Full text data of RAB13
RAB13
[Confidence: low (only semi-automatic identification from reviews)]
Ras-related protein Rab-13 (Cell growth-inhibiting gene 4 protein; Flags: Precursor)
Ras-related protein Rab-13 (Cell growth-inhibiting gene 4 protein; Flags: Precursor)
UniProt
P51153
ID RAB13_HUMAN Reviewed; 203 AA.
AC P51153; A8K6B5; D3DV67; Q5U0A6; Q6GPG6; Q96GU4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Ras-related protein Rab-13;
DE AltName: Full=Cell growth-inhibiting gene 4 protein;
DE Flags: Precursor;
GN Name=RAB13; ORFNames=GIG4;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8294494; DOI=10.1083/jcb.124.1.101;
RA Zahraoui A., Joberty G., Arpin M., Fontaine J.J., Hellio R.,
RA Tavitian A., Louvard D.;
RT "A small rab GTPase is distributed in cytoplasmic vesicles in non
RT polarized cells but colocalizes with the tight junction marker ZO-1 in
RT polarized epithelial cells.";
RL J. Cell Biol. 124:101-115(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human growth inhibition gene 4 (GIG4).";
RL Submitted (SEP-2003) 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=Placenta;
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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].
RC TISSUE=Ovary, Placenta, and PNS;
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 ISOPRENYLATION AT CYS-200.
RX PubMed=8375503; DOI=10.1016/0014-5793(93)80897-4;
RA Joberty G., Tavitian A., Zahraoui A.;
RT "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif.";
RL FEBS Lett. 330:323-328(1993).
RN [10]
RP INTERACTION WITH PDE6D.
RX PubMed=9712853; DOI=10.1074/jbc.273.35.22340;
RA Marzesco A.M., Galli T., Louvard D., Zahraoui A.;
RT "The rod cGMP phosphodiesterase delta subunit dissociates the small
RT GTPase Rab13 from membranes.";
RL J. Biol. Chem. 273:22340-22345(1998).
RN [11]
RP FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND SUBCELLULAR LOCATION.
RX PubMed=12058051; DOI=10.1091/mbc.02-02-0029;
RA Marzesco A.M., Dunia I., Pandjaitan R., Recouvreur M., Dauzonne D.,
RA Benedetti E.L., Louvard D., Zahraoui A.;
RT "The small GTPase Rab13 regulates assembly of functional tight
RT junctions in epithelial cells.";
RL Mol. Biol. Cell 13:1819-1831(2002).
RN [12]
RP FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND INTERACTION WITH PRKACA.
RX PubMed=15096524; DOI=10.1083/jcb.200312118;
RA Koehler K., Louvard D., Zahraoui A.;
RT "Rab13 regulates PKA signaling during tight junction assembly.";
RL J. Cell Biol. 165:175-180(2004).
RN [13]
RP FUNCTION IN ENDOCYTIC RECYLING, AND SUBCELLULAR LOCATION.
RX PubMed=15528189; DOI=10.1074/jbc.M406906200;
RA Morimoto S., Nishimura N., Terai T., Manabe S., Yamamoto Y.,
RA Shinahara W., Miyake H., Tashiro S., Shimada M., Sasaki T.;
RT "Rab13 mediates the continuous endocytic recycling of occludin to the
RT cell surface.";
RL J. Biol. Chem. 280:2220-2228(2005).
RN [14]
RP FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND INTERACTION WITH MICALL2.
RX PubMed=16525024; DOI=10.1091/mbc.E05-09-0826;
RA Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
RT "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
RT endocytic recycling of occludin.";
RL Mol. Biol. Cell 17:2465-2475(2006).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-22 AND GLN-67.
RX PubMed=18779367; DOI=10.1083/jcb.200802176;
RA Nokes R.L., Fields I.C., Collins R.N., Foelsch H.;
RT "Rab13 regulates membrane trafficking between TGN and recycling
RT endosomes in polarized epithelial cells.";
RL J. Cell Biol. 182:845-853(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP ENZYME REGULATION.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [18]
RP FUNCTION IN NEURITE OUTGROWTH, AND INTERACTION WITH MICALL2.
RX PubMed=20008558; DOI=10.1128/MCB.01067-09;
RA Sakane A., Honda K., Sasaki T.;
RT "Rab13 regulates neurite outgrowth in PC12 cells through its effector
RT protein, JRAB/MICAL-L2.";
RL Mol. Cell. Biol. 30:1077-1087(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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 [21]
RP INTERACTION WITH MICALL1.
RC TISSUE=Uterine adenocarcinoma;
RX PubMed=21795389; DOI=10.1091/mbc.E11-01-0030;
RA Abou-Zeid N., Pandjaitan R., Sengmanivong L., David V., Le Pavec G.,
RA Salamero J., Zahraoui A.;
RT "MICAL-like1 mediates epidermal growth factor receptor endocytosis.";
RL Mol. Biol. Cell 22:3431-3441(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP INDUCTION.
RX PubMed=22562557; DOI=10.1369/0022155412448069;
RA Hirvonen M.J., Mulari M.T., Bueki K.G., Vihko P., Haerkoenen P.L.,
RA Vaeaenaenen H.K.;
RT "Rab13 is upregulated during osteoclast differentiation and associates
RT with small vesicles revealing polarized distribution in resorbing
RT cells.";
RL J. Histochem. Cytochem. 60:537-549(2012).
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 sets of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab is involved in endocytic recycling
CC and regulates the transport to the plasma membrane of
CC transmembrane proteins like the tight junction protein
CC OCLN/occludin. Thereby, it regulates the assembly and the activity
CC of tight junctions. Moreover, it may also regulate tight junction
CC assembly by activating the PKA signaling pathway and by
CC reorganizing the actin cytoskeleton through the activation of the
CC downstream effectors PRKACA and MICALL2 respectively. Through its
CC role in tight junction assembly, may play a role in the
CC establishment of Sertoli cell barrier. Plays also a role in
CC angiogenesis through regulation of endothelial cells chemotaxis.
CC Also involved in neurite outgrowth. Has also been proposed to play
CC a role in post-Golgi membrane trafficking from the TGN to the
CC recycling endosome. Finally, it has been involved in insulin-
CC induced transport to the plasma membrane of the glucose
CC transporter GLUT4 and therefore may play a role in glucose
CC homeostasis.
CC -!- ENZYME REGULATION: Rab activation is generally mediated by a
CC guanine exchange factor (GEF), while inactivation through
CC hydrolysis of bound GTP is catalyzed by a GTPase activating
CC protein (GAP). That Rab may be activated by DENND1C, a guanine
CC exchange factor. Activated in response to insulin.
CC -!- SUBUNIT: Interacts (GTP-bound form) with MICALL2; competes with
CC RAB8A and is involved in tight junctions assembly. Interacts (GTP-
CC bound form) with MICALL1. Interacts with PRKACA; downstream
CC effector of RAB13 involved in tight junction assembly. Interacts
CC with GRB2; may recruit RAB13 to the leading edge of migrating
CC endothelial cells where it can activate RHOA. Interacts
CC (isoprenylated form) with PDE6D; dissociates RAB13 from membranes.
CC Interacts with CCDC64B/BICDR2. Interacts with LEPROT and LEPROTL1.
CC -!- INTERACTION:
CC Q6PDU4:Leprotl1 (xeno); NbExp=4; IntAct=EBI-1780121, EBI-8702651;
CC Q3TN34:Micall2 (xeno); NbExp=8; IntAct=EBI-1780121, EBI-1779852;
CC O43924:PDE6D; NbExp=2; IntAct=EBI-1780121, EBI-712685;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic
CC side. Cell junction, tight junction. Golgi apparatus, trans-Golgi
CC network membrane. Recycling endosome membrane. Cell projection,
CC lamellipodium (By similarity). Cytoplasmic vesicle, secretory
CC vesicle membrane (By similarity). Note=Tight junctions or
CC associated with vesicles scattered throughout the cytoplasm in
CC cells lacking tight junctions. Relocalizes to the leading edge of
CC lamellipodia in migrating endothelial cells.
CC -!- TISSUE SPECIFICITY: Detected in several types of epithelia,
CC including intestine, kidney, liver and in endothelial cells.
CC -!- INDUCTION: Up-regulated during osteoclast differentiation.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; X75593; CAA53266.1; -; mRNA.
DR EMBL; AY423722; AAS00485.1; -; mRNA.
DR EMBL; AF498948; AAM21096.1; -; mRNA.
DR EMBL; AK291580; BAF84269.1; -; mRNA.
DR EMBL; BT019700; AAV38506.1; -; mRNA.
DR EMBL; BT019701; AAV38507.1; -; mRNA.
DR EMBL; AL358472; CAI14031.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53249.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53250.1; -; Genomic_DNA.
DR EMBL; BC000799; AAH00799.1; -; mRNA.
DR EMBL; BC009227; AAH09227.2; -; mRNA.
DR EMBL; BC073168; AAH73168.2; -; mRNA.
DR PIR; A49647; A49647.
DR RefSeq; NP_001258967.1; NM_001272038.1.
DR RefSeq; NP_002861.1; NM_002870.3.
DR UniGene; Hs.151536; -.
DR ProteinModelPortal; P51153; -.
DR SMR; P51153; 6-172.
DR IntAct; P51153; 9.
DR MINT; MINT-3018790; -.
DR STRING; 9606.ENSP00000357564; -.
DR PhosphoSite; P51153; -.
DR DMDM; 1710016; -.
DR PaxDb; P51153; -.
DR PRIDE; P51153; -.
DR DNASU; 5872; -.
DR Ensembl; ENST00000368575; ENSP00000357564; ENSG00000143545.
DR GeneID; 5872; -.
DR KEGG; hsa:5872; -.
DR UCSC; uc001fdt.2; human.
DR CTD; 5872; -.
DR GeneCards; GC01M153954; -.
DR HGNC; HGNC:9762; RAB13.
DR HPA; HPA003996; -.
DR MIM; 602672; gene.
DR neXtProt; NX_P51153; -.
DR PharmGKB; PA34103; -.
DR eggNOG; COG1100; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P51153; -.
DR KO; K06109; -.
DR OMA; KVQREQA; -.
DR OrthoDB; EOG7VB2H4; -.
DR PhylomeDB; P51153; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; RAB13; human.
DR GeneWiki; RAB13; -.
DR GenomeRNAi; 5872; -.
DR NextBio; 22808; -.
DR PRO; PR:P51153; -.
DR ArrayExpress; P51153; -.
DR Bgee; P51153; -.
DR CleanEx; HS_RAB13; -.
DR Genevestigator; P51153; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:tight junction; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; EXP:Reactome.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0090002; P:establishment of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling cascade; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0070830; P:tight junction assembly; IMP:UniProtKB.
DR GO; GO:0044795; P:trans-Golgi network to recycling endosome 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 Cell junction; Cell membrane; Cell projection; Complete proteome;
KW Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Tight junction; Transport.
FT CHAIN 1 200 Ras-related protein Rab-13.
FT /FTId=PRO_0000121182.
FT PROPEP 201 203 Removed in mature form (Potential).
FT /FTId=PRO_0000370756.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 121 124 GTP (By similarity).
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 178 178 Phosphoserine.
FT MOD_RES 200 200 Cysteine methyl ester (Potential).
FT LIPID 200 200 S-geranylgeranyl cysteine.
FT MUTAGEN 22 22 T->N: Dominant negative.
FT MUTAGEN 67 67 Q->L: Constitutively active mutant locked
FT in the active GTP-bound form. Impairs
FT transports of cargo from the trans-Golgi
FT network to the recycling endosomes and
FT alters the assembly of functional tight
FT junctions.
SQ SEQUENCE 203 AA; 22774 MW; 141621CB998178DA CRC64;
MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNNTYIST IGIDFKIRTV DIEGKKIKLQ
VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ NWMKSIKENA SAGVERLLLG
NKCDMEAKRK VQKEQADKLA REHGIRFFET SAKSSMNVDE AFSSLARDIL LKSGGRRSGN
GNKPPSTDLK TCDKKNTNKC SLG
//
ID RAB13_HUMAN Reviewed; 203 AA.
AC P51153; A8K6B5; D3DV67; Q5U0A6; Q6GPG6; Q96GU4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Ras-related protein Rab-13;
DE AltName: Full=Cell growth-inhibiting gene 4 protein;
DE Flags: Precursor;
GN Name=RAB13; ORFNames=GIG4;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8294494; DOI=10.1083/jcb.124.1.101;
RA Zahraoui A., Joberty G., Arpin M., Fontaine J.J., Hellio R.,
RA Tavitian A., Louvard D.;
RT "A small rab GTPase is distributed in cytoplasmic vesicles in non
RT polarized cells but colocalizes with the tight junction marker ZO-1 in
RT polarized epithelial cells.";
RL J. Cell Biol. 124:101-115(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human growth inhibition gene 4 (GIG4).";
RL Submitted (SEP-2003) 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=Placenta;
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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].
RC TISSUE=Ovary, Placenta, and PNS;
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 ISOPRENYLATION AT CYS-200.
RX PubMed=8375503; DOI=10.1016/0014-5793(93)80897-4;
RA Joberty G., Tavitian A., Zahraoui A.;
RT "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif.";
RL FEBS Lett. 330:323-328(1993).
RN [10]
RP INTERACTION WITH PDE6D.
RX PubMed=9712853; DOI=10.1074/jbc.273.35.22340;
RA Marzesco A.M., Galli T., Louvard D., Zahraoui A.;
RT "The rod cGMP phosphodiesterase delta subunit dissociates the small
RT GTPase Rab13 from membranes.";
RL J. Biol. Chem. 273:22340-22345(1998).
RN [11]
RP FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND SUBCELLULAR LOCATION.
RX PubMed=12058051; DOI=10.1091/mbc.02-02-0029;
RA Marzesco A.M., Dunia I., Pandjaitan R., Recouvreur M., Dauzonne D.,
RA Benedetti E.L., Louvard D., Zahraoui A.;
RT "The small GTPase Rab13 regulates assembly of functional tight
RT junctions in epithelial cells.";
RL Mol. Biol. Cell 13:1819-1831(2002).
RN [12]
RP FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND INTERACTION WITH PRKACA.
RX PubMed=15096524; DOI=10.1083/jcb.200312118;
RA Koehler K., Louvard D., Zahraoui A.;
RT "Rab13 regulates PKA signaling during tight junction assembly.";
RL J. Cell Biol. 165:175-180(2004).
RN [13]
RP FUNCTION IN ENDOCYTIC RECYLING, AND SUBCELLULAR LOCATION.
RX PubMed=15528189; DOI=10.1074/jbc.M406906200;
RA Morimoto S., Nishimura N., Terai T., Manabe S., Yamamoto Y.,
RA Shinahara W., Miyake H., Tashiro S., Shimada M., Sasaki T.;
RT "Rab13 mediates the continuous endocytic recycling of occludin to the
RT cell surface.";
RL J. Biol. Chem. 280:2220-2228(2005).
RN [14]
RP FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND INTERACTION WITH MICALL2.
RX PubMed=16525024; DOI=10.1091/mbc.E05-09-0826;
RA Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
RT "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
RT endocytic recycling of occludin.";
RL Mol. Biol. Cell 17:2465-2475(2006).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-22 AND GLN-67.
RX PubMed=18779367; DOI=10.1083/jcb.200802176;
RA Nokes R.L., Fields I.C., Collins R.N., Foelsch H.;
RT "Rab13 regulates membrane trafficking between TGN and recycling
RT endosomes in polarized epithelial cells.";
RL J. Cell Biol. 182:845-853(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP ENZYME REGULATION.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [18]
RP FUNCTION IN NEURITE OUTGROWTH, AND INTERACTION WITH MICALL2.
RX PubMed=20008558; DOI=10.1128/MCB.01067-09;
RA Sakane A., Honda K., Sasaki T.;
RT "Rab13 regulates neurite outgrowth in PC12 cells through its effector
RT protein, JRAB/MICAL-L2.";
RL Mol. Cell. Biol. 30:1077-1087(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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 [21]
RP INTERACTION WITH MICALL1.
RC TISSUE=Uterine adenocarcinoma;
RX PubMed=21795389; DOI=10.1091/mbc.E11-01-0030;
RA Abou-Zeid N., Pandjaitan R., Sengmanivong L., David V., Le Pavec G.,
RA Salamero J., Zahraoui A.;
RT "MICAL-like1 mediates epidermal growth factor receptor endocytosis.";
RL Mol. Biol. Cell 22:3431-3441(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP INDUCTION.
RX PubMed=22562557; DOI=10.1369/0022155412448069;
RA Hirvonen M.J., Mulari M.T., Bueki K.G., Vihko P., Haerkoenen P.L.,
RA Vaeaenaenen H.K.;
RT "Rab13 is upregulated during osteoclast differentiation and associates
RT with small vesicles revealing polarized distribution in resorbing
RT cells.";
RL J. Histochem. Cytochem. 60:537-549(2012).
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 sets of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab is involved in endocytic recycling
CC and regulates the transport to the plasma membrane of
CC transmembrane proteins like the tight junction protein
CC OCLN/occludin. Thereby, it regulates the assembly and the activity
CC of tight junctions. Moreover, it may also regulate tight junction
CC assembly by activating the PKA signaling pathway and by
CC reorganizing the actin cytoskeleton through the activation of the
CC downstream effectors PRKACA and MICALL2 respectively. Through its
CC role in tight junction assembly, may play a role in the
CC establishment of Sertoli cell barrier. Plays also a role in
CC angiogenesis through regulation of endothelial cells chemotaxis.
CC Also involved in neurite outgrowth. Has also been proposed to play
CC a role in post-Golgi membrane trafficking from the TGN to the
CC recycling endosome. Finally, it has been involved in insulin-
CC induced transport to the plasma membrane of the glucose
CC transporter GLUT4 and therefore may play a role in glucose
CC homeostasis.
CC -!- ENZYME REGULATION: Rab activation is generally mediated by a
CC guanine exchange factor (GEF), while inactivation through
CC hydrolysis of bound GTP is catalyzed by a GTPase activating
CC protein (GAP). That Rab may be activated by DENND1C, a guanine
CC exchange factor. Activated in response to insulin.
CC -!- SUBUNIT: Interacts (GTP-bound form) with MICALL2; competes with
CC RAB8A and is involved in tight junctions assembly. Interacts (GTP-
CC bound form) with MICALL1. Interacts with PRKACA; downstream
CC effector of RAB13 involved in tight junction assembly. Interacts
CC with GRB2; may recruit RAB13 to the leading edge of migrating
CC endothelial cells where it can activate RHOA. Interacts
CC (isoprenylated form) with PDE6D; dissociates RAB13 from membranes.
CC Interacts with CCDC64B/BICDR2. Interacts with LEPROT and LEPROTL1.
CC -!- INTERACTION:
CC Q6PDU4:Leprotl1 (xeno); NbExp=4; IntAct=EBI-1780121, EBI-8702651;
CC Q3TN34:Micall2 (xeno); NbExp=8; IntAct=EBI-1780121, EBI-1779852;
CC O43924:PDE6D; NbExp=2; IntAct=EBI-1780121, EBI-712685;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic
CC side. Cell junction, tight junction. Golgi apparatus, trans-Golgi
CC network membrane. Recycling endosome membrane. Cell projection,
CC lamellipodium (By similarity). Cytoplasmic vesicle, secretory
CC vesicle membrane (By similarity). Note=Tight junctions or
CC associated with vesicles scattered throughout the cytoplasm in
CC cells lacking tight junctions. Relocalizes to the leading edge of
CC lamellipodia in migrating endothelial cells.
CC -!- TISSUE SPECIFICITY: Detected in several types of epithelia,
CC including intestine, kidney, liver and in endothelial cells.
CC -!- INDUCTION: Up-regulated during osteoclast differentiation.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; X75593; CAA53266.1; -; mRNA.
DR EMBL; AY423722; AAS00485.1; -; mRNA.
DR EMBL; AF498948; AAM21096.1; -; mRNA.
DR EMBL; AK291580; BAF84269.1; -; mRNA.
DR EMBL; BT019700; AAV38506.1; -; mRNA.
DR EMBL; BT019701; AAV38507.1; -; mRNA.
DR EMBL; AL358472; CAI14031.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53249.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53250.1; -; Genomic_DNA.
DR EMBL; BC000799; AAH00799.1; -; mRNA.
DR EMBL; BC009227; AAH09227.2; -; mRNA.
DR EMBL; BC073168; AAH73168.2; -; mRNA.
DR PIR; A49647; A49647.
DR RefSeq; NP_001258967.1; NM_001272038.1.
DR RefSeq; NP_002861.1; NM_002870.3.
DR UniGene; Hs.151536; -.
DR ProteinModelPortal; P51153; -.
DR SMR; P51153; 6-172.
DR IntAct; P51153; 9.
DR MINT; MINT-3018790; -.
DR STRING; 9606.ENSP00000357564; -.
DR PhosphoSite; P51153; -.
DR DMDM; 1710016; -.
DR PaxDb; P51153; -.
DR PRIDE; P51153; -.
DR DNASU; 5872; -.
DR Ensembl; ENST00000368575; ENSP00000357564; ENSG00000143545.
DR GeneID; 5872; -.
DR KEGG; hsa:5872; -.
DR UCSC; uc001fdt.2; human.
DR CTD; 5872; -.
DR GeneCards; GC01M153954; -.
DR HGNC; HGNC:9762; RAB13.
DR HPA; HPA003996; -.
DR MIM; 602672; gene.
DR neXtProt; NX_P51153; -.
DR PharmGKB; PA34103; -.
DR eggNOG; COG1100; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P51153; -.
DR KO; K06109; -.
DR OMA; KVQREQA; -.
DR OrthoDB; EOG7VB2H4; -.
DR PhylomeDB; P51153; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; RAB13; human.
DR GeneWiki; RAB13; -.
DR GenomeRNAi; 5872; -.
DR NextBio; 22808; -.
DR PRO; PR:P51153; -.
DR ArrayExpress; P51153; -.
DR Bgee; P51153; -.
DR CleanEx; HS_RAB13; -.
DR Genevestigator; P51153; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:tight junction; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; EXP:Reactome.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0090002; P:establishment of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling cascade; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0070830; P:tight junction assembly; IMP:UniProtKB.
DR GO; GO:0044795; P:trans-Golgi network to recycling endosome 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 Cell junction; Cell membrane; Cell projection; Complete proteome;
KW Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Tight junction; Transport.
FT CHAIN 1 200 Ras-related protein Rab-13.
FT /FTId=PRO_0000121182.
FT PROPEP 201 203 Removed in mature form (Potential).
FT /FTId=PRO_0000370756.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 121 124 GTP (By similarity).
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 178 178 Phosphoserine.
FT MOD_RES 200 200 Cysteine methyl ester (Potential).
FT LIPID 200 200 S-geranylgeranyl cysteine.
FT MUTAGEN 22 22 T->N: Dominant negative.
FT MUTAGEN 67 67 Q->L: Constitutively active mutant locked
FT in the active GTP-bound form. Impairs
FT transports of cargo from the trans-Golgi
FT network to the recycling endosomes and
FT alters the assembly of functional tight
FT junctions.
SQ SEQUENCE 203 AA; 22774 MW; 141621CB998178DA CRC64;
MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNNTYIST IGIDFKIRTV DIEGKKIKLQ
VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ NWMKSIKENA SAGVERLLLG
NKCDMEAKRK VQKEQADKLA REHGIRFFET SAKSSMNVDE AFSSLARDIL LKSGGRRSGN
GNKPPSTDLK TCDKKNTNKC SLG
//
MIM
602672
*RECORD*
*FIELD* NO
602672
*FIELD* TI
*602672 RAS-ASSOCIATED PROTEIN RAB13; RAB13
*FIELD* TX
CLONING
The Rab proteins comprise the largest group of Ras-associated small
read moreGTPases and in mammalian cells at least 40 proteins have been identified
(Novick and Zerial, 1997). Rab proteins are specific regulators of
vesicular traffic and the complexity of the Rab protein family
correlates with the diversity of cellular vesicle transport routes. A
different Rab protein may be required for each step of vesicular
transport. For example, the yeast Sec4 protein appears to be required
exclusively for the delivery of Golgi-derived secretory vesicles to the
plasma membrane (Salminen and Novick, 1987). By screening a human
intestinal epithelial cell (Caco-2) cDNA library with a degenerate
oligonucleotide based on a sequence present in the effector domain of
the Sec4 protein, Zahraoui et al. (1994) isolated a cDNA encoding RAB13.
The predicted 203-amino acid protein has the typical structural features
of Ras-related proteins, including a conserved GTP-binding site. RAB13
displays 61% and 56% amino acid identity with the human RAB8 (165040)
and yeast Sec4 proteins, respectively. These proteins share a long
conserved N-terminal region but have divergent C-terminal portions.
Northern blot analysis showed that RAB13 is expressed as a 1.2-kb
transcript in Caco-2 cells. Immunoblot analysis using antibodies against
RAB13 detected a 24-kD protein in Caco-2 cell lysates.
Immunofluorescence studies demonstrated that RAB13 colocalizes with the
tight junction marker ZO1 (TJP1; 601009) in epithelial cells. In cells
devoid of tight junctions, RAB13 associates with vesicles dispersed
throughout the cytoplasm.
MAPPING
Leek et al. (1997) mapped the RAB13 gene to chromosome 12q13 by in situ
hybridization. However, Gross (2011) mapped the RAB13 gene to chromosome
1q21.3 based on an alignment of the RAB13 sequence (GenBank GENBANK
BC073168) with the genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 2/17/2011.
2. Leek, J. P.; Hamlin, P. J.; Wilton, J.; Lench, N. J.: Assignment
of the Rab13 gene (RAB13) to human chromosome band 12q13 by in situ
hybridization. Cytogenet. Cell Genet. 79: 210-211, 1997.
3. Novick, P.; Zerial, M.: The diversity of Rab proteins in vesicle
transport. Curr. Opin. Cell Biol. 9: 496-504, 1997.
4. Salminen, A.; Novick, P. J.: A ras-like protein is required for
a post-Golgi event in yeast secretion. Cell 49: 527-538, 1987.
5. Zahraoui, A.; Joberty, G.; Arpin, M.; Fontaine, J. J.; Hellio,
R.; Tavitian, A.; Louvard, D.: A small rab GTPase is distributed
in cytoplasmic vesicles in nonpolarized cells but colocalizes with
the tight junction marker ZO-1 in polarized epithelial cells. J.
Cell. Biol. 124: 101-115, 1994.
*FIELD* CN
Matthew B. Gross - updated: 02/17/2011
Patti M. Sherman - updated: 7/30/1998
*FIELD* CD
Victor A. McKusick: 5/30/1998
*FIELD* ED
mgross: 02/17/2011
alopez: 2/4/2009
alopez: 3/22/1999
carol: 8/3/1998
carol: 5/30/1998
*RECORD*
*FIELD* NO
602672
*FIELD* TI
*602672 RAS-ASSOCIATED PROTEIN RAB13; RAB13
*FIELD* TX
CLONING
The Rab proteins comprise the largest group of Ras-associated small
read moreGTPases and in mammalian cells at least 40 proteins have been identified
(Novick and Zerial, 1997). Rab proteins are specific regulators of
vesicular traffic and the complexity of the Rab protein family
correlates with the diversity of cellular vesicle transport routes. A
different Rab protein may be required for each step of vesicular
transport. For example, the yeast Sec4 protein appears to be required
exclusively for the delivery of Golgi-derived secretory vesicles to the
plasma membrane (Salminen and Novick, 1987). By screening a human
intestinal epithelial cell (Caco-2) cDNA library with a degenerate
oligonucleotide based on a sequence present in the effector domain of
the Sec4 protein, Zahraoui et al. (1994) isolated a cDNA encoding RAB13.
The predicted 203-amino acid protein has the typical structural features
of Ras-related proteins, including a conserved GTP-binding site. RAB13
displays 61% and 56% amino acid identity with the human RAB8 (165040)
and yeast Sec4 proteins, respectively. These proteins share a long
conserved N-terminal region but have divergent C-terminal portions.
Northern blot analysis showed that RAB13 is expressed as a 1.2-kb
transcript in Caco-2 cells. Immunoblot analysis using antibodies against
RAB13 detected a 24-kD protein in Caco-2 cell lysates.
Immunofluorescence studies demonstrated that RAB13 colocalizes with the
tight junction marker ZO1 (TJP1; 601009) in epithelial cells. In cells
devoid of tight junctions, RAB13 associates with vesicles dispersed
throughout the cytoplasm.
MAPPING
Leek et al. (1997) mapped the RAB13 gene to chromosome 12q13 by in situ
hybridization. However, Gross (2011) mapped the RAB13 gene to chromosome
1q21.3 based on an alignment of the RAB13 sequence (GenBank GENBANK
BC073168) with the genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 2/17/2011.
2. Leek, J. P.; Hamlin, P. J.; Wilton, J.; Lench, N. J.: Assignment
of the Rab13 gene (RAB13) to human chromosome band 12q13 by in situ
hybridization. Cytogenet. Cell Genet. 79: 210-211, 1997.
3. Novick, P.; Zerial, M.: The diversity of Rab proteins in vesicle
transport. Curr. Opin. Cell Biol. 9: 496-504, 1997.
4. Salminen, A.; Novick, P. J.: A ras-like protein is required for
a post-Golgi event in yeast secretion. Cell 49: 527-538, 1987.
5. Zahraoui, A.; Joberty, G.; Arpin, M.; Fontaine, J. J.; Hellio,
R.; Tavitian, A.; Louvard, D.: A small rab GTPase is distributed
in cytoplasmic vesicles in nonpolarized cells but colocalizes with
the tight junction marker ZO-1 in polarized epithelial cells. J.
Cell. Biol. 124: 101-115, 1994.
*FIELD* CN
Matthew B. Gross - updated: 02/17/2011
Patti M. Sherman - updated: 7/30/1998
*FIELD* CD
Victor A. McKusick: 5/30/1998
*FIELD* ED
mgross: 02/17/2011
alopez: 2/4/2009
alopez: 3/22/1999
carol: 8/3/1998
carol: 5/30/1998