Full text data of DRG2
DRG2
[Confidence: low (only semi-automatic identification from reviews)]
Developmentally-regulated GTP-binding protein 2; DRG-2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Developmentally-regulated GTP-binding protein 2; DRG-2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P55039
ID DRG2_HUMAN Reviewed; 364 AA.
AC P55039; B2R8G5; Q53Y50; Q9BWB2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Developmentally-regulated GTP-binding protein 2;
DE Short=DRG-2;
GN Name=DRG2;
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].
RC TISSUE=Lung;
RX PubMed=7929244;
RA Schenker T., Lach C., Kessler B., Calderara S., Trueb B.;
RT "A novel GTP-binding protein which is selectively repressed in SV40
RT transformed fibroblasts.";
RL J. Biol. Chem. 269:25447-25453(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-194.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-194.
RC TISSUE=Lung;
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 [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: May play a role in cell proliferation, differentiation
CC and death.
CC -!- SUBUNIT: Interacts with RWDD1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highest levels in skeletal muscle, heart and
CC kidney. Low levels in colon, thymus, spleen, small intestine, lung
CC and Leukocytes.
CC -!- PTM: Polyubiquitinated; which induces proteolytic degradation and
CC is impaired by interaction with RWDD1 (By similarity).
CC -!- SIMILARITY: Belongs to the GTP1/OBG family.
CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X80754; CAA56730.1; -; mRNA.
DR EMBL; BT006976; AAP35622.1; -; mRNA.
DR EMBL; AK313362; BAG36162.1; -; mRNA.
DR EMBL; CH471196; EAW55669.1; -; Genomic_DNA.
DR EMBL; BC000493; AAH00493.1; -; mRNA.
DR PIR; A55014; A55014.
DR RefSeq; NP_001379.1; NM_001388.4.
DR UniGene; Hs.78582; -.
DR ProteinModelPortal; P55039; -.
DR SMR; P55039; 4-364.
DR IntAct; P55039; 2.
DR MINT; MINT-1453971; -.
DR STRING; 9606.ENSP00000225729; -.
DR PhosphoSite; P55039; -.
DR DMDM; 1706518; -.
DR PaxDb; P55039; -.
DR PRIDE; P55039; -.
DR DNASU; 1819; -.
DR Ensembl; ENST00000225729; ENSP00000225729; ENSG00000108591.
DR GeneID; 1819; -.
DR KEGG; hsa:1819; -.
DR UCSC; uc002gsh.2; human.
DR CTD; 1819; -.
DR GeneCards; GC17P017992; -.
DR HGNC; HGNC:3030; DRG2.
DR HPA; HPA007716; -.
DR MIM; 602986; gene.
DR neXtProt; NX_P55039; -.
DR PharmGKB; PA27484; -.
DR eggNOG; COG1163; -.
DR HOGENOM; HOG000112078; -.
DR HOVERGEN; HBG000948; -.
DR InParanoid; P55039; -.
DR KO; K06944; -.
DR OMA; IRIYTKR; -.
DR OrthoDB; EOG7PZRXJ; -.
DR PhylomeDB; P55039; -.
DR GeneWiki; DRG2; -.
DR GenomeRNAi; 1819; -.
DR NextBio; 7413; -.
DR PRO; PR:P55039; -.
DR ArrayExpress; P55039; -.
DR Bgee; P55039; -.
DR CleanEx; HS_DRG2; -.
DR Genevestigator; P55039; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR006073; GTP_binding_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF02824; TGS; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Polymorphism; Reference proteome; Ubl conjugation.
FT CHAIN 1 364 Developmentally-regulated GTP-binding
FT protein 2.
FT /FTId=PRO_0000205427.
FT DOMAIN 74 172 G.
FT NP_BIND 69 76 GTP (By similarity).
FT NP_BIND 115 119 GTP (By similarity).
FT NP_BIND 246 249 GTP (By similarity).
FT VARIANT 194 194 T -> M (in dbSNP:rs17855350).
FT /FTId=VAR_067452.
FT VARIANT 224 224 S -> T (in dbSNP:rs61256737).
FT /FTId=VAR_067453.
SQ SEQUENCE 364 AA; 40746 MW; D1754BEB02671F85 CRC64;
MGILEKISEI EKEIARTQKN KATEYHLGLL KAKLAKYRAQ LLEPSKSASS KGEGFDVMKS
GDARVALIGF PSVGKSTFLS LMTSTASEAA SYEFTTLTCI PGVIEYKGAN IQLLDLPGII
EGAAQGKGRG RQVIAVARTA DVIIMMLDAT KGEVQRSLLE KELESVGIRL NKHKPNIYFK
PKKGGGISFN STVTLTQCSE KLVQLILHEY KIFNAEVLFR EDCSPDEFID VIVGNRVYMP
CLYVYNKIDQ ISMEEVDRLA RKPNSVVISC GMKLNLDYLL EMLWEYLALT CIYTKKRGQR
PDFTDAIILR KGASVEHVCH RIHRSLASQF KYALVWGTST KYSPQRVGLT HTMEHEDVIQ
IVKK
//
ID DRG2_HUMAN Reviewed; 364 AA.
AC P55039; B2R8G5; Q53Y50; Q9BWB2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Developmentally-regulated GTP-binding protein 2;
DE Short=DRG-2;
GN Name=DRG2;
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].
RC TISSUE=Lung;
RX PubMed=7929244;
RA Schenker T., Lach C., Kessler B., Calderara S., Trueb B.;
RT "A novel GTP-binding protein which is selectively repressed in SV40
RT transformed fibroblasts.";
RL J. Biol. Chem. 269:25447-25453(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-194.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-194.
RC TISSUE=Lung;
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 [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: May play a role in cell proliferation, differentiation
CC and death.
CC -!- SUBUNIT: Interacts with RWDD1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highest levels in skeletal muscle, heart and
CC kidney. Low levels in colon, thymus, spleen, small intestine, lung
CC and Leukocytes.
CC -!- PTM: Polyubiquitinated; which induces proteolytic degradation and
CC is impaired by interaction with RWDD1 (By similarity).
CC -!- SIMILARITY: Belongs to the GTP1/OBG family.
CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X80754; CAA56730.1; -; mRNA.
DR EMBL; BT006976; AAP35622.1; -; mRNA.
DR EMBL; AK313362; BAG36162.1; -; mRNA.
DR EMBL; CH471196; EAW55669.1; -; Genomic_DNA.
DR EMBL; BC000493; AAH00493.1; -; mRNA.
DR PIR; A55014; A55014.
DR RefSeq; NP_001379.1; NM_001388.4.
DR UniGene; Hs.78582; -.
DR ProteinModelPortal; P55039; -.
DR SMR; P55039; 4-364.
DR IntAct; P55039; 2.
DR MINT; MINT-1453971; -.
DR STRING; 9606.ENSP00000225729; -.
DR PhosphoSite; P55039; -.
DR DMDM; 1706518; -.
DR PaxDb; P55039; -.
DR PRIDE; P55039; -.
DR DNASU; 1819; -.
DR Ensembl; ENST00000225729; ENSP00000225729; ENSG00000108591.
DR GeneID; 1819; -.
DR KEGG; hsa:1819; -.
DR UCSC; uc002gsh.2; human.
DR CTD; 1819; -.
DR GeneCards; GC17P017992; -.
DR HGNC; HGNC:3030; DRG2.
DR HPA; HPA007716; -.
DR MIM; 602986; gene.
DR neXtProt; NX_P55039; -.
DR PharmGKB; PA27484; -.
DR eggNOG; COG1163; -.
DR HOGENOM; HOG000112078; -.
DR HOVERGEN; HBG000948; -.
DR InParanoid; P55039; -.
DR KO; K06944; -.
DR OMA; IRIYTKR; -.
DR OrthoDB; EOG7PZRXJ; -.
DR PhylomeDB; P55039; -.
DR GeneWiki; DRG2; -.
DR GenomeRNAi; 1819; -.
DR NextBio; 7413; -.
DR PRO; PR:P55039; -.
DR ArrayExpress; P55039; -.
DR Bgee; P55039; -.
DR CleanEx; HS_DRG2; -.
DR Genevestigator; P55039; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR006073; GTP_binding_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF02824; TGS; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Polymorphism; Reference proteome; Ubl conjugation.
FT CHAIN 1 364 Developmentally-regulated GTP-binding
FT protein 2.
FT /FTId=PRO_0000205427.
FT DOMAIN 74 172 G.
FT NP_BIND 69 76 GTP (By similarity).
FT NP_BIND 115 119 GTP (By similarity).
FT NP_BIND 246 249 GTP (By similarity).
FT VARIANT 194 194 T -> M (in dbSNP:rs17855350).
FT /FTId=VAR_067452.
FT VARIANT 224 224 S -> T (in dbSNP:rs61256737).
FT /FTId=VAR_067453.
SQ SEQUENCE 364 AA; 40746 MW; D1754BEB02671F85 CRC64;
MGILEKISEI EKEIARTQKN KATEYHLGLL KAKLAKYRAQ LLEPSKSASS KGEGFDVMKS
GDARVALIGF PSVGKSTFLS LMTSTASEAA SYEFTTLTCI PGVIEYKGAN IQLLDLPGII
EGAAQGKGRG RQVIAVARTA DVIIMMLDAT KGEVQRSLLE KELESVGIRL NKHKPNIYFK
PKKGGGISFN STVTLTQCSE KLVQLILHEY KIFNAEVLFR EDCSPDEFID VIVGNRVYMP
CLYVYNKIDQ ISMEEVDRLA RKPNSVVISC GMKLNLDYLL EMLWEYLALT CIYTKKRGQR
PDFTDAIILR KGASVEHVCH RIHRSLASQF KYALVWGTST KYSPQRVGLT HTMEHEDVIQ
IVKK
//
MIM
602986
*RECORD*
*FIELD* NO
602986
*FIELD* TI
*602986 DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN 2; DRG2
*FIELD* TX
CLONING
read moreUsing a subtractive hybridization strategy, Schenker et al. (1994)
identified embryonic lung fibroblast cDNAs whose expression was
selectively repressed in SV40-transformed cells. One cDNA encoded a
predicted 364-amino acid protein that was designated DRG2. DRG2 contains
the 5 sequence motifs that are conserved in all GTP-binding proteins.
Northern blot analysis detected DRG2 expression as a major 2-kb and a
minor 1.5-kb transcript in various tissues. The shorter mRNA appeared to
result from use of an alternative polyadenylation site.
MAPPING
By fluorescence in situ hybridization, Schenker and Trueb (1997) mapped
the DRG2 gene to 17p13-p12. Vlangos et al. (2000) mapped the DRG2 gene
to 17p11.2 within the Smith-Magenis syndrome critical region by somatic
cell hybrid analysis.
*FIELD* RF
1. Schenker, T.; Lach, C.; Kessler, B.; Calderara, S.; Trueb, B.:
A novel GTP-binding protein which is selectively repressed in SV40
transformed fibroblasts. J. Biol. Chem. 269: 25447-25453, 1994.
2. Schenker, T.; Trueb, B.: Assignment of the gene for a developmentally
regulated GTP-binding protein (DRG2) to human chromosome bands 17p13-p12
by in situ hybridization. Cytogenet. Cell Genet. 79: 274-275, 1997.
3. Vlangos, C. N.; Das, P.; Patel, P. I.; Elsea, S. H.: Assignment
of developmentally regulated GTP-binding protein (DRG2) to human chromosome
band 17p11.2 with somatic cell hybrids and localization to the Smith-Magenis
syndrome critical interval. Cytogenet. Cell Genet. 88: 283-285,
2000.
*FIELD* CN
Joanna S. Amberger - updated: 3/6/2001
*FIELD* CD
Rebekah S. Rasooly: 8/19/1998
*FIELD* ED
carol: 06/14/2012
terry: 3/7/2001
joanna: 3/6/2001
alopez: 8/19/1998
*RECORD*
*FIELD* NO
602986
*FIELD* TI
*602986 DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN 2; DRG2
*FIELD* TX
CLONING
read moreUsing a subtractive hybridization strategy, Schenker et al. (1994)
identified embryonic lung fibroblast cDNAs whose expression was
selectively repressed in SV40-transformed cells. One cDNA encoded a
predicted 364-amino acid protein that was designated DRG2. DRG2 contains
the 5 sequence motifs that are conserved in all GTP-binding proteins.
Northern blot analysis detected DRG2 expression as a major 2-kb and a
minor 1.5-kb transcript in various tissues. The shorter mRNA appeared to
result from use of an alternative polyadenylation site.
MAPPING
By fluorescence in situ hybridization, Schenker and Trueb (1997) mapped
the DRG2 gene to 17p13-p12. Vlangos et al. (2000) mapped the DRG2 gene
to 17p11.2 within the Smith-Magenis syndrome critical region by somatic
cell hybrid analysis.
*FIELD* RF
1. Schenker, T.; Lach, C.; Kessler, B.; Calderara, S.; Trueb, B.:
A novel GTP-binding protein which is selectively repressed in SV40
transformed fibroblasts. J. Biol. Chem. 269: 25447-25453, 1994.
2. Schenker, T.; Trueb, B.: Assignment of the gene for a developmentally
regulated GTP-binding protein (DRG2) to human chromosome bands 17p13-p12
by in situ hybridization. Cytogenet. Cell Genet. 79: 274-275, 1997.
3. Vlangos, C. N.; Das, P.; Patel, P. I.; Elsea, S. H.: Assignment
of developmentally regulated GTP-binding protein (DRG2) to human chromosome
band 17p11.2 with somatic cell hybrids and localization to the Smith-Magenis
syndrome critical interval. Cytogenet. Cell Genet. 88: 283-285,
2000.
*FIELD* CN
Joanna S. Amberger - updated: 3/6/2001
*FIELD* CD
Rebekah S. Rasooly: 8/19/1998
*FIELD* ED
carol: 06/14/2012
terry: 3/7/2001
joanna: 3/6/2001
alopez: 8/19/1998