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Q62835 (RABE2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Rab GTPase-binding effector protein 2
Alternative name(s):
MP13 protein
Rabaptin-5beta
Gene names
Name:Rabep2
Synonyms:Rabpt5b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a role in membrane trafficking and in homotypic early endosome fusion By similarity.

Subunit structure

Heterodimer with RABGEF1. The dimer binds RAB5A that has been activated by GTP-binding By similarity.

Subcellular location

Cytoplasm By similarity. Early endosome By similarity.

Sequence similarities

Belongs to the rabaptin family.

Ontologies

Keywords
   Biological processEndocytosis
Protein transport
Transport
   Cellular componentCytoplasm
Endosome
   DomainCoiled coil
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of GTPase activity

Inferred from electronic annotation. Source: GOC

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentearly endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTPase activator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 554554Rab GTPase-binding effector protein 2
PRO_0000187561

Regions

Coiled coil15 – 173159 Potential
Coiled coil274 – 512239 Potential
Compositional bias96 – 1005Poly-Gln
Compositional bias270 – 420151Gln-rich

Sequences

Sequence LengthMass (Da)Tools
Q62835 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 39448FAF2B41A004

FASTA55461,973
        10         20         30         40         50         60 
MAAAPAALAL DPQPQEEQKD ASESSELSRL RAELAGALAE METMKAVAEV SESTKAEAVA 

        70         80         90        100        110        120 
AVQRQCQEEV ASLQAILKDS ISSYETQIAA LKQERQQQQQ DSEEKERELG HLKQLLARAH 

       130        140        150        160        170        180 
PLDSLEKQME KAHEDSEKLR EIVLPMEQEI AELKVKLLRA EELIQEIQRR PRQPASLHGS 

       190        200        210        220        230        240 
TELLPLSRNP SPPLEPSEEP SGDAGPAAEA FAHNCDDSAS ISSFSLGGAA GSVSLRGPQG 

       250        260        270        280        290        300 
LSPEQEETAS LVSTGTLVPE GIYLPPPGYQ LVPDSQWEQL QVEGRQLQKE LESVRRERDE 

       310        320        330        340        350        360 
LQEGLSRSNE DCAKQMQVLL AQVQNSEQLL RTLQGTVSQA QERVQRQMAE LATSHKCLSQ 

       370        380        390        400        410        420 
EVKRLNEENR GLRAEQLPSS ALQGSEQQED QDEALPSSIQ ELHQLVRHTR QQARARQQAQ 

       430        440        450        460        470        480 
EHEAERLRIE IVKLREALDE ETAAKASLEG QLRVQREETD VLEASLCSLR IETERVQQEH 

       490        500        510        520        530        540 
HKAQLTDLLS EQRAKALRLQ AELETSEQVQ RDFVRLSQAL QVRLEQIRQA DTLEQVRSIL 

       550 
DEAPLRDIKD IKDS

« Hide

References

[1]"Cloning and expression of MP13 gene from rat hippocampus, a new factor related to guanosine triphosphate regulation."
Feng Z., Hong J., Qi Q., Han Y., Wilson B., Iadarola M., Tiao N., Bing G.
Neurosci. Lett. 296:129-132(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer 344.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U34932 mRNA. Translation: AAA79137.1.
IPIIPI00209181.
RefSeqNP_085074.1. NM_030585.1.
UniGeneRn.3228.

3D structure databases

ProteinModelPortalQ62835.
SMRQ62835. Positions 495-545.
ModBaseSearch...

Proteomic databases

PaxDbQ62835.
PRIDEQ62835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID80754.
KEGGrno:80754.

Organism-specific databases

CTD79874.
RGD621416. Rabep2.

Phylogenomic databases

eggNOGNOG266403.
HOGENOMHOG000154063.
HOVERGENHBG108391.
OrthoDBEOG4TXBS2.

Gene expression databases

ArrayExpressQ62835.
GenevestigatorQ62835.

Family and domain databases

InterProIPR003914. Rabaptin.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PfamPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 2 hits.
[Graphical view]
PRINTSPR01432. RABAPTIN.
ProtoNetSearch...

Other

NextBio614862.

Entry information

Entry nameRABE2_RAT
AccessionPrimary (citable) accession number: Q62835
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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