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Protein

Ras-related protein Rap-2a

Gene

RAP2A

Organism
Homo sapiens (Human)
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. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading.6 Publications

Enzyme regulationi

Activated by the guanine nucleotide-exchange factors RAPGEF3 and RAPGEF4 in a cAMP-dependent manner. Nucleotide exchange is also specifically stimulated by RAPGEF5, RASGEF1A and RASGEF1B.1 Publication

Regions

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

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • cellular protein localization Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • establishment of protein localization Source: MGI
  • intracellular protein transport Source: InterPro
  • microvillus assembly Source: UniProtKB
  • negative regulation of cell migration Source: Ensembl
  • nucleocytoplasmic transport Source: InterPro
  • positive regulation of protein autophosphorylation Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • protein localization to plasma membrane Source: UniProtKB
  • Rap protein signal transduction Source: UniProtKB
  • regulation of dendrite morphogenesis Source: UniProtKB
  • regulation of JNK cascade Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiP10114.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rap-2a
Alternative name(s):
RbBP-30
Gene namesi
Name:RAP2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:9861. RAP2A.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • recycling endosome Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51K → R: Reduced NEDD4-dependent ubiquitination; when associated with R-94; R-148 and R-150. 1 Publication
Mutagenesisi12 – 121G → V: Dominant active. 2-fold decrease in GDP dissociation rate constant and GTPase activity. No change in interaction with TNIK. 2 Publications
Mutagenesisi17 – 171S → N: Dominant negative. Severely impairs GTP-binding and partial loss of interaction with MAP4K4, MINK1 and TNIK. 2 Publications
Mutagenesisi35 – 351T → A: Decreases affinity for GTP and 3-fold reduction of GTPase activity. 1 Publication
Mutagenesisi39 – 391F → S: Loss of RASGEF1A- and RASGEF1B-mediated GDP to GTP exchange. Complete loss of interaction with MAP4K4, MINK1 and TNIK, and loss of ubiquitination by NEDD4. 3 Publications
Mutagenesisi94 – 941K → R: Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-148 and R-150. 1 Publication
Mutagenesisi145 – 1451T → I: Imperfect binding of guanyl nucleotides. 1 Publication
Mutagenesisi148 – 1481K → R: Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-94 and R-150. 1 Publication
Mutagenesisi150 – 1501K → R: Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-94 and R-148. 1 Publication

Organism-specific databases

PharmGKBiPA34222.

Polymorphism and mutation databases

BioMutaiRAP2A.
DMDMi131852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Ras-related protein Rap-2aPRO_0000082687Add
BLAST
Propeptidei181 – 1833Removed in mature form1 PublicationPRO_0000281336

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi176 – 1761S-palmitoyl cysteineBy similarity
Lipidationi177 – 1771S-palmitoyl cysteineBy similarity
Modified residuei180 – 1801Cysteine methyl ester1 Publication
Lipidationi180 – 1801S-farnesyl cysteine1 Publication

Post-translational modificationi

Ubiquitinated; undergoes 'Lys-63' monoubiquitination and diubiquitination by NEDD4. Multiple lysine residues are probably modified. Ubiquitination requires TNIK, prevents interaction with effectors and inactivates RAP2A.1 Publication
Palmitoylated. Palmitoylation is required for association with recycling endosome membranes and activation of TNIK.By similarity

Keywords - PTMi

Lipoprotein, Methylation, Palmitate, Prenylation, Ubl conjugation

Proteomic databases

EPDiP10114.
MaxQBiP10114.
PaxDbiP10114.
PRIDEiP10114.

PTM databases

iPTMnetiP10114.
PhosphoSiteiP10114.
SwissPalmiP10114.

Expressioni

Gene expression databases

BgeeiP10114.
CleanExiHS_RAP2A.
ExpressionAtlasiP10114. baseline and differential.
GenevisibleiP10114. HS.

Organism-specific databases

HPAiCAB018552.

Interactioni

Subunit structurei

Interacts (GTP-bound form) with RUNDC3A. Interacts with RGS14; the interaction is GTP-dependent (By similarity). Interacts with PLCE1. Interacts with ARHGAP29, SGSM1, SGSM2 and SGSM3. Interacts (GTP-bound form preferentially) with TNIK (via the CNH domain); the interaction is direct and recruits RAP2A to the E3 ubiquitin ligase NEDD4. Interacts with MINK1. Interacts (GTP-bound form preferentially) with MAP4K4. Interacts with cytoskeletal actin.By similarity8 Publications

Protein-protein interaction databases

BioGridi111846. 41 interactions.
IntActiP10114. 13 interactions.
MINTiMINT-1172095.
STRINGi9606.ENSP00000245304.

Structurei

Secondary structure

1
183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi16 – 2510Combined sources
Beta strandi38 – 469Combined sources
Beta strandi49 – 579Combined sources
Helixi65 – 7410Combined sources
Beta strandi76 – 838Combined sources
Helixi87 – 10317Combined sources
Turni104 – 1063Combined sources
Beta strandi111 – 1166Combined sources
Helixi118 – 1236Combined sources
Helixi128 – 13811Combined sources
Beta strandi142 – 1454Combined sources
Helixi150 – 16617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KAOX-ray1.70A1-167[»]
2RAPX-ray2.60A1-167[»]
3RAPX-ray2.20R/S1-167[»]
DisProtiDP00167.
ProteinModelPortaliP10114.
SMRiP10114. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10114.

Family & Domainsi

Motif

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

Domaini

The effector domain mediates the interaction with RUNDC3A.By similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP10114.
KOiK07837.
OMAiEINGASW.
OrthoDBiEOG7QVM41.
PhylomeDBiP10114.
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]
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.

P10114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP
60 70 80 90 100
SVLEILDTAG TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI
110 120 130 140 150
IRVKRYEKVP VILVGNKVDL ESEREVSSSE GRALAEEWGC PFMETSAKSK
160 170 180
TMVDELFAEI VRQMNYAAQP DKDDPCCSAC NIQ
Length:183
Mass (Da):20,615
Last modified:July 1, 1989 - v1
Checksum:i047D49762765F0B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12534 mRNA. Translation: CAA31052.1.
AF205602 mRNA. Translation: AAN71845.1.
AF493914 mRNA. Translation: AAM12628.1.
AK315139 mRNA. Translation: BAG37588.1.
AL442067 Genomic DNA. Translation: CAI39499.1.
CH471085 Genomic DNA. Translation: EAX08974.1.
BC041333 mRNA. Translation: AAH41333.1.
BC070031 mRNA. Translation: AAH70031.1.
CCDSiCCDS9485.1.
PIRiS03180.
RefSeqiNP_066361.1. NM_021033.6.
UniGeneiHs.508480.

Genome annotation databases

EnsembliENST00000245304; ENSP00000245304; ENSG00000125249.
GeneIDi5911.
KEGGihsa:5911.
UCSCiuc001vnd.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12534 mRNA. Translation: CAA31052.1.
AF205602 mRNA. Translation: AAN71845.1.
AF493914 mRNA. Translation: AAM12628.1.
AK315139 mRNA. Translation: BAG37588.1.
AL442067 Genomic DNA. Translation: CAI39499.1.
CH471085 Genomic DNA. Translation: EAX08974.1.
BC041333 mRNA. Translation: AAH41333.1.
BC070031 mRNA. Translation: AAH70031.1.
CCDSiCCDS9485.1.
PIRiS03180.
RefSeqiNP_066361.1. NM_021033.6.
UniGeneiHs.508480.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KAOX-ray1.70A1-167[»]
2RAPX-ray2.60A1-167[»]
3RAPX-ray2.20R/S1-167[»]
DisProtiDP00167.
ProteinModelPortaliP10114.
SMRiP10114. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111846. 41 interactions.
IntActiP10114. 13 interactions.
MINTiMINT-1172095.
STRINGi9606.ENSP00000245304.

PTM databases

iPTMnetiP10114.
PhosphoSiteiP10114.
SwissPalmiP10114.

Polymorphism and mutation databases

BioMutaiRAP2A.
DMDMi131852.

Proteomic databases

EPDiP10114.
MaxQBiP10114.
PaxDbiP10114.
PRIDEiP10114.

Protocols and materials databases

DNASUi5911.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245304; ENSP00000245304; ENSG00000125249.
GeneIDi5911.
KEGGihsa:5911.
UCSCiuc001vnd.4. human.

Organism-specific databases

CTDi5911.
GeneCardsiRAP2A.
HGNCiHGNC:9861. RAP2A.
HPAiCAB018552.
MIMi179540. gene.
neXtProtiNX_P10114.
PharmGKBiPA34222.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP10114.
KOiK07837.
OMAiEINGASW.
OrthoDBiEOG7QVM41.
PhylomeDBiP10114.
TreeFamiTF313014.

Enzyme and pathway databases

SignaLinkiP10114.

Miscellaneous databases

ChiTaRSiRAP2A. human.
EvolutionaryTraceiP10114.
GeneWikiiRAP2A.
GenomeRNAii5911.
PROiP10114.
SOURCEiSearch...

Gene expression databases

BgeeiP10114.
CleanExiHS_RAP2A.
ExpressionAtlasiP10114. baseline and differential.
GenevisibleiP10114. HS.

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]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region."
    Pizon V., Chardin P., Lerosey I., Olofsson B., Tavitian A.
    Oncogene 3:201-204(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A novel new gene associated with pRb."
    Fan Z.S., Ao S.Z.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymph node.
  3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Amygdala.
  5. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Brain.
  8. "The product of the rap2 gene, member of the ras superfamily. Biochemical characterization and site-directed mutagenesis."
    Lerosey I., Chardin P., de Gunzburg J., Tavitian A.
    J. Biol. Chem. 266:4315-4321(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: GTPASE ACTIVITY, GTP-BINDING, MUTAGENESIS OF GLY-12; SER-17; THR-35 AND THR-145.
  9. "Prenyl group identification of rap2 proteins: a ras superfamily member other than ras that is farnesylated."
    Farrell F.X., Yamamoto K., Lapetina E.G.
    Biochem. J. 289:349-355(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-180.
  10. "Localization of rap1 and rap2 proteins in the gelatinase-containing granules of human neutrophils."
    Mollinedo F., Perez-Sala D., Gajate C., Jimenez B., Rodriguez P., Lacal J.C.
    FEBS Lett. 326:209-214(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Association of Rap1a and Rap1b proteins with late endocytic/phagocytic compartments and Rap2a with the Golgi complex."
    Pizon V., Desjardins M., Bucci C., Parton R.G., Zerial M.
    J. Cell Sci. 107:1661-1670(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Interaction of the low-molecular-weight GTP-binding protein rap2 with the platelet cytoskeleton is mediated by direct binding to the actin filaments."
    Torti M., Bertoni A., Canobbio I., Sinigaglia F., Lapetina E.G., Balduini C.
    J. Cell. Biochem. 75:675-685(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACTIN.
  13. "Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs."
    de Rooij J., Rehmann H., van Triest M., Cool R.H., Wittinghofer A., Bos J.L.
    J. Biol. Chem. 275:20829-20836(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVATION BY RAPGEF3; RAPGEF4 AND RAPGEF5.
  14. "Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon."
    Song C., Satoh T., Edamatsu H., Wu D., Tadano M., Gao X., Kataoka T.
    Oncogene 21:8105-8113(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLCE1.
  15. "Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase."
    Machida N., Umikawa M., Takei K., Sakima N., Myagmar B.E., Taira K., Uezato H., Ogawa Y., Kariya K.
    J. Biol. Chem. 279:15711-15714(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAP4K4.
  16. "The Traf2- and Nck-interacting kinase as a putative effector of Rap2 to regulate actin cytoskeleton."
    Taira K., Umikawa M., Takei K., Myagmar B.-E., Shinzato M., Machida N., Uezato H., Nonaka S., Kariya K.
    J. Biol. Chem. 279:49488-49496(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TNIK, MUTAGENESIS OF GLY-12; SER-17 AND PHE-39.
  17. "PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative Rap2 effector."
    Myagmar B.-E., Umikawa M., Asato T., Taira K., Oshiro M., Hino A., Takei K., Uezato H., Kariya K.
    Biochem. Biophys. Res. Commun. 329:1046-1052(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP29.
  18. "Biochemical characterization of RGS14: RGS14 activity towards G-protein alpha subunits is independent of its binding to Rap2A."
    Mittal V., Linder M.E.
    Biochem. J. 394:309-315(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Rap2, but not Rap1 GTPase is expressed in human red blood cells and is involved in vesiculation."
    Greco F., Ciana A., Pietra D., Balduini C., Minetti G., Torti M.
    Biochim. Biophys. Acta 1763:330-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway."
    Yang H., Sasaki T., Minoshima S., Shimizu N.
    Genomics 90:249-260(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
  21. Cited for: FUNCTION, INTERACTION WITH MINK1.
  22. Cited for: SUBCELLULAR LOCATION.
  23. "RasGEF1A and RasGEF1B are guanine nucleotide exchange factors that discriminate between Rap GTP-binding proteins and mediate Rap2-specific nucleotide exchange."
    Yaman E., Gasper R., Koerner C., Wittinghofer A., Tazebay U.H.
    FEBS J. 276:4607-4616(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-39, ACTIVATION BY RASGEF1A AND RASGEF1B.
  24. Cited for: FUNCTION, INTERACTION WITH NEDD4 AND TNIK, UBIQUITINATION BY NEDD4, MUTAGENESIS OF LYS-5; PHE-39; LYS-94; LYS-148 AND LYS-150.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Coiled-coil domain containing protein 124 is a novel centrosome and midbody protein that interacts with the ras-guanine nucleotide exchange factor 1B and is involved in cytokinesis."
    Telkoparan P., Erkek S., Yaman E., Alotaibi H., Bayik D., Tazebay U.H.
    PLoS ONE 8:E69289-E69289(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ENZYME REGULATION BY RASGEF1B.
  27. "Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS."
    Cherfils J., Menetrey J., Le Bras G., Janoueix-Lerosey I., de Gunzburg J., Garel J.-R., Auzat I.
    EMBO J. 16:5582-5591(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  28. "Structure of the small G protein Rap2 in a non-catalytic complex with GTP."
    Menetrey J., Cherfils J.
    Proteins 37:465-473(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiRAP2A_HUMAN
AccessioniPrimary (citable) accession number: P10114
Secondary accession number(s): B2RCJ1, Q5JSC1, Q5JSC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 8, 2016
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.