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P51153 (RAB13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-13
Alternative name(s):
Cell growth-inhibiting gene 4 protein
Gene names
Name:RAB13
ORF Names:GIG4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18

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. Ref.17

Subunit structure

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. Ref.10 Ref.12 Ref.14 Ref.18 Ref.21

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Cell junctiontight junction. Golgi apparatustrans-Golgi network membrane. Recycling endosome membrane. Cell projectionlamellipodium By similarity. Cytoplasmic vesiclesecretory vesicle membrane By similarity. Note: Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions. Relocalizes to the leading edge of lamellipodia in migrating endothelial cells. Ref.1 Ref.11 Ref.13 Ref.15

Tissue specificity

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

Induction

Up-regulated during osteoclast differentiation. Ref.17 Ref.23

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasmic vesicle
Endosome
Golgi apparatus
Membrane
Tight junction
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from experiment. Source: GOC

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cortical actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

endocytic recycling

Inferred from mutant phenotype Ref.13. Source: UniProtKB

endosomal transport

Inferred from mutant phenotype Ref.15. Source: UniProtKB

endothelial cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of Sertoli cell barrier

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of protein localization to plasma membrane

Inferred from mutant phenotype Ref.12. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

neuron projection development

Inferred from mutant phenotype Ref.18. Source: UniProtKB

protein kinase A signaling

Inferred from mutant phenotype Ref.12. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

tight junction assembly

Inferred from mutant phenotype Ref.11Ref.12. Source: UniProtKB

trans-Golgi network to recycling endosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic vesicle

Inferred from direct assay Ref.1. Source: UniProtKB

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

endocytic vesicle

Inferred from direct assay Ref.13. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

insulin-responsive compartment

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

lateral plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

neuron projection

Inferred from direct assay Ref.18. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.13Ref.15. Source: UniProtKB

recycling endosome

Inferred from direct assay Ref.15. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

tight junction

Inferred from direct assay Ref.11Ref.1. Source: UniProtKB

trans-Golgi network

Inferred from direct assay Ref.15. Source: UniProtKB

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from direct assay Ref.17. Source: UniProtKB

GTPase activity

Inferred from experiment. Source: Reactome

protein binding

Inferred from physical interaction Ref.18Ref.21Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Leprotl1Q6PDU44EBI-1780121,EBI-8702651From a different organism.
Micall2Q3TN348EBI-1780121,EBI-1779852From a different organism.
PDE6DO439242EBI-1780121,EBI-712685

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Ras-related protein Rab-13
PRO_0000121182
Propeptide201 – 2033Removed in mature form Potential
PRO_0000370756

Regions

Nucleotide binding15 – 228GTP By similarity
Nucleotide binding63 – 675GTP By similarity
Nucleotide binding121 – 1244GTP By similarity
Motif37 – 459Effector region By similarity

Amino acid modifications

Modified residue1781Phosphoserine Ref.16 Ref.19 Ref.22
Modified residue2001Cysteine methyl ester Potential
Lipidation2001S-geranylgeranyl cysteine Ref.9

Experimental info

Mutagenesis221T → N: Dominant negative. Ref.15
Mutagenesis671Q → 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. Ref.15

Sequences

Sequence LengthMass (Da)Tools
P51153 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 141621CB998178DA

FASTA20322,774
        10         20         30         40         50         60 
MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNNTYIST IGIDFKIRTV DIEGKKIKLQ 

        70         80         90        100        110        120 
VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ NWMKSIKENA SAGVERLLLG 

       130        140        150        160        170        180 
NKCDMEAKRK VQKEQADKLA REHGIRFFET SAKSSMNVDE AFSSLARDIL LKSGGRRSGN 

       190        200 
GNKPPSTDLK TCDKKNTNKC SLG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"MICAL-like1 mediates epidermal growth factor receptor endocytosis."
Abou-Zeid N., Pandjaitan R., Sengmanivong L., David V., Le Pavec G., Salamero J., Zahraoui A.
Mol. Biol. Cell 22:3431-3441(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1058.1.
PIRA49647.
RefSeqNP_001258967.1. NM_001272038.1.
NP_002861.1. NM_002870.3.
UniGeneHs.151536.

3D structure databases

ProteinModelPortalP51153.
SMRP51153. Positions 6-172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111810. 8 interactions.
DIPDIP-40268N.
IntActP51153. 9 interactions.
MINTMINT-3018790.
STRING9606.ENSP00000357564.

PTM databases

PhosphoSiteP51153.

Polymorphism databases

DMDM1710016.

Proteomic databases

MaxQBP51153.
PaxDbP51153.
PRIDEP51153.

Protocols and materials databases

DNASU5872.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368575; ENSP00000357564; ENSG00000143545.
GeneID5872.
KEGGhsa:5872.
UCSCuc001fdt.2. human.

Organism-specific databases

CTD5872.
GeneCardsGC01M153954.
HGNCHGNC:9762. RAB13.
HPAHPA003996.
MIM602672. gene.
neXtProtNX_P51153.
PharmGKBPA34103.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG009351.
InParanoidP51153.
KOK06109.
OMAKVQREQA.
OrthoDBEOG7VB2H4.
PhylomeDBP51153.
TreeFamTF314097.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressP51153.
BgeeP51153.
CleanExHS_RAB13.
GenevestigatorP51153.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB13. human.
GeneWikiRAB13.
GenomeRNAi5872.
NextBio22808.
PROP51153.
SOURCESearch...

Entry information

Entry nameRAB13_HUMAN
AccessionPrimary (citable) accession number: P51153
Secondary accession number(s): A8K6B5 expand/collapse secondary AC list , D3DV67, Q5U0A6, Q6GPG6, Q96GU4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM