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P20339 (RAB5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-5A
Gene names
Name:RAB5A
Synonyms:RAB5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
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. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. Ref.10 Ref.14 Ref.15 Ref.17 Ref.24

Enzyme regulation

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP.

Subunit structure

Interacts with SGSM1 and SGSM3 By similarity. Interacts with PIK3CB By similarity. Interacts with GDI1; this promotes dissociation from membranes. Interacts with EEA1. Interacts with RIN1 and GAPVD1, which regulate its pathway, probably by acting as a GEF. Interacts with RINL. Interacts with ALS2CL, SUN2, ZFYVE20 and RUFY1. Interacts with RABEP1; one RABEP1 homodimer binds two RAB5A chains, but at opposite sides of the dimer. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.21 Ref.24 Ref.25

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Early endosome membrane; Lipid-anchor By similarity. Melanosome. Cytoplasmic vesicle By similarity. Cell projectionruffle By similarity. Membrane. Cytoplasmcytosol. Note: Enriched in stage I melanosomes. Alternates between membrane-bound and cytosolic forms. Ref.18 Ref.21

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processDifferentiation
Endocytosis
Neurogenesis
Protein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Endosome
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.24. Source: GOC

blood coagulation

Traceable author statement. Source: Reactome

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

endocytosis

Inferred from direct assay Ref.24. Source: UniProtKB

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of exocytosis

Inferred from mutant phenotype PubMed 19966785. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

receptor internalization involved in canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 16890161. Source: BHF-UCL

regulation of filopodium assembly

Inferred from direct assay Ref.15. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 21266579. Source: MGI

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome

Inferred from direct assay Ref.24. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

endosome membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane raft

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGDP binding

Inferred from direct assay Ref.24. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.24. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.24. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Ras-related protein Rab-5A
PRO_0000121104

Regions

Nucleotide binding27 – 359GTP
Nucleotide binding46 – 527GTP
Nucleotide binding75 – 795GTP
Nucleotide binding133 – 1364GTP
Nucleotide binding163 – 1653GTP
Motif49 – 579Effector region By similarity

Amino acid modifications

Lipidation2121S-geranylgeranyl cysteine Ref.2
Lipidation2131S-geranylgeranyl cysteine Ref.2

Experimental info

Mutagenesis541G → Q: Strongly decreases ZFYVE20 binding affinity. Ref.16
Mutagenesis561A → E: Strongly decreases ZFYVE20 binding affinity. Ref.16
Mutagenesis571F → A: Strongly decreases RABEP1 and ZFYVE20 binding affinity. Ref.16 Ref.24
Mutagenesis741W → A: Strongly decreases RABEP1 binding affinity. Ref.24
Mutagenesis791Q → L: Loss of GTPase activity. Does not inhibit filopodia formation. Ref.15 Ref.24
Mutagenesis821Y → A: Strongly decreases RABEP1 binding affinity. Impairs endosome fusion. Ref.24
Mutagenesis891Y → A: Strongly decreases RABEP1 binding affinity. Ref.24
Mutagenesis1161K → E: No effect on RABEP1 binding affinity. Ref.24
Mutagenesis1201R → E: No effect on RABEP1 binding affinity. Ref.24
Sequence conflict811R → G in AAA60245. Ref.1
Sequence conflict1971R → G in AAA60245. Ref.1

Secondary structure

............................. 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20339 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: EC03DDF96BBEF821

FASTA21523,659
        10         20         30         40         50         60 
MASRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQ 

        70         80         90        100        110        120 
TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFAR AKNWVKELQR 

       130        140        150        160        170        180 
QASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTSMNV NEIFMAIAKK 

       190        200        210 
LPKNEPQNPG ANSARGRGVD LTEPTQPTRN QCCSN 

« Hide

References

« Hide 'large scale' references
[1]"The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion."
Zahraoui A., Touchot N., Chardin P., Tavitian A.
J. Biol. Chem. 264:12394-12401(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."
Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.
Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ISOPRENYLATION AT CYS-212 AND CYS-213, IDENTIFICATION BY MASS SPECTROMETRY.
[3]"Identification of a new oncogene in human cancers."
Kim J.W.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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.
[5]"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: Brain.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]Mural R.J., Istrail S., Sutton 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 (JUL-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: Cervix and Placenta.
[9]"Direct interaction of EEA1 with Rab5b."
Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.
Eur. J. Biochem. 265:361-366(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EEA1.
[10]"A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion."
Hoffenberg S., Liu X., Nikolova L., Hall H.S., Dai W., Baughn R.E., Dickey B.F., Barbieri M.A., Aballay A., Stahl P.D., Knoll B.J.
J. Biol. Chem. 275:24661-24669(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUN2, FUNCTION.
[11]"Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain."
Nielsen E., Christoforidis S., Uttenweiler-Joseph S., Miaczynska M., Dewitte F., Wilm M., Hoflack B., Zerial M.
J. Cell Biol. 151:601-612(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFYVE20.
Tissue: Cervix carcinoma.
[12]"Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1."
Tall G.G., Barbieri M.A., Stahl P.D., Horazdovsky B.F.
Dev. Cell 1:73-82(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION BY RIN1.
[13]"ALS2CL, the novel protein highly homologous to the carboxy-terminal half of ALS2, binds to Rab5 and modulates endosome dynamics."
Hadano S., Otomo A., Suzuki-Utsunomiya K., Kunita R., Yanagisawa Y., Showguchi-Miyata J., Mizumura H., Ikeda J.-E.
FEBS Lett. 575:64-70(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALS2CL.
[14]"Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes."
Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J., van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.
Mol. Biol. Cell 15:611-624(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RUFY1.
[15]"Regulation of dendritic branching and filopodia formation in hippocampal neurons by specific acylated protein motifs."
Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.
Mol. Biol. Cell 15:2205-2217(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLN-79.
[16]"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
Eathiraj S., Pan X., Ritacco C., Lambright D.G.
Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFYVE20, MUTAGENESIS OF GLY-54; ALA-56 AND PHE-57.
[17]"Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis."
Hunker C.M., Galvis A., Kruk I., Giambini H., Veisaga M.L., Barbieri M.A.
Biochem. Biophys. Res. Commun. 340:967-975(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GAPVD1.
[18]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[19]"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: 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]"Rab1a and Rab5a preferentially bind to binary lipid compositions with higher stored curvature elastic energy."
Kirsten M.L., Baron R.A., Seabra M.C., Ces O.
Mol. Membr. Biol. 30:303-314(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GDI1, SUBCELLULAR LOCATION.
[22]"High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop."
Zhu G., Liu J., Terzyan S., Zhai P., Li G., Zhang X.C.
J. Biol. Chem. 278:2452-2460(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[23]"Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution."
Terzyan S., Zhu G., Li G., Zhang X.C.
Acta Crystallogr. D 60:54-60(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 15-184 IN COMPLEX WITH GTP ANALOG.
[24]"Structural basis of Rab5-Rabaptin5 interaction in endocytosis."
Zhu G., Zhai P., Liu J., Terzyan S., Li G., Zhang X.C.
Nat. Struct. Mol. Biol. 11:975-983(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-184 IN COMPLEX WITH GTP ANALOG; GDP AND RABEP1, FUNCTION, INTERACTION WITH RABEP1, MUTAGENESIS OF PHE-57; TRP-74; GLN-79; TYR-82; TYR-89; LYS-116 AND ARG-120.
[25]"Structural basis for Rab GTPase recognition and endosome tethering by the C2H2 zinc finger of early endosomal autoantigen 1 (EEA1)."
Mishra A., Eathiraj S., Corvera S., Lambright D.G.
Proc. Natl. Acad. Sci. U.S.A. 107:10866-10871(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 16-183 OF MUTANT LEU-79 IN COMPLEX WITH EEA1, INTERACTION WITH EEA1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28215 mRNA. Translation: AAA60245.1.
AF464088 mRNA. Translation: AAO15677.1.
AF498936 mRNA. Translation: AAM21084.1.
AK312618 mRNA. Translation: BAG35504.1.
CR536492 mRNA. Translation: CAG38731.1.
CH471055 Genomic DNA. Translation: EAW64301.1.
BC001267 mRNA. Translation: AAH01267.1.
BC018288 mRNA. Translation: AAH18288.1.
PIRF34323.
RefSeqNP_004153.2. NM_004162.4.
UniGeneHs.475663.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N6HX-ray1.51A15-184[»]
1N6IX-ray1.60A15-184[»]
1N6KX-ray1.55A15-184[»]
1N6LX-ray1.60A15-184[»]
1N6NX-ray1.60A15-184[»]
1N6OX-ray1.80A15-184[»]
1N6PX-ray1.54A15-184[»]
1N6RX-ray1.55A15-184[»]
1R2QX-ray1.05A15-184[»]
1TU3X-ray2.31A/B/C/D/E15-184[»]
1TU4X-ray2.20A/B/C/D15-184[»]
3MJHX-ray2.03A/C16-183[»]
ProteinModelPortalP20339.
SMRP20339. Positions 15-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111806. 63 interactions.
DIPDIP-380N.
IntActP20339. 21 interactions.
MINTMINT-209361.
STRING9606.ENSP00000273047.

PTM databases

PhosphoSiteP20339.

Polymorphism databases

DMDM1346958.

Proteomic databases

PaxDbP20339.
PRIDEP20339.

Protocols and materials databases

DNASU5868.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273047; ENSP00000273047; ENSG00000144566.
GeneID5868.
KEGGhsa:5868.
UCSCuc003cbn.3. human.

Organism-specific databases

CTD5868.
GeneCardsGC03P019963.
HGNCHGNC:9783. RAB5A.
HPACAB004567.
MIM179512. gene.
neXtProtNX_P20339.
PharmGKBPA34143.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP20339.
KOK07887.
OMARYWIREL.
OrthoDBEOG77DJ7M.
PhylomeDBP20339.
TreeFamTF300199.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP20339.
BgeeP20339.
CleanExHS_RAB5A.
GenevestigatorP20339.

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

ChiTaRSRAB5A. human.
EvolutionaryTraceP20339.
GeneWikiRAB5A.
GenomeRNAi5868.
NextBio22790.
PROP20339.
SOURCESearch...

Entry information

Entry nameRAB5A_HUMAN
AccessionPrimary (citable) accession number: P20339
Secondary accession number(s): Q6FI44
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 159 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM