PGAM5_HUMAN - dbPTM
PGAM5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGAM5_HUMAN
UniProt AC Q96HS1
Protein Name Serine/threonine-protein phosphatase PGAM5, mitochondrial
Gene Name PGAM5
Organism Homo sapiens (Human).
Sequence Length 289
Subcellular Localization Mitochondrion outer membrane
Single-pass membrane protein . Isoform 2 overexpression results in the formation of disconnected punctuate mitochondria distributed throughout the cytoplasm. Isoform 1 overexpression results in the clustering of mitocho
Protein Description Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore..
Protein Sequence MAFRQALQLAACGLAGGSAAVLFSAVAVGKPRAGGDAEPRPAEPPAWAGGARPGPGVWDPNWDRREPLSLINVRKRNVESGEEELASKLDHYKAKATRHIFLIRHSQYHVDGSLEKDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDIISRHLPGVCKVSTDLLREGAPIEPDPPVSHWKPEAVQYYEDGARIEAAFRNYIHRADARQEEDSYEIFICHANVIRYIVCRALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMPPDKITRS
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
75AcetylationLSLINVRKRNVESGE
CCCEEEHHHCCCCCH		44.0020167786
75UbiquitinationLSLINVRKRNVESGE
CCCEEEHHHCCCCCH		44.00-
80PhosphorylationVRKRNVESGEEELAS
EHHHCCCCCHHHHHH		47.4223401153
87PhosphorylationSGEEELASKLDHYKA
CCHHHHHHHHHHHHH		46.5030266825
88 (in isoform 2)Ubiquitination-52.9421890473
88UbiquitinationGEEELASKLDHYKAK
CHHHHHHHHHHHHHH		52.9421890473
88UbiquitinationGEEELASKLDHYKAK
CHHHHHHHHHHHHHH		52.9423000965
882-HydroxyisobutyrylationGEEELASKLDHYKAK
CHHHHHHHHHHHHHH		52.94-
88AcetylationGEEELASKLDHYKAK
CHHHHHHHHHHHHHH		52.9423954790
88 (in isoform 1)Ubiquitination-52.9421890473
88MalonylationGEEELASKLDHYKAK
CHHHHHHHHHHHHHH		52.9426320211
88UbiquitinationGEEELASKLDHYKAK
CHHHHHHHHHHHHHH		52.9421890473
92PhosphorylationLASKLDHYKAKATRH
HHHHHHHHHHHHHEE		16.5930266825
93UbiquitinationASKLDHYKAKATRHI
HHHHHHHHHHHHEEE		39.7423000965
93AcetylationASKLDHYKAKATRHI
HHHHHHHHHHHHEEE		39.7423749302
932-HydroxyisobutyrylationASKLDHYKAKATRHI
HHHHHHHHHHHHEEE		39.74-
106PhosphorylationHIFLIRHSQYHVDGS
EEEEEECCEEECCCC		23.6820860994
108PhosphorylationFLIRHSQYHVDGSLE
EEEECCEEECCCCCC		13.5620860994
113PhosphorylationSQYHVDGSLEKDRTL
CEEECCCCCCCCCCC		28.9729214152
116UbiquitinationHVDGSLEKDRTLTPL
ECCCCCCCCCCCCCC		58.7822505724
116AcetylationHVDGSLEKDRTLTPL
ECCCCCCCCCCCCCC		58.7819608861
1162-HydroxyisobutyrylationHVDGSLEKDRTLTPL
ECCCCCCCCCCCCCC		58.78-
131PhosphorylationGREQAELTGLRLASL
CHHHHHHHCHHHHHH		26.1920068231
141UbiquitinationRLASLGLKFNKIVHS
HHHHHCCCHHHHHHH		45.1323000965
141 (in isoform 1)Ubiquitination-45.1321890473
141UbiquitinationRLASLGLKFNKIVHS
HHHHHCCCHHHHHHH		45.1321890473
141UbiquitinationRLASLGLKFNKIVHS
HHHHHCCCHHHHHHH		45.1321890473
141NeddylationRLASLGLKFNKIVHS
HHHHHCCCHHHHHHH		45.1332015554
1412-HydroxyisobutyrylationRLASLGLKFNKIVHS
HHHHHCCCHHHHHHH		45.13-
141AcetylationRLASLGLKFNKIVHS
HHHHHCCCHHHHHHH		45.1325825284
141 (in isoform 2)Ubiquitination-45.1321890473
144MalonylationSLGLKFNKIVHSSMT
HHCCCHHHHHHHHHC		49.6032601280
144UbiquitinationSLGLKFNKIVHSSMT
HHCCCHHHHHHHHHC		49.6023000965
144AcetylationSLGLKFNKIVHSSMT
HHCCCHHHHHHHHHC		49.6019608861
148PhosphorylationKFNKIVHSSMTRAIE
CHHHHHHHHHCHHHH		15.7730001349
149PhosphorylationFNKIVHSSMTRAIET
HHHHHHHHHCHHHHH		14.8630001349
151PhosphorylationKIVHSSMTRAIETTD
HHHHHHHCHHHHHHH		20.9230001349
156PhosphorylationSMTRAIETTDIISRH
HHCHHHHHHHHHHHH		24.5327251275
157PhosphorylationMTRAIETTDIISRHL
HCHHHHHHHHHHHHC		16.6527251275
161PhosphorylationIETTDIISRHLPGVC
HHHHHHHHHHCCCCE		17.6227251275
168S-palmitoylationSRHLPGVCKVSTDLL
HHHCCCCEEECHHHH		4.4621044946
169 (in isoform 1)Ubiquitination-36.4921890473
169 (in isoform 2)Ubiquitination-36.4921890473
169UbiquitinationRHLPGVCKVSTDLLR
HHCCCCEEECHHHHH		36.4922817900
169AcetylationRHLPGVCKVSTDLLR
HHCCCCEEECHHHHH		36.4925953088
171PhosphorylationLPGVCKVSTDLLREG
CCCCEEECHHHHHCC		11.1623312004
172PhosphorylationPGVCKVSTDLLREGA
CCCEEECHHHHHCCC		33.3823312004
188PhosphorylationIEPDPPVSHWKPEAV
CCCCCCCCCCCHHHH		29.4230108239
191UbiquitinationDPPVSHWKPEAVQYY
CCCCCCCCHHHHHHH		27.7919608861
191AcetylationDPPVSHWKPEAVQYY
CCCCCCCCHHHHHHH		27.7919608861
197PhosphorylationWKPEAVQYYEDGARI
CCHHHHHHHHCCHHH		11.3930108239
198PhosphorylationKPEAVQYYEDGARIE
CHHHHHHHHCCHHHH		7.1730108239
253PhosphorylationPEGWLRLSLNNGSIT
CCCEEEEEECCCCEE		23.7129523821
258PhosphorylationRLSLNNGSITHLVIR
EEEECCCCEEEEEEC		26.8329523821
284UbiquitinationDTGFMPPDKITRS--
CCCCCCCHHCCCC--		49.4724816145
285UbiquitinationTGFMPPDKITRS---
CCCCCCHHCCCC---		52.3224816145
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
-KUbiquitinationE3 ubiquitin ligaseXIAPP98170
PMID:23201124
-KUbiquitinationE3 ubiquitin ligaseBIRC2Q13490
PMID:23201124
-KUbiquitinationE3 ubiquitin ligaseKEAP1Q14145
PMID:17046835
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGAM5_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 PGAM5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SETB1_HUMANSETDB1physical
16169070
ZBT16_HUMANZBTB16physical
16169070
KEAP1_HUMANKEAP1physical
17046835
B2CL1_HUMANBCL2L1physical
17046835
CUL3_HUMANCUL3physical
17046835
RBX1_HUMANRBX1physical
17046835
PINK1_HUMANPINK1physical
21151955
KEAP1_HUMANKEAP1physical
18387606
BIRC2_HUMANBIRC2physical
23201124
XIAP_HUMANXIAPphysical
23201124
PGAM5_HUMANPGAM5physical
27218139
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGAM5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-144 AND LYS-191,AND MASS SPECTROMETRY.

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