SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P61226

- RAP2B_MOUSE

UniProt

P61226 - RAP2B_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ras-related protein Rap-2b
Gene
Rap2b
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTP By similarity
Nucleotide bindingi57 – 615GTP By similarity
Nucleotide bindingi116 – 1194GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. protein domain specific binding Source: MGI

GO - Biological processi

  1. GTP catabolic process Source: InterPro
  2. Rap protein signal transduction Source: UniProtKB
  3. negative regulation of cell migration Source: MGI
  4. positive regulation of protein autophosphorylation Source: MGI
  5. regulation of protein tyrosine kinase activity Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rap-2b
Gene namesi
Name:Rap2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1921262. Rap2b.

Subcellular locationi

Recycling endosome membrane; Lipid-anchor; Cytoplasmic side
Note: Associated with red blood cells-released vesicles By similarity.1 Publication

GO - Cellular componenti

  1. cytosol Source: MGI
  2. membrane Source: MGI
  3. recycling endosome Source: MGI
  4. recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1761C → G: Reduced association with the recycling endosome membranes and loss of TNIK activation; when associated with G-177. 1 Publication
Mutagenesisi177 – 1771C → G: Reduced association with the recycling endosome membranes and loss of TNIK activation; when associated with G-176. 1 Publication
Mutagenesisi180 – 1801C → A: Loss of association with membranes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Ras-related protein Rap-2b
PRO_0000030217Add
BLAST
Propeptidei181 – 1833Removed in mature form By similarity
PRO_0000030218

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801Cysteine methyl ester By similarity
Lipidationi180 – 1801S-geranylgeranyl cysteine By similarity

Post-translational modificationi

Palmitoylated. Palmitoylation is required for association with recycling endosome membranes and activation of TNIK.1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Palmitate, Prenylation

Proteomic databases

MaxQBiP61226.
PaxDbiP61226.
PRIDEiP61226.

PTM databases

PhosphoSiteiP61226.

Expressioni

Gene expression databases

ArrayExpressiP61226.
BgeeiP61226.
CleanExiMM_RAP2B.
GenevestigatoriP61226.

Interactioni

Subunit structurei

Interacts with PLCE1. Interacts with SGSM1, SGSM2 and SGSM3 By similarity. The GTP-bound form of RAP2B interacts with RUNDC3A.1 Publication

Protein-protein interaction databases

BioGridi216422. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP61226.
SMRiP61226. Positions 1-167.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector region Inferred

Domaini

The effector domain mediates the interaction with RUNDC3A.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP61226.
KOiK07838.
OMAiPNGDEQC.
OrthoDBiEOG7QVM41.
PhylomeDBiP61226.
TreeFamiTF313014.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61226-1 [UniParc]FASTAAdd to Basket

« Hide

MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP    50
SVLEILDTAG TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI 100
IRVKRYERVP MILVGNKVDL EGEREVSYGE GKALAEEWSC PFMETSAKNK 150
ASVDELFAEI VRQMNYAAQP NGDEGCCSAC VIL 183
Length:183
Mass (Da):20,504
Last modified:May 10, 2004 - v1
Checksum:iA1139C2D5E7F5865
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK014462 mRNA. Translation: BAB29368.1.
BC032168 mRNA. Translation: AAH32168.1.
BC046528 mRNA. Translation: AAH46528.1.
CCDSiCCDS17378.1.
RefSeqiNP_082988.1. NM_028712.4.
UniGeneiMm.422674.
Mm.477648.

Genome annotation databases

EnsembliENSMUST00000049064; ENSMUSP00000038841; ENSMUSG00000036894.
GeneIDi74012.
KEGGimmu:74012.
UCSCiuc008pjl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK014462 mRNA. Translation: BAB29368.1 .
BC032168 mRNA. Translation: AAH32168.1 .
BC046528 mRNA. Translation: AAH46528.1 .
CCDSi CCDS17378.1.
RefSeqi NP_082988.1. NM_028712.4.
UniGenei Mm.422674.
Mm.477648.

3D structure databases

ProteinModelPortali P61226.
SMRi P61226. Positions 1-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 216422. 1 interaction.

PTM databases

PhosphoSitei P61226.

Proteomic databases

MaxQBi P61226.
PaxDbi P61226.
PRIDEi P61226.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049064 ; ENSMUSP00000038841 ; ENSMUSG00000036894 .
GeneIDi 74012.
KEGGi mmu:74012.
UCSCi uc008pjl.1. mouse.

Organism-specific databases

CTDi 5912.
MGIi MGI:1921262. Rap2b.

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233973.
HOVERGENi HBG009351.
InParanoidi P61226.
KOi K07838.
OMAi PNGDEQC.
OrthoDBi EOG7QVM41.
PhylomeDBi P61226.
TreeFami TF313014.

Miscellaneous databases

ChiTaRSi RAP2B. mouse.
NextBioi 339528.
PROi P61226.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61226.
Bgeei P61226.
CleanExi MM_RAP2B.
Genevestigatori P61226.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view ]
PANTHERi PTHR24070. PTHR24070. 1 hit.
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00173. RAS. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51421. RAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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. Cited for: FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, MUTAGENESIS OF CYS-176; CYS-177 AND CYS-180.

Entry informationi

Entry nameiRAP2B_MOUSE
AccessioniPrimary (citable) accession number: P61226
Secondary accession number(s): P17964, Q96EG5, Q9CXG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi