Ras-related protein Rab-5A - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P20339 (RAB5A_HUMAN)

Last modified June 16, 2009. Version 109. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Ras-related protein Rab-5A

Gene names

Name:	RAB5A
Synonyms:	RAB5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Required for the fusion of plasma membranes and early endosomes.
Enzyme regulation	Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP.
Subunit structure	Binds EEA1. Interacts with RIN1 and GAPVD1, which regulate its pathway, probably by acting as a GEF. Interacts with ALS2CL, UNC84B, ZFYVE20 and RUFY1. Interacts with SGSM1 and SGSM3 By similarity.
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Early endosome membrane; Lipid-anchor By similarity. Melanosome. Note: Enriched in stage I melanosomes.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

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Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Endosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Phosphoprotein Prenylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	endocytosis Traceable author statement. Source: ProtInc protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
EEA1	Q15075	3	EBI-399437,EBI-298113
PIK3R1	P23727	2	EBI-399437,EBI-520244	From a different organism.
RAB5C	P51148	1	EBI-399437,EBI-1054923
RIN1	Q13671	1	EBI-399437,EBI-366017

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

Ras-related protein Rab-5A

PRO_0000121104

Regions

Nucleotide binding

27 – 34

GTP By similarity

Nucleotide binding

75 – 79

GTP By similarity

Nucleotide binding

133 – 136

GTP By similarity

Motif

49 – 57

Effector region By similarity

Amino acid modifications

Modified residue

202

Phosphothreonine Ref.13

Modified residue

205

Phosphothreonine Ref.13

Modified residue

208

Phosphothreonine Ref.13

Lipidation

212

S-geranylgeranyl cysteine

Lipidation

213

S-geranylgeranyl cysteine

Experimental info

Sequence conflict

R → G in AAA60245. Ref.1

Sequence conflict

197

R → G in AAA60245. Ref.1

Secondary structure

215

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P20339-1 [UniParc].

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

215

23,659

        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

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References

	« Hide 'large scale' referencesShow '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: 2501306] [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: 7991565] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ISOPRENYLATION AT CYS-212 AND CYS-213, MASS SPECTROMETRY.
[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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix and Placenta.
[5]	"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: 10491193] [Abstract] Cited for: INTERACTION WITH EEA1.
[6]	"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: 10818110] [Abstract] Cited for: INTERACTION WITH UNC84B.
[7]	"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: 11062261] [Abstract] Cited for: INTERACTION WITH ZFYVE20. Tissue: Cervix carcinoma.
[8]	"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: 11703925] [Abstract] Cited for: ACTIVATION BY RIN1.
[9]	"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: 15388334] [Abstract] Cited for: INTERACTION WITH ALS2CL.
[10]	"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: 14617813] [Abstract] Cited for: INTERACTION WITH RUFY1.
[11]	"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: 16410077] [Abstract] Cited for: INTERACTION WITH GAPVD1.
[12]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202; THR-205 AND THR-208, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"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: 12433916] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M28215 mRNA. Translation: AAA60245.1.
AF498936 mRNA. Translation: AAM21084.1.
BC001267 mRNA. Translation: AAH01267.1.
BC018288 mRNA. Translation: AAH18288.1.

IPI

IPI00023510.

PIR

F34323.

RefSeq

NP_004153.2.

UniGene

Hs.475663

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N6H	X-ray	1.51	A	15-184	[»]
1N6I	X-ray	1.60	A	15-184	[»]
1N6K	X-ray	1.55	A	15-184	[»]
1N6L	X-ray	1.60	A	15-184	[»]
1N6N	X-ray	1.60	A	15-184	[»]
1N6O	X-ray	1.80	A	15-184	[»]
1N6P	X-ray	1.54	A	15-184	[»]
1N6R	X-ray	1.55	A	15-184	[»]
1R2Q	X-ray	1.05	A	15-184	[»]
1TU3	X-ray	2.31	A/B/C/D/E	15-184	[»]
1TU4	X-ray	2.20	A/B/C/D	15-184	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:380N.

IntAct

P20339. 8 interactions.

PTM databases

PhosphoSite

P20339.

Proteomic databases

PRIDE

P20339.

Genome annotation databases

Ensembl

ENSG00000144566. Homo sapiens. [Contig view]

GeneID

5868.

KEGG

hsa:5868.

Organism-specific databases

GeneCards

GC03P019963.

H-InvDB

HIX0003118.

HGNC

HGNC:9783. RAB5A.

HPA

CAB004567.

MIM

179512. gene.

PharmGKB

PA34143.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P20339.

HOVERGEN

P20339.

OMA

P20339. PTRNQCC.

Enzyme and pathway databases

Pathway_Interaction_DB

p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Gene expression databases

ArrayExpress

P20339.

Bgee

P20339.

CleanEx

HS_RAB5A.

GermOnline

ENSG00000144566. Homo sapiens.

Family and domain databases

InterPro

IPR003579. GTPase_Rab.
IPR015599. Rab5-like.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]

PANTHER

PTHR11708:SF254. Rab5_like. 1 hit.

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

22790.

SOURCE

Search...

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Entry information

Entry name

RAB5A_HUMAN

Accession

Primary (citable) accession number: P20339

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 3

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents