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Protein

Peroxisomal 2,4-dienoyl-CoA reductase

Gene

DECR2

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. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid.

Catalytic activityi

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

Kineticsi

  1. KM=59 µM for 2,4-hexadienoyl-CoA2 Publications
  2. KM=6 µM for 2,4-decadienoyl-CoA2 Publications
  3. KM=102 µM for 2,4,7,10,13,16,19-docosaheptaenoyl-CoA2 Publications
  1. Vmax=1.75 µmol/min/mg enzyme toward 2,4-Hexadienoyl CoA2 Publications
  2. Vmax=1.37 µmol/min/mg enzyme toward 2,4-Decadienoyl CoA2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Substrate
Binding sitei86 – 861NADP1 Publication
Binding sitei88 – 881Substrate
Binding sitei118 – 1181Substrate
Binding sitei182 – 1821NADP1 Publication
Binding sitei219 – 2191Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 406NADP1 Publication
Nucleotide bindingi60 – 645NADP1 Publication
Nucleotide bindingi208 – 2147NADP1 Publication

GO - Molecular functioni

  • 2,4-dienoyl-CoA reductase (NADPH) activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.3.1.34. 2681.
ReactomeiR-HSA-535734. Fatty acid, triacylglycerol, and ketone body metabolism.

Chemistry

SwissLipidsiSLP:000001050.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal 2,4-dienoyl-CoA reductase (EC:1.3.1.34)
Short name:
pDCR
Alternative name(s):
2,4-dienoyl-CoA reductase 2
Short chain dehydrogenase/reductase family 17C member 1
Gene namesi
Name:DECR2
Synonyms:PDCR, SDR17C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2754. DECR2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861D → A: Reduces enzyme activity by 98%. 1 Publication
Mutagenesisi137 – 1371D → A: Reduces enzyme activity by 97%. 1 Publication
Mutagenesisi186 – 1861D → A: Reduces enzyme activity by about 95%. 1 Publication
Mutagenesisi268 – 2681D → A: Reduces enzyme activity by 97%. 1 Publication

Organism-specific databases

PharmGKBiPA27235.

Polymorphism and mutation databases

BioMutaiDECR2.
DMDMi84029527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 292291Peroxisomal 2,4-dienoyl-CoA reductasePRO_0000054559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei151 – 1511N6-acetyllysineCombined sources
Modified residuei287 – 2871PhosphoserineCombined sources
Modified residuei291 – 2911N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NUI1.
MaxQBiQ9NUI1.
PaxDbiQ9NUI1.
PeptideAtlasiQ9NUI1.
PRIDEiQ9NUI1.

PTM databases

iPTMnetiQ9NUI1.
PhosphoSiteiQ9NUI1.

Expressioni

Gene expression databases

BgeeiQ9NUI1.
CleanExiHS_DECR2.
ExpressionAtlasiQ9NUI1. baseline and differential.
GenevisibleiQ9NUI1. HS.

Organism-specific databases

HPAiHPA047631.

Interactioni

Subunit structurei

Monomer, dimer and oligomer.1 Publication

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117525. 14 interactions.
IntActiQ9NUI1. 8 interactions.
MINTiMINT-2819394.
STRINGi9606.ENSP00000219481.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124Combined sources
Turni23 – 286Combined sources
Beta strandi30 – 345Combined sources
Turni35 – 373Combined sources
Helixi39 – 4911Combined sources
Turni50 – 523Combined sources
Beta strandi54 – 607Combined sources
Helixi62 – 7615Combined sources
Beta strandi80 – 845Combined sources
Helixi90 – 10415Combined sources
Beta strandi109 – 1124Combined sources
Helixi122 – 1243Combined sources
Helixi127 – 13711Combined sources
Helixi139 – 15113Combined sources
Helixi153 – 1564Combined sources
Beta strandi158 – 1636Combined sources
Helixi167 – 1704Combined sources
Helixi176 – 19621Combined sources
Helixi197 – 1993Combined sources
Beta strandi201 – 2088Combined sources
Beta strandi211 – 2144Combined sources
Helixi215 – 2206Combined sources
Helixi224 – 2329Combined sources
Helixi242 – 25312Combined sources
Helixi255 – 2573Combined sources
Beta strandi264 – 2685Combined sources
Helixi271 – 2744Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FC6X-ray2.10A/B/C/D2-278[»]
4FC7X-ray1.84A/B/C/D2-278[»]
ProteinModelPortaliQ9NUI1.
SMRiQ9NUI1. Positions 3-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 1283Substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi290 – 2923Microbody targeting signalBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0725. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG100327.
InParanoidiQ9NUI1.
KOiK13237.
OMAiDDTEGMR.
OrthoDBiEOG789CBR.
PhylomeDBiQ9NUI1.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NUI1-1) [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
MAQPPPDVEG DDCLPAYRHL FCPDLLRDKV AFITGGGSGI GFRIAEIFMR
60 70 80 90 100
HGCHTVIASR SLPRVLTAAR KLAGATGRRC LPLSMDVRAP PAVMAAVDQA
110 120 130 140 150
LKEFGRIDIL INCAAGNFLC PAGALSFNAF KTVMDIDTSG TFNVSRVLYE
160 170 180 190 200
KFFRDHGGVI VNITATLGNR GQALQVHAGS AKAAVDAMTR HLAVEWGPQN
210 220 230 240 250
IRVNSLAPGP ISGTEGLRRL GGPQASLSTK VTASPLQRLG NKTEIAHSVL
260 270 280 290
YLASPLASYV TGAVLVADGG AWLTFPNGVK GLPDFASFSA KL
Length:292
Mass (Da):30,778
Last modified:October 1, 2000 - v1
Checksum:i9E7CD2995CE598D6
GO
Isoform 2 (identifier: Q9NUI1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-50: R → RASEDQMGHCSSSGTCLAGVATFMVIVGKQPPNQKSRETKEQGRQIPFVCVR
     114-160: AAGNFLCPAG...KFFRDHGGVI → SSSSCGLPFC...RHLQCVSCAL
     161-292: Missing.

Note: No experimental confirmation available.
Show »
Length:211
Mass (Da):23,130
Checksum:i34B6F2CFF91F1827
GO
Isoform 3 (identifier: Q9NUI1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Note: No experimental confirmation available.
Show »
Length:244
Mass (Da):25,589
Checksum:iCF192E5F987E311C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848Missing in isoform 3. 1 PublicationVSP_013629Add
BLAST
Alternative sequencei50 – 501R → RASEDQMGHCSSSGTCLAGV ATFMVIVGKQPPNQKSRETK EQGRQIPFVCVR in isoform 2. 1 PublicationVSP_013630
Alternative sequencei114 – 16047AAGNF…HGGVI → SSSSCGLPFCRCGRELPVPR WRLVLQRLQDRDGHRYQRHL QCVSCAL in isoform 2. 1 PublicationVSP_013631Add
BLAST
Alternative sequencei161 – 292132Missing in isoform 2. 1 PublicationVSP_013632Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293009 mRNA. Translation: CAC05664.1.
AE006463 Genomic DNA. Translation: AAK61231.1.
AK128012 mRNA. Translation: BAC87232.1.
AL023881 Genomic DNA. Translation: CAB92744.1.
BC010740 mRNA. Translation: AAH10740.1.
BC011968 mRNA. Translation: AAH11968.1.
CCDSiCCDS10409.1. [Q9NUI1-1]
RefSeqiNP_065715.1. NM_020664.3. [Q9NUI1-1]
UniGeneiHs.628831.

Genome annotation databases

EnsembliENST00000219481; ENSP00000219481; ENSG00000242612. [Q9NUI1-1]
ENST00000439661; ENSP00000399697; ENSG00000242612. [Q9NUI1-2]
ENST00000613476; ENSP00000481547; ENSG00000274296. [Q9NUI1-1]
ENST00000631856; ENSP00000488824; ENSG00000274296. [Q9NUI1-2]
GeneIDi26063.
KEGGihsa:26063.
UCSCiuc002chb.4. human. [Q9NUI1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293009 mRNA. Translation: CAC05664.1.
AE006463 Genomic DNA. Translation: AAK61231.1.
AK128012 mRNA. Translation: BAC87232.1.
AL023881 Genomic DNA. Translation: CAB92744.1.
BC010740 mRNA. Translation: AAH10740.1.
BC011968 mRNA. Translation: AAH11968.1.
CCDSiCCDS10409.1. [Q9NUI1-1]
RefSeqiNP_065715.1. NM_020664.3. [Q9NUI1-1]
UniGeneiHs.628831.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FC6X-ray2.10A/B/C/D2-278[»]
4FC7X-ray1.84A/B/C/D2-278[»]
ProteinModelPortaliQ9NUI1.
SMRiQ9NUI1. Positions 3-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117525. 14 interactions.
IntActiQ9NUI1. 8 interactions.
MINTiMINT-2819394.
STRINGi9606.ENSP00000219481.

Chemistry

SwissLipidsiSLP:000001050.

PTM databases

iPTMnetiQ9NUI1.
PhosphoSiteiQ9NUI1.

Polymorphism and mutation databases

BioMutaiDECR2.
DMDMi84029527.

Proteomic databases

EPDiQ9NUI1.
MaxQBiQ9NUI1.
PaxDbiQ9NUI1.
PeptideAtlasiQ9NUI1.
PRIDEiQ9NUI1.

Protocols and materials databases

DNASUi26063.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219481; ENSP00000219481; ENSG00000242612. [Q9NUI1-1]
ENST00000439661; ENSP00000399697; ENSG00000242612. [Q9NUI1-2]
ENST00000613476; ENSP00000481547; ENSG00000274296. [Q9NUI1-1]
ENST00000631856; ENSP00000488824; ENSG00000274296. [Q9NUI1-2]
GeneIDi26063.
KEGGihsa:26063.
UCSCiuc002chb.4. human. [Q9NUI1-1]

Organism-specific databases

CTDi26063.
GeneCardsiDECR2.
H-InvDBHIX0012648.
HIX0079832.
HIX0173312.
HGNCiHGNC:2754. DECR2.
HPAiHPA047631.
MIMi615839. gene.
neXtProtiNX_Q9NUI1.
PharmGKBiPA27235.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0725. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG100327.
InParanoidiQ9NUI1.
KOiK13237.
OMAiDDTEGMR.
OrthoDBiEOG789CBR.
PhylomeDBiQ9NUI1.
TreeFamiTF315256.

Enzyme and pathway databases

BRENDAi1.3.1.34. 2681.
ReactomeiR-HSA-535734. Fatty acid, triacylglycerol, and ketone body metabolism.

Miscellaneous databases

ChiTaRSiDECR2. human.
GeneWikiiDECR2.
GenomeRNAii26063.
PROiQ9NUI1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUI1.
CleanExiHS_DECR2.
ExpressionAtlasiQ9NUI1. baseline and differential.
GenevisibleiQ9NUI1. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase."
    De Nys K., Meyhi E., Mannaerts G.P., Fransen M., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1533:66-72(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  2. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Testis.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 3).
    Tissue: Lung.
  6. "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-151 AND LYS-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Studies of human 2,4-dienoyl CoA reductase shed new light on peroxisomal beta-oxidation of unsaturated fatty acids."
    Hua T., Wu D., Ding W., Wang J., Shaw N., Liu Z.J.
    J. Biol. Chem. 287:28956-28965(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 2-278 IN COMPLEX WITH HEXADIENOYL COA AND NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-86; ASP-137; ASP-186 AND ASP-268.

Entry informationi

Entry nameiDECR2_HUMAN
AccessioniPrimary (citable) accession number: Q9NUI1
Secondary accession number(s): Q6ZRS7, Q96ET0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 127 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 16
    Human chromosome 16: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.