Reviewed, UniProtKB/Swiss-Prot P57735 (RAB25_HUMAN)

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 not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May selectively regulate the apical recycling and/or transcytotic pathways By similarity.
Subunit structure	Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. Ref.6
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-1050500,EBI-1050500
D2HGDH	Q8N465	1	EBI-1050500,EBI-1053783
PKIG	Q9Y2B9	1	EBI-1050500,EBI-1052231

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 – 26

8

GTP By similarity

Nucleotide binding

67 – 71

5

GTP By similarity

Nucleotide binding

125 – 128

4

GTP By similarity

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)
	P57735-1 [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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.632469

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P57735. 5 interactions.

Proteomic databases

PRIDE

P57735.

Genome annotation databases

Ensembl

ENSG00000132698. Homo sapiens. [Contig view]

GeneID

57111.

KEGG

hsa:57111.

Organism-specific databases

GeneCards

GC01P154297.

H-InvDB

HIX0001145.

HGNC

HGNC:18238. RAB25.

HPA

HPA010872.

PharmGKB

PA34115.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P57735.

OMA

P57735. EDDYNFV.

Gene expression databases

ArrayExpress

P57735.

Bgee

P57735.

CleanEx

HS_RAB25.

GermOnline

ENSG00000132698. Homo sapiens.

Family and domain databases

InterPro

IPR003579. GTPase_Rab.
IPR015595. Rab11.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]

PANTHER

PTHR11708:SF213. Rab11. 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

62967.

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:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)