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Protein Page:
AMACR (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
AMACR 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. Belongs to the CaiB/BaiF CoA-transferase family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Mitochondrial; Isomerase; EC 5.1.99.4; Lipid Metabolism - primary bile acid biosynthesis
Chromosomal Location of Human Ortholog: 5p13
Cellular Component: peroxisomal matrix; mitochondrion; cytoplasm; peroxisome
Molecular Function: alpha-methylacyl-CoA racemase activity; receptor binding
Biological Process: bile acid biosynthetic process; fatty acid beta-oxidation using acyl-CoA oxidase; bile acid metabolic process; cellular lipid metabolic process
Reference #:  Q9UHK6 (UniProtKB)
Alt. Names/Synonyms: 2-methylacyl-CoA racemase; Alpha-methylacyl-CoA racemase; AMACR; CBAS4; RACE; RM
Gene Symbols: AMACR
Molecular weight: 42,387 Da
Basal Isoelectric point: 6.07  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

AMACR

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 3 S39 VRVDRPGSRYDVSRL
0 1 Y41 VDRPGSRYDVSRLGR
0 33 K58 RSLVLDLKQPRGAAV
0 2 K58 RSLVLDLKQPRGAAV
0 1 K87 FRRGVMEKLQLGPEI
0 1 K87 FRRGVMEKLQLGPEI
0 1 R101 ILQRENPRLIYARLS
0 1 R101 ILQRENPRLIYARLS
0 2 R101 ILQRENPRLIYARLS
0 1 S113 RLSGFGQSGSFCRLA
0 1 S115 SGFGQSGSFCRLAGH
0 2 R118 GQSGSFCRLAGHDIN
0 1 R118 GQSGSFCRLAGHDIN
0 1 R118 GQSGSFCRLAGHDIN
0 1 Y126 LAGHDINYLALSGVL
0 1 S130 DINYLALSGVLSKIG
0 1 K135 ALSGVLSKIGRSGEN
0 1 K135 ALSGVLSKIGRSGEN
0 1 - gap
0 1 E205 TQKLSLWEAPRGQNM
0 1 E205 TQKLSLWEAPRGQNM
0 1 K268 MDDWPEMKKKFADVF
0 1 K268 MDDWPEMKKKFADVF
0 3 E277 KFADVFAEKTKAEWC
0 2 E277 KFADVFAEKTKAEWC
0 1 S314 DHNKERGSFITSEEQ
0 1 S324 TSEEQDVSPRPAPLL
0 1 F345 PSFKRDPFIGEHTEE
0 1 K379 IIESNKVKASL____
  AMACR iso2  
S39 VRVDRPGSRYDVSRL
Y41 VDRPGSRYDVSRLGR
K58 RSLVLDLKQPRGAAV
K58 RSLVLDLKQPRGAAV
K87 FRRGVMEKLQLGPEI
K87 FRRGVMEKLQLGPEI
R101 ILQRENPRLIYARLS
R101 ILQRENPRLIYARLS
R101 ILQRENPRLIYARLS
S113 RLSGFGQSGsFCRLA
S115-p SGFGQSGsFCRLAGH
R118 GQSGsFCRLAGHDIN
R118 GQSGsFCRLAGHDIN
R118 GQSGsFCRLAGHDIN
Y126-p LAGHDINyLALsGGR
S130-p DINyLALsGGRNSIF
- gap
- gap
T153-p EIESVGStSRTEHVG
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

 
S39-p VRVNRLGstGENFLA
T40-p RVNRLGstGENFLAR
K57-ac RSLALDLkRSQGVTV
K57-sc RSLALDLkRSQGVTV
K86-ac FRCGVMEkLQLGPET
K86-sc FRCGVMEkLQLGPET
K100-ac TLLQDNPkLIYARLS
K100-ub TLLQDNPkLIYARLS
K100-sc TLLQDNPkLIYARLS
S112-p RLSGFGQsGIFSkVA
I114 SGFGQsGIFSkVAGH
K117-ac GQsGIFSkVAGHDIN
K117-ub GQsGIFSkVAGHDIN
K117-sc GQsGIFSkVAGHDIN
Y125 VAGHDINYLALSGVL
S129 DINYLALSGVLSkIG
K134-ub ALSGVLSkIGRSGEN
K134-sc ALSGVLSkIGRSGEN
- gap
K204-ub TQPMGLWkQPRGQNI
K204-sc TQPMGLWkQPRGQNI
K267-ac SADWPEMkKKFADVF
K267-sc SADWPEMkKKFADVF
K276-ac KFADVFAkKTKAEWC
K276-sc KFADVFAkKTKAEWC
S313-p QHNRERAsFITDGEQ
S323-p TDGEQLPsPRPAPLL
S344-p PSAKRDPsVGEHTVE
K378-sc IVESDKLkANL____
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