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P43155

- CACP_HUMAN

UniProt

P43155 - CACP_HUMAN

Protein

Carnitine O-acetyltransferase

Gene

CRAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 5 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.

    Catalytic activityi

    Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei343 – 3431Proton acceptorCurated
    Binding sitei419 – 4191Coenzyme ABy similarity
    Binding sitei452 – 4521Carnitine1 Publication
    Binding sitei454 – 4541Carnitine1 Publication
    Binding sitei456 – 4561Coenzyme A; via amide nitrogenBy similarity
    Binding sitei465 – 4651Carnitine1 Publication
    Binding sitei504 – 5041Coenzyme ABy similarity
    Binding sitei555 – 5551Coenzyme A; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. carnitine O-acetyltransferase activity Source: UniProtKB
    2. receptor binding Source: UniProtKB

    GO - Biological processi

    1. carnitine metabolic process, CoA-linked Source: UniProtKB
    2. cellular lipid metabolic process Source: Reactome
    3. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01816-MONOMER.
    ReactomeiREACT_17017. Beta-oxidation of pristanoyl-CoA.
    REACT_17062. Beta-oxidation of very long chain fatty acids.
    SABIO-RKP43155.

    Protein family/group databases

    TCDBi4.C.2.1.1. the carnitine o-acyl transferase (crat) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carnitine O-acetyltransferase (EC:2.3.1.7)
    Short name:
    Carnitine acetylase
    Alternative name(s):
    Carnitine acetyltransferase
    Short name:
    CAT
    Short name:
    CrAT
    Gene namesi
    Name:CRAT
    Synonyms:CAT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:2342. CRAT.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. mitochondrial inner membrane Source: UniProtKB-SubCell
    3. mitochondrion Source: UniProtKB
    4. peroxisomal matrix Source: Reactome
    5. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi452 – 4521Y → A: Increases the KM for carnitine 100-fold. 1 Publication
    Mutagenesisi452 – 4521Y → F: Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold. 1 Publication
    Mutagenesisi465 – 4651T → A: Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold. 1 Publication
    Mutagenesisi518 – 5181R → Q: Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold. 1 Publication
    Mutagenesisi566 – 5661F → A: Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold. 1 Publication
    Mutagenesisi566 – 5661F → Y: No effect. 1 Publication

    Organism-specific databases

    PharmGKBiPA26862.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 626626Carnitine O-acetyltransferasePRO_0000210172Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei93 – 931N6-succinyllysineBy similarity
    Modified residuei261 – 2611N6-acetyllysine; alternate1 Publication
    Modified residuei261 – 2611N6-succinyllysine; alternateBy similarity
    Modified residuei268 – 2681N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP43155.
    PaxDbiP43155.
    PRIDEiP43155.

    PTM databases

    PhosphoSiteiP43155.

    Expressioni

    Tissue specificityi

    Mostly in skeletal muscle, less in heart, liver and pancreas, only weakly detectable in brain, placenta, lung and kidney.

    Gene expression databases

    ArrayExpressiP43155.
    BgeeiP43155.
    CleanExiHS_CRAT.
    GenevestigatoriP43155.

    Organism-specific databases

    HPAiHPA019230.
    HPA020260.
    HPA022815.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi107774. 3 interactions.
    IntActiP43155. 10 interactions.
    STRINGi9606.ENSP00000315013.

    Structurei

    Secondary structure

    1
    626
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 5412
    Turni55 – 573
    Helixi60 – 7415
    Helixi79 – 9315
    Beta strandi94 – 963
    Helixi99 – 1068
    Turni107 – 1093
    Turni116 – 1183
    Beta strandi121 – 1233
    Helixi132 – 15423
    Helixi171 – 1755
    Beta strandi179 – 1824
    Beta strandi185 – 1873
    Beta strandi189 – 1924
    Beta strandi196 – 1983
    Beta strandi202 – 2076
    Beta strandi210 – 2156
    Helixi226 – 23813
    Helixi248 – 2536
    Helixi256 – 26611
    Helixi270 – 28112
    Beta strandi285 – 2895
    Beta strandi297 – 2993
    Helixi300 – 31011
    Turni314 – 3196
    Beta strandi325 – 3328
    Beta strandi337 – 3415
    Helixi348 – 36316
    Beta strandi379 – 3813
    Helixi387 – 40620
    Beta strandi407 – 4148
    Helixi420 – 4245
    Helixi429 – 44517
    Beta strandi451 – 4566
    Beta strandi465 – 4695
    Helixi473 – 48210
    Helixi489 – 51123
    Helixi517 – 52913
    Helixi536 – 5394
    Helixi541 – 5466
    Beta strandi550 – 5556
    Beta strandi559 – 5613
    Beta strandi563 – 5653
    Beta strandi574 – 5807
    Beta strandi585 – 5928
    Helixi600 – 61920

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NM8X-ray1.60A35-626[»]
    1S5OX-ray1.80A35-626[»]
    DisProtiDP00305.
    ProteinModelPortaliP43155.
    SMRiP43155. Positions 31-620.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43155.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni423 – 4308Coenzyme A bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi624 – 6263Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG70127.
    HOGENOMiHOG000233845.
    HOVERGENiHBG107717.
    InParanoidiP43155.
    KOiK00624.
    OMAiYLERALL.
    OrthoDBiEOG7WHH90.
    PhylomeDBiP43155.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P43155-1) [UniParc]FASTAAdd to Basket

    Also known as: SM-1400

    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

    MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY    50
    LKALQPIVSE EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE 100
    WWLKTAYLQY RQPVVIYSSP GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK 150
    VMIDNETLPV EYLGGKPLCM NQYYQILSSC RVPGPKQDTV SNFSKTKKPP 200
    THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS LQTNKEPVGI 250
    LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY 300
    RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP 350
    IVTLLDYVIE YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL 400
    SIMIQDLDIT VMVFHHFGKD FPKSEKLSPD AFIQMALQLA YYRIYGQACA 450
    TYESASLRMF HLGRTDTIRS ASMDSLTFVK AMDDSSVTEH QKVELLRKAV 500
    QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD TSYAIAMHFH 550
    LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA 600
    ARLAHYLEKA LLDMRALLQS HPRAKL 626
    Length:626
    Mass (Da):70,858
    Last modified:November 25, 2008 - v5
    Checksum:i51B65E7C94E458D7
    GO
    Isoform 2 (identifier: P43155-2) [UniParc]FASTAAdd to Basket

    Also known as: SM-1200

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:605
    Mass (Da):68,569
    Checksum:i915540218D46D9C7
    GO
    Isoform 3 (identifier: P43155-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         282-363: Missing.

    Show »
    Length:544
    Mass (Da):61,870
    Checksum:i2AD5B9AA49773E5C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 881E → G in CAA55359. (PubMed:7829107)Curated
    Sequence conflicti349 – 3491P → F in CAA55359. (PubMed:7829107)Curated
    Sequence conflicti517 – 5171D → G in CAA55359. (PubMed:7829107)Curated
    Sequence conflicti534 – 5341M → T in CAA55359. (PubMed:7829107)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti372 – 3721L → M.3 Publications
    Corresponds to variant rs3118635 [ dbSNP | Ensembl ].
    VAR_047780
    Natural varianti624 – 6241A → P.
    Corresponds to variant rs17459086 [ dbSNP | Ensembl ].
    VAR_047781

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121Missing in isoform 2. CuratedVSP_000792Add
    BLAST
    Alternative sequencei282 – 36382Missing in isoform 3. 2 PublicationsVSP_012798Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT006801 mRNA. Translation: AAP35447.1.
    AL158151 Genomic DNA. Translation: CAI12869.1.
    BC000723 mRNA. Translation: AAH00723.1.
    X79825 Genomic DNA. No translation available.
    X79827 Genomic DNA. No translation available.
    X78706 mRNA. Translation: CAA55359.1.
    CCDSiCCDS6919.1. [P43155-1]
    PIRiA55720.
    RefSeqiNP_000746.2. NM_000755.3.
    NP_001244292.1. NM_001257363.1.
    XP_005251765.1. XM_005251708.1. [P43155-2]
    XP_005251766.1. XM_005251709.2. [P43155-2]
    UniGeneiHs.12068.

    Genome annotation databases

    EnsembliENST00000318080; ENSP00000315013; ENSG00000095321. [P43155-1]
    GeneIDi1384.
    KEGGihsa:1384.
    UCSCiuc004bxh.3. human. [P43155-1]

    Polymorphism databases

    DMDMi215274265.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT006801 mRNA. Translation: AAP35447.1 .
    AL158151 Genomic DNA. Translation: CAI12869.1 .
    BC000723 mRNA. Translation: AAH00723.1 .
    X79825 Genomic DNA. No translation available.
    X79827 Genomic DNA. No translation available.
    X78706 mRNA. Translation: CAA55359.1 .
    CCDSi CCDS6919.1. [P43155-1 ]
    PIRi A55720.
    RefSeqi NP_000746.2. NM_000755.3.
    NP_001244292.1. NM_001257363.1.
    XP_005251765.1. XM_005251708.1. [P43155-2 ]
    XP_005251766.1. XM_005251709.2. [P43155-2 ]
    UniGenei Hs.12068.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NM8 X-ray 1.60 A 35-626 [» ]
    1S5O X-ray 1.80 A 35-626 [» ]
    DisProti DP00305.
    ProteinModelPortali P43155.
    SMRi P43155. Positions 31-620.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107774. 3 interactions.
    IntActi P43155. 10 interactions.
    STRINGi 9606.ENSP00000315013.

    Chemistry

    BindingDBi P43155.
    ChEMBLi CHEMBL3184.
    DrugBanki DB00583. L-Carnitine.

    Protein family/group databases

    TCDBi 4.C.2.1.1. the carnitine o-acyl transferase (crat) family.

    PTM databases

    PhosphoSitei P43155.

    Polymorphism databases

    DMDMi 215274265.

    Proteomic databases

    MaxQBi P43155.
    PaxDbi P43155.
    PRIDEi P43155.

    Protocols and materials databases

    DNASUi 1384.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318080 ; ENSP00000315013 ; ENSG00000095321 . [P43155-1 ]
    GeneIDi 1384.
    KEGGi hsa:1384.
    UCSCi uc004bxh.3. human. [P43155-1 ]

    Organism-specific databases

    CTDi 1384.
    GeneCardsi GC09M131857.
    H-InvDB HIX0169130.
    HGNCi HGNC:2342. CRAT.
    HPAi HPA019230.
    HPA020260.
    HPA022815.
    MIMi 600184. gene.
    neXtProti NX_P43155.
    PharmGKBi PA26862.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70127.
    HOGENOMi HOG000233845.
    HOVERGENi HBG107717.
    InParanoidi P43155.
    KOi K00624.
    OMAi YLERALL.
    OrthoDBi EOG7WHH90.
    PhylomeDBi P43155.
    TreeFami TF313836.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01816-MONOMER.
    Reactomei REACT_17017. Beta-oxidation of pristanoyl-CoA.
    REACT_17062. Beta-oxidation of very long chain fatty acids.
    SABIO-RK P43155.

    Miscellaneous databases

    EvolutionaryTracei P43155.
    GeneWikii CRAT_(gene).
    GenomeRNAii 1384.
    NextBioi 5619.
    PROi P43155.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43155.
    Bgeei P43155.
    CleanExi HS_CRAT.
    Genevestigatori P43155.

    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. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT MET-372.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 3), VARIANT MET-372.
      Tissue: Placenta.
    4. "Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations."
      Corti O., DiDonato S., Finocchiaro G.
      Biochem. J. 303:37-41(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    5. "Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1."
      Corti O., Finocchiaro G., Rossi E., Zuffardi O., Didonato S.
      Genomics 23:94-99(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-626 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT MET-372.
    6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-261 AND LYS-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer."
      Wu D., Govindasamy L., Lian W., Gu Y., Kukar T., Agbandje-McKenna M., McKenna R.
      J. Biol. Chem. 278:13159-13165(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 35-626, SUBUNIT.
    8. "Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase."
      Govindasamy L., Kukar T., Lian W., Pedersen B., Gu Y., Agbandje-McKenna M., Jin S., McKenna R., Wu D.
      J. Struct. Biol. 146:416-424(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 35-626 IN COMPLEX WITH CARNITINE, MUTAGENESIS OF TYR-452; THR-465; ARG-518 AND PHE-566.

    Entry informationi

    Entry nameiCACP_HUMAN
    AccessioniPrimary (citable) accession number: P43155
    Secondary accession number(s): Q5T952, Q9BW16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 145 of the entry and version 5 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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