Full text data of RASA2
RASA2
(GAP1M, RASGAP)
[Confidence: low (only semi-automatic identification from reviews)]
Ras GTPase-activating protein 2 (GTPase-activating protein 1m; GAP1m)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ras GTPase-activating protein 2 (GTPase-activating protein 1m; GAP1m)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15283
ID RASA2_HUMAN Reviewed; 850 AA.
AC Q15283; A8K7K1; G3V0F9; O00695; Q15284; Q92594; Q99577; Q9UEQ2;
read moreDT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 3.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Ras GTPase-activating protein 2;
DE AltName: Full=GTPase-activating protein 1m;
DE Short=GAP1m;
GN Name=RASA2; Synonyms=GAP1M, RASGAP;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=8917095; DOI=10.1016/0378-1119(96)00144-8;
RA Kobayashi M., Masui T., Kusuda J., Kameoka Y., Hashimoto K.,
RA Iwashita S.;
RT "Human rasGTPase-activating protein (human counterpart of GAP1m):
RT sequence of the cDNA, primary structure of the protein, production and
RT chromosomal localization.";
RL Gene 175:173-177(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=8812506; DOI=10.1006/geno.1996.0412;
RA Li S., Satoh H., Watanabe T., Nakamura S., Hattori S.;
RT "cDNA cloning and chromosomal mapping of a novel human GAP (GAP1M), a
RT GTPase-activating protein of Ras.";
RL Genomics 35:625-627(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Blood;
RX PubMed=9382842; DOI=10.1016/S0960-9822(06)00423-4;
RA Lockyer P.J., Bottomley J.R., Reynolds J.S., McNulty T.J.,
RA Venkateswarlu K., Potter B.V.L., Dempsey C.E., Cullen P.J.;
RT "Distinct subcellular localisations of the putative inositol 1,3,4,5-
RT tetrakisphosphate receptors GAP1(IP4BP) and GAP1m result from the
RT GAP1(IP4BP) PH domain directing plasma membrane targeting.";
RL Curr. Biol. 7:1007-1010(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.
CC Binds inositol tetrakisphosphate (IP4).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15283-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15283-2; Sequence=VSP_046545;
CC -!- SIMILARITY: Contains 1 Btk-type zinc finger.
CC -!- SIMILARITY: Contains 2 C2 domains.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 Ras-GAP domain.
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DR EMBL; D78155; BAA11230.1; -; mRNA.
DR EMBL; D78156; BAA11231.1; -; Genomic_DNA.
DR EMBL; D82880; BAA11621.1; -; mRNA.
DR EMBL; D82881; BAA11622.1; -; Genomic_DNA.
DR EMBL; AF115573; AAD09821.1; -; mRNA.
DR EMBL; AC010184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78999.1; -; Genomic_DNA.
DR EMBL; AK292016; BAF84705.1; -; mRNA.
DR PIR; JC5047; JC5047.
DR RefSeq; NP_006497.2; NM_006506.2.
DR RefSeq; XP_005247744.1; XM_005247687.1.
DR RefSeq; XP_005247745.1; XM_005247688.1.
DR UniGene; Hs.655941; -.
DR ProteinModelPortal; Q15283; -.
DR SMR; Q15283; 30-598, 608-739.
DR STRING; 9606.ENSP00000286364; -.
DR PhosphoSite; Q15283; -.
DR DMDM; 13959563; -.
DR PaxDb; Q15283; -.
DR PRIDE; Q15283; -.
DR DNASU; 5922; -.
DR Ensembl; ENST00000286364; ENSP00000286364; ENSG00000155903.
DR Ensembl; ENST00000452898; ENSP00000391677; ENSG00000155903.
DR GeneID; 5922; -.
DR KEGG; hsa:5922; -.
DR UCSC; uc003eua.1; human.
DR CTD; 5922; -.
DR GeneCards; GC03P141205; -.
DR HGNC; HGNC:9872; RASA2.
DR HPA; HPA035374; -.
DR MIM; 601589; gene.
DR neXtProt; NX_Q15283; -.
DR PharmGKB; PA34233; -.
DR eggNOG; NOG323905; -.
DR HOGENOM; HOG000007183; -.
DR HOVERGEN; HBG055643; -.
DR InParanoid; Q15283; -.
DR KO; K08053; -.
DR OMA; KPCTAGV; -.
DR OrthoDB; EOG7J17Z6; -.
DR GenomeRNAi; 5922; -.
DR NextBio; 23062; -.
DR PRO; PR:Q15283; -.
DR ArrayExpress; Q15283; -.
DR Bgee; Q15283; -.
DR CleanEx; HS_RASA2; -.
DR Genevestigator; Q15283; -.
DR GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031235; C:intrinsic to cytoplasmic side of plasma membrane; IBA:RefGenome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0005099; F:Ras GTPase activator activity; IBA:RefGenome.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IBA:RefGenome.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR001936; RasGAP.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001562; Znf_Btk_motif.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 1.
DR PRINTS; PR00402; TECBTKDOMAIN.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW GTPase activation; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 850 Ras GTPase-activating protein 2.
FT /FTId=PRO_0000056638.
FT DOMAIN 25 122 C2 1.
FT DOMAIN 158 273 C2 2.
FT DOMAIN 356 550 Ras-GAP.
FT DOMAIN 604 706 PH.
FT ZN_FING 708 744 Btk-type.
FT COMPBIAS 2 26 Ala-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 646 646 Missing (in isoform 2).
FT /FTId=VSP_046545.
FT CONFLICT 216 216 T -> A (in Ref. 1; BAA11230).
FT CONFLICT 225 225 F -> S (in Ref. 4; BAF84705).
FT CONFLICT 645 645 G -> EFIER (in Ref. 2; BAA11621).
SQ SEQUENCE 850 AA; 96614 MW; 1F357940CA106E5E CRC64;
MAAAAPAAAA ASSEAPAASA TAEPEAGDQD SREVRVLQSL RGKICEAKNL LPYLGPHKMR
DCFCTINLDQ EEVYRTQVVE KSLSPFFSEE FYFEIPRTFQ YLSFYVYDKN VLQRDLRIGK
VAIKKEDLCN HSGKETWFSL QPVDSNSEVQ GKVHLELKLN ELITENGTVC QQLVVHIKAC
HGLPLINGQS CDPYATVSLV GPSRNDQKKT KVKKKTSNPQ FNEIFYFEVT RSSSYTRKSQ
FQVEEEDIEK LEIRIDLWNN GNLVQDVFLG EIKVPVNVLR TDSSHQAWYL LQPRDNGNKS
SKTDDLGSLR LNICYTEDYV LPSEYYGPLK TLLLKSPDVQ PISASAAYIL SEICRDKNDA
VLPLVRLLLH HDKLVPFATA VAELDLKDTQ DANTIFRGNS LATRCLDEMM KIVGGHYLKV
TLKPILDEIC DSSKSCEIDP IKLKEGDNVE NNKENLRYYV DKLFNTIVKS SMSCPTVMCD
IFYSLRQMAT QRFPNDPHVQ YSAVSSFVFL RFFAVAVVSP HTFHLRPHHP DAQTIRTLTL
ISKTIQTLGS WGSLSKSKSS FKETFMCEFF KMFQEEGYII AVKKFLDEIS STETKESSGT
SEPVHLKEGE MYKRAQGRTR IGKKNFKKRW FCLTSRELTY HKQPGSKDAI YTIPVKNILA
VEKLEESSFN KKNMFQVIHT EKPLYVQANN CVEANEWIDV LCRVSRCNQN RLSFYHPSVY
LNGNWLCCQE TGENTLGCKP CTAGVPADIQ IDIDEDRETE RIYSLFTLSL LKLQKMEEAC
GTIAVYQGPQ KEPDDYSNFV IEDSVTTFKT IQQIKSIIEK LDEPHEKYRK KRSSSAKYGS
KENPIVGKAS
//
ID RASA2_HUMAN Reviewed; 850 AA.
AC Q15283; A8K7K1; G3V0F9; O00695; Q15284; Q92594; Q99577; Q9UEQ2;
read moreDT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 3.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Ras GTPase-activating protein 2;
DE AltName: Full=GTPase-activating protein 1m;
DE Short=GAP1m;
GN Name=RASA2; Synonyms=GAP1M, RASGAP;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=8917095; DOI=10.1016/0378-1119(96)00144-8;
RA Kobayashi M., Masui T., Kusuda J., Kameoka Y., Hashimoto K.,
RA Iwashita S.;
RT "Human rasGTPase-activating protein (human counterpart of GAP1m):
RT sequence of the cDNA, primary structure of the protein, production and
RT chromosomal localization.";
RL Gene 175:173-177(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=8812506; DOI=10.1006/geno.1996.0412;
RA Li S., Satoh H., Watanabe T., Nakamura S., Hattori S.;
RT "cDNA cloning and chromosomal mapping of a novel human GAP (GAP1M), a
RT GTPase-activating protein of Ras.";
RL Genomics 35:625-627(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Blood;
RX PubMed=9382842; DOI=10.1016/S0960-9822(06)00423-4;
RA Lockyer P.J., Bottomley J.R., Reynolds J.S., McNulty T.J.,
RA Venkateswarlu K., Potter B.V.L., Dempsey C.E., Cullen P.J.;
RT "Distinct subcellular localisations of the putative inositol 1,3,4,5-
RT tetrakisphosphate receptors GAP1(IP4BP) and GAP1m result from the
RT GAP1(IP4BP) PH domain directing plasma membrane targeting.";
RL Curr. Biol. 7:1007-1010(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.
CC Binds inositol tetrakisphosphate (IP4).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15283-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15283-2; Sequence=VSP_046545;
CC -!- SIMILARITY: Contains 1 Btk-type zinc finger.
CC -!- SIMILARITY: Contains 2 C2 domains.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 Ras-GAP domain.
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DR EMBL; D78155; BAA11230.1; -; mRNA.
DR EMBL; D78156; BAA11231.1; -; Genomic_DNA.
DR EMBL; D82880; BAA11621.1; -; mRNA.
DR EMBL; D82881; BAA11622.1; -; Genomic_DNA.
DR EMBL; AF115573; AAD09821.1; -; mRNA.
DR EMBL; AC010184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78999.1; -; Genomic_DNA.
DR EMBL; AK292016; BAF84705.1; -; mRNA.
DR PIR; JC5047; JC5047.
DR RefSeq; NP_006497.2; NM_006506.2.
DR RefSeq; XP_005247744.1; XM_005247687.1.
DR RefSeq; XP_005247745.1; XM_005247688.1.
DR UniGene; Hs.655941; -.
DR ProteinModelPortal; Q15283; -.
DR SMR; Q15283; 30-598, 608-739.
DR STRING; 9606.ENSP00000286364; -.
DR PhosphoSite; Q15283; -.
DR DMDM; 13959563; -.
DR PaxDb; Q15283; -.
DR PRIDE; Q15283; -.
DR DNASU; 5922; -.
DR Ensembl; ENST00000286364; ENSP00000286364; ENSG00000155903.
DR Ensembl; ENST00000452898; ENSP00000391677; ENSG00000155903.
DR GeneID; 5922; -.
DR KEGG; hsa:5922; -.
DR UCSC; uc003eua.1; human.
DR CTD; 5922; -.
DR GeneCards; GC03P141205; -.
DR HGNC; HGNC:9872; RASA2.
DR HPA; HPA035374; -.
DR MIM; 601589; gene.
DR neXtProt; NX_Q15283; -.
DR PharmGKB; PA34233; -.
DR eggNOG; NOG323905; -.
DR HOGENOM; HOG000007183; -.
DR HOVERGEN; HBG055643; -.
DR InParanoid; Q15283; -.
DR KO; K08053; -.
DR OMA; KPCTAGV; -.
DR OrthoDB; EOG7J17Z6; -.
DR GenomeRNAi; 5922; -.
DR NextBio; 23062; -.
DR PRO; PR:Q15283; -.
DR ArrayExpress; Q15283; -.
DR Bgee; Q15283; -.
DR CleanEx; HS_RASA2; -.
DR Genevestigator; Q15283; -.
DR GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031235; C:intrinsic to cytoplasmic side of plasma membrane; IBA:RefGenome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0005099; F:Ras GTPase activator activity; IBA:RefGenome.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IBA:RefGenome.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR001936; RasGAP.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001562; Znf_Btk_motif.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 1.
DR PRINTS; PR00402; TECBTKDOMAIN.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW GTPase activation; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 850 Ras GTPase-activating protein 2.
FT /FTId=PRO_0000056638.
FT DOMAIN 25 122 C2 1.
FT DOMAIN 158 273 C2 2.
FT DOMAIN 356 550 Ras-GAP.
FT DOMAIN 604 706 PH.
FT ZN_FING 708 744 Btk-type.
FT COMPBIAS 2 26 Ala-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 646 646 Missing (in isoform 2).
FT /FTId=VSP_046545.
FT CONFLICT 216 216 T -> A (in Ref. 1; BAA11230).
FT CONFLICT 225 225 F -> S (in Ref. 4; BAF84705).
FT CONFLICT 645 645 G -> EFIER (in Ref. 2; BAA11621).
SQ SEQUENCE 850 AA; 96614 MW; 1F357940CA106E5E CRC64;
MAAAAPAAAA ASSEAPAASA TAEPEAGDQD SREVRVLQSL RGKICEAKNL LPYLGPHKMR
DCFCTINLDQ EEVYRTQVVE KSLSPFFSEE FYFEIPRTFQ YLSFYVYDKN VLQRDLRIGK
VAIKKEDLCN HSGKETWFSL QPVDSNSEVQ GKVHLELKLN ELITENGTVC QQLVVHIKAC
HGLPLINGQS CDPYATVSLV GPSRNDQKKT KVKKKTSNPQ FNEIFYFEVT RSSSYTRKSQ
FQVEEEDIEK LEIRIDLWNN GNLVQDVFLG EIKVPVNVLR TDSSHQAWYL LQPRDNGNKS
SKTDDLGSLR LNICYTEDYV LPSEYYGPLK TLLLKSPDVQ PISASAAYIL SEICRDKNDA
VLPLVRLLLH HDKLVPFATA VAELDLKDTQ DANTIFRGNS LATRCLDEMM KIVGGHYLKV
TLKPILDEIC DSSKSCEIDP IKLKEGDNVE NNKENLRYYV DKLFNTIVKS SMSCPTVMCD
IFYSLRQMAT QRFPNDPHVQ YSAVSSFVFL RFFAVAVVSP HTFHLRPHHP DAQTIRTLTL
ISKTIQTLGS WGSLSKSKSS FKETFMCEFF KMFQEEGYII AVKKFLDEIS STETKESSGT
SEPVHLKEGE MYKRAQGRTR IGKKNFKKRW FCLTSRELTY HKQPGSKDAI YTIPVKNILA
VEKLEESSFN KKNMFQVIHT EKPLYVQANN CVEANEWIDV LCRVSRCNQN RLSFYHPSVY
LNGNWLCCQE TGENTLGCKP CTAGVPADIQ IDIDEDRETE RIYSLFTLSL LKLQKMEEAC
GTIAVYQGPQ KEPDDYSNFV IEDSVTTFKT IQQIKSIIEK LDEPHEKYRK KRSSSAKYGS
KENPIVGKAS
//
MIM
601589
*RECORD*
*FIELD* NO
601589
*FIELD* TI
*601589 RAS p21 PROTEIN ACTIVATOR 2; RASA2
;;GTPase-ACTIVATING PROTEIN OF RAS; GAP1M
read more*FIELD* TX
CLONING
Maekawa et al. (1994) isolated a mammalian GTPase-activating protein of
RAS from rat (GAP1M) that shows sequence similarity to the suppressor of
RAS (see 190020) function in Drosophila, known as Gap1 (Gaul et al.,
1992). Expression was relatively high in brain, placenta, and kidney but
lower in other tissues. A recombinantly expressed protein containing the
GAP-related domain was shown to stimulate GTPase activity of RAS.
Li et al. (1996) isolated the human homolog of rat GAP1M from a brain
cDNA library. The deduced 853-amino acid protein is 89.4% identical to
the rat protein.
MAPPING
Using a panel of somatic cell hybrid DNAs, Li et al. (1996) mapped the
human GAP1M gene to chromosome 3. By fluroescence in situ hybridization,
they mapped GAP1M to 3q22-q23.
*FIELD* RF
1. Gaul, U.; Mardon, G.; Rubin, G. M.: A putative Ras GTPase activating
protein acts as a negative regulator of signaling by the Sevenless
receptor tyrosine kinase. Cell 68: 1007-1019, 1992.
2. Li, S.; Satoh, H.; Watanabe, T.; Nakamura, S.; Hattori, S.: cDNA
cloning and chromosomal mapping of a novel human GAP (GAP1M), a GTPase-activating
protein of Ras. Genomics 35: 625-627, 1996.
3. Maekawa, M.; Li, S.; Iwamatsu, A.; Morishita, T.; Yokota, K.; Imai,
Y.; Kohsaka, S.; Nakamura, S.; Hattori, S.: A novel mammalian Ras
GTPase-activating protein which has phospholipid-binding and Btk homology
regions. Molec. Cell. Biol. 14: 6879-6885, 1994.
*FIELD* CD
Alan F. Scott: 12/18/1996
*FIELD* ED
carol: 06/08/2010
psherman: 8/12/1999
jamie: 1/6/1997
jamie: 12/19/1996
*RECORD*
*FIELD* NO
601589
*FIELD* TI
*601589 RAS p21 PROTEIN ACTIVATOR 2; RASA2
;;GTPase-ACTIVATING PROTEIN OF RAS; GAP1M
read more*FIELD* TX
CLONING
Maekawa et al. (1994) isolated a mammalian GTPase-activating protein of
RAS from rat (GAP1M) that shows sequence similarity to the suppressor of
RAS (see 190020) function in Drosophila, known as Gap1 (Gaul et al.,
1992). Expression was relatively high in brain, placenta, and kidney but
lower in other tissues. A recombinantly expressed protein containing the
GAP-related domain was shown to stimulate GTPase activity of RAS.
Li et al. (1996) isolated the human homolog of rat GAP1M from a brain
cDNA library. The deduced 853-amino acid protein is 89.4% identical to
the rat protein.
MAPPING
Using a panel of somatic cell hybrid DNAs, Li et al. (1996) mapped the
human GAP1M gene to chromosome 3. By fluroescence in situ hybridization,
they mapped GAP1M to 3q22-q23.
*FIELD* RF
1. Gaul, U.; Mardon, G.; Rubin, G. M.: A putative Ras GTPase activating
protein acts as a negative regulator of signaling by the Sevenless
receptor tyrosine kinase. Cell 68: 1007-1019, 1992.
2. Li, S.; Satoh, H.; Watanabe, T.; Nakamura, S.; Hattori, S.: cDNA
cloning and chromosomal mapping of a novel human GAP (GAP1M), a GTPase-activating
protein of Ras. Genomics 35: 625-627, 1996.
3. Maekawa, M.; Li, S.; Iwamatsu, A.; Morishita, T.; Yokota, K.; Imai,
Y.; Kohsaka, S.; Nakamura, S.; Hattori, S.: A novel mammalian Ras
GTPase-activating protein which has phospholipid-binding and Btk homology
regions. Molec. Cell. Biol. 14: 6879-6885, 1994.
*FIELD* CD
Alan F. Scott: 12/18/1996
*FIELD* ED
carol: 06/08/2010
psherman: 8/12/1999
jamie: 1/6/1997
jamie: 12/19/1996