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P50416

- CPT1A_HUMAN

UniProt

P50416 - CPT1A_HUMAN

Protein

Carnitine O-palmitoyltransferase 1, liver isoform

Gene

CPT1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in triglyceride metabolism.

    Catalytic activityi

    Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.2 Publications

    Enzyme regulationi

    Inhibited by malonyl-CoA.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei473 – 4731Proton acceptorBy similarity
    Binding sitei589 – 5891CarnitineBy similarity
    Binding sitei602 – 6021CarnitineBy similarity

    GO - Molecular functioni

    1. carnitine O-palmitoyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. carnitine metabolic process Source: UniProtKB
    2. carnitine shuttle Source: Reactome
    3. cellular lipid metabolic process Source: Reactome
    4. cellular response to fatty acid Source: Ensembl
    5. eating behavior Source: Ensembl
    6. epithelial cell differentiation Source: UniProt
    7. fatty acid beta-oxidation Source: ProtInc
    8. glucose metabolic process Source: Ensembl
    9. long-chain fatty acid metabolic process Source: UniProtKB
    10. positive regulation of fatty acid beta-oxidation Source: Ensembl
    11. protein homooligomerization Source: Ensembl
    12. regulation of insulin secretion Source: Ensembl
    13. response to drug Source: Ensembl
    14. response to organic cyclic compound Source: Ensembl
    15. small molecule metabolic process Source: Reactome
    16. triglyceride metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03286-MONOMER.
    BRENDAi2.3.1.21. 2681.
    ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    SABIO-RKP50416.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carnitine O-palmitoyltransferase 1, liver isoform (EC:2.3.1.21)
    Short name:
    CPT1-L
    Alternative name(s):
    Carnitine O-palmitoyltransferase I, liver isoform
    Short name:
    CPT I
    Short name:
    CPTI-L
    Carnitine palmitoyltransferase 1A
    Gene namesi
    Name:CPT1A
    Synonyms:CPT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2328. CPT1A.

    Subcellular locationi

    Mitochondrion outer membrane 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

    1. integral component of mitochondrial outer membrane Source: UniProtKB
    2. membrane Source: UniProtKB
    3. mitochondrial inner membrane Source: Ensembl
    4. mitochondrial outer membrane Source: Reactome
    5. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Involvement in diseasei

    Carnitine palmitoyltransferase 1A deficiency (CPT1AD) [MIM:255120]: Rare autosomal recessive metabolic disorder of long-chain fatty acid oxidation characterized by severe episodes of hypoketotic hypoglycemia usually occurring after fasting or illness. Onset is in infancy or early childhood.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231R → C in CPT1AD. 1 Publication
    VAR_020546
    Natural varianti304 – 3041C → W in CPT1AD. 1 Publication
    VAR_020548
    Natural varianti314 – 3141T → I in CPT1AD. 1 Publication
    VAR_020549
    Natural varianti316 – 3161R → G in CPT1AD. 1 Publication
    VAR_046767
    Natural varianti343 – 3431F → V in CPT1AD. 1 Publication
    VAR_046768
    Natural varianti357 – 3571R → W in CPT1AD; decreased stability. 1 Publication
    VAR_020550
    Natural varianti360 – 3601E → G in CPT1AD; reduced protein levels.
    Corresponds to variant rs28936372 [ dbSNP | Ensembl ].
    VAR_020551
    Natural varianti395 – 3951Missing in CPT1AD; loss of activity. 1 Publication
    VAR_020552
    Natural varianti414 – 4141A → V in CPT1AD; decreased activity. 1 Publication
    Corresponds to variant rs28936373 [ dbSNP | Ensembl ].
    VAR_020553
    Natural varianti454 – 4541D → G in CPT1AD. 1 Publication
    VAR_020554
    Natural varianti465 – 4651G → W in CPT1AD. 1 Publication
    VAR_046769
    Natural varianti479 – 4791P → L in CPT1AD; decreased activity. 1 Publication
    VAR_020555
    Natural varianti484 – 4841L → P in CPT1AD. 1 Publication
    VAR_020556
    Natural varianti498 – 4981Y → C in CPT1AD; decreased activity. 1 Publication
    VAR_020557
    Natural varianti709 – 7091G → E in CPT1AD; loss of activity. 1 Publication
    Corresponds to variant rs28936374 [ dbSNP | Ensembl ].
    VAR_020558
    Natural varianti710 – 7101G → E in CPT1AD; loss of activity. 1 Publication
    VAR_020559

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi255120. phenotype.
    Orphaneti156. Carnitine palmitoyl transferase 1A deficiency.
    PharmGKBiPA26847.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 773772Carnitine O-palmitoyltransferase 1, liver isoformPRO_0000210159Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei282 – 2821Nitrated tyrosineBy similarity
    Modified residuei588 – 5881PhosphothreonineBy similarity
    Modified residuei589 – 5891Nitrated tyrosineBy similarity
    Modified residuei604 – 6041PhosphothreonineBy similarity
    Modified residuei741 – 7411PhosphoserineBy similarity
    Modified residuei747 – 7471PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP50416.
    PaxDbiP50416.
    PeptideAtlasiP50416.
    PRIDEiP50416.

    PTM databases

    PhosphoSiteiP50416.

    Expressioni

    Tissue specificityi

    Strong expression in kidney and heart, and lower in liver and skeletal muscle.

    Inductioni

    Up-regulated by fatty acids.1 Publication

    Gene expression databases

    ArrayExpressiP50416.
    BgeeiP50416.
    CleanExiHS_CPT1A.
    GenevestigatoriP50416.

    Organism-specific databases

    HPAiHPA008835.

    Interactioni

    Subunit structurei

    Homohexamer and homotrimer. Identified in a complex that contains at least CPT1A, ACSL1 and VDAC1. Also identified in complexes with ACSL1 and VDAC2 and VDAC3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi107765. 28 interactions.
    IntActiP50416. 13 interactions.
    MINTiMINT-3018357.
    STRINGi9606.ENSP00000265641.

    Structurei

    Secondary structure

    1
    773
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74
    Beta strandi9 – 157
    Beta strandi18 – 236
    Helixi25 – 3915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LE3NMR-A1-42[»]
    ProteinModelPortaliP50416.
    SMRiP50416. Positions 1-42, 180-765.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 4746CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini74 – 10229Mitochondrial intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini123 – 773651CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei48 – 7326HelicalSequence AnalysisAdd
    BLAST
    Transmembranei103 – 12220HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni555 – 56713Coenzyme A bindingBy similarityAdd
    BLAST

    Domaini

    A conformation change in the N-terminal region spanning the first 42 residues plays an important role in the regulation of enzyme activity by malonyl-CoA.1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG70127.
    HOGENOMiHOG000233542.
    HOVERGENiHBG003458.
    InParanoidiP50416.
    KOiK08765.
    OMAiIASEKHQ.
    OrthoDBiEOG7J17ZQ.
    PhylomeDBiP50416.
    TreeFamiTF313836.

    Family and domain databases

    InterProiIPR000542. Carn_acyl_trans.
    [Graphical view]
    PANTHERiPTHR22589. PTHR22589. 1 hit.
    PfamiPF00755. Carn_acyltransf. 1 hit.
    [Graphical view]
    PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view]

    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: P50416-1) [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

    MAEAHQAVAF QFTVTPDGID LRLSHEALRQ IYLSGLHSWK KKFIRFKNGI    50
    ITGVYPASPS SWLIVVVGVM TTMYAKIDPS LGIIAKINRT LETANCMSSQ 100
    TKNVVSGVLF GTGLWVALIV TMRYSLKVLL SYHGWMFTEH GKMSRATKIW 150
    MGMVKIFSGR KPMLYSFQTS LPRLPVPAVK DTVNRYLQSV RPLMKEEDFK 200
    RMTALAQDFA VGLGPRLQWY LKLKSWWATN YVSDWWEEYI YLRGRGPLMV 250
    NSNYYAMDLL YILPTHIQAA RAGNAIHAIL LYRRKLDREE IKPIRLLGST 300
    IPLCSAQWER MFNTSRIPGE ETDTIQHMRD SKHIVVYHRG RYFKVWLYHD 350
    GRLLKPREME QQMQRILDNT SEPQPGEARL AALTAGDRVP WARCRQAYFG 400
    RGKNKQSLDA VEKAAFFVTL DETEEGYRSE DPDTSMDSYA KSLLHGRCYD 450
    RWFDKSFTFV VFKNGKMGLN AEHSWADAPI VAHLWEYVMS IDSLQLGYAE 500
    DGHCKGDINP NIPYPTRLQW DIPGECQEVI ETSLNTANLL ANDVDFHSFP 550
    FVAFGKGIIK KCRTSPDAFV QLALQLAHYK DMGKFCLTYE ASMTRLFREG 600
    RTETVRSCTT ESCDFVRAMV DPAQTVEQRL KLFKLASEKH QHMYRLAMTG 650
    SGIDRHLFCL YVVSKYLAVE SPFLKEVLSE PWRLSTSQTP QQQVELFDLE 700
    NNPEYVSSGG GFGPVADDGY GVSYILVGEN LINFHISSKF SCPETDSHRF 750
    GRHLKEAMTD IITLFGLSSN SKK 773
    Length:773
    Mass (Da):88,368
    Last modified:December 7, 2004 - v2
    Checksum:iE5DC9141B6301947
    GO
    Isoform 2 (identifier: P50416-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         746-773: DSHRFGRHLKEAMTDIITLFGLSSNSKK → GIISQGPSSDT

    Show »
    Length:756
    Mass (Da):86,239
    Checksum:iC7B0ED8A26285110
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti479 – 4791P → Q in AAC41748. (PubMed:7892212)Curated
    Sequence conflicti568 – 5681A → T in AAC41748. (PubMed:7892212)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231R → C in CPT1AD. 1 Publication
    VAR_020546
    Natural varianti275 – 2751A → T.2 Publications
    Corresponds to variant rs2229738 [ dbSNP | Ensembl ].
    VAR_020547
    Natural varianti304 – 3041C → W in CPT1AD. 1 Publication
    VAR_020548
    Natural varianti314 – 3141T → I in CPT1AD. 1 Publication
    VAR_020549
    Natural varianti316 – 3161R → G in CPT1AD. 1 Publication
    VAR_046767
    Natural varianti343 – 3431F → V in CPT1AD. 1 Publication
    VAR_046768
    Natural varianti357 – 3571R → W in CPT1AD; decreased stability. 1 Publication
    VAR_020550
    Natural varianti360 – 3601E → G in CPT1AD; reduced protein levels.
    Corresponds to variant rs28936372 [ dbSNP | Ensembl ].
    VAR_020551
    Natural varianti395 – 3951Missing in CPT1AD; loss of activity. 1 Publication
    VAR_020552
    Natural varianti414 – 4141A → V in CPT1AD; decreased activity. 1 Publication
    Corresponds to variant rs28936373 [ dbSNP | Ensembl ].
    VAR_020553
    Natural varianti454 – 4541D → G in CPT1AD. 1 Publication
    VAR_020554
    Natural varianti465 – 4651G → W in CPT1AD. 1 Publication
    VAR_046769
    Natural varianti479 – 4791P → L in CPT1AD; decreased activity. 1 Publication
    VAR_020555
    Natural varianti484 – 4841L → P in CPT1AD. 1 Publication
    VAR_020556
    Natural varianti498 – 4981Y → C in CPT1AD; decreased activity. 1 Publication
    VAR_020557
    Natural varianti709 – 7091G → E in CPT1AD; loss of activity. 1 Publication
    Corresponds to variant rs28936374 [ dbSNP | Ensembl ].
    VAR_020558
    Natural varianti710 – 7101G → E in CPT1AD; loss of activity. 1 Publication
    VAR_020559

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei746 – 77328DSHRF…SNSKK → GIISQGPSSDT in isoform 2. 2 PublicationsVSP_012167Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39211 mRNA. Translation: AAC41748.1.
    AJ420747 Genomic DNA. Translation: CAD12625.1.
    AJ420748 Genomic DNA. Translation: CAD59673.1.
    BT009791 mRNA. Translation: AAP88793.1.
    BC000185 mRNA. Translation: AAH00185.1.
    CCDSiCCDS31624.1. [P50416-2]
    CCDS8185.1. [P50416-1]
    PIRiI59351.
    RefSeqiNP_001027017.1. NM_001031847.2. [P50416-2]
    NP_001867.2. NM_001876.3. [P50416-1]
    UniGeneiHs.503043.

    Genome annotation databases

    EnsembliENST00000265641; ENSP00000265641; ENSG00000110090. [P50416-1]
    ENST00000376618; ENSP00000365803; ENSG00000110090. [P50416-2]
    ENST00000539743; ENSP00000446108; ENSG00000110090. [P50416-1]
    ENST00000540367; ENSP00000439084; ENSG00000110090. [P50416-2]
    GeneIDi1374.
    KEGGihsa:1374.
    UCSCiuc001oof.4. human. [P50416-2]
    uc001oog.4. human. [P50416-1]

    Polymorphism databases

    DMDMi56405343.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39211 mRNA. Translation: AAC41748.1 .
    AJ420747 Genomic DNA. Translation: CAD12625.1 .
    AJ420748 Genomic DNA. Translation: CAD59673.1 .
    BT009791 mRNA. Translation: AAP88793.1 .
    BC000185 mRNA. Translation: AAH00185.1 .
    CCDSi CCDS31624.1. [P50416-2 ]
    CCDS8185.1. [P50416-1 ]
    PIRi I59351.
    RefSeqi NP_001027017.1. NM_001031847.2. [P50416-2 ]
    NP_001867.2. NM_001876.3. [P50416-1 ]
    UniGenei Hs.503043.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LE3 NMR - A 1-42 [» ]
    ProteinModelPortali P50416.
    SMRi P50416. Positions 1-42, 180-765.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107765. 28 interactions.
    IntActi P50416. 13 interactions.
    MINTi MINT-3018357.
    STRINGi 9606.ENSP00000265641.

    Chemistry

    ChEMBLi CHEMBL1293194.
    DrugBanki DB00583. L-Carnitine.
    DB01074. Perhexiline.

    PTM databases

    PhosphoSitei P50416.

    Polymorphism databases

    DMDMi 56405343.

    Proteomic databases

    MaxQBi P50416.
    PaxDbi P50416.
    PeptideAtlasi P50416.
    PRIDEi P50416.

    Protocols and materials databases

    DNASUi 1374.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265641 ; ENSP00000265641 ; ENSG00000110090 . [P50416-1 ]
    ENST00000376618 ; ENSP00000365803 ; ENSG00000110090 . [P50416-2 ]
    ENST00000539743 ; ENSP00000446108 ; ENSG00000110090 . [P50416-1 ]
    ENST00000540367 ; ENSP00000439084 ; ENSG00000110090 . [P50416-2 ]
    GeneIDi 1374.
    KEGGi hsa:1374.
    UCSCi uc001oof.4. human. [P50416-2 ]
    uc001oog.4. human. [P50416-1 ]

    Organism-specific databases

    CTDi 1374.
    GeneCardsi GC11M068524.
    GeneReviewsi CPT1A.
    HGNCi HGNC:2328. CPT1A.
    HPAi HPA008835.
    MIMi 255120. phenotype.
    600528. gene.
    neXtProti NX_P50416.
    Orphaneti 156. Carnitine palmitoyl transferase 1A deficiency.
    PharmGKBi PA26847.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70127.
    HOGENOMi HOG000233542.
    HOVERGENi HBG003458.
    InParanoidi P50416.
    KOi K08765.
    OMAi IASEKHQ.
    OrthoDBi EOG7J17ZQ.
    PhylomeDBi P50416.
    TreeFami TF313836.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci MetaCyc:HS03286-MONOMER.
    BRENDAi 2.3.1.21. 2681.
    Reactomei REACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    SABIO-RK P50416.

    Miscellaneous databases

    ChiTaRSi CPT1A. human.
    GenomeRNAii 1374.
    NextBioi 5569.
    PROi P50416.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50416.
    Bgeei P50416.
    CleanExi HS_CPT1A.
    Genevestigatori P50416.

    Family and domain databases

    InterProi IPR000542. Carn_acyl_trans.
    [Graphical view ]
    PANTHERi PTHR22589. PTHR22589. 1 hit.
    Pfami PF00755. Carn_acyltransf. 1 hit.
    [Graphical view ]
    PROSITEi PS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene."
      Britton C.H., Schultz R.A., Zhang B., Esser V., Foster D.W., McGarry J.D.
      Proc. Natl. Acad. Sci. U.S.A. 92:1984-1988(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Organization of the human liver carnitine palmitoyltransferase 1 gene (CPT1A) and identification of novel mutations in hypoketotic hypoglycaemia."
      Gobin S., Bonnefont J.-P., Prip-Buus C., Mugnier C., Ferrec M., Demaugre F., Saudubray J.-M., Rostane H., Djouadi F., Wilcox W., Cederbaum S., Haas R., Nyhan W.L., Green A., Gray G., Girard J., Thuillier L.
      Hum. Genet. 111:179-189(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CPT1AD VAL-414 AND CYS-498, VARIANT THR-275.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Eye.
    5. "An intronic peroxisome proliferator-activated receptor-binding sequence mediates fatty acid induction of the human carnitine palmitoyltransferase 1A."
      Napal L., Marrero P.F., Haro D.
      J. Mol. Biol. 354:751-759(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY FATTY ACIDS.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Structural model of carnitine palmitoyltransferase I based on the carnitine acetyltransferase crystal."
      Morillas M., Lopez-Vinas E., Valencia A., Serra D., Gomez-Puertas P., Hegardt F.G., Asins G.
      Biochem. J. 379:777-784(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    8. "An environment-dependent structural switch underlies the regulation of carnitine palmitoyltransferase 1A."
      Rao J.N., Warren G.Z., Estolt-Povedano S., Zammit V.A., Ulmer T.S.
      J. Biol. Chem. 286:42545-42554(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-42, DOMAIN.
    9. "Molecular basis of hepatic carnitine palmitoyltransferase I deficiency."
      IJlst L., Mandel H., Oostheim W., Ruiter J.P.N., Gutman A., Wanders R.J.
      J. Clin. Invest. 102:527-531(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CPT1AD GLY-454.
    10. "Molecular characterization of L-CPT I deficiency in six patients: insights into function of the native enzyme."
      Brown N.F., Mullur R.S., Subramanian I., Esser V., Bennett M.J., Saudubray J.-M., Feigenbaum A.S., Kobari J.A., Macleod P.M., McGarry J.D., Cohen J.C.
      J. Lipid Res. 42:1134-1142(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CPT1AD CYS-123; TRP-304; TRP-357; ARG-395 DEL; LEU-479 AND PRO-484, VARIANT THR-275.
    11. "Molecular and enzymatic characterization of a unique carnitine palmitoyltransferase 1A mutation in the Hutterite community."
      Prip-Buus C., Thuillier L., Abadi N., Prasad C., Dilling L., Klasing J., Demaugre F., Greenberg C.R., Haworth J.C., Droin V., Kadhom N., Gobin S., Kamoun P., Girard J., Bonnefont J.-P.
      Mol. Genet. Metab. 73:46-54(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CPT1AD GLU-710, CHARACTERIZATION OF VARIANT CPT1AD GLU-710, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    12. "Expression analysis of two mutations in carnitine palmitoyltransferase IA deficiency."
      Ogawa E., Kanazawa M., Yamamoto S., Ohtsuka S., Ogawa A., Ohtake A., Takayanagi M., Kohno Y.
      J. Hum. Genet. 47:342-347(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT CPT1AD GLY-360.
    13. "Functional and structural basis of carnitine palmitoyltransferase 1A deficiency."
      Gobin S., Thuillier L., Jogl G., Faye A., Tong L., Chi M., Bonnefont J.-P., Girard J., Prip-Buus C.
      J. Biol. Chem. 278:50428-50434(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CPT1AD GLU-709, CHARACTERIZATION OF VARIANTS CPT1AD THR-275; VAL-414; CYS-498; GLU-709 AND GLU-710, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION.
    14. "Successful long-term treatment of hepatic carnitine palmitoyltransferase I deficiency and a novel mutation."
      Stoler J.M., Sabry M.A., Hanley C., Hoppel C.L., Shih V.E.
      J. Inherit. Metab. Dis. 27:679-684(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CPT1AD ILE-314.
    15. "Novel mutations in CPT 1A define molecular heterogeneity of hepatic carnitine palmitoyltransferase I deficiency."
      Bennett M.J., Boriack R.L., Narayan S., Rutledge S.L., Raff M.L.
      Mol. Genet. Metab. 82:59-63(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CPT1AD GLY-316; VAL-343 AND TRP-465.

    Entry informationi

    Entry nameiCPT1A_HUMAN
    AccessioniPrimary (citable) accession number: P50416
    Secondary accession number(s): Q8TCU0, Q9BWK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 139 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 11
      Human chromosome 11: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3