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Protein

Ras-related protein Rab-13

Gene

RAB13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Enzyme regulationi

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228GTPBy similarity
Nucleotide bindingi63 – 675GTPBy similarity
Nucleotide bindingi121 – 1244GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: Reactome
  • GTP binding Source: UniProtKB

GO - Biological processi

  • bicellular tight junction assembly Source: UniProtKB
  • cellular response to insulin stimulus Source: UniProtKB
  • cortical actin cytoskeleton organization Source: UniProtKB
  • endocytic recycling Source: UniProtKB
  • endosomal transport Source: UniProtKB
  • endothelial cell chemotaxis Source: UniProtKB
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • establishment of Sertoli cell barrier Source: UniProtKB
  • intracellular protein transport Source: GO_Central
  • membrane organization Source: Reactome
  • metabolic process Source: GOC
  • neuron projection development Source: UniProtKB
  • protein kinase A signaling Source: UniProtKB
  • protein localization to cell leading edge Source: Ensembl
  • Rab protein signal transduction Source: GO_Central
  • trans-Golgi network to recycling endosome transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-13
Alternative name(s):
Cell growth-inhibiting gene 4 protein
Gene namesi
Name:RAB13
ORF Names:GIG4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9762. RAB13.

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • cytoplasm Source: HPA
  • cytoplasmic vesicle Source: UniProtKB
  • cytoplasmic vesicle membrane Source: Reactome
  • endocytic vesicle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • insulin-responsive compartment Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • lateral plasma membrane Source: UniProtKB
  • neuron projection Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • recycling endosome Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB-SubCell
  • trans-Golgi network Source: UniProtKB
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221T → N: Dominant negative. 1 Publication
Mutagenesisi67 – 671Q → 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. 1 Publication

Organism-specific databases

PharmGKBiPA34103.

Polymorphism and mutation databases

DMDMi1710016.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 200200Ras-related protein Rab-13PRO_0000121182Add
BLAST
Propeptidei201 – 2033Removed in mature formSequence AnalysisPRO_0000370756

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781Phosphoserine3 Publications
Modified residuei200 – 2001Cysteine methyl esterSequence Analysis
Lipidationi200 – 2001S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP51153.
PaxDbiP51153.
PRIDEiP51153.

PTM databases

PhosphoSiteiP51153.

Expressioni

Tissue specificityi

Detected in several types of epithelia, including intestine, kidney, liver and in endothelial cells.

Inductioni

Up-regulated during osteoclast differentiation.1 Publication

Gene expression databases

BgeeiP51153.
CleanExiHS_RAB13.
ExpressionAtlasiP51153. baseline.
GenevisibleiP51153. HS.

Organism-specific databases

HPAiHPA003996.

Interactioni

Subunit structurei

Interacts (GTP-bound form) with MICALL2; competes with RAB8A and is involved in tight junctions assembly. Interacts (GTP-bound form) with MICALL1. 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 CCDC64B/BICDR2. Interacts with LEPROT and LEPROTL1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Leprotl1Q6PDU44EBI-1780121,EBI-8702651From a different organism.
Micall2Q3TN348EBI-1780121,EBI-1779852From a different organism.
PDE6DO439242EBI-1780121,EBI-712685

Protein-protein interaction databases

BioGridi111810. 9 interactions.
DIPiDIP-40268N.
IntActiP51153. 9 interactions.
MINTiMINT-3018790.
STRINGi9606.ENSP00000357564.

Structurei

3D structure databases

ProteinModelPortaliP51153.
SMRiP51153. Positions 6-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 459Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOVERGENiHBG009351.
InParanoidiP51153.
KOiK06109.
OMAiKVQREQA.
OrthoDBiEOG7VB2H4.
PhylomeDBiP51153.
TreeFamiTF314097.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNNTYIST IGIDFKIRTV
60 70 80 90 100
DIEGKKIKLQ VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ
110 120 130 140 150
NWMKSIKENA SAGVERLLLG NKCDMEAKRK VQKEQADKLA REHGIRFFET
160 170 180 190 200
SAKSSMNVDE AFSSLARDIL LKSGGRRSGN GNKPPSTDLK TCDKKNTNKC

SLG
Length:203
Mass (Da):22,774
Last modified:October 1, 1996 - v1
Checksum:i141621CB998178DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75593 mRNA. Translation: CAA53266.1.
AY423722 mRNA. Translation: AAS00485.1.
AF498948 mRNA. Translation: AAM21096.1.
AK291580 mRNA. Translation: BAF84269.1.
BT019700 mRNA. Translation: AAV38506.1.
BT019701 mRNA. Translation: AAV38507.1.
AL358472 Genomic DNA. Translation: CAI14031.1.
CH471121 Genomic DNA. Translation: EAW53249.1.
CH471121 Genomic DNA. Translation: EAW53250.1.
BC000799 mRNA. Translation: AAH00799.1.
BC009227 mRNA. Translation: AAH09227.2.
BC073168 mRNA. Translation: AAH73168.2.
CCDSiCCDS1058.1.
PIRiA49647.
RefSeqiNP_001258967.1. NM_001272038.1.
NP_002861.1. NM_002870.3.
UniGeneiHs.151536.

Genome annotation databases

EnsembliENST00000368575; ENSP00000357564; ENSG00000143545.
GeneIDi5872.
KEGGihsa:5872.
UCSCiuc001fdt.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75593 mRNA. Translation: CAA53266.1.
AY423722 mRNA. Translation: AAS00485.1.
AF498948 mRNA. Translation: AAM21096.1.
AK291580 mRNA. Translation: BAF84269.1.
BT019700 mRNA. Translation: AAV38506.1.
BT019701 mRNA. Translation: AAV38507.1.
AL358472 Genomic DNA. Translation: CAI14031.1.
CH471121 Genomic DNA. Translation: EAW53249.1.
CH471121 Genomic DNA. Translation: EAW53250.1.
BC000799 mRNA. Translation: AAH00799.1.
BC009227 mRNA. Translation: AAH09227.2.
BC073168 mRNA. Translation: AAH73168.2.
CCDSiCCDS1058.1.
PIRiA49647.
RefSeqiNP_001258967.1. NM_001272038.1.
NP_002861.1. NM_002870.3.
UniGeneiHs.151536.

3D structure databases

ProteinModelPortaliP51153.
SMRiP51153. Positions 6-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111810. 9 interactions.
DIPiDIP-40268N.
IntActiP51153. 9 interactions.
MINTiMINT-3018790.
STRINGi9606.ENSP00000357564.

PTM databases

PhosphoSiteiP51153.

Polymorphism and mutation databases

DMDMi1710016.

Proteomic databases

MaxQBiP51153.
PaxDbiP51153.
PRIDEiP51153.

Protocols and materials databases

DNASUi5872.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368575; ENSP00000357564; ENSG00000143545.
GeneIDi5872.
KEGGihsa:5872.
UCSCiuc001fdt.2. human.

Organism-specific databases

CTDi5872.
GeneCardsiGC01M153954.
HGNCiHGNC:9762. RAB13.
HPAiHPA003996.
MIMi602672. gene.
neXtProtiNX_P51153.
PharmGKBiPA34103.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOVERGENiHBG009351.
InParanoidiP51153.
KOiK06109.
OMAiKVQREQA.
OrthoDBiEOG7VB2H4.
PhylomeDBiP51153.
TreeFamiTF314097.

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

ChiTaRSiRAB13. human.
GeneWikiiRAB13.
GenomeRNAii5872.
NextBioi22808.
PROiP51153.
SOURCEiSearch...

Gene expression databases

BgeeiP51153.
CleanExiHS_RAB13.
ExpressionAtlasiP51153. baseline.
GenevisibleiP51153. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Zahraoui A., Joberty G., Arpin M., Fontaine J.J., Hellio R., Tavitian A., Louvard D.
    J. Cell Biol. 124:101-115(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "Identification of a human growth inhibition gene 4 (GIG4)."
    Kim J.W.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    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.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary, Placenta and PNS.
  9. "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif."
    Joberty G., Tavitian A., Zahraoui A.
    FEBS Lett. 330:323-328(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-200.
  10. "The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes."
    Marzesco A.M., Galli T., Louvard D., Zahraoui A.
    J. Biol. Chem. 273:22340-22345(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDE6D.
  11. "The small GTPase Rab13 regulates assembly of functional tight junctions in epithelial cells."
    Marzesco A.M., Dunia I., Pandjaitan R., Recouvreur M., Dauzonne D., Benedetti E.L., Louvard D., Zahraoui A.
    Mol. Biol. Cell 13:1819-1831(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TIGHT JUNCTION ASSEMBLY, SUBCELLULAR LOCATION.
  12. "Rab13 regulates PKA signaling during tight junction assembly."
    Koehler K., Louvard D., Zahraoui A.
    J. Cell Biol. 165:175-180(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TIGHT JUNCTION ASSEMBLY, INTERACTION WITH PRKACA.
  13. "Rab13 mediates the continuous endocytic recycling of occludin to the cell surface."
    Morimoto S., Nishimura N., Terai T., Manabe S., Yamamoto Y., Shinahara W., Miyake H., Tashiro S., Shimada M., Sasaki T.
    J. Biol. Chem. 280:2220-2228(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOCYTIC RECYLING, SUBCELLULAR LOCATION.
  14. "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin."
    Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.
    Mol. Biol. Cell 17:2465-2475(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TIGHT JUNCTION ASSEMBLY, INTERACTION WITH MICALL2.
  15. "Rab13 regulates membrane trafficking between TGN and recycling endosomes in polarized epithelial cells."
    Nokes R.L., Fields I.C., Collins R.N., Foelsch H.
    J. Cell Biol. 182:845-853(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-22 AND GLN-67.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors."
    Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.
    J. Cell Biol. 191:367-381(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  18. "Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/MICAL-L2."
    Sakane A., Honda K., Sasaki T.
    Mol. Cell. Biol. 30:1077-1087(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEURITE OUTGROWTH, INTERACTION WITH MICALL2.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: INTERACTION WITH MICALL1.
    Tissue: Uterine adenocarcinoma.
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Rab13 is upregulated during osteoclast differentiation and associates with small vesicles revealing polarized distribution in resorbing cells."
    Hirvonen M.J., Mulari M.T., Bueki K.G., Vihko P., Haerkoenen P.L., Vaeaenaenen H.K.
    J. Histochem. Cytochem. 60:537-549(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiRAB13_HUMAN
AccessioniPrimary (citable) accession number: P51153
Secondary accession number(s): A8K6B5
, D3DV67, Q5U0A6, Q6GPG6, Q96GU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.