Full text data of RAP2C
RAP2C
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ras-related protein Rap-2c; Flags: Precursor
Ras-related protein Rap-2c; Flags: Precursor
UniProt
Q9Y3L5
ID RAP2C_HUMAN Reviewed; 183 AA.
AC Q9Y3L5; B3KWD6; Q5H9H9; Q9BTS0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Ras-related protein Rap-2c;
DE Flags: Precursor;
GN Name=RAP2C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=17447155; DOI=10.1007/s11033-006-9023-9;
RA Guo Z., Yuan J., Tang W., Chen X., Gu X., Luo K., Wang Y., Wan B.,
RA Yu L.;
RT "Cloning and characterization of the human gene RAP2C, a novel member
RT of Ras family, which activates transcriptional activities of SRE.";
RL Mol. Biol. Rep. 34:137-144(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Rhodes S., Huckle E.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP GTP-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=16213650; DOI=10.1016/j.biochi.2005.08.007;
RA Paganini S., Guidetti G.F., Catricala S., Trionfini P., Panelli S.,
RA Balduini C., Torti M.;
RT "Identification and biochemical characterization of Rap2C, a new
RT member of the Rap family of small GTP-binding proteins.";
RL Biochimie 88:285-295(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Small GTP-binding protein which cycles between a GDP-
CC bound inactive and a GTP-bound active form. May play a role in
CC cytoskeletal rearrangements and regulate cell spreading through
CC activation of the effector TNIK. May play a role in SRE-mediated
CC gene transcription.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Recycling endosome membrane;
CC Lipid-anchor; Cytoplasmic side (By similarity).
CC -!- TISSUE SPECIFICITY: Expressed in liver, skeletal muscle, prostate,
CC uterus, rectum, stomach, and bladder and to a lower extent in
CC brain, kidney, pancreas, and bone marrow. Expressed in mononuclear
CC leukocytes and megakaryocytes.
CC -!- PTM: Palmitoylated. Palmitoylation is required for association
CC with recycling endosome membranes and activation of TNIK (By
CC similarity).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
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DR EMBL; AY298955; AAP55684.1; -; mRNA.
DR EMBL; AL049685; CAB41256.1; -; mRNA.
DR EMBL; AK124801; BAG54098.1; -; mRNA.
DR EMBL; Z78022; CAI42719.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11782.1; -; Genomic_DNA.
DR EMBL; BC003403; AAH03403.1; -; mRNA.
DR RefSeq; NP_001258115.1; NM_001271186.1.
DR RefSeq; NP_001258116.1; NM_001271187.1.
DR RefSeq; NP_067006.3; NM_021183.4.
DR UniGene; Hs.119889; -.
DR UniGene; Hs.743556; -.
DR ProteinModelPortal; Q9Y3L5; -.
DR SMR; Q9Y3L5; 1-167.
DR IntAct; Q9Y3L5; 1.
DR STRING; 9606.ENSP00000340274; -.
DR PhosphoSite; Q9Y3L5; -.
DR DMDM; 47117343; -.
DR PaxDb; Q9Y3L5; -.
DR PeptideAtlas; Q9Y3L5; -.
DR PRIDE; Q9Y3L5; -.
DR DNASU; 57826; -.
DR Ensembl; ENST00000342983; ENSP00000340274; ENSG00000123728.
DR Ensembl; ENST00000370874; ENSP00000359911; ENSG00000123728.
DR GeneID; 57826; -.
DR KEGG; hsa:57826; -.
DR UCSC; uc004ewp.4; human.
DR CTD; 57826; -.
DR GeneCards; GC0XM131337; -.
DR HGNC; HGNC:21165; RAP2C.
DR neXtProt; NX_Q9Y3L5; -.
DR PharmGKB; PA134899238; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233973; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9Y3L5; -.
DR KO; K07839; -.
DR OMA; KEKKSYC; -.
DR OrthoDB; EOG7QVM41; -.
DR PhylomeDB; Q9Y3L5; -.
DR GenomeRNAi; 57826; -.
DR NextBio; 64807; -.
DR PRO; PR:Q9Y3L5; -.
DR Bgee; Q9Y3L5; -.
DR CleanEx; HS_RAP2C; -.
DR Genevestigator; Q9Y3L5; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00173; RAS; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Endosome; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1 180 Ras-related protein Rap-2c.
FT /FTId=PRO_0000030221.
FT PROPEP 181 183 Removed in mature form (By similarity).
FT /FTId=PRO_0000030222.
FT NP_BIND 10 17 GTP (By similarity).
FT NP_BIND 57 61 GTP (By similarity).
FT NP_BIND 116 119 GTP (By similarity).
FT MOTIF 32 40 Effector region (Probable).
FT MOD_RES 180 180 Cysteine methyl ester (By similarity).
FT LIPID 180 180 S-geranylgeranyl cysteine (By
FT similarity).
FT CONFLICT 135 135 A -> V (in Ref. 6; AAH03403).
SQ SEQUENCE 183 AA; 20745 MW; 6763385F76638324 CRC64;
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI VRVKRYEKVP LILVGNKVDL
EPEREVMSSE GRALAQEWGC PFMETSAKSK SMVDELFAEI VRQMNYSSLP EKQDQCCTTC
VVQ
//
ID RAP2C_HUMAN Reviewed; 183 AA.
AC Q9Y3L5; B3KWD6; Q5H9H9; Q9BTS0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Ras-related protein Rap-2c;
DE Flags: Precursor;
GN Name=RAP2C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=17447155; DOI=10.1007/s11033-006-9023-9;
RA Guo Z., Yuan J., Tang W., Chen X., Gu X., Luo K., Wang Y., Wan B.,
RA Yu L.;
RT "Cloning and characterization of the human gene RAP2C, a novel member
RT of Ras family, which activates transcriptional activities of SRE.";
RL Mol. Biol. Rep. 34:137-144(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Rhodes S., Huckle E.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP GTP-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=16213650; DOI=10.1016/j.biochi.2005.08.007;
RA Paganini S., Guidetti G.F., Catricala S., Trionfini P., Panelli S.,
RA Balduini C., Torti M.;
RT "Identification and biochemical characterization of Rap2C, a new
RT member of the Rap family of small GTP-binding proteins.";
RL Biochimie 88:285-295(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Small GTP-binding protein which cycles between a GDP-
CC bound inactive and a GTP-bound active form. May play a role in
CC cytoskeletal rearrangements and regulate cell spreading through
CC activation of the effector TNIK. May play a role in SRE-mediated
CC gene transcription.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Recycling endosome membrane;
CC Lipid-anchor; Cytoplasmic side (By similarity).
CC -!- TISSUE SPECIFICITY: Expressed in liver, skeletal muscle, prostate,
CC uterus, rectum, stomach, and bladder and to a lower extent in
CC brain, kidney, pancreas, and bone marrow. Expressed in mononuclear
CC leukocytes and megakaryocytes.
CC -!- PTM: Palmitoylated. Palmitoylation is required for association
CC with recycling endosome membranes and activation of TNIK (By
CC similarity).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
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DR EMBL; AY298955; AAP55684.1; -; mRNA.
DR EMBL; AL049685; CAB41256.1; -; mRNA.
DR EMBL; AK124801; BAG54098.1; -; mRNA.
DR EMBL; Z78022; CAI42719.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11782.1; -; Genomic_DNA.
DR EMBL; BC003403; AAH03403.1; -; mRNA.
DR RefSeq; NP_001258115.1; NM_001271186.1.
DR RefSeq; NP_001258116.1; NM_001271187.1.
DR RefSeq; NP_067006.3; NM_021183.4.
DR UniGene; Hs.119889; -.
DR UniGene; Hs.743556; -.
DR ProteinModelPortal; Q9Y3L5; -.
DR SMR; Q9Y3L5; 1-167.
DR IntAct; Q9Y3L5; 1.
DR STRING; 9606.ENSP00000340274; -.
DR PhosphoSite; Q9Y3L5; -.
DR DMDM; 47117343; -.
DR PaxDb; Q9Y3L5; -.
DR PeptideAtlas; Q9Y3L5; -.
DR PRIDE; Q9Y3L5; -.
DR DNASU; 57826; -.
DR Ensembl; ENST00000342983; ENSP00000340274; ENSG00000123728.
DR Ensembl; ENST00000370874; ENSP00000359911; ENSG00000123728.
DR GeneID; 57826; -.
DR KEGG; hsa:57826; -.
DR UCSC; uc004ewp.4; human.
DR CTD; 57826; -.
DR GeneCards; GC0XM131337; -.
DR HGNC; HGNC:21165; RAP2C.
DR neXtProt; NX_Q9Y3L5; -.
DR PharmGKB; PA134899238; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233973; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9Y3L5; -.
DR KO; K07839; -.
DR OMA; KEKKSYC; -.
DR OrthoDB; EOG7QVM41; -.
DR PhylomeDB; Q9Y3L5; -.
DR GenomeRNAi; 57826; -.
DR NextBio; 64807; -.
DR PRO; PR:Q9Y3L5; -.
DR Bgee; Q9Y3L5; -.
DR CleanEx; HS_RAP2C; -.
DR Genevestigator; Q9Y3L5; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00173; RAS; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Endosome; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1 180 Ras-related protein Rap-2c.
FT /FTId=PRO_0000030221.
FT PROPEP 181 183 Removed in mature form (By similarity).
FT /FTId=PRO_0000030222.
FT NP_BIND 10 17 GTP (By similarity).
FT NP_BIND 57 61 GTP (By similarity).
FT NP_BIND 116 119 GTP (By similarity).
FT MOTIF 32 40 Effector region (Probable).
FT MOD_RES 180 180 Cysteine methyl ester (By similarity).
FT LIPID 180 180 S-geranylgeranyl cysteine (By
FT similarity).
FT CONFLICT 135 135 A -> V (in Ref. 6; AAH03403).
SQ SEQUENCE 183 AA; 20745 MW; 6763385F76638324 CRC64;
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI VRVKRYEKVP LILVGNKVDL
EPEREVMSSE GRALAQEWGC PFMETSAKSK SMVDELFAEI VRQMNYSSLP EKQDQCCTTC
VVQ
//