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Q9BV79

- MECR_HUMAN

UniProt

Q9BV79 - MECR_HUMAN

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Protein

Trans-2-enoyl-CoA reductase, mitochondrial

Gene
MECR, NBRF1, CGI-63
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-CoA (1 Publication)2 Publications
  2. KM=7.1 µM for trans-2-decenoyl-CoA (1 Publication)
  3. KM=3.6 µM for trans-dodec-2-enoyl-CoA (1 Publication)
  4. KM=10.4 µM for trans-dec-2-enoyl-CoA (1 Publication)
  5. KM=10.2 µM for trans-oct-2-enoyl-CoA (1 Publication)
  6. KM=4.3 µM for trans-tetradec-2-enoyl-CoA (1 Publication)
  7. KM=6.6 µM for trans-hexadec-2-enoyl-CoA (1 Publication)
  8. KM=63.5 µM for trans-hex-2-enoyl-CoA (1 Publication)

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1964NADP By similarity
Nucleotide bindingi216 – 2183NADP By similarity
Nucleotide bindingi285 – 2884NADP By similarity
Nucleotide bindingi310 – 3123NADP By 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 – 5353Mitochondrion Reviewed predictionAdd
BLAST
Chaini54 – 373320Trans-2-enoyl-CoA reductase, mitochondrialPRO_0000000888Add
BLAST

Amino acid modifications

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

ArrayExpressiQ9BV79.
BgeeiQ9BV79.
CleanExiHS_MECR.
GenevestigatoriQ9BV79.

Organism-specific databases

HPAiHPA022018.
HPA022030.
HPA028740.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi119291. 7 interactions.
STRINGi9606.ENSP00000263702.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9BV79.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0604.
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

MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH    50
HGDPAKVVEL KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGFLPEL 100
PAVGGNEGVA QVVAVGSNVT GLKPGDWVIP ANAGLGTWRT EAVFSEEALI 150
QVPSDIPLQS AATLGVNPCT AYRMLMDFEQ LQPGDSVIQN ASNSGVGQAV 200
IQIAAALGLR TINVVRDRPD IQKLSDRLKS LGAEHVITEE ELRRPEMKNF 250
FKDMPQPRLA LNCVGGKSST ELLRQLARGG TMVTYGGMAK QPVVASVSLL 300
IFKDLKLRGF WLSQWKKDHS PDQFKELILT LCDLIRRGQL TAPACSQVPL 350
QDYQSALEAS MKPFISSKQI LTM 373
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.

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. VSP_041131Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462AL → GV in AAD34058. 1 Publication
Sequence conflicti373 – 3731M → I in CAG32984. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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. 7 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.
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

ArrayExpressi Q9BV79.
Bgeei Q9BV79.
CleanExi HS_MECR.
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: July 9, 2014
This is version 117 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

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