O43583 (DENR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Density-regulated protein
Short name=DRP

Alternative name(s):
Protein DRP1
Smooth muscle cell-associated protein 3
Short name=SMAP-3

Gene names

Name:	DENR
Synonyms:	DRP1
ORF Names:	H14

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. 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. Ref.6 Ref.7
Subunit structure	Interacts with MCTS1. Ref.6
Tissue specificity	Highly expressed in heart and skeletal muscle and moderately expressed in the brain, placenta, liver and pancreas. Weakly expressed in the lung and kidney. Ref.1
Induction	Up-regulated with increasing cell-density by HNRNPD. Up-regulated in ovarian and breast cancer cells by ERBB2 overexpression. Not induced by TGFB1. Ref.1 Ref.5 Ref.7
Sequence similarities	Belongs to the DENR family. Contains 1 SUI1 domain.
Sequence caution	The sequence AAC02985.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	protein binding Inferred from physical interaction. Source: IntAct translation initiation factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
COBRA1	Q8WX92	2	EBI-716083,EBI-347721

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 198	197	Density-regulated protein		PRO_0000130600
Regions
	Domain	115 – 182	68	SUI1
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.10
	Modified residue	69	1	Phosphothreonine Ref.8 Ref.10
	Modified residue	73	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11
	Modified residue	86	1	Phosphothreonine Ref.10
Experimental info
	Sequence conflict	49 – 50	2	DV → HE in AAF02420. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O43583 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: 023F70E0C6C0B25D	FASTA	198	22,092
	10 20 30 40 50 60 MAADISESSG ADCKGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN 70 80 90 100 110 120 FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI 130 140 150 160 170 180 PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE 190 KWPEVDDDSI EDLGEVKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9628587] [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: 16541075] [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: 15489334] [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: 10497265] [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: 16982740] [Abstract] Cited for: FUNCTION, INTERACTION WITH MCTS1.
[7]	"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: 17878526] [Abstract] Cited for: FUNCTION, INDUCTION BY HNRNPD.
[8]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69 AND SER-73, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; SER-73 AND THR-86, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00306280.
RefSeq	NP_003668.2. NM_003677.3.
UniGene	Hs.22393.
3D structure databases
ProteinModelPortal	O43583.
SMR	O43583. Positions 113-194.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43583. 2 interactions.
MINT	MINT-1405155.
STRING	O43583.
PTM databases
PhosphoSite	O43583.
Proteomic databases
PRIDE	O43583.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000280557; ENSP00000280557; ENSG00000139726.
GeneID	8562.
KEGG	hsa:8562.
UCSC	uc001uda.1. human.
Organism-specific databases
CTD	8562.
GeneCards	GC12P123237.
H-InvDB	HIX0011097.
HGNC	HGNC:2769. DENR.
MIM	604550. gene.
neXtProt	NX_O43583.
PharmGKB	PA27252.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20106.
GeneTree	ENSGT00390000014349.
HOVERGEN	HBG005471.
InParanoid	O43583.
OrthoDB	EOG49PB0M.
PhylomeDB	O43583.
Gene expression databases
ArrayExpress	O43583.
Bgee	O43583.
CleanEx	HS_DENR.
Genevestigator	O43583.
GermOnline	ENSG00000139726. Homo sapiens.
Family and domain databases
InterPro	IPR005873. Drp1. IPR001950. TIF_SUI1. [Graphical view]
Pfam	PF01253. SUI1. 1 hit. [Graphical view]
SUPFAM	SSF55159. TIF_SUI1. 1 hit.
TIGRFAMs	TIGR01159. DRP1. 1 hit.
PROSITE	PS50296. SUI1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	32095.
SOURCE	Search...

Entry information

Entry name

DENR_HUMAN

Accession

Primary (citable) accession number: O43583
Secondary accession number(s): Q9H3U6, Q9UKZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	April 27, 2001
Last modified:	January 25, 2012
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.