P61226 (RAP2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rap-2b

Gene names

Name:

Rap2b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Palmitate Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rap protein signal transduction Inferred from direct assay Ref.5. Source: UniProtKB negative regulation of cell migration Inferred from direct assay Ref.5. Source: MGI positive regulation of protein autophosphorylation Inferred from direct assay Ref.5. Source: MGI regulation of protein tyrosine kinase activity Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay Ref.5. Source: MGI recycling endosome membrane Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 180	180	Ras-related protein Rap-2b		PRO_0000030217
	Propeptide	181 – 183	3	Removed in mature form By similarity		PRO_0000030218
Regions
	Nucleotide binding	10 – 17	8	GTP By similarity
	Nucleotide binding	57 – 61	5	GTP By similarity
	Nucleotide binding	116 – 119	4	GTP By similarity
	Motif	32 – 40	9	Effector region Probable
Amino acid modifications
	Modified residue	180	1	Cysteine methyl ester By similarity
	Lipidation	180	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Mutagenesis	176	1	C → G: Reduced association with the recycling endosome membranes and loss of TNIK activation; when associated with G-177. Ref.5
	Mutagenesis	177	1	C → G: Reduced association with the recycling endosome membranes and loss of TNIK activation; when associated with G-176. Ref.5
	Mutagenesis	180	1	C → A: Loss of association with membranes. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P61226 [UniParc]. Last modified May 10, 2004. Version 1. Checksum: A1139C2D5E7F5865	FASTA	183	20,504
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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.
IPI	IPI00138716.
RefSeq	NP_082988.1. NM_028712.4.
UniGene	Mm.422674. Mm.477648.
3D structure databases
ProteinModelPortal	P61226.
ModBase	Search...
PTM databases
PhosphoSite	P61226.
Proteomic databases
PaxDb	P61226.
PRIDE	P61226.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000049064; ENSMUSP00000038841; ENSMUSG00000036894.
GeneID	74012.
KEGG	mmu:74012.
Organism-specific databases
CTD	5912.
MGI	MGI:1921262. Rap2b.
Phylogenomic databases
eggNOG	COG1100.
HOGENOM	HOG000233973.
HOVERGEN	HBG009351.
InParanoid	P61226.
KO	K07838.
OMA	RVCAVEL.
OrthoDB	EOG4P2Q3G.
Gene expression databases
ArrayExpress	P61226.
Bgee	P61226.
CleanEx	MM_RAP2B.
Genevestigator	P61226.
GermOnline	ENSMUSG00000036894. Mus musculus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR020849. Small_GTPase_Ras. [Graphical view]
PANTHER	PTHR24070. PTHR24070. 1 hit.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00173. RAS. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51421. RAS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RAP2B. mouse.
NextBio	339528.
SOURCE	Search...

Entry information

Entry name

RAP2B_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program