CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009659
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
 AAA37869.1; AAC52836.1; AAB18391.1; BAC29016.1; BAC36065.1; BAE26523.1; BAE27374.1; BAE27588.1; BAE28187.1; BAE29591.1; BAE29612.1; BAE29780.1; BAE29990.1; BAE30081.1; BAE30135.1; BAE30272.1; BAE30398.1; BAE30465.1; BAE30484.1; BAE30681.1; BAE30707.1; BAE30753.1; BAE30776.1; BAE30822.1; BAE30861.1; BAE31346.1; BAE31427.1; BAE31432.1; BAE31508.1; BAE31664.1; BAE32204.1; BAE35116.1; BAE37581.1; BAE38912.1; BAE38970.1; BAE39005.1; BAE39012.1; BAE39036.1; BAE39053.1; BAE39065.1; BAE39076.1; BAE39084.1; BAE39109.1; BAE39111.1; BAE39113.1; BAE39127.1; BAE39211.1; BAE39269.1; BAE39270.1; BAE39280.1; BAE39304.1; BAE39344.1; BAE39353.1; BAE39865.1; BAE39917.1; BAE40379.1; BAE40398.1; BAE40419.1; BAE40553.1; BAE40590.1; BAE40612.1; BAE40704.1; BAE40745.1; BAE40876.1; BAE40957.1; BAE41004.1; BAE41049.1; AAH06722.1; AAH66191.1; AAH85486.1; AAH89322.1; AAH89457.1; AAI06194.1; CAA38267.1; CAA38268.1; CAA38269.1 
Protein Name
 Heat shock cognate 71 kDa protein 
Protein Synonyms/Alias
 Heat shock 70 kDa protein 8 
Gene Name
 Hspa8 
Gene Synonyms/Alias
 Hsc70; Hsc73 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MSKGPAVGIDacetylation[1]
3*****MSKGPAVGIDubiquitination[2]
56RLIGDAAKNQVAMNPacetylation[1]
56RLIGDAAKNQVAMNPubiquitination[2]
71TNTVFDAKRLIGRRFubiquitination[2]
88AVVQSDMKHWPFMVVubiquitination[2]
108PKVQVEYKGETKSFYacetylation[1]
108PKVQVEYKGETKSFYubiquitination[2]
112VEYKGETKSFYPEEVacetylation[3]
112VEYKGETKSFYPEEVubiquitination[2]
126VSSMVLTKMKEIAEAacetylation[3]
126VSSMVLTKMKEIAEAubiquitination[2]
128SMVLTKMKEIAEAYLacetylation[3, 4]
128SMVLTKMKEIAEAYLsuccinylation[4]
128SMVLTKMKEIAEAYLubiquitination[2]
137IAEAYLGKTVTNAVVubiquitination[2]
159DSQRQATKDAGTIAGacetylation[4]
159DSQRQATKDAGTIAGsuccinylation[4]
159DSQRQATKDAGTIAGubiquitination[2]
187AIAYGLDKKVGAERNubiquitination[2]
188IAYGLDKKVGAERNVubiquitination[2]
246NHFIAEFKRKHKKDIacetylation[1, 3, 4, 5]
246NHFIAEFKRKHKKDIsuccinylation[4]
246NHFIAEFKRKHKKDIubiquitination[2]
257KKDISENKRAVRRLRubiquitination[2]
319GTLDPVEKALRDAKLacetylation[1, 3, 4, 5]
319GTLDPVEKALRDAKLsuccinylation[4]
319GTLDPVEKALRDAKLubiquitination[2]
325EKALRDAKLDKSQIHubiquitination[2]
328LRDAKLDKSQIHDIVacetylation[4]
328LRDAKLDKSQIHDIVsuccinylation[4]
328LRDAKLDKSQIHDIVubiquitination[2]
345GGSTRIPKIQKLLQDubiquitination[2]
348TRIPKIQKLLQDFFNubiquitination[2]
357LQDFFNGKELNKSINubiquitination[2]
361FNGKELNKSINPDEAacetylation[3]
361FNGKELNKSINPDEAubiquitination[2]
423RNTTIPTKQTQTFTTubiquitination[2]
451EGERAMTKDNNLLGKubiquitination[2]
458KDNNLLGKFELTGIPubiquitination[2]
497AVDKSTGKENKITITubiquitination[2]
500KSTGKENKITITNDKubiquitination[2]
507KITITNDKGRLSKEDubiquitination[2]
512NDKGRLSKEDIERMVacetylation[4]
512NDKGRLSKEDIERMVsuccinylation[4]
512NDKGRLSKEDIERMVubiquitination[2]
524RMVQEAEKYKAEDEKacetylation[3, 4]
524RMVQEAEKYKAEDEKubiquitination[2]
526VQEAEKYKAEDEKQRacetylation[1, 3]
526VQEAEKYKAEDEKQRubiquitination[2]
531KYKAEDEKQRDKVSSubiquitination[2]
539QRDKVSSKNSLESYAacetylation[4]
539QRDKVSSKNSLESYAsuccinylation[4]
539QRDKVSSKNSLESYAubiquitination[2]
550ESYAFNMKATVEDEKubiquitination[2]
573DKQKILDKCNEIISWacetylation[3]
573DKQKILDKCNEIISWubiquitination[2]
583EIISWLDKNQTAEKEubiquitination[2]
589DKNQTAEKEEFEHQQacetylation[1, 3]
589DKNQTAEKEEFEHQQubiquitination[2]
597EEFEHQQKELEKVCNacetylation[1, 3, 4, 6]
597EEFEHQQKELEKVCNubiquitination[2]
601HQQKELEKVCNPIITacetylation[1, 3, 4, 6, 7, 8]
601HQQKELEKVCNPIITubiquitination[2]
609VCNPIITKLYQSAGGubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] 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]
 [7] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [8] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 
Functional Description
 Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (By similarity). 
Sequence Annotation
 REGION 186 377 Interaction with BAG1 (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 15 15 Phosphotyrosine.
 MOD_RES 41 41 Phosphotyrosine.
 MOD_RES 153 153 Phosphoserine (By similarity).
 MOD_RES 246 246 N6-acetyllysine (By similarity).
 MOD_RES 319 319 N6-acetyllysine (By similarity).
 MOD_RES 362 362 Phosphoserine (By similarity).
 MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A; in
 MOD_RES 589 589 N6-acetyllysine (By similarity).
 MOD_RES 597 597 N6-acetyllysine (By similarity).
 MOD_RES 601 601 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; Spliceosome; Stress response; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 646 AA 
Protein Sequence
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 60
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS 120
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA 180
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH 240
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 300
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN 360
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI 420
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI 480
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN 540
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE 600
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD 646 
Gene Ontology
 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005829; C:cytosol; IDA:MGI.
 GO:0070062; C:extracellular vesicular exosome; IDA:MGI.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0000974; C:Prp19 complex; ISS:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
 GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042623; F:ATPase activity, coupled; IDA:MGI.
 GO:0051085; P:chaperone mediated protein folding requiring cofactor; IGI:MGI.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0051726; P:regulation of cell cycle; IDA:MGI.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 
Pfam
 PF00012; HSP70 
SMART
  
PROSITE
 PS00297; HSP70_1
 PS00329; HSP70_2
 PS01036; HSP70_3 
PRINTS
 PR00301; HEATSHOCK70.