Full text data of RANGRF
RANGRF
(MOG1, RANGNRF)
[Confidence: low (only semi-automatic identification from reviews)]
Ran guanine nucleotide release factor; RanGNRF (Ran-binding protein MOG1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ran guanine nucleotide release factor; RanGNRF (Ran-binding protein MOG1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9HD47
ID MOG1_HUMAN Reviewed; 186 AA.
AC Q9HD47; D3DTR6; Q68DI3; Q9BR68; Q9HD48; Q9NRU9; Q9P001; Q9P0P2;
read moreDT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 72.
DE RecName: Full=Ran guanine nucleotide release factor;
DE Short=RanGNRF;
DE AltName: Full=Ran-binding protein MOG1;
GN Name=RANGRF; Synonyms=MOG1, RANGNRF; ORFNames=HSPC165, HSPC236, MDS5;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11290418; DOI=10.1016/S0378-1119(01)00364-X;
RA Marfatia K.A., Harreman M.T., Fanara P., Vertino P.M., Corbett A.H.;
RT "Identification and characterization of the human MOG1 gene.";
RL Gene 266:45-56(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J.,
RA Gu J., Huang Q., Yu Y., Xu S., Ren S., Fu G.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT Myelodysplastic Syndromes patient.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
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 MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Prostate;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
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 (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Bone marrow, Lung, and Uterus;
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 [10]
RP FUNCTION, AND INTERACTION WITH SCN5A.
RX PubMed=18184654; DOI=10.1074/jbc.M709721200;
RA Wu L., Yong S.L., Fan C., Ni Y., Yoo S., Zhang T., Zhang X.,
RA Obejero-Paz C.A., Rho H.J., Ke T., Szafranski P., Jones S.W., Chen Q.,
RA Wang Q.K.;
RT "Identification of a new co-factor, MOG1, required for the full
RT function of cardiac sodium channel Nav1.5.";
RL J. Biol. Chem. 283:6968-6978(2008).
RN [11]
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: May regulate the intracellular trafficking of RAN. In
CC cardiac cells seems to regulate the cell surface localization of
CC SCN5A.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with RAN, RAN-GTP and
CC RAN-GDP. Forms a complex with RAN-GTP and RANBP1 (By similarity).
CC Interacts with the cytoplasmic loop 2 of SCN5A.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC the nucleus and cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=MOG1a;
CC IsoId=Q9HD47-1; Sequence=Displayed;
CC Name=2; Synonyms=MOG1b;
CC IsoId=Q9HD47-2; Sequence=VSP_033060;
CC Name=3;
CC IsoId=Q9HD47-3; Sequence=VSP_033059, VSP_033061;
CC Name=4;
CC IsoId=Q9HD47-4; Sequence=VSP_033057, VSP_033058;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are ubiquitously
CC expressed.
CC -!- SIMILARITY: Belongs to the MOG1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29129.1; Type=Frameshift; Positions=62, 93;
CC Sequence=AAF87316.1; Type=Frameshift; Positions=62;
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DR EMBL; AF265205; AAG01291.1; -; mRNA.
DR EMBL; AF265206; AAG01292.1; -; mRNA.
DR EMBL; AF168714; AAF87316.1; ALT_FRAME; mRNA.
DR EMBL; AF151070; AAF36156.1; -; mRNA.
DR EMBL; AF161514; AAF29129.1; ALT_FRAME; mRNA.
DR EMBL; AK290399; BAF83088.1; -; mRNA.
DR EMBL; CR457206; CAG33487.1; -; mRNA.
DR EMBL; CR749387; CAH18237.1; -; mRNA.
DR EMBL; CH471108; EAW90064.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90065.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90066.1; -; Genomic_DNA.
DR EMBL; BC006486; AAH06486.1; -; mRNA.
DR EMBL; BC012552; AAH12552.1; -; mRNA.
DR EMBL; BC100017; AAI00018.1; -; mRNA.
DR RefSeq; NP_001171272.1; NM_001177801.1.
DR RefSeq; NP_001171273.1; NM_001177802.1.
DR RefSeq; NP_057576.2; NM_016492.4.
DR RefSeq; XP_005256675.1; XM_005256618.1.
DR UniGene; Hs.408233; -.
DR ProteinModelPortal; Q9HD47; -.
DR SMR; Q9HD47; 5-161.
DR STRING; 9606.ENSP00000226105; -.
DR PhosphoSite; Q9HD47; -.
DR DMDM; 74718913; -.
DR PaxDb; Q9HD47; -.
DR PRIDE; Q9HD47; -.
DR Ensembl; ENST00000226105; ENSP00000226105; ENSG00000108961.
DR Ensembl; ENST00000407006; ENSP00000383940; ENSG00000108961.
DR Ensembl; ENST00000439238; ENSP00000413190; ENSG00000108961.
DR Ensembl; ENST00000580434; ENSP00000462310; ENSG00000108961.
DR GeneID; 29098; -.
DR KEGG; hsa:29098; -.
DR UCSC; uc002gkv.3; human.
DR CTD; 29098; -.
DR GeneCards; GC17P008191; -.
DR H-InvDB; HIX0013522; -.
DR HGNC; HGNC:17679; RANGRF.
DR MIM; 607954; gene.
DR neXtProt; NX_Q9HD47; -.
DR PharmGKB; PA162400661; -.
DR eggNOG; NOG287645; -.
DR HOVERGEN; HBG075266; -.
DR InParanoid; Q9HD47; -.
DR OMA; NQPPPDN; -.
DR OrthoDB; EOG7992RS; -.
DR PhylomeDB; Q9HD47; -.
DR GenomeRNAi; 29098; -.
DR NextBio; 52124; -.
DR PRO; PR:Q9HD47; -.
DR Bgee; Q9HD47; -.
DR CleanEx; HS_RANGRF; -.
DR Genevestigator; Q9HD47; -.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISS:BHF-UCL.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:BHF-UCL.
DR GO; GO:0008565; F:protein transporter activity; IMP:BHF-UCL.
DR GO; GO:0008536; F:Ran GTPase binding; ISS:BHF-UCL.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:BHF-UCL.
DR GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:BHF-UCL.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:BHF-UCL.
DR GO; GO:0002027; P:regulation of heart rate; TAS:BHF-UCL.
DR GO; GO:1900825; P:regulation of membrane depolarization involved in regulation of cardiac muscle cell action potential; TAS:BHF-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
DR Gene3D; 3.40.1000.10; -; 1.
DR InterPro; IPR007681; Mog1.
DR InterPro; IPR016123; Mog1/PsbP_a/b/a-sand.
DR Pfam; PF04603; Mog1; 1.
DR SUPFAM; SSF55724; SSF55724; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Guanine-nucleotide releasing factor; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 186 Ran guanine nucleotide release factor.
FT /FTId=PRO_0000330636.
FT VAR_SEQ 118 118 V -> P (in isoform 4).
FT /FTId=VSP_033057.
FT VAR_SEQ 119 186 Missing (in isoform 4).
FT /FTId=VSP_033058.
FT VAR_SEQ 119 163 AKDVTLHQALLRLPQYQTDLLLTFNQPPPDNRSSLGPENLS
FT PAPW -> RARECVMSWKGGSGDAEIQVSILTLIPLGSKGR
FT DTSSGLAEAAPVPD (in isoform 3).
FT /FTId=VSP_033059.
FT VAR_SEQ 147 186 Missing (in isoform 2).
FT /FTId=VSP_033060.
FT VAR_SEQ 164 186 Missing (in isoform 3).
FT /FTId=VSP_033061.
FT CONFLICT 94 96 ALR -> PE (in Ref. 3; AAF36156).
SQ SEQUENCE 186 AA; 20448 MW; BE2C459C90459042 CRC64;
MEPTRDCPLF GGAFSAILPM GAIDVSDLRP VPDNQEVFCH PVTDQSLIVE LLELQAHVRG
EAAARYHFED VGGVQGARAV HVESVQPLSL ENLALRGRCQ EAWVLSGKQQ IAKENQQVAK
DVTLHQALLR LPQYQTDLLL TFNQPPPDNR SSLGPENLSP APWSLGDFEQ LVTSLTLHDP
NIFGPQ
//
ID MOG1_HUMAN Reviewed; 186 AA.
AC Q9HD47; D3DTR6; Q68DI3; Q9BR68; Q9HD48; Q9NRU9; Q9P001; Q9P0P2;
read moreDT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 72.
DE RecName: Full=Ran guanine nucleotide release factor;
DE Short=RanGNRF;
DE AltName: Full=Ran-binding protein MOG1;
GN Name=RANGRF; Synonyms=MOG1, RANGNRF; ORFNames=HSPC165, HSPC236, MDS5;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11290418; DOI=10.1016/S0378-1119(01)00364-X;
RA Marfatia K.A., Harreman M.T., Fanara P., Vertino P.M., Corbett A.H.;
RT "Identification and characterization of the human MOG1 gene.";
RL Gene 266:45-56(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J.,
RA Gu J., Huang Q., Yu Y., Xu S., Ren S., Fu G.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT Myelodysplastic Syndromes patient.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
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 MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Prostate;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
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 (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Bone marrow, Lung, and Uterus;
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 [10]
RP FUNCTION, AND INTERACTION WITH SCN5A.
RX PubMed=18184654; DOI=10.1074/jbc.M709721200;
RA Wu L., Yong S.L., Fan C., Ni Y., Yoo S., Zhang T., Zhang X.,
RA Obejero-Paz C.A., Rho H.J., Ke T., Szafranski P., Jones S.W., Chen Q.,
RA Wang Q.K.;
RT "Identification of a new co-factor, MOG1, required for the full
RT function of cardiac sodium channel Nav1.5.";
RL J. Biol. Chem. 283:6968-6978(2008).
RN [11]
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: May regulate the intracellular trafficking of RAN. In
CC cardiac cells seems to regulate the cell surface localization of
CC SCN5A.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with RAN, RAN-GTP and
CC RAN-GDP. Forms a complex with RAN-GTP and RANBP1 (By similarity).
CC Interacts with the cytoplasmic loop 2 of SCN5A.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC the nucleus and cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=MOG1a;
CC IsoId=Q9HD47-1; Sequence=Displayed;
CC Name=2; Synonyms=MOG1b;
CC IsoId=Q9HD47-2; Sequence=VSP_033060;
CC Name=3;
CC IsoId=Q9HD47-3; Sequence=VSP_033059, VSP_033061;
CC Name=4;
CC IsoId=Q9HD47-4; Sequence=VSP_033057, VSP_033058;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are ubiquitously
CC expressed.
CC -!- SIMILARITY: Belongs to the MOG1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29129.1; Type=Frameshift; Positions=62, 93;
CC Sequence=AAF87316.1; Type=Frameshift; Positions=62;
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DR EMBL; AF265205; AAG01291.1; -; mRNA.
DR EMBL; AF265206; AAG01292.1; -; mRNA.
DR EMBL; AF168714; AAF87316.1; ALT_FRAME; mRNA.
DR EMBL; AF151070; AAF36156.1; -; mRNA.
DR EMBL; AF161514; AAF29129.1; ALT_FRAME; mRNA.
DR EMBL; AK290399; BAF83088.1; -; mRNA.
DR EMBL; CR457206; CAG33487.1; -; mRNA.
DR EMBL; CR749387; CAH18237.1; -; mRNA.
DR EMBL; CH471108; EAW90064.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90065.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90066.1; -; Genomic_DNA.
DR EMBL; BC006486; AAH06486.1; -; mRNA.
DR EMBL; BC012552; AAH12552.1; -; mRNA.
DR EMBL; BC100017; AAI00018.1; -; mRNA.
DR RefSeq; NP_001171272.1; NM_001177801.1.
DR RefSeq; NP_001171273.1; NM_001177802.1.
DR RefSeq; NP_057576.2; NM_016492.4.
DR RefSeq; XP_005256675.1; XM_005256618.1.
DR UniGene; Hs.408233; -.
DR ProteinModelPortal; Q9HD47; -.
DR SMR; Q9HD47; 5-161.
DR STRING; 9606.ENSP00000226105; -.
DR PhosphoSite; Q9HD47; -.
DR DMDM; 74718913; -.
DR PaxDb; Q9HD47; -.
DR PRIDE; Q9HD47; -.
DR Ensembl; ENST00000226105; ENSP00000226105; ENSG00000108961.
DR Ensembl; ENST00000407006; ENSP00000383940; ENSG00000108961.
DR Ensembl; ENST00000439238; ENSP00000413190; ENSG00000108961.
DR Ensembl; ENST00000580434; ENSP00000462310; ENSG00000108961.
DR GeneID; 29098; -.
DR KEGG; hsa:29098; -.
DR UCSC; uc002gkv.3; human.
DR CTD; 29098; -.
DR GeneCards; GC17P008191; -.
DR H-InvDB; HIX0013522; -.
DR HGNC; HGNC:17679; RANGRF.
DR MIM; 607954; gene.
DR neXtProt; NX_Q9HD47; -.
DR PharmGKB; PA162400661; -.
DR eggNOG; NOG287645; -.
DR HOVERGEN; HBG075266; -.
DR InParanoid; Q9HD47; -.
DR OMA; NQPPPDN; -.
DR OrthoDB; EOG7992RS; -.
DR PhylomeDB; Q9HD47; -.
DR GenomeRNAi; 29098; -.
DR NextBio; 52124; -.
DR PRO; PR:Q9HD47; -.
DR Bgee; Q9HD47; -.
DR CleanEx; HS_RANGRF; -.
DR Genevestigator; Q9HD47; -.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISS:BHF-UCL.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:BHF-UCL.
DR GO; GO:0008565; F:protein transporter activity; IMP:BHF-UCL.
DR GO; GO:0008536; F:Ran GTPase binding; ISS:BHF-UCL.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:BHF-UCL.
DR GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:BHF-UCL.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:BHF-UCL.
DR GO; GO:0002027; P:regulation of heart rate; TAS:BHF-UCL.
DR GO; GO:1900825; P:regulation of membrane depolarization involved in regulation of cardiac muscle cell action potential; TAS:BHF-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
DR Gene3D; 3.40.1000.10; -; 1.
DR InterPro; IPR007681; Mog1.
DR InterPro; IPR016123; Mog1/PsbP_a/b/a-sand.
DR Pfam; PF04603; Mog1; 1.
DR SUPFAM; SSF55724; SSF55724; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Guanine-nucleotide releasing factor; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 186 Ran guanine nucleotide release factor.
FT /FTId=PRO_0000330636.
FT VAR_SEQ 118 118 V -> P (in isoform 4).
FT /FTId=VSP_033057.
FT VAR_SEQ 119 186 Missing (in isoform 4).
FT /FTId=VSP_033058.
FT VAR_SEQ 119 163 AKDVTLHQALLRLPQYQTDLLLTFNQPPPDNRSSLGPENLS
FT PAPW -> RARECVMSWKGGSGDAEIQVSILTLIPLGSKGR
FT DTSSGLAEAAPVPD (in isoform 3).
FT /FTId=VSP_033059.
FT VAR_SEQ 147 186 Missing (in isoform 2).
FT /FTId=VSP_033060.
FT VAR_SEQ 164 186 Missing (in isoform 3).
FT /FTId=VSP_033061.
FT CONFLICT 94 96 ALR -> PE (in Ref. 3; AAF36156).
SQ SEQUENCE 186 AA; 20448 MW; BE2C459C90459042 CRC64;
MEPTRDCPLF GGAFSAILPM GAIDVSDLRP VPDNQEVFCH PVTDQSLIVE LLELQAHVRG
EAAARYHFED VGGVQGARAV HVESVQPLSL ENLALRGRCQ EAWVLSGKQQ IAKENQQVAK
DVTLHQALLR LPQYQTDLLL TFNQPPPDNR SSLGPENLSP APWSLGDFEQ LVTSLTLHDP
NIFGPQ
//
MIM
607954
*RECORD*
*FIELD* NO
607954
*FIELD* TI
*607954 RAN GUANINE NUCLEOTIDE RELEASE FACTOR
;;RANGNRF;;
MOG1, S. CEREVISIAE, HOMOLOG OF; MOG1
read more*FIELD* TX
CLONING
Steggerda and Paschal (2000) cloned mouse Mog1. The deduced protein
contains 185 amino acids. Epitope-tagged Mog1 localized to nuclei of
transfected baby hamster kidney cells, but it was excluded from
nucleoli.
By screening an EST database for homologs of S. cerevisiae Mog1,
Marfatia et al. (2001) identified 2 alternately spliced variants of
MOG1. One variant, which they designated MOG1a, contains 187 amino acids
and has a calculated molecular mass of about 20 kD. The other variant,
MOG1b, contains 146 amino acids and has a calculated molecular mass of
about 16 kD. MOG1a and MOG1b share 29% and 30% amino acid identity with
S. cerevisiae Mog1, respectively. Northern blot analysis detected a
0.85-kb MOG1a transcript and a 1.1-kb MOG1b transcript in all tissues
examined, with MOG1a being the predominant transcript. PCR of a breast
cancer cell line showed multiple products, suggesting the presence of
additional splice variants. SDS-PAGE of in vitro translated MOG1a
indicated that the protein migrates with an apparent molecular mass of
about 28 kD. Transfection of fluorescence-labeled MOG1 into HEK293 cells
resulted in overall staining with a nuclear concentration.
GENE FUNCTION
Using chromatography and both solution- and solid-phase binding assays,
Steggerda and Paschal (2000) determined that mouse Mog1 formed a complex
with Ran (601179) and Ranbp1 (601180). Mog1 stably bound to
nucleotide-free Ran in the absence of Ranbp1, and it bound to RanGTP in
the presence of Ranbp1. Mog1 and Ranbp1 did not interact directly,
indicating that RanGTP acted as a bridge. Steggerda and Paschal (2000)
showed that Mog1 stimulated the release of GTP from Ran, and following
GTP release, Mog1 remained bound to nucleotide-free Ran in a
conformation that prevented rebinding of the guanine nucleotide.
By yeast 2-hybrid analysis and in vitro binding assays, Marfatia et al.
(2001) confirmed that MOG1 interacts with both human and S. cerevisiae
Ran. The interaction was independent of guanine nucleotides, as MOG1
interacted with Ran-GTP, Ran-GDT, nucleotide-free Ran, and Ran
preincubated with nonhydrolyzable guanine nucleotide analogs. Human MOG1
partially complemented the growth defect of a Mog1 null yeast cell line.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RANGNRF
gene to chromosome 17 (TMAP A006E21).
*FIELD* RF
1. Marfatia, K. A.; Harreman, M. T.; Fanara, P.; Vertino, P. M.; Corbett,
A. H.: Identification and characterization of the human MOG1 gene. Gene 266:
45-56, 2001.
2. Steggerda, S. M.; Paschal, B. M.: The mammalian Mog1 protein is
a guanine nucleotide release factor for Ran. J. Biol. Chem. 275:
23175-23180, 2000.
*FIELD* CD
Patricia A. Hartz: 7/17/2003
*FIELD* ED
mgross: 07/17/2003
*RECORD*
*FIELD* NO
607954
*FIELD* TI
*607954 RAN GUANINE NUCLEOTIDE RELEASE FACTOR
;;RANGNRF;;
MOG1, S. CEREVISIAE, HOMOLOG OF; MOG1
read more*FIELD* TX
CLONING
Steggerda and Paschal (2000) cloned mouse Mog1. The deduced protein
contains 185 amino acids. Epitope-tagged Mog1 localized to nuclei of
transfected baby hamster kidney cells, but it was excluded from
nucleoli.
By screening an EST database for homologs of S. cerevisiae Mog1,
Marfatia et al. (2001) identified 2 alternately spliced variants of
MOG1. One variant, which they designated MOG1a, contains 187 amino acids
and has a calculated molecular mass of about 20 kD. The other variant,
MOG1b, contains 146 amino acids and has a calculated molecular mass of
about 16 kD. MOG1a and MOG1b share 29% and 30% amino acid identity with
S. cerevisiae Mog1, respectively. Northern blot analysis detected a
0.85-kb MOG1a transcript and a 1.1-kb MOG1b transcript in all tissues
examined, with MOG1a being the predominant transcript. PCR of a breast
cancer cell line showed multiple products, suggesting the presence of
additional splice variants. SDS-PAGE of in vitro translated MOG1a
indicated that the protein migrates with an apparent molecular mass of
about 28 kD. Transfection of fluorescence-labeled MOG1 into HEK293 cells
resulted in overall staining with a nuclear concentration.
GENE FUNCTION
Using chromatography and both solution- and solid-phase binding assays,
Steggerda and Paschal (2000) determined that mouse Mog1 formed a complex
with Ran (601179) and Ranbp1 (601180). Mog1 stably bound to
nucleotide-free Ran in the absence of Ranbp1, and it bound to RanGTP in
the presence of Ranbp1. Mog1 and Ranbp1 did not interact directly,
indicating that RanGTP acted as a bridge. Steggerda and Paschal (2000)
showed that Mog1 stimulated the release of GTP from Ran, and following
GTP release, Mog1 remained bound to nucleotide-free Ran in a
conformation that prevented rebinding of the guanine nucleotide.
By yeast 2-hybrid analysis and in vitro binding assays, Marfatia et al.
(2001) confirmed that MOG1 interacts with both human and S. cerevisiae
Ran. The interaction was independent of guanine nucleotides, as MOG1
interacted with Ran-GTP, Ran-GDT, nucleotide-free Ran, and Ran
preincubated with nonhydrolyzable guanine nucleotide analogs. Human MOG1
partially complemented the growth defect of a Mog1 null yeast cell line.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RANGNRF
gene to chromosome 17 (TMAP A006E21).
*FIELD* RF
1. Marfatia, K. A.; Harreman, M. T.; Fanara, P.; Vertino, P. M.; Corbett,
A. H.: Identification and characterization of the human MOG1 gene. Gene 266:
45-56, 2001.
2. Steggerda, S. M.; Paschal, B. M.: The mammalian Mog1 protein is
a guanine nucleotide release factor for Ran. J. Biol. Chem. 275:
23175-23180, 2000.
*FIELD* CD
Patricia A. Hartz: 7/17/2003
*FIELD* ED
mgross: 07/17/2003