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Protein

Alpha-methylacyl-CoA racemase

Gene

AMACR

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

Functioni

Racemization of 2-methyl-branched fatty acid CoA esters. Responsible for the conversion of pristanoyl-CoA and C27-bile acyl-CoAs to their (S)-stereoisomers.

Catalytic activityi

(2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521NucleophileBy similarity

GO - Molecular functioni

  1. alpha-methylacyl-CoA racemase activity Source: UniProtKB
  2. receptor binding Source: UniProtKB

GO - Biological processi

  1. bile acid biosynthetic process Source: Reactome
  2. bile acid metabolic process Source: UniProtKB
  3. cellular lipid metabolic process Source: Reactome
  4. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciMetaCyc:HS01416-MONOMER.
BRENDAi5.1.99.4. 2681.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_17017. Beta-oxidation of pristanoyl-CoA.
SABIO-RKQ9UHK6.
UniPathwayiUPA00199.
UPA00221.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-methylacyl-CoA racemase (EC:5.1.99.4)
Alternative name(s):
2-methylacyl-CoA racemase
Gene namesi
Name:AMACR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:451. AMACR.

Subcellular locationi

  1. Peroxisome 1 Publication
  2. Mitochondrion 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. mitochondrion Source: UniProtKB
  3. peroxisomal matrix Source: Reactome
  4. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

Pathology & Biotechi

Involvement in diseasei

Alpha-methylacyl-CoA racemase deficiency (AMACRD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare autosomal recessive peroxisomal disorder characterized by elevated plasma concentrations of pristanic acid C27-bile-acid intermediates, and adult onset of variable neurodegenerative symptoms affecting the central and peripheral nervous systems. Features may include seizures, visual failure, sensorimotor neuropathy, spasticity, migraine, and white matter hyperintensities on brain imaging.

See also OMIM:614307
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521S → P in AMACRD and CBAS4; inactive enzyme. 2 Publications
VAR_010661
Congenital bile acid synthesis defect 4 (CBAS4)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by the presence of trihydroxycoprostanic acid in the bile and absence of cholic acid. Patients manifest neonatal jaundice, intrahepatic cholestasis and bile duct deficiency.

See also OMIM:214950
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521S → P in AMACRD and CBAS4; inactive enzyme. 2 Publications
VAR_010661
Natural varianti107 – 1071L → P in CBAS4; inactive enzyme. 1 Publication
VAR_010665

Keywords - Diseasei

Disease mutation, Intrahepatic cholestasis

Organism-specific databases

MIMi214950. phenotype.
614307. phenotype.
Orphaneti79095. Congenital bile acid synthesis defect type 4.
PharmGKBiPA24757.

Polymorphism and mutation databases

BioMutaiAMACR.
DMDMi313104070.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 382381Alpha-methylacyl-CoA racemasePRO_0000194705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei87 – 871N6-acetyllysine; alternateBy similarity
Modified residuei87 – 871N6-succinyllysine; alternateBy similarity
Modified residuei268 – 2681N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UHK6.
PaxDbiQ9UHK6.
PRIDEiQ9UHK6.

PTM databases

PhosphoSiteiQ9UHK6.

Expressioni

Gene expression databases

BgeeiQ9UHK6.
CleanExiHS_AMACR.
ExpressionAtlasiQ9UHK6. baseline and differential.
GenevestigatoriQ9UHK6.

Organism-specific databases

HPAiCAB001809.
HPA019527.
HPA020912.

Interactioni

Protein-protein interaction databases

BioGridi117134. 2 interactions.
STRINGi9606.ENSP00000334424.

Structurei

3D structure databases

ProteinModelPortaliQ9UHK6.
SMRiQ9UHK6. Positions 3-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi380 – 3823Microbody targeting signal

Sequence similaritiesi

Belongs to the CaiB/BaiF CoA-transferase family.Curated

Phylogenomic databases

eggNOGiCOG1804.
GeneTreeiENSGT00530000063418.
HOGENOMiHOG000219744.
HOVERGENiHBG060891.
InParanoidiQ9UHK6.
KOiK01796.
OMAiNPERGAN.
OrthoDBiEOG78SQJF.
PhylomeDBiQ9UHK6.
TreeFamiTF314188.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
InterProiIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
PANTHERiPTHR11837. PTHR11837. 1 hit.
PfamiPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UHK6-1) [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

        10         20         30         40         50
MALQGISVVE LSGLAPGPFC AMVLADFGAR VVRVDRPGSR YDVSRLGRGK
60 70 80 90 100
RSLVLDLKQP RGAAVLRRLC KRSDVLLEPF RRGVMEKLQL GPEILQRENP
110 120 130 140 150
RLIYARLSGF GQSGSFCRLA GHDINYLALS GVLSKIGRSG ENPYAPLNLL
160 170 180 190 200
ADFAGGGLMC ALGIIMALFD RTRTGKGQVI DANMVEGTAY LSSFLWKTQK
210 220 230 240 250
LSLWEAPRGQ NMLDGGAPFY TTYRTADGEF MAVGAIEPQF YELLIKGLGL
260 270 280 290 300
KSDELPNQMS MDDWPEMKKK FADVFAEKTK AEWCQIFDGT DACVTPVLTF
310 320 330 340 350
EEVVHHDHNK ERGSFITSEE QDVSPRPAPL LLNTPAIPSF KRDPFIGEHT
360 370 380
EEILEEFGFS REEIYQLNSD KIIESNKVKA SL
Length:382
Mass (Da):42,387
Last modified:November 30, 2010 - v2
Checksum:iE967D3221A90BEF8
GO
Isoform 2 (identifier: Q9UHK6-2) [UniParc]FASTAAdd to basket

Also known as: IBLi

The sequence of this isoform differs from the canonical sequence as follows:
     132-229: VLSKIGRSGE...YTTYRTADGE → GRNSIFKFFS...LRPCYFLGQK
     230-382: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:229
Mass (Da):25,914
Checksum:iFC361E1AC140CAF4
GO
Isoform 3 (identifier: Q9UHK6-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-198: VLSKIGRSGE...AYLSSFLWKT → GRNSIFKFFS...AADQRTWTKV
     199-382: Missing.

Show »
Length:198
Mass (Da):22,183
Checksum:i1D677621A6EBD986
GO
Isoform 4 (identifier: Q9UHK6-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: VKASL → AGSKFWILYPTHSNIQK

Note: Expression is elevated in prostate cancer.

Show »
Length:394
Mass (Da):43,860
Checksum:i55B6E53900632287
GO

Sequence cautioni

The sequence ACL67853.1 differs from that shown.Aberrant splicing.Curated
The sequence ACL67854.1 differs from that shown.Aberrant splicing.Curated
The sequence CAB44062.1 differs from that shown. Reason: Frameshift at positions 62, 65 and 114. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181P → R in CAB44062 (PubMed:11060344).Curated
Sequence conflicti128 – 1281A → T in ABQ59031 (PubMed:17974005).Curated
Sequence conflicti150 – 1501L → V in CAB44062 (PubMed:11060344).Curated
Sequence conflicti183 – 1831N → D in AAD10205 (Ref. 4) Curated
Sequence conflicti257 – 2571N → S in AAD10205 (Ref. 4) Curated
Sequence conflicti327 – 3271P → L in CAB44062 (PubMed:11060344).Curated
Sequence conflicti340 – 3423FKR → SKG in CAB44062 (PubMed:11060344).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91V → M.5 Publications
Corresponds to variant rs3195676 [ dbSNP | Ensembl ].
VAR_010660
Natural varianti52 – 521S → P in AMACRD and CBAS4; inactive enzyme. 2 Publications
VAR_010661
Natural varianti107 – 1071L → P in CBAS4; inactive enzyme. 1 Publication
VAR_010665
Natural varianti118 – 1181R → Q.
Corresponds to variant rs16892150 [ dbSNP | Ensembl ].
VAR_055616
Natural varianti175 – 1751G → D.2 Publications
Corresponds to variant rs10941112 [ dbSNP | Ensembl ].
VAR_010662
Natural varianti201 – 2011L → S.4 Publications
Corresponds to variant rs2287939 [ dbSNP | Ensembl ].
VAR_010663
Natural varianti238 – 2381P → S.
Corresponds to variant rs9282594 [ dbSNP | Ensembl ].
VAR_055617
Natural varianti239 – 2391Q → H.
Corresponds to variant rs34677 [ dbSNP | Ensembl ].
VAR_055618
Natural varianti261 – 2611M → I.
Corresponds to variant rs9282593 [ dbSNP | Ensembl ].
VAR_055619
Natural varianti261 – 2611M → T.2 Publications
Corresponds to variant rs3195678 [ dbSNP | Ensembl ].
VAR_055620
Natural varianti277 – 2771E → K.4 Publications
Corresponds to variant rs2278008 [ dbSNP | Ensembl ].
VAR_010664

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei132 – 22998VLSKI…TADGE → GRNSIFKFFSVENSEIESVG STSRTEHVGWWSTFLYDLQD SRWGIHGCWSNRTPVLRAAD QRSLIPYFNLYLQFLNISMQ NLFKVHTLLRPCYFLGQK in isoform 2. 1 PublicationVSP_037321Add
BLAST
Alternative sequencei132 – 19867VLSKI…FLWKT → GRNSIFKFFSVENSEIESVG STSRTEHVGWWSTFLYDLQD SRWGIHGCWSNRTPVLRAAD QRTWTKV in isoform 3. 2 PublicationsVSP_037323Add
BLAST
Alternative sequencei199 – 382184Missing in isoform 3. 2 PublicationsVSP_037324Add
BLAST
Alternative sequencei230 – 382153Missing in isoform 2. 1 PublicationVSP_037326Add
BLAST
Alternative sequencei378 – 3825VKASL → AGSKFWILYPTHSNIQK in isoform 4. 1 PublicationVSP_044875

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ130733 mRNA. Translation: CAB44062.1. Frameshift.
AF158378 mRNA. Translation: AAF22610.1.
AY935981 mRNA. Translation: AAY16192.1.
AF047020 mRNA. Translation: AAD10205.1.
FJ498906 mRNA. Translation: ACL67853.1. Sequence problems.
FJ498907 mRNA. Translation: ACL67854.1. Sequence problems.
FJ498908 mRNA. Translation: ACL67855.1.
BT007193 mRNA. Translation: AAP35857.1.
EF560721 mRNA. Translation: ABQ59031.1.
AC139783 Genomic DNA. No translation available.
CH471118 Genomic DNA. Translation: EAX10816.1.
BC009471 mRNA. Translation: AAH09471.1.
CCDSiCCDS3902.1. [Q9UHK6-1]
CCDS3903.1. [Q9UHK6-4]
CCDS54836.1. [Q9UHK6-5]
RefSeqiNP_001161067.1. NM_001167595.1. [Q9UHK6-5]
NP_055139.4. NM_014324.5. [Q9UHK6-1]
NP_976316.1. NM_203382.2. [Q9UHK6-4]
UniGeneiHs.508343.

Genome annotation databases

EnsembliENST00000335606; ENSP00000334424; ENSG00000242110. [Q9UHK6-1]
ENST00000382072; ENSP00000371504; ENSG00000242110. [Q9UHK6-4]
ENST00000382085; ENSP00000371517; ENSG00000242110. [Q9UHK6-5]
ENST00000506639; ENSP00000427227; ENSG00000242110. [Q9UHK6-2]
GeneIDi23600.
KEGGihsa:23600.
UCSCiuc003jig.3. human. [Q9UHK6-1]
uc003jih.3. human. [Q9UHK6-4]

Polymorphism and mutation databases

BioMutaiAMACR.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ130733 mRNA. Translation: CAB44062.1. Frameshift.
AF158378 mRNA. Translation: AAF22610.1.
AY935981 mRNA. Translation: AAY16192.1.
AF047020 mRNA. Translation: AAD10205.1.
FJ498906 mRNA. Translation: ACL67853.1. Sequence problems.
FJ498907 mRNA. Translation: ACL67854.1. Sequence problems.
FJ498908 mRNA. Translation: ACL67855.1.
BT007193 mRNA. Translation: AAP35857.1.
EF560721 mRNA. Translation: ABQ59031.1.
AC139783 Genomic DNA. No translation available.
CH471118 Genomic DNA. Translation: EAX10816.1.
BC009471 mRNA. Translation: AAH09471.1.
CCDSiCCDS3902.1. [Q9UHK6-1]
CCDS3903.1. [Q9UHK6-4]
CCDS54836.1. [Q9UHK6-5]
RefSeqiNP_001161067.1. NM_001167595.1. [Q9UHK6-5]
NP_055139.4. NM_014324.5. [Q9UHK6-1]
NP_976316.1. NM_203382.2. [Q9UHK6-4]
UniGeneiHs.508343.

3D structure databases

ProteinModelPortaliQ9UHK6.
SMRiQ9UHK6. Positions 3-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117134. 2 interactions.
STRINGi9606.ENSP00000334424.

PTM databases

PhosphoSiteiQ9UHK6.

Polymorphism and mutation databases

BioMutaiAMACR.
DMDMi313104070.

Proteomic databases

MaxQBiQ9UHK6.
PaxDbiQ9UHK6.
PRIDEiQ9UHK6.

Protocols and materials databases

DNASUi23600.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335606; ENSP00000334424; ENSG00000242110. [Q9UHK6-1]
ENST00000382072; ENSP00000371504; ENSG00000242110. [Q9UHK6-4]
ENST00000382085; ENSP00000371517; ENSG00000242110. [Q9UHK6-5]
ENST00000506639; ENSP00000427227; ENSG00000242110. [Q9UHK6-2]
GeneIDi23600.
KEGGihsa:23600.
UCSCiuc003jig.3. human. [Q9UHK6-1]
uc003jih.3. human. [Q9UHK6-4]

Organism-specific databases

CTDi23600.
GeneCardsiGC05M033986.
HGNCiHGNC:451. AMACR.
HPAiCAB001809.
HPA019527.
HPA020912.
MIMi214950. phenotype.
604489. gene.
614307. phenotype.
neXtProtiNX_Q9UHK6.
Orphaneti79095. Congenital bile acid synthesis defect type 4.
PharmGKBiPA24757.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1804.
GeneTreeiENSGT00530000063418.
HOGENOMiHOG000219744.
HOVERGENiHBG060891.
InParanoidiQ9UHK6.
KOiK01796.
OMAiNPERGAN.
OrthoDBiEOG78SQJF.
PhylomeDBiQ9UHK6.
TreeFamiTF314188.

Enzyme and pathway databases

UniPathwayiUPA00199.
UPA00221.
BioCyciMetaCyc:HS01416-MONOMER.
BRENDAi5.1.99.4. 2681.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_17017. Beta-oxidation of pristanoyl-CoA.
SABIO-RKQ9UHK6.

Miscellaneous databases

ChiTaRSiAMACR. human.
GeneWikiiAlpha-methylacyl-CoA_racemase.
GenomeRNAii23600.
NextBioi46278.
PROiQ9UHK6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHK6.
CleanExiHS_AMACR.
ExpressionAtlasiQ9UHK6. baseline and differential.
GenevestigatoriQ9UHK6.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
InterProiIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
PANTHERiPTHR11837. PTHR11837. 1 hit.
PfamiPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase in humans."
    Amery L., Fransen M., De Nys K., Mannaerts G.P., Van Veldhoven P.P.
    J. Lipid Res. 41:1752-1759(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-175; SER-201; THR-261 AND LYS-277, SUBCELLULAR LOCATION, MICROBODY TARGETING.
  2. "Mutations in the gene encoding peroxisomal alpha-methylacyl-CoA racemase cause adult-onset sensory motor neuropathy."
    Ferdinandusse S., Denis S., Clayton P.T., Graham A., Rees J.E., Allen J.T., McLean B.N., Brown A.Y., Vreken P., Waterham H.R., Wanders R.J.A.
    Nat. Genet. 24:188-191(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT AMACRD PRO-52, VARIANT CBAS4 PRO-107, VARIANTS SER-201 AND LYS-277, CHARACTERIZATION OF VARIANT AMACRD PRO-52, CHARACTERIZATION OF VARIANT CBAS4 PRO-107.
  3. "A variant of the alpha-methyl-acyl-CoA racemase gene created by a deletion in exon 5 and its expression in prostate cancer."
    Mubiru J.N., Valente A.J., Troyer D.A.
    Prostate 65:117-123(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS SER-201 AND LYS-277.
    Tissue: Prostate cancer.
  4. "Human alpha-methylacyl-CoA racemase cDNA sequence."
    Albers C., Schmitz W., Conzelmann E.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-9; ASP-175; SER-201; THR-261 AND LYS-277.
  5. "Expression of alpha-methylacyl-CoA racemase spliced variants in normal and malignant prostate tissue."
    Ouyang B., Leung Y.-K., Wang V., Chung E., Levin L., Bracken B., Cheng L., Ho S.-M.
    Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT MET-9.
  6. "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-9.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Salivary gland.
  8. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-9.
  10. "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-9.
    Tissue: Kidney.
  11. "Purification and characterization of an alpha-methylacyl-CoA racemase from human liver."
    Schmitz W., Albers C., Fingerhut R., Conzelmann E.
    Eur. J. Biochem. 231:815-822(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Liver.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Liver disease caused by failure to racemize trihydroxycholestanoic acid: gene mutation and effect of bile acid therapy."
    Setchell K.D.R., Heubi J.E., Bove K.E., O'Connell N.C., Brewsaugh T., Steinberg S.J., Moser A., Squires R.H. Jr.
    Gastroenterology 124:217-232(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CBAS4 PRO-52.

Entry informationi

Entry nameiAMACR_HUMAN
AccessioniPrimary (citable) accession number: Q9UHK6
Secondary accession number(s): A5YM47
, B8Y916, B8Y918, F8W9N1, O43673, Q3KT79, Q96GH1, Q9Y3Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 30, 2010
Last modified: April 29, 2015
This is version 136 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.