P10114 (RAP2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rap-2a

Alternative name(s):
RbBP-30

Gene names

Name:

RAP2A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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. 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. Ref.15 Ref.16 Ref.18 Ref.19 Ref.21 Ref.24
Enzyme regulation	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.
Subunit structure	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. Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.24
Subcellular location	Recycling endosome membrane; Lipid-anchor; Cytoplasmic side. Note: May also localize to the Golgi (Ref.11) and the gelatinase-containing granules of neutrophils (Ref.10). Ref.10 Ref.11 Ref.22
Domain	The effector domain mediates the interaction with RUNDC3A By similarity.
Post-translational modification	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. Ref.24 Palmitoylated. Palmitoylation is required for association with recycling endosome membranes and activation of TNIK By similarity.
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 Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Rap protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB actin cytoskeleton reorganization Inferred from direct assay Ref.16. Source: UniProtKB cellular protein localization Inferred from direct assay Ref.16. Source: UniProtKB establishment of protein localization Inferred from direct assay Ref.22. Source: MGI positive regulation of protein autophosphorylation Inferred from direct assay Ref.16. Source: UniProtKB regulation of JNK cascade Inferred from direct assay Ref.15. Source: UniProtKB regulation of dendrite morphogenesis Inferred from direct assay Ref.24. Source: UniProtKB
Cellular component	recycling endosome membrane Inferred from direct assay Ref.22. Source: UniProtKB
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay Ref.8. Source: UniProtKB protein binding Inferred from physical interaction Ref.15Ref.16Ref.24. Source: UniProtKB
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-2a

PRO_0000082687

Propeptide

181 – 183

3

Removed in mature form By similarity

PRO_0000281336

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 Probable

Lipidation

180

1

S-farnesyl cysteine Ref.9

Experimental info

Mutagenesis

5

1

K → R: Reduced NEDD4-dependent ubiquitination; when associated with R-94; R-148 and R-150. Ref.24

Mutagenesis

12

1

G → V: Dominant active. 2-fold decrease in GDP dissociation rate constant and GTPase activity. No change in interaction with TNIK. Ref.8 Ref.16

Mutagenesis

17

1

S → N: Dominant negative. Severely impairs GTP-binding and partial loss of interaction with MAP4K4, MINK1 and TNIK. Ref.8 Ref.16

Mutagenesis

35

1

T → A: Decreases affinity for GTP and 3-fold reduction of GTPase activity. Ref.8

Mutagenesis

39

1

F → 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. Ref.16 Ref.23 Ref.24

Mutagenesis

94

1

K → R: Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-148 and R-150. Ref.24

Mutagenesis

145

1

T → I: Imperfect binding of guanyl nucleotides. Ref.8

Mutagenesis

148

1

K → R: Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-94 and R-150. Ref.24

Mutagenesis

150

1

K → R: Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-94 and R-148. Ref.24

Secondary structure

1

.

.

.

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183

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Helix

16 – 25

10

Beta strand

38 – 46

9

Beta strand

49 – 57

9

Helix

65 – 74

10

Beta strand

76 – 83

8

Helix

87 – 103

17

Turn

104 – 106

3

Beta strand

111 – 116

6

Helix

118 – 123

6

Helix

128 – 138

11

Beta strand

142 – 145

4

Helix

150 – 166

17

Sequences

	Sequence		Length	Mass (Da)
	P10114 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 047D49762765F0B7	FASTA	183	20,615
	10 20 30 40 50 60 MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG 70 80 90 100 110 120 TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYEKVP VILVGNKVDL 130 140 150 160 170 180 ESEREVSSSE GRALAEEWGC PFMETSAKSK TMVDELFAEI VRQMNYAAQP DKDDPCCSAC NIQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3045729] [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: 14702039] [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: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 1900290] [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: 8424780] [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: 8391995] [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: 7962206] [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: 10572250] [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: 10777494] [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: 12444546] [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: 14966141] [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: 15342639] [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: 15752761] [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: 16246175] [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: 16540189] [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: 17509819] [Abstract] Cited for: INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
[21]	"MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold protein TANC1." Nonaka H., Takei K., Umikawa M., Oshiro M., Kuninaka K., Bayarjargal M., Asato T., Yamashiro Y., Uechi Y., Endo S., Suzuki T., Kariya K. Biochem. Biophys. Res. Commun. 377:573-578(2008) [PubMed: 18930710] [Abstract] Cited for: FUNCTION, INTERACTION WITH MINK1.
[22]	"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: 19061864] [Abstract] 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: 19645719] [Abstract] Cited for: MUTAGENESIS OF PHE-39, ACTIVATION BY RASGEF1A AND RASGEF1B.
[24]	"Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite development." Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M., Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E., Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O., Rhee J., Brose N. Neuron 65:358-372(2010) [PubMed: 20159449] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"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: 9312017] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[27]	"Structure of the small G protein Rap2 in a non-catalytic complex with GTP." Menetrey J., Cherfils J. Proteins 37:465-473(1999) [PubMed: 10591105] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00019346.

PIR

S03180.

RefSeq

NP_066361.1. NM_021033.6.

UniGene

Hs.508480.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KAO	X-ray	1.70	A	1-167	[»]
2RAP	X-ray	2.60	A	1-167	[»]
3RAP	X-ray	2.20	R/S	1-167	[»]

ProteinModelPortal

P10114.

SMR

P10114. Positions 1-167.

DisProt

DP00167.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10114. 13 interactions.

STRING

P10114.

PTM databases

PhosphoSite

P10114.

Polymorphism databases

DMDM

131852.

Proteomic databases

PRIDE

P10114.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000245304; ENSP00000245304; ENSG00000125249.

GeneID

5911.

KEGG

hsa:5911.

UCSC

uc001vnd.1. human.

Organism-specific databases

CTD

5911.

GeneCards

GC13P098086.

H-InvDB

HIX0037306.

HGNC

HGNC:9861. RAP2A.

HPA

CAB018552.

MIM

179540. gene.

neXtProt

NX_P10114.

PharmGKB

PA34222.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09607.

GeneTree

ENSGT00560000076632.

HOGENOM

HBG745225.

HOVERGEN

HBG009351.

InParanoid

P10114.

OMA

DCPFMET.

OrthoDB

EOG4P2Q3G.

PhylomeDB

P10114.

Gene expression databases

ArrayExpress

P10114.

Bgee

P10114.

CleanEx

HS_RAP2A.

Genevestigator

P10114.

GermOnline

ENSG00000125249. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]

KO

K07837.

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

NextBio

23004.

SOURCE

Search...

Entry information

Entry name

RAP2A_HUMAN

Accession

Primary (citable) accession number: P10114
Secondary accession number(s): B2RCJ1, Q5JSC1, Q5JSC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.