CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014263
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Stress-induced-phosphoprotein 1 
Protein Synonyms/Alias
 STI1; mSTI1; Hsc70/Hsp90-organizing protein; Hop 
Gene Name
 Stip1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
10QVNELKEKGNKALSAacetylation[1]
13ELKEKGNKALSAGNIubiquitination[2]
68GCKTVDLKPDWGKGYacetylation[3]
68GCKTVDLKPDWGKGYubiquitination[2]
73DLKPDWGKGYSRKAAacetylation[3, 4]
78WGKGYSRKAAALEFLacetylation[5]
78WGKGYSRKAAALEFLsuccinylation[5]
100RTYEEGLKHEANNLQubiquitination[2]
109EANNLQLKEGLQNMEubiquitination[2]
123EARLAERKFMNPFNLubiquitination[2]
136NLPNLYQKLENDPRTubiquitination[2]
162LIEQLQNKPSDLGTKacetylation[4]
162LIEQLQNKPSDLGTKubiquitination[2]
169KPSDLGTKLQDPRVMubiquitination[2]
252LKHYDRAKELDPTNMubiquitination[2]
284KCRELCEKAIEVGREacetylation[3]
312RIGNSYFKEEKYKDAacetylation[3, 6]
317YFKEEKYKDAIHFYNacetylation[3]
317YFKEEKYKDAIHFYNubiquitination[2]
325DAIHFYNKSLAEHRTacetylation[3, 4, 5]
364PDLALEEKNKGNECFacetylation[4]
366LALEEKNKGNECFQKacetylation[5]
373KGNECFQKGDYPQAMacetylation[3]
373KGNECFQKGDYPQAMubiquitination[2]
381GDYPQAMKHYTEAIKacetylation[3]
429QLEPTFIKGYTRKAAacetylation[3, 4]
446EAMKDYTKAMDVYQKacetylation[3, 5]
446EAMKDYTKAMDVYQKsuccinylation[5]
453KAMDVYQKALDLDSSacetylation[3]
462LDLDSSCKEAADGYQubiquitination[2]
513LILEQMQKDPQALSEacetylation[3, 4]
513LILEQMQKDPQALSEubiquitination[2]
530KNPVIAQKIQKLMDVacetylation[3, 5]
533VIAQKIQKLMDVGLIacetylation[3]
Reference
 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [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] 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]
 [5] 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]
 [6] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379] 
Functional Description
 Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB). 
Sequence Annotation
 REPEAT 4 37 TPR 1.
 REPEAT 39 71 TPR 2.
 REPEAT 73 105 TPR 3.
 DOMAIN 130 169 STI1 1.
 REPEAT 225 258 TPR 4.
 REPEAT 260 292 TPR 5.
 REPEAT 300 333 TPR 6.
 REPEAT 360 393 TPR 7.
 REPEAT 395 427 TPR 8.
 REPEAT 428 461 TPR 9.
 DOMAIN 492 531 STI1 2.
 MOTIF 222 239 Bipartite nuclear localization signal
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 8 8 N6-acetyllysine (By similarity).
 MOD_RES 16 16 Phosphoserine (By similarity).
 MOD_RES 301 301 N6-acetyllysine (By similarity).
 MOD_RES 312 312 N6-acetyllysine (By similarity).
 MOD_RES 325 325 N6-acetyllysine (By similarity).
 MOD_RES 344 344 N6-acetyllysine (By similarity).
 MOD_RES 354 354 Phosphotyrosine (By similarity).
 MOD_RES 446 446 N6-acetyllysine (By similarity).
 MOD_RES 481 481 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 543 AA 
Protein Sequence
MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK KGDYQKAYED 60
GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNLQLKE GLQNMEARLA 120
ERKFMNPFNL PNLYQKLEND PRTRSLLSDP TYRELIEQLQ NKPSDLGTKL QDPRVMTTLS 180
VLLGVDLGSM DEEEEAATPP PPPPPKKEPK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD 240
FDKALKHYDR AKELDPTNMT YITNQAAVHF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA 300
KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA 360
LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PRDAKLYSNR AACYTKLLEF QLALKDCEEC 420
IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD 480
SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI 540
AIR 543 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IEA:Compara. 
Interpro
 IPR006636; STI1_HS-bd.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF00515; TPR_1
 PF13181; TPR_8 
SMART
 SM00727; STI1
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS