RAB13_HUMAN
ID RAB13_HUMAN Reviewed; 203 AA.
AC P51153; A8K6B5; D3DV67; Q5U0A6; Q6GPG6; Q96GU4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 207.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Tavitian A.,
RA Louvard D.;
RT "A small rab GTPase is distributed in cytoplasmic vesicles in non polarized
RT cells but colocalizes with the tight junction marker ZO-1 in polarized
RT 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 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].
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., 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].
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 (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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., 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 [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 project:
RT 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 GTPase
RT 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 junctions in
RT 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 RECYCLING, AND SUBCELLULAR LOCATION.
RX PubMed=15528189; DOI=10.1074/jbc.m406906200;
RA Morimoto S., Nishimura N., Terai T., Manabe S., Yamamoto Y., Shinahara W.,
RA Miyake H., Tashiro S., Shimada M., Sasaki T.;
RT "Rab13 mediates the continuous endocytic recycling of occludin to the cell
RT 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 endosomes
RT in polarized epithelial cells.";
RL J. Cell Biol. 182:845-853(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 ACTIVITY 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., 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 [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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT 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 with
RT small vesicles revealing polarized distribution in resorbing cells.";
RL J. Histochem. Cytochem. 60:537-549(2012).
RN [24]
RP INTERACTION WITH MICAL1; MICALCL; MICAL3; EHBP1 AND EHBP1L1.
RX PubMed=27552051; DOI=10.7554/elife.18675;
RA Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S.,
RA Gazdag E.M., Muller M.P.;
RT "bMERB domains are bivalent Rab8 family effectors evolved by gene
RT duplication.";
RL Elife 5:E18675-E18675(2016).
RN [25]
RP STEAROYLATION AT LYS-194; LYS-195 AND LYS-199 (MICROBIAL INFECTION), AND
RP MUTAGENESIS OF 194-LYS--LYS-199.
RX PubMed=30061757; DOI=10.1038/s41564-018-0215-6;
RA Liu W., Zhou Y., Peng T., Zhou P., Ding X., Li Z., Zhong H., Xu Y.,
RA Chen S., Hang H.C., Shao F.;
RT "Nepsilon-fatty acylation of multiple membrane-associated proteins by
RT Shigella IcsB effector to modulate host function.";
RL Nat. Microbiol. 3:996-1009(2018).
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 sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is involved in
CC endocytic recycling and regulates the transport to the plasma membrane
CC of transmembrane proteins like the tight junction protein
CC OCLN/occludin. Thereby, it regulates the assembly and the activity of
CC tight junctions. Moreover, it may also regulate tight junction assembly
CC by activating the PKA signaling pathway and by reorganizing the actin
CC cytoskeleton through the activation of the downstream effectors PRKACA
CC and MICALL2 respectively. Through its role in tight junction assembly,
CC may play a role in the establishment of Sertoli cell barrier. Plays
CC also a role in angiogenesis through regulation of endothelial cells
CC chemotaxis. Also involved in neurite outgrowth. Has also been proposed
CC to play a role in post-Golgi membrane trafficking from the TGN to the
CC recycling endosome. Finally, it has been involved in insulin-induced
CC transport to the plasma membrane of the glucose transporter GLUT4 and
CC therefore may play a role in glucose homeostasis.
CC {ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:15096524,
CC ECO:0000269|PubMed:15528189, ECO:0000269|PubMed:16525024,
CC ECO:0000269|PubMed:18779367, ECO:0000269|PubMed:20008558}.
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). That Rab may be
CC activated by DENND1C, a guanine exchange factor. Activated in response
CC to insulin. {ECO:0000269|PubMed:20937701}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with MICALL2; competes with RAB8A
CC and is involved in tight junctions assembly. Interacts (GTP-bound form)
CC with MICALL1. Interacts (GTP-bound form) with MICAL1, MICAL3, MICALCL,
CC EHBP1 and EHBP1L1; ternary complexes of RAB8A, RAB13 and either MICAL1
CC or EHBP1L1 are possible. Interacts with PRKACA; downstream effector of
CC RAB13 involved in tight junction assembly. Interacts with GRB2; may
CC recruit RAB13 to the leading edge of migrating endothelial cells where
CC it can activate RHOA. Interacts (isoprenylated form) with PDE6D;
CC dissociates RAB13 from membranes. Interacts with BICDL2/BICDR2.
CC Interacts with LEPROT and LEPROTL1. {ECO:0000269|PubMed:15096524,
CC ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:20008558,
CC ECO:0000269|PubMed:21795389, ECO:0000269|PubMed:27552051,
CC ECO:0000269|PubMed:9712853}.
CC -!- INTERACTION:
CC P51153; O43924: PDE6D; NbExp=2; IntAct=EBI-1780121, EBI-712685;
CC P51153; Q6PDU4: Leprotl1; Xeno; NbExp=4; IntAct=EBI-1780121, EBI-8702651;
CC P51153; Q3TN34: Micall2; Xeno; NbExp=8; IntAct=EBI-1780121, EBI-1779852;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15528189};
CC Lipid-anchor {ECO:0000305|PubMed:8375503}; Cytoplasmic side
CC {ECO:0000305|PubMed:8375503}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:15528189, ECO:0000269|PubMed:8294494}; Lipid-anchor
CC {ECO:0000305|PubMed:8375503}; Cytoplasmic side
CC {ECO:0000305|PubMed:8375503}. Cell junction, tight junction
CC {ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:8294494}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18779367}.
CC Recycling endosome membrane {ECO:0000269|PubMed:18779367}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q9DD03}. Note=Tight
CC junctions or associated with vesicles scattered throughout the
CC cytoplasm in cells lacking tight junctions (PubMed:8294494).
CC Relocalizes to the leading edge of lamellipodia in migrating
CC endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q9DD03,
CC ECO:0000269|PubMed:8294494}.
CC -!- TISSUE SPECIFICITY: Detected in several types of epithelia, including
CC intestine, kidney, liver and in endothelial cells.
CC -!- INDUCTION: Up-regulated during osteoclast differentiation.
CC {ECO:0000269|PubMed:22562557}.
CC -!- PTM: (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty
CC acyltransferase IcsB, thereby disrupting the host actin cytoskeleton.
CC {ECO:0000269|PubMed:30061757}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS1058.1; -.
DR PIR; A49647; A49647.
DR RefSeq; NP_001258967.1; NM_001272038.1.
DR RefSeq; NP_002861.1; NM_002870.3.
DR AlphaFoldDB; P51153; -.
DR SMR; P51153; -.
DR BioGRID; 111810; 108.
DR CORUM; P51153; -.
DR DIP; DIP-40268N; -.
DR IntAct; P51153; 30.
DR MINT; P51153; -.
DR STRING; 9606.ENSP00000357564; -.
DR iPTMnet; P51153; -.
DR PhosphoSitePlus; P51153; -.
DR SwissPalm; P51153; -.
DR BioMuta; RAB13; -.
DR DMDM; 1710016; -.
DR EPD; P51153; -.
DR jPOST; P51153; -.
DR MassIVE; P51153; -.
DR MaxQB; P51153; -.
DR PaxDb; P51153; -.
DR PeptideAtlas; P51153; -.
DR PRIDE; P51153; -.
DR ProteomicsDB; 56286; -.
DR Antibodypedia; 1206; 140 antibodies from 30 providers.
DR DNASU; 5872; -.
DR Ensembl; ENST00000368575.5; ENSP00000357564.3; ENSG00000143545.10.
DR GeneID; 5872; -.
DR KEGG; hsa:5872; -.
DR MANE-Select; ENST00000368575.5; ENSP00000357564.3; NM_002870.5; NP_002861.1.
DR UCSC; uc001fdt.3; human.
DR CTD; 5872; -.
DR DisGeNET; 5872; -.
DR GeneCards; RAB13; -.
DR HGNC; HGNC:9762; RAB13.
DR HPA; ENSG00000143545; Low tissue specificity.
DR MIM; 602672; gene.
DR neXtProt; NX_P51153; -.
DR OpenTargets; ENSG00000143545; -.
DR PharmGKB; PA34103; -.
DR VEuPathDB; HostDB:ENSG00000143545; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000159989; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P51153; -.
DR OMA; LINIRNW; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P51153; -.
DR TreeFam; TF314097; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P51153; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P51153; -.
DR SIGNOR; P51153; -.
DR BioGRID-ORCS; 5872; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; RAB13; human.
DR GeneWiki; RAB13; -.
DR GenomeRNAi; 5872; -.
DR Pharos; P51153; Tbio.
DR PRO; PR:P51153; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P51153; protein.
DR Bgee; ENSG00000143545; Expressed in stromal cell of endometrium and 94 other tissues.
DR ExpressionAtlas; P51153; baseline and differential.
DR Genevisible; P51153; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; TAS:Reactome.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0005886; C:plasma membrane; 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:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
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:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; ISS:UniProtKB.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling; IMP:UniProtKB.
DR GO; GO:1902463; P:protein localization to cell leading edge; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0044795; P:trans-Golgi network to recycling endosome transport; ISS:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; 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 Cell junction; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Tight junction; Transport.
FT CHAIN 1..200
FT /note="Ras-related protein Rab-13"
FT /id="PRO_0000121182"
FT PROPEP 201..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370756"
FT REGION 173..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 200
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 194
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT LIPID 195
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT LIPID 199
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:8375503"
FT MUTAGEN 22
FT /note="T->N: Dominant negative."
FT /evidence="ECO:0000269|PubMed:18779367"
FT MUTAGEN 67
FT /note="Q->L: Constitutively active mutant locked in the
FT active GTP-bound form. Impairs transports of cargo from the
FT trans-Golgi network to the recycling endosomes and alters
FT the assembly of functional tight junctions."
FT /evidence="ECO:0000269|PubMed:18779367"
FT MUTAGEN 194..199
FT /note="KKNTNK->RRNTNR: In 3KR mutant; abolished
FT stearoylation in response to S.flexneri infection."
FT /evidence="ECO:0000269|PubMed:30061757"
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
