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P43155

- CACP_HUMAN

UniProt

P43155 - CACP_HUMAN

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Protein

Carnitine O-acetyltransferase

Gene

CRAT

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

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
Complete GO annotation...

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-KW
  2. mitochondrial inner membrane Source: UniProtKB-KW
  3. mitochondrion Source: UniProtKB
  4. peroxisomal matrix Source: Reactome
  5. peroxisome Source: UniProtKB
Complete GO annotation...

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

BgeeiP43155.
CleanExiHS_CRAT.
ExpressionAtlasiP43155. baseline and differential.
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 – 5412Combined sources
Turni55 – 573Combined sources
Helixi60 – 7415Combined sources
Helixi79 – 9315Combined sources
Beta strandi94 – 963Combined sources
Helixi99 – 1068Combined sources
Turni107 – 1093Combined sources
Turni116 – 1183Combined sources
Beta strandi121 – 1233Combined sources
Helixi132 – 15423Combined sources
Helixi171 – 1755Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi210 – 2156Combined sources
Helixi226 – 23813Combined sources
Helixi248 – 2536Combined sources
Helixi256 – 26611Combined sources
Helixi270 – 28112Combined sources
Beta strandi285 – 2895Combined sources
Beta strandi297 – 2993Combined sources
Helixi300 – 31011Combined sources
Turni314 – 3196Combined sources
Beta strandi325 – 3328Combined sources
Beta strandi337 – 3415Combined sources
Helixi348 – 36316Combined sources
Beta strandi379 – 3813Combined sources
Helixi387 – 40620Combined sources
Beta strandi407 – 4148Combined sources
Helixi420 – 4245Combined sources
Helixi429 – 44517Combined sources
Beta strandi451 – 4566Combined sources
Beta strandi465 – 4695Combined sources
Helixi473 – 48210Combined sources
Helixi489 – 51123Combined sources
Helixi517 – 52913Combined sources
Helixi536 – 5394Combined sources
Helixi541 – 5466Combined sources
Beta strandi550 – 5556Combined sources
Beta strandi559 – 5613Combined sources
Beta strandi563 – 5653Combined sources
Beta strandi574 – 5807Combined sources
Beta strandi585 – 5928Combined sources
Helixi600 – 61920Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119220.
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

        10         20         30         40         50
MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY
60 70 80 90 100
LKALQPIVSE EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE
110 120 130 140 150
WWLKTAYLQY RQPVVIYSSP GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK
160 170 180 190 200
VMIDNETLPV EYLGGKPLCM NQYYQILSSC RVPGPKQDTV SNFSKTKKPP
210 220 230 240 250
THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS LQTNKEPVGI
260 270 280 290 300
LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY
310 320 330 340 350
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP
360 370 380 390 400
IVTLLDYVIE YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL
410 420 430 440 450
SIMIQDLDIT VMVFHHFGKD FPKSEKLSPD AFIQMALQLA YYRIYGQACA
460 470 480 490 500
TYESASLRMF HLGRTDTIRS ASMDSLTFVK AMDDSSVTEH QKVELLRKAV
510 520 530 540 550
QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD TSYAIAMHFH
560 570 580 590 600
LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA
610 620
ARLAHYLEKA LLDMRALLQS HPRAKL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00760000119220.
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

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

Gene expression databases

Bgeei P43155.
CleanExi HS_CRAT.
ExpressionAtlasi P43155. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 147 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