CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002371
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glucose-6-phosphate isomerase 
Protein Synonyms/Alias
 GPI; Autocrine motility factor; AMF; Neuroleukin; NLK; Phosphoglucose isomerase; PGI; Phosphohexose isomerase; PHI 
Gene Name
 Gpi 
Gene Synonyms/Alias
 Gpi1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
12TRNPQFQKLLEWHRAubiquitination[1]
25RANSANLKLRELFEAacetylation[2]
25RANSANLKLRELFEAsuccinylation[2]
25RANSANLKLRELFEAubiquitination[1, 3]
73QMLVELAKSRGVEAAubiquitination[1]
89DNMFSGSKINYTENRacetylation[2]
89DNMFSGSKINYTENRsuccinylation[2]
89DNMFSGSKINYTENRubiquitination[1]
112NRSNTPIKVDGKDVMubiquitination[1]
116TPIKVDGKDVMPEVNacetylation[4]
116TPIKVDGKDVMPEVNubiquitination[1]
130NRVLDKMKSFCQRVRubiquitination[1]
142RVRSGDWKGYTGKSIacetylation[2, 5]
226ITNAETAKEWFLEAAubiquitination[1, 3]
234EWFLEAAKDPSAVAKubiquitination[1]
241KDPSAVAKHFVALSTubiquitination[1, 3]
252ALSTNTAKVKEFGIDubiquitination[1]
362GDMESNGKYITKSGAubiquitination[1]
423IRKGLHHKILLANFLacetylation[6]
438AQTEALMKGKLPEEAubiquitination[1]
447KLPEEARKELQAAGKubiquitination[1]
454KELQAAGKSPEDLEKacetylation[4]
466LEKLLPHKVFEGNRPubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. 
Sequence Annotation
 ACT_SITE 358 358 Proton donor.
 ACT_SITE 389 389
 ACT_SITE 519 519
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 12 12 N6-acetyllysine (By similarity).
 MOD_RES 109 109 Phosphothreonine (By similarity).
 MOD_RES 142 142 N6-acetyllysine (By similarity).
 MOD_RES 185 185 Phosphoserine; by CK2 (By similarity).
 MOD_RES 454 454 N6-malonyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; Angiogenesis; Complete proteome; Cytokine; Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis; Growth factor; Isomerase; Phosphoprotein; Reference proteome; Secreted; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 558 AA 
Protein Sequence
MAALTRNPQF QKLLEWHRAN SANLKLRELF EADPERFNNF SLNLNTNHGH ILVDYSKNLV 60
NKEVMQMLVE LAKSRGVEAA RDNMFSGSKI NYTENRAVLH VALRNRSNTP IKVDGKDVMP 120
EVNRVLDKMK SFCQRVRSGD WKGYTGKSIT DIINIGIGGS DLGPLMVTEA LKPYSKGGPR 180
VWFVSNIDGT HIAKTLASLS PETSLFIIAS KTFTTQETIT NAETAKEWFL EAAKDPSAVA 240
KHFVALSTNT AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DHFEQLLSGA 300
HWMDQHFLKT PLEKNAPVLL ALLGIWYINC YGCETHALLP YDQYMHRFAA YFQQGDMESN 360
GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL 420
HHKILLANFL AQTEALMKGK LPEEARKELQ AAGKSPEDLE KLLPHKVFEG NRPTNSIVFT 480
KLTPFILGAL IAMYEHKIFV QGIMWDINSF DQWGVELGKQ LAKKIEPELE GSSAVTSHDS 540
STNGLISFIK QQRDTKLE 558 
Gene Ontology
 GO:0060170; C:cilium membrane; IDA:MGI.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
 GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:MGI.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
 GO:0006006; P:glucose metabolic process; IC:MGI.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway. 
Interpro
 IPR001672; G6P_Isomerase.
 IPR023096; G6P_Isomerase_C.
 IPR018189; Phosphoglucose_isomerase_CS. 
Pfam
 PF00342; PGI 
SMART
  
PROSITE
 PS00765; P_GLUCOSE_ISOMERASE_1
 PS00174; P_GLUCOSE_ISOMERASE_2
 PS51463; P_GLUCOSE_ISOMERASE_3 
PRINTS
 PR00662; G6PISOMERASE.