Hmdb loader
Identification
HMDB Protein ID HMDBP09154
Secondary Accession Numbers
  • 14909
Name Serine/threonine-protein phosphatase PGAM5, mitochondrial
Synonyms
  1. Bcl-XL-binding protein v68
  2. Phosphoglycerate mutase family member 5
Gene Name PGAM5
Protein Type Enzyme
Biological Properties
General Function Involved in phosphoprotein phosphatase activity
Specific Function 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.
Pathways Not Available
Reactions
A phosphoprotein + Water → a protein + Phosphate details
GO Classification
Cellular Component
mitochondrial outer membrane
integral to membrane
Molecular Function
phosphoprotein phosphatase activity
Cellular Location
  1. Mitochondrion
  2. Membrane
  3. Mitochondrion outer membrane
  4. Single-pass membrane protein (Potential)
Gene Properties
Chromosome Location 12
Locus 12q24.33
SNPs PGAM5
Gene Sequence
>870 bp
ATGGCGTTCCGGCAGGCGCTGCAGCTGGCGGCCTGCGGGCTGGCCGGGGGCTCGGCCGCC
GTGCTCTTCTCGGCCGTGGCGGTAGGGAAGCCGCGCGCAGGCGGGGACGCGGAGCCACGC
CCGGCTGAGCCGCCGGCCTGGGCGGGGGGCGCGCGGCCGGGCCCCGGTGTCTGGGACCCC
AACTGGGACAGGCGAGAACCACTGTCTCTGATCAACGTGCGGAAGAGGAACGTGGAATCT
GGGGAAGAAGAGCTGGCGTCCAAGCTGGACCACTACAAAGCCAAGGCCACGCGGCACATC
TTCCTCATCAGGCATTCCCAGTACCACGTGGATGGCTCCCTGGAGAAGGACCGCACTCTG
ACCCCGCTGGGTCGGGAGCAGGCTGAACTCACTGGGCTCCGCCTGGCAAGCTTGGGGTTG
AAGTTTAATAAAATCGTCCATTCGTCTATGACGCGCGCCATAGAGACCACCGATATCATC
AGCCGGCACCTGCCAGGCGTCTGCAAAGTCAGCACAGATCTGCTGCGGGAAGGCGCCCCC
ATCGAGCCAGACCCGCCCGTGTCTCATTGGAAGCCGGAAGCTGTGCAGTATTACGAAGAC
GGAGCCCGGATCGAGGCCGCCTTCCGGAACTACATCCACCGCGCAGATGCCAGGCAGGAG
GAGGACAGTTACGAGATCTTCATCTGTCACGCCAACGTCATCCGCTACATCGTGTGCAGA
GCACTGCAGTTTCCTCCTGAAGGCTGGCTCCGGCTCTCCCTCAATAATGGCAGCATCACC
CACCTGGTGATCCGACCCAACGGCCGAGTTGCGCTCAGGACCCTCGGGGACACGGGGTTC
ATGCCTCCCGACAAGATCACTCGATCCTGA
Protein Properties
Number of Residues 289
Molecular Weight 32004.11
Theoretical pI 8.679
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Serine/threonine-protein phosphatase PGAM5, mitochondrial
MAFRQALQLAACGLAGGSAAVLFSAVAVGKPRAGGDAEPRPAEPPAWAGGARPGPGVWDP
NWDRREPLSLINVRKRNVESGEEELASKLDHYKAKATRHIFLIRHSQYHVDGSLEKDRTL
TPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDIISRHLPGVCKVSTDLLREGAP
IEPDPPVSHWKPEAVQYYEDGARIEAAFRNYIHRADARQEEDSYEIFICHANVIRYIVCR
ALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMPPDKITRS
GenBank ID Protein 281604136
UniProtKB/Swiss-Prot ID Q96HS1
UniProtKB/Swiss-Prot Entry Name PGAM5_HUMAN
PDB IDs
GenBank Gene ID NM_001170543.1
GeneCard ID PGAM5
GenAtlas ID PGAM5
HGNC ID HGNC:28763
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed:16541075 ]
  4. Lo SC, Hannink M: PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex. J Biol Chem. 2006 Dec 8;281(49):37893-903. Epub 2006 Oct 17. [PubMed:17046835 ]
  5. Takeda K, Komuro Y, Hayakawa T, Oguchi H, Ishida Y, Murakami S, Noguchi T, Kinoshita H, Sekine Y, Iemura S, Natsume T, Ichijo H: Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1. Proc Natl Acad Sci U S A. 2009 Jul 28;106(30):12301-5. doi: 10.1073/pnas.0901823106. Epub 2009 Jul 9. [PubMed:19590015 ]
  6. Hammond PW, Alpin J, Rise CE, Wright M, Kreider BL: In vitro selection and characterization of Bcl-X(L)-binding proteins from a mix of tissue-specific mRNA display libraries. J Biol Chem. 2001 Jun 15;276(24):20898-906. Epub 2001 Mar 30. [PubMed:11283018 ]
  7. Lo SC, Hannink M: PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria. Exp Cell Res. 2008 May 1;314(8):1789-803. doi: 10.1016/j.yexcr.2008.02.014. Epub 2008 Mar 5. [PubMed:18387606 ]