Skip Header

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

Ras-related protein Rap-2b

Gene

Rap2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi116 – 1194GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: MGI
  2. GTP binding Source: MGI
  3. protein domain specific binding Source: MGI

GO - Biological processi

  1. GTP catabolic process Source: InterPro
  2. negative regulation of cell migration Source: MGI
  3. platelet activation Source: MGI
  4. platelet aggregation Source: MGI
  5. positive regulation of protein autophosphorylation Source: MGI
  6. Rap protein signal transduction Source: UniProtKB
  7. 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 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication
Note: Associated with red blood cells-released vesicles.By similarity

GO - Cellular componenti

  1. cytosol Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. membrane Source: MGI
  4. membrane raft Source: MGI
  5. plasma membrane Source: MGI
  6. recycling endosome Source: MGI
  7. 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-2bPRO_0000030217Add
BLAST
Propeptidei181 – 1833Removed in mature formBy similarityPRO_0000030218

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801Cysteine methyl esterBy similarity
Lipidationi180 – 1801S-geranylgeranyl cysteineBy 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

BgeeiP61226.
CleanExiMM_RAP2B.
ExpressionAtlasiP61226. baseline and differential.
GenevestigatoriP61226.

Interactioni

Subunit structurei

Interacts with PLCE1. Interacts with SGSM1, SGSM2 and SGSM3 (By similarity). The GTP-bound form of RAP2B interacts with RUNDC3A.By similarity1 Publication

Protein-protein interaction databases

BioGridi216422. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP61226.
SMRiP61226. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Domaini

The effector domain mediates the interaction with RUNDC3A.1 Publication

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

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

        10         20         30         40         50
MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP
60 70 80 90 100
SVLEILDTAG TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI
110 120 130 140 150
IRVKRYERVP MILVGNKVDL EGEREVSYGE GKALAEEWSC PFMETSAKNK
160 170 180
ASVDELFAEI VRQMNYAAQP NGDEGCCSAC VIL
Length:183
Mass (Da):20,504
Last modified:May 10, 2004 - v1
Checksum:iA1139C2D5E7F5865
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP61226.
SMRiP61226. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216422. 1 interaction.

PTM databases

PhosphoSiteiP61226.

Proteomic databases

MaxQBiP61226.
PaxDbiP61226.
PRIDEiP61226.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5912.
MGIiMGI:1921262. Rap2b.

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiRap2b. mouse.
NextBioi339528.
PROiP61226.
SOURCEiSearch...

Gene expression databases

BgeeiP61226.
CleanExiMM_RAP2B.
ExpressionAtlasiP61226. baseline and differential.
GenevestigatoriP61226.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 110 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.