Full text data of DENR
DENR
(DRP1)
[Confidence: low (only semi-automatic identification from reviews)]
Density-regulated protein; DRP (Protein DRP1; Smooth muscle cell-associated protein 3; SMAP-3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Density-regulated protein; DRP (Protein DRP1; Smooth muscle cell-associated protein 3; SMAP-3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43583
ID DENR_HUMAN Reviewed; 198 AA.
AC O43583; Q9H3U6; Q9UKZ0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-APR-2001, sequence version 2.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Density-regulated protein;
DE Short=DRP;
DE AltName: Full=Protein DRP1;
DE AltName: Full=Smooth muscle cell-associated protein 3;
DE Short=SMAP-3;
GN Name=DENR; Synonyms=DRP1; ORFNames=H14;
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9628587; DOI=10.1089/dna.1998.17.437;
RA Deyo J.E., Chiao P.J., Tainsky M.A.;
RT "Drp, a novel protein expressed at high cell density but not during
RT growth arrest.";
RL DNA Cell Biol. 17:437-447(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Nishimoto S., Toyoda H., Tawara J., Aoki T., Komurasaki T.;
RT "Molecular cloning and characterization of human smooth muscle cell
RT associated protein-3 (SMAP-3).";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-198, AND INDUCTION BY ERBB2.
RX PubMed=10497265; DOI=10.1093/nar/27.20.4008;
RA Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.;
RT "Identification of differentially expressed genes associated with HER-
RT 2/neu overexpression in human breast cancer cells.";
RL Nucleic Acids Res. 27:4008-4017(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH MCTS1.
RX PubMed=16982740; DOI=10.1158/0008-5472.CAN-06-1999;
RA Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M.,
RA Bachman K.E., He H., Gartenhaus R.B.;
RT "MCT-1 protein interacts with the cap complex and modulates messenger
RT RNA translational profiles.";
RL Cancer Res. 66:8994-9001(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, AND INDUCTION BY HNRNPD.
RX PubMed=17878526;
RA Mazan-Mamczarz K., Gartenhaus R.B.;
RT "Post-transcriptional control of the MCT-1-associated protein DENR/DRP
RT by RNA-binding protein AUF1.";
RL Cancer Genomics Proteomics 4:233-239(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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 be involved in the translation of target mRNAs by
CC scanning and recognition of the initiation codon. Plays a role in
CC the modulation of the translational profile of a subset of cancer-
CC related mRNAs when recruited to the translational initiation
CC complex by the oncogene MCTS1.
CC -!- SUBUNIT: Interacts with MCTS1.
CC -!- INTERACTION:
CC Q9NX47:MARCH5; NbExp=2; IntAct=EBI-716083, EBI-2341610;
CC Q8WX92:NELFB; NbExp=2; IntAct=EBI-716083, EBI-347721;
CC P0CG48:UBC; NbExp=3; IntAct=EBI-716083, EBI-3390054;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle
CC and moderately expressed in the brain, placenta, liver and
CC pancreas. Weakly expressed in the lung and kidney.
CC -!- INDUCTION: Up-regulated with increasing cell-density by HNRNPD.
CC Up-regulated in ovarian and breast cancer cells by ERBB2
CC overexpression. Not induced by TGFB1.
CC -!- SIMILARITY: Belongs to the DENR family.
CC -!- SIMILARITY: Contains 1 SUI1 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02985.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DENRID40295ch12q24.html";
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DR EMBL; AF038554; AAC02985.2; ALT_INIT; mRNA.
DR EMBL; AB014731; BAB20268.1; -; mRNA.
DR EMBL; AC026331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007860; AAH07860.1; -; mRNA.
DR EMBL; AF103800; AAF02420.1; -; mRNA.
DR RefSeq; NP_003668.2; NM_003677.3.
DR UniGene; Hs.22393; -.
DR ProteinModelPortal; O43583; -.
DR SMR; O43583; 111-193.
DR IntAct; O43583; 5.
DR MINT; MINT-1405155; -.
DR STRING; 9606.ENSP00000280557; -.
DR PhosphoSite; O43583; -.
DR PaxDb; O43583; -.
DR PRIDE; O43583; -.
DR DNASU; 8562; -.
DR Ensembl; ENST00000280557; ENSP00000280557; ENSG00000139726.
DR GeneID; 8562; -.
DR KEGG; hsa:8562; -.
DR UCSC; uc001uda.3; human.
DR CTD; 8562; -.
DR GeneCards; GC12P123237; -.
DR HGNC; HGNC:2769; DENR.
DR HPA; HPA021783; -.
DR MIM; 604550; gene.
DR neXtProt; NX_O43583; -.
DR PharmGKB; PA27252; -.
DR eggNOG; COG0023; -.
DR HOGENOM; HOG000237611; -.
DR HOVERGEN; HBG005471; -.
DR InParanoid; O43583; -.
DR OMA; SGGHDCK; -.
DR OrthoDB; EOG7T4MMN; -.
DR ChiTaRS; DENR; human.
DR GenomeRNAi; 8562; -.
DR NextBio; 32095; -.
DR PRO; PR:O43583; -.
DR ArrayExpress; O43583; -.
DR Bgee; O43583; -.
DR CleanEx; HS_DENR; -.
DR Genevestigator; O43583; -.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR Gene3D; 3.30.780.10; -; 1.
DR InterPro; IPR005873; Drp1.
DR InterPro; IPR001950; TIF_SUI1.
DR Pfam; PF01253; SUI1; 1.
DR SUPFAM; SSF55159; SSF55159; 2.
DR TIGRFAMs; TIGR01159; DRP1; 1.
DR PROSITE; PS50296; SUI1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 198 Density-regulated protein.
FT /FTId=PRO_0000130600.
FT DOMAIN 115 182 SUI1.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 73 73 Phosphoserine.
FT CONFLICT 49 50 DV -> HE (in Ref. 5; AAF02420).
SQ SEQUENCE 198 AA; 22092 MW; 023F70E0C6C0B25D CRC64;
MAADISESSG ADCKGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN
FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI
PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE
KWPEVDDDSI EDLGEVKK
//
ID DENR_HUMAN Reviewed; 198 AA.
AC O43583; Q9H3U6; Q9UKZ0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-APR-2001, sequence version 2.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Density-regulated protein;
DE Short=DRP;
DE AltName: Full=Protein DRP1;
DE AltName: Full=Smooth muscle cell-associated protein 3;
DE Short=SMAP-3;
GN Name=DENR; Synonyms=DRP1; ORFNames=H14;
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9628587; DOI=10.1089/dna.1998.17.437;
RA Deyo J.E., Chiao P.J., Tainsky M.A.;
RT "Drp, a novel protein expressed at high cell density but not during
RT growth arrest.";
RL DNA Cell Biol. 17:437-447(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Nishimoto S., Toyoda H., Tawara J., Aoki T., Komurasaki T.;
RT "Molecular cloning and characterization of human smooth muscle cell
RT associated protein-3 (SMAP-3).";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-198, AND INDUCTION BY ERBB2.
RX PubMed=10497265; DOI=10.1093/nar/27.20.4008;
RA Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.;
RT "Identification of differentially expressed genes associated with HER-
RT 2/neu overexpression in human breast cancer cells.";
RL Nucleic Acids Res. 27:4008-4017(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH MCTS1.
RX PubMed=16982740; DOI=10.1158/0008-5472.CAN-06-1999;
RA Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M.,
RA Bachman K.E., He H., Gartenhaus R.B.;
RT "MCT-1 protein interacts with the cap complex and modulates messenger
RT RNA translational profiles.";
RL Cancer Res. 66:8994-9001(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, AND INDUCTION BY HNRNPD.
RX PubMed=17878526;
RA Mazan-Mamczarz K., Gartenhaus R.B.;
RT "Post-transcriptional control of the MCT-1-associated protein DENR/DRP
RT by RNA-binding protein AUF1.";
RL Cancer Genomics Proteomics 4:233-239(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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 be involved in the translation of target mRNAs by
CC scanning and recognition of the initiation codon. Plays a role in
CC the modulation of the translational profile of a subset of cancer-
CC related mRNAs when recruited to the translational initiation
CC complex by the oncogene MCTS1.
CC -!- SUBUNIT: Interacts with MCTS1.
CC -!- INTERACTION:
CC Q9NX47:MARCH5; NbExp=2; IntAct=EBI-716083, EBI-2341610;
CC Q8WX92:NELFB; NbExp=2; IntAct=EBI-716083, EBI-347721;
CC P0CG48:UBC; NbExp=3; IntAct=EBI-716083, EBI-3390054;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle
CC and moderately expressed in the brain, placenta, liver and
CC pancreas. Weakly expressed in the lung and kidney.
CC -!- INDUCTION: Up-regulated with increasing cell-density by HNRNPD.
CC Up-regulated in ovarian and breast cancer cells by ERBB2
CC overexpression. Not induced by TGFB1.
CC -!- SIMILARITY: Belongs to the DENR family.
CC -!- SIMILARITY: Contains 1 SUI1 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02985.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DENRID40295ch12q24.html";
CC -----------------------------------------------------------------------
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DR EMBL; AF038554; AAC02985.2; ALT_INIT; mRNA.
DR EMBL; AB014731; BAB20268.1; -; mRNA.
DR EMBL; AC026331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007860; AAH07860.1; -; mRNA.
DR EMBL; AF103800; AAF02420.1; -; mRNA.
DR RefSeq; NP_003668.2; NM_003677.3.
DR UniGene; Hs.22393; -.
DR ProteinModelPortal; O43583; -.
DR SMR; O43583; 111-193.
DR IntAct; O43583; 5.
DR MINT; MINT-1405155; -.
DR STRING; 9606.ENSP00000280557; -.
DR PhosphoSite; O43583; -.
DR PaxDb; O43583; -.
DR PRIDE; O43583; -.
DR DNASU; 8562; -.
DR Ensembl; ENST00000280557; ENSP00000280557; ENSG00000139726.
DR GeneID; 8562; -.
DR KEGG; hsa:8562; -.
DR UCSC; uc001uda.3; human.
DR CTD; 8562; -.
DR GeneCards; GC12P123237; -.
DR HGNC; HGNC:2769; DENR.
DR HPA; HPA021783; -.
DR MIM; 604550; gene.
DR neXtProt; NX_O43583; -.
DR PharmGKB; PA27252; -.
DR eggNOG; COG0023; -.
DR HOGENOM; HOG000237611; -.
DR HOVERGEN; HBG005471; -.
DR InParanoid; O43583; -.
DR OMA; SGGHDCK; -.
DR OrthoDB; EOG7T4MMN; -.
DR ChiTaRS; DENR; human.
DR GenomeRNAi; 8562; -.
DR NextBio; 32095; -.
DR PRO; PR:O43583; -.
DR ArrayExpress; O43583; -.
DR Bgee; O43583; -.
DR CleanEx; HS_DENR; -.
DR Genevestigator; O43583; -.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR Gene3D; 3.30.780.10; -; 1.
DR InterPro; IPR005873; Drp1.
DR InterPro; IPR001950; TIF_SUI1.
DR Pfam; PF01253; SUI1; 1.
DR SUPFAM; SSF55159; SSF55159; 2.
DR TIGRFAMs; TIGR01159; DRP1; 1.
DR PROSITE; PS50296; SUI1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 198 Density-regulated protein.
FT /FTId=PRO_0000130600.
FT DOMAIN 115 182 SUI1.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 73 73 Phosphoserine.
FT CONFLICT 49 50 DV -> HE (in Ref. 5; AAF02420).
SQ SEQUENCE 198 AA; 22092 MW; 023F70E0C6C0B25D CRC64;
MAADISESSG ADCKGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN
FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI
PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE
KWPEVDDDSI EDLGEVKK
//
MIM
604550
*RECORD*
*FIELD* NO
604550
*FIELD* TI
*604550 DENSITY-REGULATED PROTEIN; DENR
;;DRP
*FIELD* TX
Cell contact with adjacent living and nonliving elements is the basis
read morefor many biologic events, including growth regulation, metastasis, and
embryonic pattern formation. Deyo et al. (1998) isolated a cDNA
corresponding to a novel density-regulated protein, which they
designated DRP, from the human teratocarcinoma cell line PA-1. The DRP
cDNA predicts a 243-amino acid peptide with consensus sites for
N-myristoylation, cAMP- and/or cGMP-dependent protein kinase
phosphorylation, and protein kinase C (see 176960) phosphorylation.
Northern blot analysis detected a doublet of approximately 2.8 and 3.2
kb in a wide range of adult tissues, with highest levels of expression
in skeletal and cardiac muscles. Western blot analysis using antipeptide
antisera detected increasing amounts of a 70-kD protein in PA-1 cells
concomitant with increasing cell number. Growth arrest effected by serum
starvation did not induce DRP mRNA. TGF-beta (190180), which causes
growth arrest in a variety of cells, also did not induce DRP expression.
*FIELD* RF
1. Deyo, J. E.; Chiao, P. J.; Tainsky, M. A.: Drp, a novel protein
expressed at high cell density but not during growth arrest. DNA
Cell Biol. 17: 437-447, 1998.
*FIELD* CD
Stefanie A. Nelson: 2/16/2000
*FIELD* ED
alopez: 02/16/2000
alopez: 2/16/2000
*RECORD*
*FIELD* NO
604550
*FIELD* TI
*604550 DENSITY-REGULATED PROTEIN; DENR
;;DRP
*FIELD* TX
Cell contact with adjacent living and nonliving elements is the basis
read morefor many biologic events, including growth regulation, metastasis, and
embryonic pattern formation. Deyo et al. (1998) isolated a cDNA
corresponding to a novel density-regulated protein, which they
designated DRP, from the human teratocarcinoma cell line PA-1. The DRP
cDNA predicts a 243-amino acid peptide with consensus sites for
N-myristoylation, cAMP- and/or cGMP-dependent protein kinase
phosphorylation, and protein kinase C (see 176960) phosphorylation.
Northern blot analysis detected a doublet of approximately 2.8 and 3.2
kb in a wide range of adult tissues, with highest levels of expression
in skeletal and cardiac muscles. Western blot analysis using antipeptide
antisera detected increasing amounts of a 70-kD protein in PA-1 cells
concomitant with increasing cell number. Growth arrest effected by serum
starvation did not induce DRP mRNA. TGF-beta (190180), which causes
growth arrest in a variety of cells, also did not induce DRP expression.
*FIELD* RF
1. Deyo, J. E.; Chiao, P. J.; Tainsky, M. A.: Drp, a novel protein
expressed at high cell density but not during growth arrest. DNA
Cell Biol. 17: 437-447, 1998.
*FIELD* CD
Stefanie A. Nelson: 2/16/2000
*FIELD* ED
alopez: 02/16/2000
alopez: 2/16/2000