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Protein

Ras-related protein Rab-25

Gene

RAB25

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (PubMed:17925226). Involved in the regulation of epithelial morphogenesis through the control of CLDN4 expression and localization at tight junctions (By similarity). May selectively regulate the apical recycling pathway. Together with MYO5B regulates transcytosis (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279GTP
Nucleotide bindingi67 – 715GTPBy similarity
Nucleotide bindingi125 – 1284GTP
Nucleotide bindingi155 – 1573GTP

GO - Molecular functioni

  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • myosin V binding Source: UniProtKB

GO - Biological processi

  • epithelial cell morphogenesis Source: UniProtKB
  • exocytosis Source: GO_Central
  • intracellular protein transport Source: GO_Central
  • melanosome transport Source: GO_Central
  • metabolic process Source: GOC
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of epithelial cell migration Source: UniProtKB
  • pseudopodium organization Source: UniProtKB
  • Rab protein signal transduction Source: GO_Central
  • regulation of vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-25
Alternative name(s):
CATX-8
Gene namesi
Name:RAB25Imported
Synonyms:CATX8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18238. RAB25.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • pseudopodium Source: UniProtKB
  • pseudopodium membrane Source: UniProtKB-SubCell
  • recycling endosome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34115.

Polymorphism and mutation databases

BioMutaiRAB25.
DMDMi46577696.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Ras-related protein Rab-25PRO_0000121215Add
BLAST
Propeptidei211 – 2133Removed in mature formSequence AnalysisPRO_0000370821

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi209 – 2091S-geranylgeranyl cysteineBy similarity
Modified residuei210 – 2101Cysteine methyl esterSequence Analysis
Lipidationi210 – 2101S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP57735.
PaxDbiP57735.
PRIDEiP57735.

PTM databases

PhosphoSiteiP57735.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP57735.
CleanExiHS_RAB25.
GenevisibleiP57735. HS.

Organism-specific databases

HPAiHPA010872.

Interactioni

Subunit structurei

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.3 Publications

Protein-protein interaction databases

BioGridi121377. 14 interactions.
STRINGi9606.ENSP00000354376.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 199Combined sources
Helixi25 – 3410Combined sources
Beta strandi46 – 5611Combined sources
Beta strandi59 – 6810Combined sources
Helixi78 – 825Combined sources
Beta strandi87 – 937Combined sources
Helixi97 – 1015Combined sources
Helixi103 – 1119Combined sources
Beta strandi119 – 1257Combined sources
Helixi127 – 1326Combined sources
Helixi137 – 14610Combined sources
Beta strandi150 – 1534Combined sources
Turni156 – 1583Combined sources
Helixi162 – 17716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OILX-ray2.30A7-180[»]
3TSOX-ray1.80A/B7-180[»]
ProteinModelPortaliP57735.
SMRiP57735. Positions 10-178.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57735.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi41 – 499Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP57735.
KOiK07906.
OrthoDBiEOG7SFHZ2.
PhylomeDBiP57735.
TreeFamiTF300099.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P57735-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNGTEEDYN FVFKVVLIGE SGVGKTNLLS RFTRNEFSHD SRTTIGVEFS
60 70 80 90 100
TRTVMLGTAA VKAQIWDTAG LERYRAITSA YYRGAVGALL VFDLTKHQTY
110 120 130 140 150
AVVERWLKEL YDHAEATIVV MLVGNKSDLS QAREVPTEEA RMFAENNGLL
160 170 180 190 200
FLETSALDST NVELAFETVL KEIFAKVSKQ RQNSIRTNAI TLGSAQAGQE
210
PGPGEKRACC ISL
Length:213
Mass (Da):23,496
Last modified:April 26, 2004 - v2
Checksum:i119523C3036C370E
GO

Sequence cautioni

The sequence AAF98238.1 differs from that shown. Reason: Frameshift at position 196. Curated
The sequence AAM69362.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031P → L in AAF98238 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41413.1.
RefSeqiNP_065120.2. NM_020387.2.
UniGeneiHs.632469.

Genome annotation databases

EnsembliENST00000361084; ENSP00000354376; ENSG00000132698.
GeneIDi57111.
KEGGihsa:57111.
UCSCiuc001fnc.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41413.1.
RefSeqiNP_065120.2. NM_020387.2.
UniGeneiHs.632469.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OILX-ray2.30A7-180[»]
3TSOX-ray1.80A/B7-180[»]
ProteinModelPortaliP57735.
SMRiP57735. Positions 10-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121377. 14 interactions.
STRINGi9606.ENSP00000354376.

PTM databases

PhosphoSiteiP57735.

Polymorphism and mutation databases

BioMutaiRAB25.
DMDMi46577696.

Proteomic databases

MaxQBiP57735.
PaxDbiP57735.
PRIDEiP57735.

Protocols and materials databases

DNASUi57111.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361084; ENSP00000354376; ENSG00000132698.
GeneIDi57111.
KEGGihsa:57111.
UCSCiuc001fnc.3. human.

Organism-specific databases

CTDi57111.
GeneCardsiGC01P156030.
HGNCiHGNC:18238. RAB25.
HPAiHPA010872.
MIMi612942. gene.
neXtProtiNX_P57735.
PharmGKBiPA34115.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP57735.
KOiK07906.
OrthoDBiEOG7SFHZ2.
PhylomeDBiP57735.
TreeFamiTF300099.

Miscellaneous databases

EvolutionaryTraceiP57735.
GeneWikiiRAB25.
GenomeRNAii57111.
NextBioi62967.
PROiP57735.
SOURCEiSearch...

Gene expression databases

BgeeiP57735.
CleanExiHS_RAB25.
GenevisibleiP57735. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary, Pancreas and Skin.
  6. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ITGAV AND ITGB1.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.

Entry informationi

Entry nameiRAB25_HUMAN
AccessioniPrimary (citable) accession number: P57735
Secondary accession number(s): Q5VYA2
, Q8NG24, Q96GB1, Q9BT12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: April 26, 2004
Last modified: July 22, 2015
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.