
AND RAB11FIP3, AND MUTAGENESIS OF GLN-70.
PubMed=17007872; DOI=10.1016/j.jmb.2006.08.064;
Eathiraj S., Mishra A., Prekeris R., Lambright D.G.;
"Structural basis for Rab11-mediated recruitment of FIP3 to recycling
endosomes.";
J. Mol. Biol. 364:121-135(2006).
[42]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 7-173 IN COMPLEX WITH GTP,
INTERACTION WITH RAB11FIP3 AND RAB11FIP4, AND MUTAGENESIS OF GLN-70.
PubMed=17030804; DOI=10.1073/pnas.0605357103;
Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K.,
Wakatsuki S.;
"Structural basis for Rab11-dependent membrane recruitment of a family
of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.";
Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
[43]
X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP,
INTERACTION WITH RAB11FIP2, AND MUTAGENESIS OF GLN-70.
PubMed=16905101; DOI=10.1016/j.str.2006.06.010;
Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W.,
Khan A.R.;
"Crystal structure of rab11 in complex with rab11 family interacting
protein 2.";
Structure 14:1273-1283(2006).
-!- 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 regulates endocytic recycling. Acts
as a major regulator of membrane delivery during cytokinesis.
Together with MYO5B and RAB8A participates in epithelial cell
polarization. Together with RAB3IP, RAB8A, the exocyst complex,
PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of
PODXL to the apical membrane initiation sites (AMIS), apical
surface formation and lumenogenesis. Together with MYO5B
participates in CFTR trafficking to the plasma membrane and TF
(Transferrin) recycling in nonpolarized cells. Required in a
complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to
the plasma membrane. Participates in the sorting and basolateral
transport of CDH1 from the Golgi apparatus to the plasma membrane.
Regulates the recycling of FCGRT (receptor of Fc region of
monomeric Ig G) to basolateral membranes. May also play a role in
melanosome transport and release from melanocytes.
{ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:15689490,
ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:19542231,
ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21282656}.
-!- SUBUNIT: Interacts with RIP11 and STXBP6. Interacts with SGSM1,
SGSM2 and SGSM3 (By similarity). Interacts with EXOC6 in a GTP-
dependent manner (By similarity). Interacts with RAB11FIP1,
RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4. Interacts
with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and
compete for binding RAB11A. Interacts with VIPAS39. Interacts with
MYO5B. Found in a complex with MYO5B and CFTR. Interacts with
NPC1L1. Interacts (GDP-bound form) with ZFYVE27 (PubMed:21976701,
PubMed:17082457). Interacts with BIRC6/bruce. May interact with
TBC1D14. Interacts with UNC119; in a cell cycle-dependent manner.
GDP-bound and nucleotide-free forms interact with SH3BP5
(PubMed:26506309). Interacts (GDP-bound form) with KIF5A in a
ZFYVE27-dependent manner (PubMed:21976701). {ECO:0000250,
ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:11786538,
ECO:0000269|PubMed:12470645, ECO:0000269|PubMed:15173169,
ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15280022,
ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:15837192,
ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16148947,
ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872,
ECO:0000269|PubMed:17030804, ECO:0000269|PubMed:17082457,
ECO:0000269|PubMed:17229837, ECO:0000269|PubMed:17462998,
ECO:0000269|PubMed:18329369, ECO:0000269|PubMed:19542231,
ECO:0000269|PubMed:20190753, ECO:0000269|PubMed:21282656,
ECO:0000269|PubMed:21976701, ECO:0000269|PubMed:22613832,
ECO:0000269|PubMed:23535298, ECO:0000269|PubMed:26506309}.
-!- INTERACTION:
Q7LBR1:CHMP1B; NbExp=3; IntAct=EBI-745098, EBI-2118090;
Q6WKZ4:RAB11FIP1; NbExp=2; IntAct=EBI-745098, EBI-1043591;
Q7L804:RAB11FIP2; NbExp=3; IntAct=EBI-745098, EBI-1049676;
Q9BXF6:RAB11FIP5; NbExp=2; IntAct=EBI-745098, EBI-1387068;
Q5T4F4:ZFYVE27; NbExp=4; IntAct=EBI-745098, EBI-3892947;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15304524};
Lipid-anchor {ECO:0000305|PubMed:24023390}. Recycling endosome
membrane {ECO:0000269|PubMed:11994279,
ECO:0000269|PubMed:15181150}; Lipid-anchor
{ECO:0000305|PubMed:24023390}. Cleavage furrow
{ECO:0000269|PubMed:15601896}. Cytoplasmic vesicle, phagosome
{ECO:0000269|PubMed:21255211}. Note=Translocates with RAB11FIP2
from the vesicles of the endocytic recycling compartment (ERC) to
the plasma membrane (PubMed:11994279). Localizes to the cleavage
furrow (PubMed:15601896). Colocalizes with PARD3, PRKCI, EXOC5,
OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS)
during the generation of apical surface and lumenogenesis
(PubMed:20890297). Recruited to phagosomes containing S.aureus or
M.tuberculosis (PubMed:21255211). {ECO:0000269|PubMed:11994279,
ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:20890297,
ECO:0000269|PubMed:21255211}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62491-1; Sequence=Displayed;
Name=2;
IsoId=P62491-2; Sequence=VSP_046755;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X53143; CAA37300.1; -; mRNA.
EMBL; X56740; CAA40064.1; -; mRNA.
EMBL; AF000231; AAC32887.1; -; mRNA.
EMBL; AF498946; AAM21094.1; -; mRNA.
EMBL; CR407669; CAG28597.1; -; mRNA.
EMBL; CR536493; CAG38732.1; -; mRNA.
EMBL; BT020151; AAV38953.1; -; mRNA.
EMBL; BT020154; AAV38956.1; -; mRNA.
EMBL; AK300008; BAG61825.1; -; mRNA.
EMBL; AK311770; BAG34713.1; -; mRNA.
EMBL; AC011939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77752.1; -; Genomic_DNA.
EMBL; BC013348; AAH13348.1; -; mRNA.
CCDS; CCDS10212.1; -. [P62491-1]
CCDS; CCDS58373.1; -. [P62491-2]
PIR; S47169; S47169.
RefSeq; NP_001193765.1; NM_001206836.1. [P62491-2]
RefSeq; NP_004654.1; NM_004663.4. [P62491-1]
UniGene; Hs.321541; -.
PDB; 1OIV; X-ray; 1.98 A; A/B=1-173.
PDB; 1OIW; X-ray; 2.05 A; A=1-173.
PDB; 1OIX; X-ray; 1.70 A; A=1-173.
PDB; 1YZK; X-ray; 2.00 A; A=8-175.
PDB; 2D7C; X-ray; 1.75 A; A/B=7-173.
PDB; 2GZD; X-ray; 2.44 A; A/B=2-173.
PDB; 2GZH; X-ray; 2.47 A; A=2-173.
PDB; 2HV8; X-ray; 1.86 A; A/B/C=6-175.
PDB; 4C4P; X-ray; 2.00 A; A=1-173.
PDB; 4D0L; X-ray; 2.94 A; B/D/F=1-216.
PDB; 4D0M; X-ray; 6.00 A; B/D/H/J/N/P/R/T/X/Z/d/h=1-216.
PDB; 4LWZ; X-ray; 2.55 A; A/C=1-177.
PDB; 4LX0; X-ray; 2.19 A; A/C=1-177.
PDB; 4UJ3; X-ray; 3.00 A; A/D/G/J/M/P/S/V=4-186.
PDB; 4UJ4; X-ray; 4.20 A; A/D/G/J=4-186.
PDB; 4UJ5; X-ray; 2.60 A; A/B=6-186.
PDB; 5C46; X-ray; 2.65 A; F=1-216.
PDB; 5C4G; X-ray; 3.20 A; B=1-216.
PDB; 5EUQ; X-ray; 3.20 A; B=1-216.
PDB; 5EZ5; X-ray; 2.40 A; A/B=8-175.
PDB; 5FBL; X-ray; 3.37 A; B=1-216.
PDB; 5FBQ; X-ray; 3.79 A; B=1-216.
PDB; 5FBR; X-ray; 3.28 A; B=1-216.
PDB; 5FBV; X-ray; 3.29 A; B=1-216.
PDB; 5FBW; X-ray; 3.49 A; B=1-216.
PDB; 5JCZ; X-ray; 2.06 A; A/D/I=1-177.
PDBsum; 1OIV; -.
PDBsum; 1OIW; -.
PDBsum; 1OIX; -.
PDBsum; 1YZK; -.
PDBsum; 2D7C; -.
PDBsum; 2GZD; -.
PDBsum; 2GZH; -.
PDBsum; 2HV8; -.
PDBsum; 4C4P; -.
PDBsum; 4D0L; -.
PDBsum; 4D0M; -.
PDBsum; 4LWZ; -.
PDBsum; 4LX0; -.
PDBsum; 4UJ3; -.
PDBsum; 4UJ4; -.
PDBsum; 4UJ5; -.
PDBsum; 5C46; -.
PDBsum; 5C4G; -.
PDBsum; 5EUQ; -.
PDBsum; 5EZ5; -.
PDBsum; 5FBL; -.
PDBsum; 5FBQ; -.
PDBsum; 5FBR; -.
PDBsum; 5FBV; -.
PDBsum; 5FBW; -.
PDBsum; 5JCZ; -.
ProteinModelPortal; P62491; -.
SMR; P62491; -.
BioGrid; 114299; 91.
CORUM; P62491; -.
DIP; DIP-29138N; -.
IntAct; P62491; 45.
MINT; MINT-1434585; -.
STRING; 9606.ENSP00000261890; -.
DrugBank; DB01864; 5'-Guanosine-Diphosphate-Monothiophosphate.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
iPTMnet; P62491; -.
PhosphoSitePlus; P62491; -.
SwissPalm; P62491; -.
BioMuta; RAB11A; -.
DMDM; 50402542; -.
OGP; P62491; -.
MaxQB; P62491; -.
PaxDb; P62491; -.
PeptideAtlas; P62491; -.
PRIDE; P62491; -.
TopDownProteomics; P62491-1; -. [P62491-1]
DNASU; 8766; -.
Ensembl; ENST00000261890; ENSP00000261890; ENSG00000103769. [P62491-1]
Ensembl; ENST00000569896; ENSP00000456420; ENSG00000103769. [P62491-2]
GeneID; 8766; -.
KEGG; hsa:8766; -.
UCSC; uc002apk.4; human. [P62491-1]
CTD; 8766; -.
DisGeNET; 8766; -.
EuPathDB; HostDB:ENSG00000103769.9; -.
GeneCards; RAB11A; -.
HGNC; HGNC:9760; RAB11A.
HPA; CAB013097; -.
HPA; HPA051697; -.
HPA; HPA060686; -.
MIM; 605570; gene.
neXtProt; NX_P62491; -.
OpenTargets; ENSG00000103769; -.
PharmGKB; PA34101; -.
eggNOG; KOG0087; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000118841; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; P62491; -.
KO; K07904; -.
OMA; YESVSRW; -.
OrthoDB; EOG091G0O1R; -.
PhylomeDB; P62491; -.
TreeFam; TF300099; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
Reactome; R-HSA-8854214; TBC/RABGAPs.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
SignaLink; P62491; -.
ChiTaRS; RAB11A; human.
EvolutionaryTrace; P62491; -.
GeneWiki; RAB11A; -.
GenomeRNAi; 8766; -.
PRO; PR:P62491; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000103769; -.
CleanEx; HS_RAB11A; -.
ExpressionAtlas; P62491; baseline and differential.
Genevisible; P62491; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0098837; C:postsynaptic recycling endosome; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
GO; GO:0030133; C:transport vesicle; IEA:Ensembl.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
GO; GO:0019905; F:syntaxin binding; NAS:UniProtKB.
GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
GO; GO:0090150; P:establishment of protein localization to membrane; IMP:UniProtKB.
GO; GO:0072594; P:establishment of protein localization to organelle; IMP:UniProtKB.
GO; GO:0051650; P:establishment of vesicle localization; IMP:UniProtKB.
GO; GO:1990182; P:exosomal secretion; IMP:UniProtKB.
GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0036258; P:multivesicular body assembly; IMP:UniProtKB.
GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IEA:Ensembl.
GO; GO:0048227; P:plasma membrane to endosome transport; NAS:UniProtKB.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0010796; P:regulation of multivesicular body size; IMP:UniProtKB.
GO; GO:0051223; P:regulation of protein transport; IEA:Ensembl.
GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell membrane; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; Endosome; GTP-binding; Lipoprotein;
Membrane; Methylation; Nucleotide-binding; Prenylation;
Protein transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.11}.
CHAIN 2 213 Ras-related protein Rab-11A.
/FTId=PRO_0000121151.
PROPEP 214 216 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000370807.
NP_BIND 18 26 GTP. {ECO:0000269|PubMed:16905101,
ECO:0000269|PubMed:17007872,
ECO:0000269|PubMed:17030804}.
NP_BIND 66 70 GTP. {ECO:0000269|PubMed:16905101,
ECO:0000269|PubMed:17007872,
ECO:0000269|PubMed:17030804}.
NP_BIND 124 127 GTP. {ECO:0000269|PubMed:16905101,
ECO:0000269|PubMed:17007872,
ECO:0000269|PubMed:17030804}.
NP_BIND 154 156 GTP. {ECO:0000269|PubMed:16905101,
ECO:0000269|PubMed:17007872,
ECO:0000269|PubMed:17030804}.
MOTIF 40 48 Effector region. {ECO:0000250}.
MOD_RES 2 2 N-acetylglycine. {ECO:0000269|Ref.11}.
MOD_RES 213 213 Cysteine methyl ester. {ECO:0000255}.
LIPID 212 212 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:24023390}.
LIPID 213 213 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:24023390}.
VAR_SEQ 147 216 GLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQMSDRREN
DMSPSNNVVPIHVPPTTENKPKVQCCQNI -> EANVRQTR
K (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046755.
MUTAGEN 25 25 S->N: Dominant-negative mutant. Induces
increased number of binucleated cells,
indicating defects in cytokinesis.
Inhibits the transport of NPC1L1 to the
plama membrane. Disrupts the trafficking
of CDH1 to the plasma membrane and
promotes accumulation of CDH1 in RAB11A
endosomes in nonpolarized cells. Promotes
mistargeting of CDH1 to the apical
membrane in polarized cells.
{ECO:0000269|PubMed:15601896,
ECO:0000269|PubMed:15689490,
ECO:0000269|PubMed:19542231}.
MUTAGEN 70 70 Q->L: Constitutively active mutant.
Decreases GTPase activity. Disrupts the
trafficking of CDH1 to the plasma
membrane and promotes accumulation of
CDH1 in RAB11A endosomes in nonpolarized
cells. Promotes mistargeting of CDH1 to
the apical membrane in polarized cells.
{ECO:0000269|PubMed:15689490,
ECO:0000269|PubMed:15837192,
ECO:0000269|PubMed:16905101,
ECO:0000269|PubMed:17007872,
ECO:0000269|PubMed:17030804}.
STRAND 9 18 {ECO:0000244|PDB:1OIX}.
HELIX 24 33 {ECO:0000244|PDB:1OIX}.
STRAND 45 55 {ECO:0000244|PDB:1OIX}.
STRAND 58 67 {ECO:0000244|PDB:1OIX}.
STRAND 72 74 {ECO:0000244|PDB:1OIX}.
HELIX 78 81 {ECO:0000244|PDB:1OIX}.
STRAND 86 92 {ECO:0000244|PDB:1OIX}.
HELIX 96 100 {ECO:0000244|PDB:1OIX}.
HELIX 102 112 {ECO:0000244|PDB:1OIX}.
STRAND 118 124 {ECO:0000244|PDB:1OIX}.
HELIX 126 131 {ECO:0000244|PDB:1OIX}.
HELIX 136 145 {ECO:0000244|PDB:1OIX}.
STRAND 149 152 {ECO:0000244|PDB:1OIX}.
TURN 155 157 {ECO:0000244|PDB:1OIX}.
HELIX 161 172 {ECO:0000244|PDB:1OIX}.
SEQUENCE 216 AA; 24394 MW; 76FC1E113A29B269 CRC64;
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM
LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ
MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI


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