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Ras-related protein Rab-13 (Cell growth-inhibiting gene 4 protein)

 RAB13_HUMAN             Reviewed;         203 AA.
P51153; A8K6B5; D3DV67; Q5U0A6; Q6GPG6; Q96GU4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
20-DEC-2017, entry version 178.
RecName: Full=Ras-related protein Rab-13;
AltName: Full=Cell growth-inhibiting gene 4 protein;
Flags: Precursor;
Name=RAB13; ORFNames=GIG4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=8294494; DOI=10.1083/jcb.124.1.101;
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 non
polarized cells but colocalizes with the tight junction marker ZO-1 in
polarized epithelial cells.";
J. Cell Biol. 124:101-115(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human growth inhibition gene 4 (GIG4).";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary, Placenta, and PNS;
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).
[9]
ISOPRENYLATION AT CYS-200.
PubMed=8375503; DOI=10.1016/0014-5793(93)80897-4;
Joberty G., Tavitian A., Zahraoui A.;
"Isoprenylation of Rab proteins possessing a C-terminal CaaX motif.";
FEBS Lett. 330:323-328(1993).
[10]
INTERACTION WITH PDE6D.
PubMed=9712853; DOI=10.1074/jbc.273.35.22340;
Marzesco A.M., Galli T., Louvard D., Zahraoui A.;
"The rod cGMP phosphodiesterase delta subunit dissociates the small
GTPase Rab13 from membranes.";
J. Biol. Chem. 273:22340-22345(1998).
[11]
FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND SUBCELLULAR LOCATION.
PubMed=12058051; DOI=10.1091/mbc.02-02-0029;
Marzesco A.M., Dunia I., Pandjaitan R., Recouvreur M., Dauzonne D.,
Benedetti E.L., Louvard D., Zahraoui A.;
"The small GTPase Rab13 regulates assembly of functional tight
junctions in epithelial cells.";
Mol. Biol. Cell 13:1819-1831(2002).
[12]
FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND INTERACTION WITH PRKACA.
PubMed=15096524; DOI=10.1083/jcb.200312118;
Koehler K., Louvard D., Zahraoui A.;
"Rab13 regulates PKA signaling during tight junction assembly.";
J. Cell Biol. 165:175-180(2004).
[13]
FUNCTION IN ENDOCYTIC RECYCLING, AND SUBCELLULAR LOCATION.
PubMed=15528189; DOI=10.1074/jbc.M406906200;
Morimoto S., Nishimura N., Terai T., Manabe S., Yamamoto Y.,
Shinahara W., Miyake H., Tashiro S., Shimada M., Sasaki T.;
"Rab13 mediates the continuous endocytic recycling of occludin to the
cell surface.";
J. Biol. Chem. 280:2220-2228(2005).
[14]
FUNCTION IN TIGHT JUNCTION ASSEMBLY, AND INTERACTION WITH MICALL2.
PubMed=16525024; DOI=10.1091/mbc.E05-09-0826;
Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
"JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
endocytic recycling of occludin.";
Mol. Biol. Cell 17:2465-2475(2006).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-22 AND GLN-67.
PubMed=18779367; DOI=10.1083/jcb.200802176;
Nokes R.L., Fields I.C., Collins R.N., Foelsch H.;
"Rab13 regulates membrane trafficking between TGN and recycling
endosomes in polarized epithelial cells.";
J. Cell Biol. 182:845-853(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
ENZYME REGULATION.
PubMed=20937701; DOI=10.1083/jcb.201008051;
Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
"Family-wide characterization of the DENN domain Rab GDP-GTP exchange
factors.";
J. Cell Biol. 191:367-381(2010).
[18]
FUNCTION IN NEURITE OUTGROWTH, AND INTERACTION WITH MICALL2.
PubMed=20008558; DOI=10.1128/MCB.01067-09;
Sakane A., Honda K., Sasaki T.;
"Rab13 regulates neurite outgrowth in PC12 cells through its effector
protein, JRAB/MICAL-L2.";
Mol. Cell. Biol. 30:1077-1087(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
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).
[21]
INTERACTION WITH MICALL1.
TISSUE=Uterine adenocarcinoma;
PubMed=21795389; DOI=10.1091/mbc.E11-01-0030;
Abou-Zeid N., Pandjaitan R., Sengmanivong L., David V., Le Pavec G.,
Salamero J., Zahraoui A.;
"MICAL-like1 mediates epidermal growth factor receptor endocytosis.";
Mol. Biol. Cell 22:3431-3441(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
INDUCTION.
PubMed=22562557; DOI=10.1369/0022155412448069;
Hirvonen M.J., Mulari M.T., Bueki K.G., Vihko P., Haerkoenen P.L.,
Vaeaenaenen H.K.;
"Rab13 is upregulated during osteoclast differentiation and associates
with small vesicles revealing polarized distribution in resorbing
cells.";
J. Histochem. Cytochem. 60:537-549(2012).
[24]
INTERACTION WITH MICAL1; MICALCL; MICAL3; EHBP1 AND EHBP1L1.
PubMed=27552051; DOI=10.7554/eLife.18675;
Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S.,
Gazdag E.M., Muller M.P.;
"bMERB domains are bivalent Rab8 family effectors evolved by gene
duplication.";
Elife 5:E18675-E18675(2016).
-!- 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 sets of downstream
effectors directly responsible for vesicle formation, movement,
tethering and fusion. That Rab is involved in endocytic recycling
and regulates the transport to the plasma membrane of
transmembrane proteins like the tight junction protein
OCLN/occludin. Thereby, it regulates the assembly and the activity
of tight junctions. Moreover, it may also regulate tight junction
assembly by activating the PKA signaling pathway and by
reorganizing the actin cytoskeleton through the activation of the
downstream effectors PRKACA and MICALL2 respectively. Through its
role in tight junction assembly, may play a role in the
establishment of Sertoli cell barrier. Plays also a role in
angiogenesis through regulation of endothelial cells chemotaxis.
Also involved in neurite outgrowth. Has also been proposed to play
a role in post-Golgi membrane trafficking from the TGN to the
recycling endosome. Finally, it has been involved in insulin-
induced transport to the plasma membrane of the glucose
transporter GLUT4 and therefore may play a role in glucose
homeostasis. {ECO:0000269|PubMed:12058051,
ECO:0000269|PubMed:15096524, ECO:0000269|PubMed:15528189,
ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:18779367,
ECO:0000269|PubMed:20008558}.
-!- ENZYME REGULATION: Rab activation is generally mediated by a
guanine exchange factor (GEF), while inactivation through
hydrolysis of bound GTP is catalyzed by a GTPase activating
protein (GAP). That Rab may be activated by DENND1C, a guanine
exchange factor. Activated in response to insulin.
{ECO:0000269|PubMed:20937701}.
-!- SUBUNIT: Interacts (GTP-bound form) with MICALL2; competes with
RAB8A and is involved in tight junctions assembly. Interacts (GTP-
bound form) with MICALL1. Interacts (GTP-bound form) with MICAL1,
MICAL3, MICALCL, EHBP1 and EHBP1L1; ternary complexes of RAB8A,
RAB13 and either MICAL1 or EHBP1L1 are possible. Interacts with
PRKACA; downstream effector of RAB13 involved in tight junction
assembly. Interacts with GRB2; may recruit RAB13 to the leading
edge of migrating endothelial cells where it can activate RHOA.
Interacts (isoprenylated form) with PDE6D; dissociates RAB13 from
membranes. Interacts with BICDL2/BICDR2. Interacts with LEPROT and
LEPROTL1. {ECO:0000269|PubMed:15096524,
ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:20008558,
ECO:0000269|PubMed:21795389, ECO:0000269|PubMed:27552051,
ECO:0000269|PubMed:9712853}.
-!- INTERACTION:
Q6PDU4:Leprotl1 (xeno); NbExp=4; IntAct=EBI-1780121, EBI-8702651;
Q3TN34:Micall2 (xeno); NbExp=8; IntAct=EBI-1780121, EBI-1779852;
O43924:PDE6D; NbExp=2; IntAct=EBI-1780121, EBI-712685;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15528189};
Lipid-anchor {ECO:0000305|PubMed:8375503}; Cytoplasmic side
{ECO:0000305|PubMed:8375503}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:15528189, ECO:0000269|PubMed:8294494}; Lipid-
anchor {ECO:0000305|PubMed:8375503}; Cytoplasmic side
{ECO:0000305|PubMed:8375503}. Cell junction, tight junction
{ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:8294494}. Golgi
apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:18779367}. Recycling endosome membrane
{ECO:0000269|PubMed:18779367}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:Q9DD03}. Note=Tight junctions or associated
with vesicles scattered throughout the cytoplasm in cells lacking
tight junctions (PubMed:8294494). Relocalizes to the leading edge
of lamellipodia in migrating endothelial cells (By similarity).
{ECO:0000250|UniProtKB:Q9DD03, ECO:0000269|PubMed:8294494}.
-!- TISSUE SPECIFICITY: Detected in several types of epithelia,
including intestine, kidney, liver and in endothelial cells.
-!- INDUCTION: Up-regulated during osteoclast differentiation.
{ECO:0000269|PubMed:22562557}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; X75593; CAA53266.1; -; mRNA.
EMBL; AY423722; AAS00485.1; -; mRNA.
EMBL; AF498948; AAM21096.1; -; mRNA.
EMBL; AK291580; BAF84269.1; -; mRNA.
EMBL; BT019700; AAV38506.1; -; mRNA.
EMBL; BT019701; AAV38507.1; -; mRNA.
EMBL; AL358472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53249.1; -; Genomic_DNA.
EMBL; CH471121; EAW53250.1; -; Genomic_DNA.
EMBL; BC000799; AAH00799.1; -; mRNA.
EMBL; BC009227; AAH09227.2; -; mRNA.
EMBL; BC073168; AAH73168.2; -; mRNA.
CCDS; CCDS1058.1; -.
PIR; A49647; A49647.
RefSeq; NP_001258967.1; NM_001272038.1.
RefSeq; NP_002861.1; NM_002870.3.
UniGene; Hs.151536; -.
ProteinModelPortal; P51153; -.
SMR; P51153; -.
BioGrid; 111810; 21.
DIP; DIP-40268N; -.
IntAct; P51153; 12.
MINT; MINT-3018790; -.
STRING; 9606.ENSP00000357564; -.
iPTMnet; P51153; -.
PhosphoSitePlus; P51153; -.
SwissPalm; P51153; -.
DMDM; 1710016; -.
EPD; P51153; -.
MaxQB; P51153; -.
PaxDb; P51153; -.
PeptideAtlas; P51153; -.
PRIDE; P51153; -.
DNASU; 5872; -.
Ensembl; ENST00000368575; ENSP00000357564; ENSG00000143545.
GeneID; 5872; -.
KEGG; hsa:5872; -.
UCSC; uc001fdt.3; human.
CTD; 5872; -.
DisGeNET; 5872; -.
EuPathDB; HostDB:ENSG00000143545.8; -.
GeneCards; RAB13; -.
HGNC; HGNC:9762; RAB13.
HPA; HPA003996; -.
MIM; 602672; gene.
neXtProt; NX_P51153; -.
OpenTargets; ENSG00000143545; -.
PharmGKB; PA34103; -.
eggNOG; KOG0078; Eukaryota.
eggNOG; ENOG410XPUI; LUCA.
GeneTree; ENSGT00890000139330; -.
HOVERGEN; HBG009351; -.
InParanoid; P51153; -.
KO; K06109; -.
OMA; ENFFLAW; -.
OrthoDB; EOG091G0LA6; -.
PhylomeDB; P51153; -.
TreeFam; TF314097; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; RAB13; human.
GeneWiki; RAB13; -.
GenomeRNAi; 5872; -.
PRO; PR:P51153; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143545; -.
CleanEx; HS_RAB13; -.
ExpressionAtlas; P51153; baseline and differential.
Genevisible; P51153; HS.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; TAS:Reactome.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:Ensembl.
GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
GO; GO:0097368; P:establishment of Sertoli cell barrier; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0010737; P:protein kinase A signaling; IMP:UniProtKB.
GO; GO:1902463; P:protein localization to cell leading edge; IEA:Ensembl.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0044795; P:trans-Golgi network to recycling endosome transport; ISS: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;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding;
Lipoprotein; Membrane; Methylation; Nucleotide-binding;
Phosphoprotein; Prenylation; Protein transport; Reference proteome;
Tight junction; Transport.
CHAIN 1 200 Ras-related protein Rab-13.
/FTId=PRO_0000121182.
PROPEP 201 203 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000370756.
NP_BIND 15 22 GTP. {ECO:0000250}.
NP_BIND 63 67 GTP. {ECO:0000250}.
NP_BIND 121 124 GTP. {ECO:0000250}.
MOTIF 37 45 Effector region. {ECO:0000250}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 200 200 Cysteine methyl ester. {ECO:0000255}.
LIPID 200 200 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:8375503}.
MUTAGEN 22 22 T->N: Dominant negative.
{ECO:0000269|PubMed:18779367}.
MUTAGEN 67 67 Q->L: Constitutively active mutant locked
in the active GTP-bound form. Impairs
transports of cargo from the trans-Golgi
network to the recycling endosomes and
alters the assembly of functional tight
junctions. {ECO:0000269|PubMed:18779367}.
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


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