P57735 (RAB25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-25

Alternative name(s):
CATX-8

Gene names

Name:	RAB25
Synonyms:	CATX8

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	213 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	Involved in the regulation of cell survival. Promotes invasive migration of cells in which it functions to localize and maintain integrin alpha-V/beta-1 at the tips of extending pseudopodia. Increases the rates of ovarian and breast cancers progression and aggressiveness by modulating cellular processes such as proliferation, survival and migration of epithelial tumor cells. May selectively regulate the apical recycling pathway. Together with MYO5B regulates transcytosis By similarity. Ref.7 Ref.8
Subunit structure	Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. Interacts (via the hypervariable C-terminal region) with ITGB1 (via the cytoplasmic region); the interaction is GTP-dependent. Interacts with ITGAV. Associates with the integrin alpha-V/beta-1 heterodimer. Ref.6 Ref.8
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Cell projection › pseudopodium membrane. Cytoplasmic vesicle. Note: Colocalizes with integrin alpha-V/beta-1 in vesicles at the pseudopodial tips.
Tissue specificity	Expressed in ovarian epithelium (NOE) and breast tissue. Expressed in ovarian cancer; expression is increased relative to NOE cells. Expression in ovarian cancer is stage dependent, with stage III and stage IV showing higher levels than early stage cancers. Expressed in breast cancer; expression is increased relative to normal breast tissue. Ref.7
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.
Sequence caution	The sequence AAF98238.1 differs from that shown. Reason: Frameshift at position 196. The sequence AAM69362.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Cell projection Cytoplasmic vesicle Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of cell proliferation Inferred from direct assay Ref.7. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW pseudopodium organization Inferred from direct assay Ref.8. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell pseudopodium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 210

210

Ras-related protein Rab-25

PRO_0000121215

Propeptide

211 – 213

3

Removed in mature form Potential

PRO_0000370821

Regions

Nucleotide binding

19 – 27

9

GTP

Nucleotide binding

67 – 71

5

GTP By similarity

Nucleotide binding

125 – 128

4

GTP

Nucleotide binding

155 – 157

3

GTP

Motif

41 – 49

9

Effector region By similarity

Amino acid modifications

Modified residue

210

1

Cysteine methyl ester Potential

Lipidation

209

1

S-geranylgeranyl cysteine By similarity

Lipidation

210

1

S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict

203

1

P → L in AAF98238. Ref.1

Secondary structure

1

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213

Helix Strand Turn

Details...

Beta strand

10 – 20

11

Helix

25 – 34

10

Beta strand

45 – 56

12

Beta strand

59 – 69

11

Helix

78 – 82

5

Beta strand

87 – 93

7

Helix

97 – 101

5

Helix

103 – 111

9

Beta strand

119 – 125

7

Helix

127 – 132

6

Helix

137 – 146

10

Beta strand

150 – 154

5

Turn

156 – 158

3

Helix

162 – 178

17

Sequences

	Sequence		Length	Mass (Da)
	P57735 [UniParc]. Last modified April 26, 2004. Version 2. Checksum: 119523C3036C370E	FASTA	213	23,496
	10 20 30 40 50 60 MGNGTEEDYN FVFKVVLIGE SGVGKTNLLS RFTRNEFSHD SRTTIGVEFS TRTVMLGTAA 70 80 90 100 110 120 VKAQIWDTAG LERYRAITSA YYRGAVGALL VFDLTKHQTY AVVERWLKEL YDHAEATIVV 130 140 150 160 170 180 MLVGNKSDLS QAREVPTEEA RMFAENNGLL FLETSALDST NVELAFETVL KEIFAKVSKQ 190 200 210 RQNSIRTNAI TLGSAQAGQE PGPGEKRACC ISL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of novel genes from human colonic epithelial cells." Wang L., Kairo A., Gao Z.Q., Gao Z.P., Boman B.M. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Colon.
[2]	Yu L. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Ovary, Pancreas and Skin.
[6]	"Identification and characterization of a family of Rab11-interacting proteins." Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R. J. Biol. Chem. 276:39067-39075(2001) [PubMed: 11495908] [Abstract] Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
[7]	"The RAB25 small GTPase determines aggressiveness of ovarian and breast cancers." Cheng K.W., Lahad J.P., Kuo W.L., Lapuk A., Yamada K., Auersperg N., Liu J., Smith-McCune K., Lu K.H., Fishman D., Gray J.W., Mills G.B. Nat. Med. 10:1251-1256(2004) [PubMed: 15502842] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[8]	"Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments." Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K., Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I., McCaffrey M.W., Ozanne B.W., Norman J.C. Dev. Cell 13:496-510(2007) [PubMed: 17925226] [Abstract] Cited for: FUNCTION, INTERACTION WITH ITGAV AND ITGB1.
[9]	"Crystal structure of human RAB25 in complex with GDP." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 7-180 IN COMPLEX WITH GDP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF083124 mRNA. Translation: AAF98238.1. Frameshift.
AF274025 mRNA. Translation: AAM69362.1. Different initiation.
AL355388 Genomic DNA. Translation: CAH72638.1.
CH471121 Genomic DNA. Translation: EAW53003.1.
BC004416 mRNA. Translation: AAH04416.1.
BC009831 mRNA. Translation: AAH09831.1.
BC033322 mRNA. Translation: AAH33322.1.

IPI

IPI00027993.

RefSeq

NP_065120.2. NM_020387.2.

UniGene

Hs.632469.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OIL	X-ray	2.30	A	7-180	[»]

ProteinModelPortal

P57735.

SMR

P57735. Positions 7-180.

ModBase

Search...

Protein-protein interaction databases

STRING

P57735.

PTM databases

PhosphoSite

P57735.

Polymorphism databases

DMDM

46577696.

Proteomic databases

PRIDE

P57735.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361084; ENSP00000354376; ENSG00000132698.

GeneID

57111.

KEGG

hsa:57111.

UCSC

uc001fnc.1. human.

Organism-specific databases

CTD

57111.

GeneCards

GC01P156030.

H-InvDB

HIX0001145.

HGNC

HGNC:18238. RAB25.

HPA

HPA010872.

MIM

612942. gene.

neXtProt

NX_P57735.

PharmGKB

PA34115.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13023.

GeneTree

ENSGT00600000084094.

HOGENOM

HBG745225.

HOVERGEN

HBG009351.

InParanoid

P57735.

OMA

MGSDEAY.

OrthoDB

EOG4NS3CK.

PhylomeDB

P57735.

Gene expression databases

ArrayExpress

P57735.

Bgee

P57735.

CleanEx

HS_RAB25.

Genevestigator

P57735.

GermOnline

ENSG00000132698. Homo sapiens.

Family and domain databases

InterPro

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

KO

K07906.

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

NextBio

62967.

SOURCE

Search...

Entry information

Entry name

RAB25_HUMAN

Accession

Primary (citable) accession number: P57735
Secondary accession number(s): Q5VYA2 , Q8NG24, Q96GB1, Q9BT12

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	April 26, 2004
Last modified:	January 25, 2012
This is version 108 of the entry and version 2 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.