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Protein

2,4-dienoyl-CoA reductase, mitochondrial

Gene

DECR1

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

Functioni

Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.

Catalytic activityi

Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.1 Publication

Kineticsi

  1. KM=7.7 µM for NADPH1 Publication
  2. KM=14.3 µM for trans-2,trans-4-hexadienoyl-CoA1 Publication
  1. Vmax=30.3 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911NADP1 Publication
Binding sitei91 – 911SubstrateBy similarity
Binding sitei117 – 1171NADP1 Publication
Binding sitei119 – 1191Substrate1 Publication
Binding sitei149 – 1491Substrate1 Publication
Binding sitei157 – 1571Substrate1 Publication
Active sitei199 – 1991Proton acceptorSequence Analysis
Binding sitei214 – 2141NADP1 Publication
Binding sitei251 – 2511SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 716NADP1 Publication
Nucleotide bindingi240 – 2434NADP1 Publication

GO - Molecular functioni

  • 2,4-dienoyl-CoA reductase (NADPH) activity Source: UniProtKB
  • NADPH binding Source: UniProtKB
  • oxidoreductase activity, acting on NAD(P)H Source: Reactome

GO - Biological processi

  • cellular lipid metabolic process Source: Reactome
  • fatty acid beta-oxidation Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
SABIO-RKQ16698.

Names & Taxonomyi

Protein namesi
Recommended name:
2,4-dienoyl-CoA reductase, mitochondrial (EC:1.3.1.34)
Alternative name(s):
2,4-dienoyl-CoA reductase [NADPH]
Short name:
4-enoyl-CoA reductase [NADPH]
Short chain dehydrogenase/reductase family 18C member 1
Gene namesi
Name:DECR1
Synonyms:DECR, SDR18C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2753. DECR1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

2,4-dienoyl-CoA reductase deficiency (DECRD)1 Publication

The protein represented in this entry is involved in disease pathogenesis. A selective decrease in mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS.

Disease descriptionA rare, autosomal recessive, inborn error of polyunsaturated fatty acids and lysine metabolism, resulting in mitochondrial dysfunction. Affected individuals have a severe encephalopathy with neurologic and metabolic abnormalities beginning in early infancy. Laboratory studies show increased C10:2 carnitine levels and hyperlysinemia.

See also OMIM:616034

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481N → A: Reduces enzyme activity by 97%. 1 Publication
Mutagenesisi199 – 1991Y → A: Reduces enzyme activity by 99%. Strongly reduced affinity for substrate and for NADP. 1 Publication
Mutagenesisi210 – 2101S → A: Reduces enzyme activity by over 99%. 1 Publication
Mutagenesisi214 – 2141K → A: Reduces enzyme activity by over 99%. 1 Publication

Organism-specific databases

MIMi616034. phenotype.
PharmGKBiPA141.

Polymorphism and mutation databases

BioMutaiDECR1.
DMDMi3913456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434MitochondrionBy similarityAdd
BLAST
Chaini35 – 3353012,4-dienoyl-CoA reductase, mitochondrialPRO_0000031965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysine; alternateBy similarity
Modified residuei42 – 421N6-succinyllysine; alternateBy similarity
Modified residuei49 – 491N6-acetyllysine; alternateBy similarity
Modified residuei49 – 491N6-succinyllysine; alternateBy similarity
Modified residuei69 – 691Phosphothreonine1 Publication
Modified residuei73 – 731N6-succinyllysineBy similarity
Modified residuei97 – 971N6-acetyllysine; alternateBy similarity
Modified residuei97 – 971N6-succinyllysine; alternateBy similarity
Modified residuei230 – 2301N6-acetyllysine1 Publication
Modified residuei244 – 2441N6-acetyllysine; alternateBy similarity
Modified residuei244 – 2441N6-succinyllysine; alternateBy similarity
Modified residuei260 – 2601N6-acetyllysine; alternateBy similarity
Modified residuei260 – 2601N6-succinyllysine; alternateBy similarity
Modified residuei319 – 3191N6-acetyllysine; alternateBy similarity
Modified residuei319 – 3191N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16698.
PaxDbiQ16698.
PeptideAtlasiQ16698.
PRIDEiQ16698.

2D gel databases

UCD-2DPAGEQ16698.

PTM databases

PhosphoSiteiQ16698.

Expressioni

Tissue specificityi

Heart = liver = pancreas > kidney >> skeletal muscle = lung.1 Publication

Gene expression databases

BgeeiQ16698.
CleanExiHS_DECR1.
ExpressionAtlasiQ16698. baseline and differential.
GenevestigatoriQ16698.

Organism-specific databases

HPAiHPA023160.
HPA023162.
HPA023238.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi108030. 15 interactions.
IntActiQ16698. 5 interactions.
STRINGi9606.ENSP00000220764.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 438Combined sources
Turni54 – 596Combined sources
Beta strandi61 – 655Combined sources
Turni66 – 683Combined sources
Helixi70 – 8112Combined sources
Beta strandi85 – 917Combined sources
Helixi93 – 10715Combined sources
Beta strandi111 – 1155Combined sources
Helixi121 – 13414Combined sources
Beta strandi139 – 1435Combined sources
Helixi153 – 1553Combined sources
Helixi158 – 18528Combined sources
Beta strandi190 – 1956Combined sources
Helixi199 – 2024Combined sources
Helixi208 – 22821Combined sources
Helixi229 – 2313Combined sources
Beta strandi233 – 2408Combined sources
Beta strandi254 – 2563Combined sources
Helixi257 – 2637Combined sources
Helixi274 – 28411Combined sources
Helixi287 – 2893Combined sources
Beta strandi296 – 3005Combined sources
Helixi303 – 3086Combined sources
Helixi312 – 3165Combined sources
Helixi319 – 3257Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6UX-ray1.75A/B/C/D35-335[»]
1W73X-ray2.10A/B/C/D35-335[»]
1W8DX-ray2.20A/B/C/D35-335[»]
ProteinModelPortaliQ16698.
SMRiQ16698. Positions 35-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16698.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG005465.
InParanoidiQ16698.
KOiK13236.
OMAiFEKEMID.
PhylomeDBiQ16698.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16698-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKLPARVFFT LGSRLPCGLA PRRFFSYGTK ILYQNTEALQ SKFFSPLQKA
60 70 80 90 100
MLPPNSFQGK VAFITGGGTG LGKGMTTLLS SLGAQCVIAS RKMDVLKATA
110 120 130 140 150
EQISSQTGNK VHAIQCDVRD PDMVQNTVSE LIKVAGHPNI VINNAAGNFI
160 170 180 190 200
SPTERLSPNA WKTITDIVLN GTAFVTLEIG KQLIKAQKGA AFLSITTIYA
210 220 230 240 250
ETGSGFVVPS ASAKAGVEAM SKSLAAEWGK YGMRFNVIQP GPIKTKGAFS
260 270 280 290 300
RLDPTGTFEK EMIGRIPCGR LGTVEELANL AAFLCSDYAS WINGAVIKFD
310 320 330
GGEEVLISGE FNDLRKVTKE QWDTIEELIR KTKGS
Length:335
Mass (Da):36,068
Last modified:November 1, 1996 - v1
Checksum:iF04E72AACB718430
GO
Isoform 2 (identifier: Q16698-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MKLPARVFFTLGSRLPCGLAPRR → MSGLGKKHLLLMGE

Note: No experimental confirmation available.

Show »
Length:326
Mass (Da):34,994
Checksum:i81B865BEAD0F75A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871D → G in AAB09423 (Ref. 2) Curated
Sequence conflicti292 – 2921I → V in AAB09423 (Ref. 2) Curated
Sequence conflicti303 – 3031E → G in AAB09423 (Ref. 2) Curated
Sequence conflicti311 – 3111F → G in AAB09423 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti333 – 3331K → N.
Corresponds to variant rs15094 [ dbSNP | Ensembl ].
VAR_012034

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323MKLPA…LAPRR → MSGLGKKHLLLMGE in isoform 2. 1 PublicationVSP_056388Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26050 mRNA. Translation: AAA67551.1.
U49352 mRNA. Translation: AAB09423.1.
U78302
, U94980, U94981, U94982, U94983, U94984, U94985, U94986, U94987 Genomic DNA. Translation: AAB88724.1.
AK300069 mRNA. Translation: BAH13204.1.
AC004612 Genomic DNA. Translation: AAC14671.1.
AF049895 Genomic DNA. No translation available.
BC105080 mRNA. Translation: AAI05081.1.
BC105082 mRNA. Translation: AAI05083.1.
CCDSiCCDS6250.1. [Q16698-1]
PIRiS53352.
RefSeqiNP_001350.1. NM_001359.1. [Q16698-1]
UniGeneiHs.492212.

Genome annotation databases

EnsembliENST00000220764; ENSP00000220764; ENSG00000104325. [Q16698-1]
ENST00000522161; ENSP00000429779; ENSG00000104325. [Q16698-2]
GeneIDi1666.
KEGGihsa:1666.
UCSCiuc003yek.1. human. [Q16698-1]
uc011lgc.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26050 mRNA. Translation: AAA67551.1.
U49352 mRNA. Translation: AAB09423.1.
U78302
, U94980, U94981, U94982, U94983, U94984, U94985, U94986, U94987 Genomic DNA. Translation: AAB88724.1.
AK300069 mRNA. Translation: BAH13204.1.
AC004612 Genomic DNA. Translation: AAC14671.1.
AF049895 Genomic DNA. No translation available.
BC105080 mRNA. Translation: AAI05081.1.
BC105082 mRNA. Translation: AAI05083.1.
CCDSiCCDS6250.1. [Q16698-1]
PIRiS53352.
RefSeqiNP_001350.1. NM_001359.1. [Q16698-1]
UniGeneiHs.492212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6UX-ray1.75A/B/C/D35-335[»]
1W73X-ray2.10A/B/C/D35-335[»]
1W8DX-ray2.20A/B/C/D35-335[»]
ProteinModelPortaliQ16698.
SMRiQ16698. Positions 35-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108030. 15 interactions.
IntActiQ16698. 5 interactions.
STRINGi9606.ENSP00000220764.

PTM databases

PhosphoSiteiQ16698.

Polymorphism and mutation databases

BioMutaiDECR1.
DMDMi3913456.

2D gel databases

UCD-2DPAGEQ16698.

Proteomic databases

MaxQBiQ16698.
PaxDbiQ16698.
PeptideAtlasiQ16698.
PRIDEiQ16698.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220764; ENSP00000220764; ENSG00000104325. [Q16698-1]
ENST00000522161; ENSP00000429779; ENSG00000104325. [Q16698-2]
GeneIDi1666.
KEGGihsa:1666.
UCSCiuc003yek.1. human. [Q16698-1]
uc011lgc.1. human.

Organism-specific databases

CTDi1666.
GeneCardsiGC08P091082.
HGNCiHGNC:2753. DECR1.
HPAiHPA023160.
HPA023162.
HPA023238.
MIMi222745. gene.
616034. phenotype.
neXtProtiNX_Q16698.
PharmGKBiPA141.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG005465.
InParanoidiQ16698.
KOiK13236.
OMAiFEKEMID.
PhylomeDBiQ16698.
TreeFamiTF315256.

Enzyme and pathway databases

ReactomeiREACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
SABIO-RKQ16698.

Miscellaneous databases

ChiTaRSiDECR1. human.
EvolutionaryTraceiQ16698.
GenomeRNAii1666.
NextBioi35479930.
PROiQ16698.
SOURCEiSearch...

Gene expression databases

BgeeiQ16698.
CleanExiHS_DECR1.
ExpressionAtlasiQ16698. baseline and differential.
GenevestigatoriQ16698.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of cDNA for human 120 kDa mitochondrial 2,4-dienoyl-coenzyme A reductase."
    Koivuranta K.T., Hakkola E.H., Hiltunen J.K.
    Biochem. J. 304:787-792(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Liver.
  2. Ding J.H., Yang B.Z., Roe C.R.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Molecular cloning and characterization of the human mitochondrial 2,4-dienoyl-CoA reductase gene (DECR)."
    Helander H.M., Koivuranta K.T., Horelli-Kuitunen N., Palvimo J.J., Palotie A., Hiltunen J.K.
    Genomics 46:112-119(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Pericardium.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes dienoyl-CoA reductase deficiency with hyperlysinemia."
    Houten S.M., Denis S., Te Brinke H., Jongejan A., van Kampen A.H., Bradley E.J., Baas F., Hennekam R.C., Millington D.S., Young S.P., Frazier D.M., Gucsavas-Calikoglu M., Wanders R.J.
    Hum. Mol. Genet. 23:5009-5016(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DECRD.
  10. "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 THR-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site."
    Alphey M.S., Yu W., Byres E., Li D., Hunter W.N.
    J. Biol. Chem. 280:3068-3077(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 35-335 IN COMPLEX WITH NADP AND SUBSTRATE, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-148; TYR-199; SER-210 AND LYS-214.

Entry informationi

Entry nameiDECR_HUMAN
AccessioniPrimary (citable) accession number: Q16698
Secondary accession number(s): B7Z6B8, Q2M304, Q93085
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 138 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.