P61006 (RAB8A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-8A

Alternative name(s):
Oncogene c-mel

Gene names

Name:	RAB8A
Synonyms:	MEL, RAB8

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization. Ref.15 Ref.18
Subunit structure	Interacts with MAP4K2 and SYTL4. Interacts with SGSM1 and SGSM3 By similarity. Interacts with RABIF, RIMS2, RPH3A and RPH3A By similarity. Interacts with OPTN. Interacts with RAB3IP. Interacts with MYO5B. Interacts with PIFO. Interacts with BIRC6/bruce. Interacts with OCRL. Ref.9 Ref.10 Ref.12 Ref.14 Ref.18 Ref.21
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Golgi apparatus. Cytoplasm › perinuclear region. Cell projection. Cytoplasmic vesicle › phagosome. Cytoplasmic vesicle › phagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane. In the GDP-bound form, present in the perinuclear region. Shows a polarized distribution to distal regions of cell protrusions in the GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.9 Ref.10 Ref.15 Ref.20
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Cell projection Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane
Disease	Proto-oncogene
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome Golgi vesicle fusion to target membrane Inferred from direct assay PubMed 17574030. Source: BHF-UCL axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB cilium assembly Inferred from direct assay PubMed 17574030. Source: BHF-UCL protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of long-term neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara regulation of protein transport Inferred from electronic annotation. Source: Compara small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro vesicle docking involved in exocytosis Inferred from direct assay PubMed 17574030. Source: BHF-UCL
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome cytoplasmic vesicle membrane Traceable author statement. Source: Reactome microtubule basal body Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara nonmotile primary cilium Inferred from direct assay PubMed 17574030. Source: BHF-UCL perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic vesicle Inferred from direct assay Ref.20. Source: UniProtKB phagocytic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from electronic annotation. Source: Compara recycling endosome Inferred from electronic annotation. Source: Compara
Molecular_function	GDP binding Inferred from direct assay PubMed 20937701. Source: UniProtKB GTP binding Inferred from direct assay PubMed 20937701. Source: UniProtKB GTPase activity Inferred from experiment. Source: Reactome Rab GTPase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 204

204

Ras-related protein Rab-8A

PRO_0000121130

Propeptide

205 – 207

3

Removed in mature form Potential

PRO_0000370793

Regions

Nucleotide binding

15 – 22

8

GTP By similarity

Nucleotide binding

63 – 67

5

GTP By similarity

Nucleotide binding

121 – 124

4

GTP By similarity

Motif

37 – 45

9

Effector region By similarity

Amino acid modifications

Modified residue

181

1

Phosphoserine Ref.16

Modified residue

185

1

Phosphoserine Ref.11 Ref.16 Ref.19

Modified residue

204

1

Cysteine methyl ester Potential

Lipidation

204

1

S-geranylgeranyl cysteine Ref.8

Experimental info

Sequence conflict

177 – 183

7

LEGNSPQ → WKATAP in AAB19681. Ref.2

Secondary structure

1

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207

Helix Strand Turn

Details...

Beta strand

8 – 14

7

Helix

21 – 30

10

Beta strand

41 – 52

12

Beta strand

55 – 63

9

Helix

68 – 70

3

Helix

71 – 74

4

Helix

75 – 77

3

Beta strand

82 – 89

8

Helix

93 – 97

5

Helix

99 – 109

11

Beta strand

115 – 121

7

Helix

126 – 128

3

Helix

133 – 142

10

Beta strand

146 – 149

4

Turn

152 – 155

4

Helix

158 – 175

18

Sequences

	Sequence		Length	Mass (Da)
	P61006 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: AA52DBF54A2CD056	FASTA	207	23,668
	10 20 30 40 50 60 MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI ELDGKRIKLQ 70 80 90 100 110 120 IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR NWIRNIEEHA SADVEKMILG 130 140 150 160 170 180 NKCDVNDKRQ VSKERGEKLA LDYGIKFMET SAKANINVEN AFFTLARDIK AKMDKKLEGN 190 200 SPQGSNQGVK ITPDQQKRSS FFRCVLL

References

	« Hide 'large scale' referencesShow '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].
[2]	"The MEL gene: a new member of the RAB/YPT class of RAS-related genes." Nimmo E.R., Sanders P.G., Padua R.A., Hughes D., Williamson R., Johnson K.J. Oncogene 6:1347-1351(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [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]	"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Skin.
[8]	"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-204.
[9]	"A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport." Hattula K., Furuhjelm J., Arffman A., Peranen J. Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB3IP, SUBCELLULAR LOCATION. Tissue: Brain.
[10]	"Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis." Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., Buss F. J. Cell Biol. 169:285-295(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OPTN.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Final stages of cytokinesis and midbody ring formation are controlled by BRUCE." Pohl C., Jentsch S. Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BIRC6/BRUCE.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"Pitchfork regulates primary cilia disassembly and left-right asymmetry." Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H. Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIFO.
[15]	"A molecular network for de novo generation of the apical surface and lumen." Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E. Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"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-181 AND SER-185, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization." Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R. Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MYO5B.
[19]	"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-185, MASS SPECTROMETRY.
[20]	"Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes." Seto S., Tsujimura K., Koide Y. Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[21]	"OCRL localizes to the primary cilium: a new role for cilia in Lowe syndrome." Luo N., West C.C., Murga-Zamalloa C.A., Sun L., Anderson R.M., Wells C.D., Weinreb R.N., Travers J.B., Khanna H., Sun Y. Hum. Mol. Genet. 21:3333-3344(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH OCRL.
[22]	"A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1." Hou X., Hagemann N., Schoebel S., Blankenfeldt W., Goody R.S., Erdmann K.S., Itzen A. EMBO J. 30:1659-1670(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-176 IN COMPLEX WITH OCRL.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X56741 mRNA. Translation: CAA40065.1.
S53268 mRNA. Translation: AAB19681.1.
AF498943 mRNA. Translation: AAM21091.1.
BT007184 mRNA. Translation: AAP35848.1.
CR536583 mRNA. Translation: CAG38820.1.
CR542274 mRNA. Translation: CAG47070.1.
CH471106 Genomic DNA. Translation: EAW84526.1.
BC002977 mRNA. Translation: AAH02977.1.

IPI

IPI00028481.

PIR

B49647.

RefSeq

NP_005361.2. NM_005370.4.

UniGene

Hs.642874.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QBT	X-ray	2.00	A/C/E/G	6-176	[»]
3TNF	X-ray	2.50	A	6-176	[»]

ProteinModelPortal

P61006.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-43703N.

IntAct

P61006. 6 interactions.

MINT

MINT-1416277.

STRING

9606.ENSP00000300935.

PTM databases

PhosphoSite

P61006.

Polymorphism databases

DMDM

46810392.

Proteomic databases

PaxDb

P61006.

PeptideAtlas

P61006.

PRIDE

P61006.

Protocols and materials databases

DNASU

4218.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300935; ENSP00000300935; ENSG00000167461.

GeneID

4218.

KEGG

hsa:4218.

UCSC

uc002ndn.4. human.

Organism-specific databases

CTD

4218.

GeneCards

GC19P016222.

HGNC

HGNC:7007. RAB8A.

MIM

165040. gene.

neXtProt

NX_P61006.

PharmGKB

PA30743.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

P61006.

KO

K07901.

OMA

SNVEQHA.

OrthoDB

EOG4K3KX6.

PhylomeDB

P61006.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpress

P61006.

Bgee

P61006.

CleanEx

HS_RAB8A.

Genevestigator

P61006.

GermOnline

ENSG00000167461. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAB8A. human.

GenomeRNAi

4218.

NextBio

16637.

SOURCE

Search...

Entry information

Entry name

RAB8A_HUMAN

Accession

Primary (citable) accession number: P61006
Secondary accession number(s): P24407, Q6FHV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	May 29, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.