PTPM1_HUMAN - dbPTM
PTPM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPM1_HUMAN
UniProt AC Q8WUK0
Protein Name Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1
Gene Name PTPMT1
Organism Homo sapiens (Human).
Sequence Length 201
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Matrix side .
Protein Description Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG) (By similarity). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle (By similarity). Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production (By similarity). Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues (By similarity). Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity). May prevent intrinsic apoptosis, probably by regulating mitochondrial membrane integrity. [PubMed: 24709986]
Protein Sequence MAATALLEAGLARVLFYPTLLYTLFRGKVPGRAHRDWYHRIDPTVLLGALPLRSLTRQLVQDENVRGVITMNEEYETRFLCNSSQEWKRLGVEQLRLSTVDMTGIPTLDNLQKGVQFALKYQSLGQCVYVHCKAGRSRSATMVAAYLIQVHKWSPEEAVRAIAKIRSYIHIRPGQLDVLKEFHKQITARATKDGTFVISKT
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
22PhosphorylationLFYPTLLYTLFRGKV
HHHHHHHHHHHCCCC
12.4324719451
23PhosphorylationFYPTLLYTLFRGKVP
HHHHHHHHHHCCCCC
21.2724719451
38PhosphorylationGRAHRDWYHRIDPTV
CCCCCCHHHCCCHHH
5.8724719451
75PhosphorylationVITMNEEYETRFLCN
EEECCHHHCEEEECC
19.20-
88 (in isoform 3)Phosphorylation-36.67-
88AcetylationCNSSQEWKRLGVEQL
CCCCHHHHHHCCCEE
36.6726051181
88SuccinylationCNSSQEWKRLGVEQL
CCCCHHHHHHCCCEE
36.6727452117
93 (in isoform 3)Phosphorylation-41.94-
164UbiquitinationEAVRAIAKIRSYIHI
HHHHHHHHHHHHHEE
32.32-
180UbiquitinationPGQLDVLKEFHKQIT
CCCHHHHHHHHHHHH
59.1721963094
184UbiquitinationDVLKEFHKQITARAT
HHHHHHHHHHHHEEC
49.0322817900
192UbiquitinationQITARATKDGTFVIS
HHHHEECCCCCEEEE
53.8529967540

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 PTPM1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPM1_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 PTPM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1C40_HUMANKRT40physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
MDFI_HUMANMDFIphysical
21516116
RGS20_HUMANRGS20physical
21516116
PTPM1_HUMANPTPMT1physical
27499296
CLPB_HUMANCLPBphysical
27499296
CLPX_HUMANCLPXphysical
27499296
STML2_HUMANSTOML2physical
27499296
TIM44_HUMANTIMM44physical
27499296
AFG32_HUMANAFG3L2physical
27499296
CHCH2_HUMANCHCHD2physical
27499296
GLSK_HUMANGLSphysical
27499296
OXA1L_HUMANOXA1Lphysical
27499296
MIC60_HUMANIMMTphysical
27499296
USMG5_HUMANUSMG5physical
27499296
PAK5_HUMANPAK7physical
27499296
ATP5H_HUMANATP5Hphysical
27499296
TXTP_HUMANSLC25A1physical
27499296
MOT1_HUMANSLC16A1physical
27499296
CYC_HUMANCYCSphysical
27499296
SNP29_HUMANSNAP29physical
27499296
ATPO_HUMANATP5Ophysical
27499296
ATP5E_HUMANATP5Ephysical
27499296
TIM50_HUMANTIMM50physical
27499296
COQ5_HUMANCOQ5physical
27499296
CISD1_HUMANCISD1physical
27499296
NDUS3_HUMANNDUFS3physical
27499296
QCR7_HUMANUQCRBphysical
27499296
AT5F1_HUMANATP5F1physical
27499296
PDIP2_HUMANPOLDIP2physical
27499296
ATD3A_HUMANATAD3Aphysical
27499296
CX7A2_HUMANCOX7A2physical
27499296
NDUF2_HUMANNDUFAF2physical
27499296
UCRI_HUMANUQCRFS1physical
27499296
ECH1_HUMANECH1physical
27499296
MPPB_HUMANPMPCBphysical
27499296
CT024_HUMANC20orf24physical
27499296
ACSL4_HUMANACSL4physical
27499296
SCOT1_HUMANOXCT1physical
27499296
SFXN1_HUMANSFXN1physical
27499296
ATPG_HUMANATP5C1physical
27499296
COQ9_HUMANCOQ9physical
27499296
LETM1_HUMANLETM1physical
27499296
COQ7_HUMANCOQ7physical
27499296
HINT3_HUMANHINT3physical
27499296
ATP5J_HUMANATP5Jphysical
27499296
C1QBP_HUMANC1QBPphysical
27499296
CPT2_HUMANCPT2physical
27499296
NDUA8_HUMANNDUFA8physical
27499296
QCR2_HUMANUQCRC2physical
27499296
COX5A_HUMANCOX5Aphysical
27499296
NIPS1_HUMANNIPSNAP1physical
27499296
MTCH2_HUMANMTCH2physical
27499296
TIM16_HUMANPAM16physical
27499296
MPCP_HUMANSLC25A3physical
27499296
AT2A2_HUMANATP2A2physical
27880917
FKBP8_HUMANFKBP8physical
27880917
IPO9_HUMANIPO9physical
27880917
NU133_HUMANNUP133physical
27880917
XPO4_HUMANXPO4physical
27880917

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTPM1_HUMAN

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Related Literatures of Post-Translational Modification

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