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Q969Q5 (RAB24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-24
Gene names
Name:RAB24
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in autophagy-related processes By similarity.

Subunit structure

Unlike other Rab family members, does not interact with GDP dissociation inhibitors (GDIs), including ARHGDIA and ARHGDIB. Interacts with ZFYVE20. Ref.5 Ref.6

Subcellular location

Cytoplasmcytosol. Membrane; Lipid-anchor By similarity. Note: Only about 20-25% is recovered in the particulate fraction. Ref.5

Induction

By extensive retinoic acid treatment, in Ntera-2 teratoma cell line induced to differentiate into post-mitotic neurons (NTN2) (at protein level). Ref.5

Post-translational modification

Isoprenylation is inefficient compared to other Rab family members.

Miscellaneous

The unusual Ser-67, instead of a conserved Gln in other family members, is the cause of low GTPase activity. As a result, the predominant nucleotide associated with the protein is GTP By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203Ras-related protein Rab-24
PRO_0000121213

Regions

Nucleotide binding14 – 229GTP By similarity
Nucleotide binding63 – 675GTP By similarity
Nucleotide binding120 – 1234GTP By similarity
Nucleotide binding154 – 1563GTP By similarity
Motif37 – 459Effector region By similarity

Amino acid modifications

Lipidation2001S-geranylgeranyl cysteine By similarity
Lipidation2011S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict55 – 562RT → AL in AAP97202. Ref.1
Sequence conflict1081S → T in AAP97202. Ref.1
Sequence conflict129 – 1302RR → QE in AAP97202. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q969Q5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 979E1AF6F7A4E5F1

FASTA20323,124
        10         20         30         40         50         60 
MSGQRVDVKV VMLGKEYVGK TSLVERYVHD RFLVGPYQNT IGAAFVAKVM SVGDRTVTLG 

        70         80         90        100        110        120 
IWDTAGSERY EAMSRIYYRG AKAAIVCYDL TDSSSFERAK FWVKELRSLE EGCQIYLCGT 

       130        140        150        160        170        180 
KSDLLEEDRR RRRVDFHDVQ DYADNIKAQL FETSSKTGQS VDELFQKVAE DYVSVAAFQV 

       190        200 
MTEDKGVDLG QKPNPYFYSC CHH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a new human cDNA homology to murine Rab24 protein mRNA."
Zhang H.L., Yu L., Ding J.B., Zhao Y., Li M.Z., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
[3]"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: Pancreas, Skin and Uterus.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-203.
Tissue: Amygdala.
[5]"Rab24 is an atypical member of the Rab GTPase family. Deficient GTPase activity, GDP dissociation inhibitor interaction, and prenylation of Rab24 expressed in cultured cells."
Erdman R.A., Shellenberger K.E., Overmeyer J.H., Maltese W.A.
J. Biol. Chem. 275:3848-3856(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION, INEFFICIENT ISOPRENYLATION, LACK OF INTERACTION WITH ARHGDIA AND ARHGDIB.
[6]"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
Eathiraj S., Pan X., Ritacco C., Lambright D.G.
Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFYVE20.
[7]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087904 mRNA. Translation: AAP97202.1.
BT007268 mRNA. Translation: AAP35932.1.
BC010006 mRNA. Translation: AAH10006.1.
BC015534 mRNA. Translation: AAH15534.1.
BC021263 mRNA. Translation: AAH21263.1.
AL833898 mRNA. Translation: CAD38754.1.
CCDSCCDS34300.1.
RefSeqNP_001026847.1. NM_001031677.3.
NP_570137.2. NM_130781.3.
UniGeneHs.16258.

3D structure databases

ProteinModelPortalQ969Q5.
SMRQ969Q5. Positions 9-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119817. 6 interactions.
IntActQ969Q5. 10 interactions.
STRING9606.ENSP00000304376.

PTM databases

PhosphoSiteQ969Q5.

Polymorphism databases

DMDM23396831.

Proteomic databases

MaxQBQ969Q5.
PaxDbQ969Q5.
PRIDEQ969Q5.

Protocols and materials databases

DNASU53917.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303251; ENSP00000304376; ENSG00000169228.
ENST00000393611; ENSP00000377235; ENSG00000169228.
GeneID53917.
KEGGhsa:53917.
UCSCuc003mfv.3. human.

Organism-specific databases

CTD53917.
GeneCardsGC05M176728.
HGNCHGNC:9765. RAB24.
MIM612415. gene.
neXtProtNX_Q969Q5.
PharmGKBPA34114.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ969Q5.
KOK07912.
OMAFWVKELQ.
OrthoDBEOG7B8S58.
PhylomeDBQ969Q5.
TreeFamTF300199.

Gene expression databases

BgeeQ969Q5.
CleanExHS_RAB24.
GenevestigatorQ969Q5.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi53917.
NextBio56226.
PROQ969Q5.
SOURCESearch...

Entry information

Entry nameRAB24_HUMAN
AccessionPrimary (citable) accession number: Q969Q5
Secondary accession number(s): Q7Z4Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM