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Protein

Density-regulated protein

Gene

DENR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitmnet of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role in the modulation of the translational profile of a subset of cancer-related mRNAs when recruited to the translational initiation complex by the oncogene MCTS1.3 Publications

GO - Molecular functioni

GO - Biological processi

  • formation of translation preinitiation complex Source: UniProtKB
  • IRES-dependent translational initiation Source: UniProtKB
  • ribosome disassembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Density-regulated protein
Short name:
DRP
Alternative name(s):
Protein DRP1
Smooth muscle cell-associated protein 3
Short name:
SMAP-3
Gene namesi
Name:DENR
Synonyms:DRP1
ORF Names:H14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2769. DENR.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27252.

Polymorphism and mutation databases

BioMutaiDENR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 198197Density-regulated proteinPRO_0000130600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei73 – 731PhosphoserineCombined sources
Modified residuei86 – 861PhosphothreonineCombined sources
Modified residuei189 – 1891PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO43583.
MaxQBiO43583.
PaxDbiO43583.
PeptideAtlasiO43583.
PRIDEiO43583.
TopDownProteomicsiO43583.

PTM databases

iPTMnetiO43583.
PhosphoSiteiO43583.

Expressioni

Tissue specificityi

Highly expressed in heart and skeletal muscle and moderately expressed in the brain, placenta, liver and pancreas. Weakly expressed in the lung and kidney.1 Publication

Inductioni

Up-regulated with increasing cell-density by HNRNPD. Up-regulated in ovarian and breast cancer cells by ERBB2 overexpression. Not induced by TGFB1.3 Publications

Gene expression databases

BgeeiO43583.
CleanExiHS_DENR.
ExpressionAtlasiO43583. baseline and differential.
GenevisibleiO43583. HS.

Organism-specific databases

HPAiHPA021783.

Interactioni

Subunit structurei

Interacts with MCTS1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MARCH5Q9NX472EBI-716083,EBI-2341610
NELFBQ8WX922EBI-716083,EBI-347721
UBCP0CG483EBI-716083,EBI-3390054

Protein-protein interaction databases

BioGridi114131. 46 interactions.
IntActiO43583. 6 interactions.
MINTiMINT-1405155.
STRINGi9606.ENSP00000280557.

Structurei

3D structure databases

ProteinModelPortaliO43583.
SMRiO43583. Positions 113-192.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini115 – 18268SUI1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the DENR family.Curated
Contains 1 SUI1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3239. Eukaryota.
COG0023. LUCA.
GeneTreeiENSGT00390000014349.
HOGENOMiHOG000237611.
HOVERGENiHBG005471.
InParanoidiO43583.
OMAiSGGHDCK.
OrthoDBiEOG7T4MMN.
PhylomeDBiO43583.
TreeFamiTF105912.

Family and domain databases

Gene3Di3.30.780.10. 1 hit.
InterProiIPR005873. Drp1.
IPR001950. TIF_SUI1.
[Graphical view]
PfamiPF01253. SUI1. 1 hit.
[Graphical view]
SUPFAMiSSF55159. SSF55159. 2 hits.
TIGRFAMsiTIGR01159. DRP1. 1 hit.
PROSITEiPS50296. SUI1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O43583-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAADISESSG ADCKGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV
60 70 80 90 100
AKCRQWLEKN FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG
110 120 130 140 150
RGQIKQKKKT VPQKVTIAKI PRAKKKYVTR VCGLATFEID LKEAQRFFAQ
160 170 180 190
KFSCGASVTG EDEIIIQGDF TDDIIDVIQE KWPEVDDDSI EDLGEVKK
Length:198
Mass (Da):22,092
Last modified:April 27, 2001 - v2
Checksum:i023F70E0C6C0B25D
GO

Sequence cautioni

The sequence AAC02985.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 502DV → HE in AAF02420 (PubMed:10497265).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038554 mRNA. Translation: AAC02985.2. Different initiation.
AB014731 mRNA. Translation: BAB20268.1.
AC026331 Genomic DNA. No translation available.
AC027290 Genomic DNA. No translation available.
BC007860 mRNA. Translation: AAH07860.1.
AF103800 mRNA. Translation: AAF02420.1.
CCDSiCCDS45003.1.
RefSeqiNP_003668.2. NM_003677.4.
UniGeneiHs.22393.

Genome annotation databases

EnsembliENST00000280557; ENSP00000280557; ENSG00000139726.
GeneIDi8562.
KEGGihsa:8562.
UCSCiuc001uda.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038554 mRNA. Translation: AAC02985.2. Different initiation.
AB014731 mRNA. Translation: BAB20268.1.
AC026331 Genomic DNA. No translation available.
AC027290 Genomic DNA. No translation available.
BC007860 mRNA. Translation: AAH07860.1.
AF103800 mRNA. Translation: AAF02420.1.
CCDSiCCDS45003.1.
RefSeqiNP_003668.2. NM_003677.4.
UniGeneiHs.22393.

3D structure databases

ProteinModelPortaliO43583.
SMRiO43583. Positions 113-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114131. 46 interactions.
IntActiO43583. 6 interactions.
MINTiMINT-1405155.
STRINGi9606.ENSP00000280557.

PTM databases

iPTMnetiO43583.
PhosphoSiteiO43583.

Polymorphism and mutation databases

BioMutaiDENR.

Proteomic databases

EPDiO43583.
MaxQBiO43583.
PaxDbiO43583.
PeptideAtlasiO43583.
PRIDEiO43583.
TopDownProteomicsiO43583.

Protocols and materials databases

DNASUi8562.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280557; ENSP00000280557; ENSG00000139726.
GeneIDi8562.
KEGGihsa:8562.
UCSCiuc001uda.4. human.

Organism-specific databases

CTDi8562.
GeneCardsiDENR.
HGNCiHGNC:2769. DENR.
HPAiHPA021783.
MIMi604550. gene.
neXtProtiNX_O43583.
PharmGKBiPA27252.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3239. Eukaryota.
COG0023. LUCA.
GeneTreeiENSGT00390000014349.
HOGENOMiHOG000237611.
HOVERGENiHBG005471.
InParanoidiO43583.
OMAiSGGHDCK.
OrthoDBiEOG7T4MMN.
PhylomeDBiO43583.
TreeFamiTF105912.

Miscellaneous databases

ChiTaRSiDENR. human.
GenomeRNAii8562.
PROiO43583.
SOURCEiSearch...

Gene expression databases

BgeeiO43583.
CleanExiHS_DENR.
ExpressionAtlasiO43583. baseline and differential.
GenevisibleiO43583. HS.

Family and domain databases

Gene3Di3.30.780.10. 1 hit.
InterProiIPR005873. Drp1.
IPR001950. TIF_SUI1.
[Graphical view]
PfamiPF01253. SUI1. 1 hit.
[Graphical view]
SUPFAMiSSF55159. SSF55159. 2 hits.
TIGRFAMsiTIGR01159. DRP1. 1 hit.
PROSITEiPS50296. SUI1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drp, a novel protein expressed at high cell density but not during growth arrest."
    Deyo J.E., Chiao P.J., Tainsky M.A.
    DNA Cell Biol. 17:437-447(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
  2. "Molecular cloning and characterization of human smooth muscle cell associated protein-3 (SMAP-3)."
    Nishimoto S., Toyoda H., Tawara J., Aoki T., Komurasaki T.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  5. "Identification of differentially expressed genes associated with HER-2/neu overexpression in human breast cancer cells."
    Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.
    Nucleic Acids Res. 27:4008-4017(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-198, INDUCTION BY ERBB2.
  6. "MCT-1 protein interacts with the cap complex and modulates messenger RNA translational profiles."
    Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M., Bachman K.E., He H., Gartenhaus R.B.
    Cancer Res. 66:8994-9001(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MCTS1.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Post-transcriptional control of the MCT-1-associated protein DENR/DRP by RNA-binding protein AUF1."
    Mazan-Mamczarz K., Gartenhaus R.B.
    Cancer Genomics Proteomics 4:233-239(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY HNRNPD.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Activities of ligatin and MCT-1/DENR in eukaryotic translation initiation and ribosomal recycling."
    Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U., Pestova T.V.
    Genes Dev. 24:1787-1801(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-73 AND THR-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDENR_HUMAN
AccessioniPrimary (citable) accession number: O43583
Secondary accession number(s): Q9H3U6, Q9UKZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 27, 2001
Last modified: July 6, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.