PM34_HUMAN - dbPTM
PM34_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PM34_HUMAN
UniProt AC O43808
Protein Name Peroxisomal membrane protein PMP34
Gene Name SLC25A17
Organism Homo sapiens (Human).
Sequence Length 307
Subcellular Localization Cytoplasm. Peroxisome membrane
Multi-pass membrane protein.
Protein Description Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extent for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal matrix by a counter-exchange mechanism. Inhibited by pyridoxal 5'-phosphate and bathophenanthroline in vitro..
Protein Sequence MASVLSYESLVHAVAGAVGSVTAMTVFFPLDTARLRLQVDEKRKSKTTHMVLLEIIKEEGLLAPYRGWFPVISSLCCSNFVYFYTFNSLKALWVKGQHSTTGKDLVVGFVAGVVNVLLTTPLWVVNTRLKLQGAKFRNEDIVPTNYKGIIDAFHQIIRDEGISALWNGTFPSLLLVFNPAIQFMFYEGLKRQLLKKRMKLSSLDVFIIGAVAKAIATTVTYPLQTVQSILRFGRHRLNPENRTLGSLRNILYLLHQRVRRFGIMGLYKGLEAKLLQTVLTAALMFLVYEKLTAATFTVMGLKRAHQH
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
20PhosphorylationAVAGAVGSVTAMTVF
HHHHHHCCEEEEEEE
15.0824719451
42UbiquitinationLRLQVDEKRKSKTTH
HHEEECHHHCCCCCE
61.74-
95UbiquitinationSLKALWVKGQHSTTG
CEEEEEECCCCCCCC
41.07-
99PhosphorylationLWVKGQHSTTGKDLV
EEECCCCCCCCCHHH
21.56-
100PhosphorylationWVKGQHSTTGKDLVV
EECCCCCCCCCHHHH
37.13-
101PhosphorylationVKGQHSTTGKDLVVG
ECCCCCCCCCHHHHH
45.29-
127PhosphorylationTPLWVVNTRLKLQGA
CCHHHHHHHHHCCCC
26.26-
130AcetylationWVVNTRLKLQGAKFR
HHHHHHHHCCCCCCC
35.1625953088
130UbiquitinationWVVNTRLKLQGAKFR
HHHHHHHHCCCCCCC
35.16-
135UbiquitinationRLKLQGAKFRNEDIV
HHHCCCCCCCCCCCC
52.24-
147UbiquitinationDIVPTNYKGIIDAFH
CCCCCCCHHHHHHHH
45.78-
228PhosphorylationYPLQTVQSILRFGRH
CCHHHHHHHHHHCCC
21.1824719451
246PhosphorylationPENRTLGSLRNILYL
CCCCHHHHHHHHHHH
27.5424719451
268UbiquitinationFGIMGLYKGLEAKLL
HCCCHHHHHHHHHHH
63.1621890473
292PhosphorylationFLVYEKLTAATFTVM
HHHHHHHHHHHHHHH
25.8825072903
295PhosphorylationYEKLTAATFTVMGLK
HHHHHHHHHHHHHHH
19.8525072903
297PhosphorylationKLTAATFTVMGLKRA
HHHHHHHHHHHHHHH
12.7725072903

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 PM34_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PM34_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 PM34_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
QCR7_HUMANUQCRBphysical
22939629
SAM50_HUMANSAMM50physical
22939629

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PM34_HUMAN

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Related Literatures of Post-Translational Modification

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