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Q9BV79

- MECR_HUMAN

UniProt

Q9BV79 - MECR_HUMAN

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Protein

Trans-2-enoyl-CoA reductase, mitochondrial

Gene

MECR

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

Functioni

Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis.1 Publication

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.2 Publications

Kineticsi

  1. KM=37 µM for trans-2-hexenoyl-CoA2 Publications
  2. KM=7.1 µM for trans-2-decenoyl-CoA2 Publications
  3. KM=3.6 µM for trans-dodec-2-enoyl-CoA2 Publications
  4. KM=10.4 µM for trans-dec-2-enoyl-CoA2 Publications
  5. KM=10.2 µM for trans-oct-2-enoyl-CoA2 Publications
  6. KM=4.3 µM for trans-tetradec-2-enoyl-CoA2 Publications
  7. KM=6.6 µM for trans-hexadec-2-enoyl-CoA2 Publications
  8. KM=63.5 µM for trans-hex-2-enoyl-CoA2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671NADPBy similarity
Binding sitei368 – 3681NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1964NADPBy similarity
Nucleotide bindingi216 – 2183NADPBy similarity
Nucleotide bindingi285 – 2884NADPBy similarity
Nucleotide bindingi310 – 3123NADPBy similarity

GO - Molecular functioni

  1. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

SABIO-RKQ9BV79.

Names & Taxonomyi

Protein namesi
Recommended name:
Trans-2-enoyl-CoA reductase, mitochondrial (EC:1.3.1.38)
Alternative name(s):
Nuclear receptor-binding factor 1
Short name:
HsNrbf-1
Short name:
NRBF-1
Gene namesi
Name:MECR
Synonyms:NBRF1
ORF Names:CGI-63
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:19691. MECR.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851S → A: Reduces catalytic activity by 68%. 1 Publication
Mutagenesisi94 – 941Y → F: Reduces catalytic activity by 95%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication
Mutagenesisi129 – 1291I → M: Strongly increases activity with trans-oct-2-enoyl-CoA. No effect on activity with trans-tetradec-2-enoyl-CoA. Decreases activity with trans-hexadec-2-enoyl-CoA by 20%. 1 Publication
Mutagenesisi165 – 1651G → S: Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 73%. Decreases activity with trans-hexadec-2-enoyl-CoA by 80%. 1 Publication
Mutagenesisi170 – 1701T → A: Reduces catalytic activity by 69%. 1 Publication
Mutagenesisi311 – 3111W → A: Reduces catalytic activity by 98%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication
Mutagenesisi311 – 3111W → L: Reduces catalytic activity by 87%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication
Mutagenesisi324 – 3241F → Y: Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 25%. Decreases activity with trans-hexadec-2-enoyl-CoA by 68%. 1 Publication

Organism-specific databases

PharmGKBiPA142671471.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionSequence AnalysisAdd
BLAST
Chaini54 – 373320Trans-2-enoyl-CoA reductase, mitochondrialPRO_0000000888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611N6-acetyllysine; alternateBy similarity
Modified residuei61 – 611N6-succinyllysine; alternateBy similarity
Modified residuei252 – 2521N6-acetyllysine; alternateBy similarity
Modified residuei252 – 2521N6-succinyllysine; alternateBy similarity
Modified residuei267 – 2671N6-acetyllysine; alternateBy similarity
Modified residuei267 – 2671N6-succinyllysine; alternateBy similarity
Modified residuei316 – 3161N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9BV79.
PaxDbiQ9BV79.
PRIDEiQ9BV79.

PTM databases

PhosphoSiteiQ9BV79.

Expressioni

Tissue specificityi

Highly expressed in skeletal and heart muscle. Expressed at lower level in placenta, liver, kidney and pancreas. Weakly or not expressed in lung.1 Publication

Gene expression databases

BgeeiQ9BV79.
CleanExiHS_MECR.
ExpressionAtlasiQ9BV79. baseline and differential.
GenevestigatoriQ9BV79.

Organism-specific databases

HPAiHPA022018.
HPA022030.
HPA028740.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi119291. 9 interactions.
STRINGi9606.ENSP00000263702.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 5210Combined sources
Helixi54 – 574Combined sources
Beta strandi58 – 636Combined sources
Beta strandi72 – 8110Combined sources
Helixi84 – 918Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi138 – 1458Combined sources
Helixi146 – 1483Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi154 – 1563Combined sources
Helixi158 – 1636Combined sources
Helixi167 – 17711Combined sources
Beta strandi186 – 1916Combined sources
Helixi195 – 20713Combined sources
Beta strandi210 – 2156Combined sources
Helixi221 – 23010Combined sources
Beta strandi234 – 2385Combined sources
Helixi239 – 2435Combined sources
Helixi245 – 2495Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi258 – 2647Combined sources
Helixi266 – 2738Combined sources
Beta strandi281 – 2844Combined sources
Beta strandi293 – 2953Combined sources
Helixi297 – 3026Combined sources
Beta strandi306 – 3094Combined sources
Helixi312 – 3187Combined sources
Helixi321 – 33616Combined sources
Beta strandi345 – 3495Combined sources
Helixi350 – 3523Combined sources
Helixi353 – 3608Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi366 – 3727Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSYX-ray1.75A40-373[»]
2VCYX-ray2.41A/B31-373[»]
ProteinModelPortaliQ9BV79.
SMRiQ9BV79. Positions 40-373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BV79.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0604.
GeneTreeiENSGT00740000115589.
HOVERGENiHBG052446.
InParanoidiQ9BV79.
KOiK07512.
OMAiCSTLWRV.
OrthoDBiEOG78M024.
PhylomeDBiQ9BV79.
TreeFamiTF312886.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.

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. Align

Isoform 1 (identifier: Q9BV79-1) [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
MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH
60 70 80 90 100
HGDPAKVVEL KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGFLPEL
110 120 130 140 150
PAVGGNEGVA QVVAVGSNVT GLKPGDWVIP ANAGLGTWRT EAVFSEEALI
160 170 180 190 200
QVPSDIPLQS AATLGVNPCT AYRMLMDFEQ LQPGDSVIQN ASNSGVGQAV
210 220 230 240 250
IQIAAALGLR TINVVRDRPD IQKLSDRLKS LGAEHVITEE ELRRPEMKNF
260 270 280 290 300
FKDMPQPRLA LNCVGGKSST ELLRQLARGG TMVTYGGMAK QPVVASVSLL
310 320 330 340 350
IFKDLKLRGF WLSQWKKDHS PDQFKELILT LCDLIRRGQL TAPACSQVPL
360 370
QDYQSALEAS MKPFISSKQI LTM
Length:373
Mass (Da):40,462
Last modified:May 31, 2011 - v2
Checksum:iDB13F6B0ED54A823
GO
Isoform 2 (identifier: Q9BV79-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.

Note: No experimental confirmation available.

Show »
Length:297
Mass (Da):32,228
Checksum:i1A27621E27728B76
GO

Sequence cautioni

The sequence AAD34058.1 differs from that shown. Reason: Frameshift at positions 14 and 19. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462AL → GV in AAD34058. (PubMed:10810093)Curated
Sequence conflicti373 – 3731M → I in CAG32984. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961F → L.5 Publications
Corresponds to variant rs1128400 [ dbSNP | Ensembl ].
VAR_027935
Natural varianti227 – 2271R → K.
Corresponds to variant rs11544658 [ dbSNP | Ensembl ].
VAR_055486
Natural varianti258 – 2581R → L.
Corresponds to variant rs34835902 [ dbSNP | Ensembl ].
VAR_055487

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7676Missing in isoform 2. 1 PublicationVSP_041131Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151821 mRNA. Translation: AAD34058.1. Frameshift.
AK095099 mRNA. Translation: BAG52984.1.
CR456703 mRNA. Translation: CAG32984.1.
AL590729 Genomic DNA. Translation: CAI14329.1.
AL590729 Genomic DNA. Translation: CAI14330.1.
CH471059 Genomic DNA. Translation: EAX07655.1.
BC001419 mRNA. Translation: AAH01419.1.
CCDSiCCDS30659.1. [Q9BV79-1]
CCDS30660.1. [Q9BV79-2]
RefSeqiNP_001019903.2. NM_001024732.2.
NP_057095.3. NM_016011.3.
XP_005245943.1. XM_005245886.1. [Q9BV79-2]
XP_005245944.1. XM_005245887.1. [Q9BV79-2]
XP_005245945.1. XM_005245888.1. [Q9BV79-2]
XP_005245946.1. XM_005245889.1. [Q9BV79-2]
XP_006710737.1. XM_006710674.1. [Q9BV79-2]
UniGeneiHs.183646.

Genome annotation databases

EnsembliENST00000263702; ENSP00000263702; ENSG00000116353. [Q9BV79-1]
ENST00000373791; ENSP00000362896; ENSG00000116353. [Q9BV79-2]
GeneIDi51102.
KEGGihsa:51102.
UCSCiuc001brp.1. human. [Q9BV79-1]

Polymorphism databases

DMDMi334302832.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151821 mRNA. Translation: AAD34058.1 . Frameshift.
AK095099 mRNA. Translation: BAG52984.1 .
CR456703 mRNA. Translation: CAG32984.1 .
AL590729 Genomic DNA. Translation: CAI14329.1 .
AL590729 Genomic DNA. Translation: CAI14330.1 .
CH471059 Genomic DNA. Translation: EAX07655.1 .
BC001419 mRNA. Translation: AAH01419.1 .
CCDSi CCDS30659.1. [Q9BV79-1 ]
CCDS30660.1. [Q9BV79-2 ]
RefSeqi NP_001019903.2. NM_001024732.2.
NP_057095.3. NM_016011.3.
XP_005245943.1. XM_005245886.1. [Q9BV79-2 ]
XP_005245944.1. XM_005245887.1. [Q9BV79-2 ]
XP_005245945.1. XM_005245888.1. [Q9BV79-2 ]
XP_005245946.1. XM_005245889.1. [Q9BV79-2 ]
XP_006710737.1. XM_006710674.1. [Q9BV79-2 ]
UniGenei Hs.183646.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZSY X-ray 1.75 A 40-373 [» ]
2VCY X-ray 2.41 A/B 31-373 [» ]
ProteinModelPortali Q9BV79.
SMRi Q9BV79. Positions 40-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119291. 9 interactions.
STRINGi 9606.ENSP00000263702.

PTM databases

PhosphoSitei Q9BV79.

Polymorphism databases

DMDMi 334302832.

Proteomic databases

MaxQBi Q9BV79.
PaxDbi Q9BV79.
PRIDEi Q9BV79.

Protocols and materials databases

DNASUi 51102.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263702 ; ENSP00000263702 ; ENSG00000116353 . [Q9BV79-1 ]
ENST00000373791 ; ENSP00000362896 ; ENSG00000116353 . [Q9BV79-2 ]
GeneIDi 51102.
KEGGi hsa:51102.
UCSCi uc001brp.1. human. [Q9BV79-1 ]

Organism-specific databases

CTDi 51102.
GeneCardsi GC01M029519.
HGNCi HGNC:19691. MECR.
HPAi HPA022018.
HPA022030.
HPA028740.
MIMi 608205. gene.
neXtProti NX_Q9BV79.
PharmGKBi PA142671471.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0604.
GeneTreei ENSGT00740000115589.
HOVERGENi HBG052446.
InParanoidi Q9BV79.
KOi K07512.
OMAi CSTLWRV.
OrthoDBi EOG78M024.
PhylomeDBi Q9BV79.
TreeFami TF312886.

Enzyme and pathway databases

SABIO-RK Q9BV79.

Miscellaneous databases

EvolutionaryTracei Q9BV79.
GeneWikii MECR.
GenomeRNAii 51102.
NextBioi 53817.
PROi Q9BV79.
SOURCEi Search...

Gene expression databases

Bgeei Q9BV79.
CleanExi HS_MECR.
ExpressionAtlasi Q9BV79. baseline and differential.
Genevestigatori Q9BV79.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-96.
  2. "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), VARIANT LEU-96.
    Tissue: Hippocampus.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-96.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-96.
  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), VARIANT LEU-96.
    Tissue: Placenta.
  7. "Characterization of 2-enoyl thioester reductase from mammals: an ortholog of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type II."
    Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T., Bergmann U., Qin Y.-M., Hiltunen J.K.
    J. Biol. Chem. 278:20154-20161(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The structure of human mitochondrial 2-enoyl thioester reductase (CGI-63)."
    Structural genomics consortium (SGC)
    Submitted (JUN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 40-373.
  10. "Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties."
    Chen Z.J., Pudas R., Sharma S., Smart O.S., Juffer A.H., Hiltunen J.K., Wierenga R.K., Haapalainen A.M.
    J. Mol. Biol. 379:830-844(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 31-373, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-85; TYR-94; ILE-129; GLY-165; THR-170; TRP-311 AND PHE-324.

Entry informationi

Entry nameiMECR_HUMAN
AccessioniPrimary (citable) accession number: Q9BV79
Secondary accession number(s): B3KT72
, Q5SYU0, Q5SYU1, Q5SYU2, Q6IBU9, Q9Y373
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 31, 2011
Last modified: November 26, 2014
This is version 120 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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