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P50416

- CPT1A_HUMAN

UniProt

P50416 - CPT1A_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP50416.
CleanExiHS_CPT1A.
ExpressionAtlasiP50416. baseline and differential.
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 – 74Combined sources
Beta strandi9 – 157Combined sources
Beta strandi18 – 236Combined sources
Helixi25 – 3915Combined sources

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.
GeneTreeiENSGT00760000119220.
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) [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
MAEAHQAVAF QFTVTPDGID LRLSHEALRQ IYLSGLHSWK KKFIRFKNGI
60 70 80 90 100
ITGVYPASPS SWLIVVVGVM TTMYAKIDPS LGIIAKINRT LETANCMSSQ
110 120 130 140 150
TKNVVSGVLF GTGLWVALIV TMRYSLKVLL SYHGWMFTEH GKMSRATKIW
160 170 180 190 200
MGMVKIFSGR KPMLYSFQTS LPRLPVPAVK DTVNRYLQSV RPLMKEEDFK
210 220 230 240 250
RMTALAQDFA VGLGPRLQWY LKLKSWWATN YVSDWWEEYI YLRGRGPLMV
260 270 280 290 300
NSNYYAMDLL YILPTHIQAA RAGNAIHAIL LYRRKLDREE IKPIRLLGST
310 320 330 340 350
IPLCSAQWER MFNTSRIPGE ETDTIQHMRD SKHIVVYHRG RYFKVWLYHD
360 370 380 390 400
GRLLKPREME QQMQRILDNT SEPQPGEARL AALTAGDRVP WARCRQAYFG
410 420 430 440 450
RGKNKQSLDA VEKAAFFVTL DETEEGYRSE DPDTSMDSYA KSLLHGRCYD
460 470 480 490 500
RWFDKSFTFV VFKNGKMGLN AEHSWADAPI VAHLWEYVMS IDSLQLGYAE
510 520 530 540 550
DGHCKGDINP NIPYPTRLQW DIPGECQEVI ETSLNTANLL ANDVDFHSFP
560 570 580 590 600
FVAFGKGIIK KCRTSPDAFV QLALQLAHYK DMGKFCLTYE ASMTRLFREG
610 620 630 640 650
RTETVRSCTT ESCDFVRAMV DPAQTVEQRL KLFKLASEKH QHMYRLAMTG
660 670 680 690 700
SGIDRHLFCL YVVSKYLAVE SPFLKEVLSE PWRLSTSQTP QQQVELFDLE
710 720 730 740 750
NNPEYVSSGG GFGPVADDGY GVSYILVGEN LINFHISSKF SCPETDSHRF
760 770
GRHLKEAMTD IITLFGLSSN SKK
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 DB01016. Glyburide.
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.
GeneTreei ENSGT00760000119220.
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

Bgeei P50416.
CleanExi HS_CPT1A.
ExpressionAtlasi P50416. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 140 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