AMACR_HUMAN - dbPTM
AMACR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMACR_HUMAN
UniProt AC Q9UHK6
Protein Name Alpha-methylacyl-CoA racemase
Gene Name AMACR
Organism Homo sapiens (Human).
Sequence Length 382
Subcellular Localization Peroxisome . Mitochondrion .
Protein Description 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..
Protein Sequence MALQGISVVELSGLAPGPFCAMVLADFGARVVRVDRPGSRYDVSRLGRGKRSLVLDLKQPRGAAVLRRLCKRSDVLLEPFRRGVMEKLQLGPEILQRENPRLIYARLSGFGQSGSFCRLAGHDINYLALSGVLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDANMVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGEFMAVGAIEPQFYELLIKGLGLKSDELPNQMSMDDWPEMKKKFADVFAEKTKAEWCQIFDGTDACVTPVLTFEEVVHHDHNKERGSFITSEEQDVSPRPAPLLLNTPAIPSFKRDPFIGEHTEEILEEFGFSREEIYQLNSDKIIESNKVKASL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
58MalonylationRSLVLDLKQPRGAAV
CEEEEECCCCCHHHH
58.9026320211
58 (in isoform 5)Malonylation-58.9026320211
58UbiquitinationRSLVLDLKQPRGAAV
CEEEEECCCCCHHHH
58.90-
58AcetylationRSLVLDLKQPRGAAV
CEEEEECCCCCHHHH
58.90-
87AcetylationFRRGVMEKLQLGPEI
HHHHHHHHHCCCHHH
24.36-
87UbiquitinationFRRGVMEKLQLGPEI
HHHHHHHHHCCCHHH
24.36-
87SuccinylationFRRGVMEKLQLGPEI
HHHHHHHHHCCCHHH
24.36-
87SuccinylationFRRGVMEKLQLGPEI
HHHHHHHHHCCCHHH
24.36-
115PhosphorylationSGFGQSGSFCRLAGH
CCCCCCCCCHHHCCC
26.81-
126 (in isoform 2)Phosphorylation-8.16-
126 (in isoform 4)Phosphorylation-8.16-
126PhosphorylationLAGHDINYLALSGVL
HCCCCCHHHHHHHHH
8.1668751039
130 (in isoform 4)Phosphorylation-22.65-
130 (in isoform 2)Phosphorylation-22.65-
135UbiquitinationALSGVLSKIGRSGEN
HHHHHHHHHCCCCCC
45.0523000965
153 (in isoform 4)Phosphorylation-5.91-
153 (in isoform 2)Phosphorylation-5.91-
198PhosphorylationLSSFLWKTQKLSLWE
HHHHHHHHCCCCCEE
21.2529083192
202PhosphorylationLWKTQKLSLWEAPRG
HHHHCCCCCEECCCC
38.1729083192
268SuccinylationMDDWPEMKKKFADVF
CCCHHHHHHHHHHHH
51.67-
268SuccinylationMDDWPEMKKKFADVF
CCCHHHHHHHHHHHH
51.67-
324PhosphorylationTSEEQDVSPRPAPLL
CCCCCCCCCCCCCCC
24.3928857561
365PhosphorylationGFSREEIYQLNSDKI
CCCHHHHHCCCCCHH
15.38110760055
365 (in isoform 5)Phosphorylation-15.3827642862
371UbiquitinationIYQLNSDKIIESNKV
HHCCCCCHHHHCCCC
45.4629967540

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of AMACR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMACR_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AMACR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FKBP5_HUMANFKBP5physical
28514442
PSMG3_HUMANPSMG3physical
28514442
PSMG4_HUMANPSMG4physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMACR_HUMAN

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Related Literatures of Post-Translational Modification

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