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P61226 (RAP2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 Rap-2b
Gene names
Name:Rap2b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells. Ref.5

Subunit structure

Interacts with PLCE1. Interacts with SGSM1, SGSM2 and SGSM3 By similarity. The GTP-bound form of RAP2B interacts with RUNDC3A. Ref.4

Subcellular location

Recycling endosome membrane; Lipid-anchor; Cytoplasmic side. Note: Associated with red blood cells-released vesicles By similarity. Ref.5

Domain

The effector domain mediates the interaction with RUNDC3A. Ref.4

Post-translational modification

Palmitoylated. Palmitoylation is required for association with recycling endosome membranes and activation of TNIK. Ref.5

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 180180Ras-related protein Rap-2b
PRO_0000030217
Propeptide181 – 1833Removed in mature form By similarity
PRO_0000030218

Regions

Nucleotide binding10 – 178GTP By similarity
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding116 – 1194GTP By similarity
Motif32 – 409Effector region Probable

Amino acid modifications

Modified residue1801Cysteine methyl ester By similarity
Lipidation1801S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis1761C → G: Reduced association with the recycling endosome membranes and loss of TNIK activation; when associated with G-177. Ref.5
Mutagenesis1771C → G: Reduced association with the recycling endosome membranes and loss of TNIK activation; when associated with G-176. Ref.5
Mutagenesis1801C → A: Loss of association with membranes. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P61226 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: A1139C2D5E7F5865

FASTA18320,504
        10         20         30         40         50         60 
MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG 

        70         80         90        100        110        120 
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYERVP MILVGNKVDL 

       130        140        150        160        170        180 
EGEREVSYGE GKALAEEWSC PFMETSAKNK ASVDELFAEI VRQMNYAAQP NGDEGCCSAC 


VIL 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic head.
[2]"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].
Strain: C57BL/6J and FVB/N.
Tissue: Cerebellum and Mammary gland.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 6-16; 43-68 AND 151-162, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"Identification of a specific effector of the small GTP-binding protein Rap2."
Janoueix-Lerosey I., Pasheva E., de Tand M.-F., Tavitian A., de Gunzburg J.
Eur. J. Biochem. 252:290-298(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUNDC3A, DOMAIN.
[5]"Rap2 function requires palmitoylation and recycling endosome localization."
Uechi Y., Bayarjargal M., Umikawa M., Oshiro M., Takei K., Yamashiro Y., Asato T., Endo S., Misaki R., Taguchi T., Kariya K.
Biochem. Biophys. Res. Commun. 378:732-737(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, MUTAGENESIS OF CYS-176; CYS-177 AND CYS-180.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK014462 mRNA. Translation: BAB29368.1.
BC032168 mRNA. Translation: AAH32168.1.
BC046528 mRNA. Translation: AAH46528.1.
RefSeqNP_082988.1. NM_028712.4.
UniGeneMm.422674.
Mm.477648.

3D structure databases

ProteinModelPortalP61226.
SMRP61226. Positions 1-167.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP61226.

Proteomic databases

PaxDbP61226.
PRIDEP61226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049064; ENSMUSP00000038841; ENSMUSG00000036894.
GeneID74012.
KEGGmmu:74012.
UCSCuc008pjl.1. mouse.

Organism-specific databases

CTD5912.
MGIMGI:1921262. Rap2b.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233973.
HOVERGENHBG009351.
InParanoidP61226.
KOK07838.
OMAQFTGINE.
OrthoDBEOG7QVM41.
PhylomeDBP61226.
TreeFamTF313014.

Gene expression databases

ArrayExpressP61226.
BgeeP61226.
CleanExMM_RAP2B.
GenevestigatorP61226.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAP2B. mouse.
NextBio339528.
PROP61226.
SOURCESearch...

Entry information

Entry nameRAP2B_MOUSE
AccessionPrimary (citable) accession number: P61226
Secondary accession number(s): P17964, Q96EG5, Q9CXG0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: April 16, 2014
This is version 102 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot