CPLM 1.0 - Compendium of Protein Lysine ModificationTag | Content |
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CPLM ID | CPLM-029381 | UniProt Accession | | Genbank Protein ID | | Genbank Nucleotide ID | | Protein Name | Heat shock cognate 71 kDa protein | Protein Synonyms/Alias | cDNA FLJ77848 | Gene Name | HSPA8 | Gene Synonyms/Alias | | Created Date | July 27, 2013 | Organism | Homo sapiens (Human) | NCBI Taxa ID | 9606 | Lysine Modification | Position | Peptide | Type | References |
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10 | NHFIAEFKRKHKKDI | acetylation | [1, 2] | 10 | NHFIAEFKRKHKKDI | ubiquitination | [3, 4, 5, 6, 7, 8] | 12 | FIAEFKRKHKKDISE | ubiquitination | [6] | 15 | EFKRKHKKDISENKR | ubiquitination | [9] | 21 | KKDISENKRAVRRLR | acetylation | [8] | 21 | KKDISENKRAVRRLR | ubiquitination | [3, 5, 9, 10] | 83 | GTLDPVEKALRDAKL | acetylation | [1, 2, 8] | 83 | GTLDPVEKALRDAKL | ubiquitination | [3, 4, 5, 6, 7, 8, 9] | 89 | EKALRDAKLDKSQIH | ubiquitination | [5, 6, 7, 8, 9, 11] | 92 | LRDAKLDKSQIHDIV | acetylation | [8] | 92 | LRDAKLDKSQIHDIV | ubiquitination | [3, 5, 6, 7, 8, 9] | 109 | GGSTRIPKIQKLLQD | ubiquitination | [6, 7, 10] | 112 | TRIPKIQKLLQDFFN | acetylation | [1, 2, 8] | 112 | TRIPKIQKLLQDFFN | ubiquitination | [3, 5, 6, 7, 8, 9, 10] | 121 | LQDFFNGKELNKSIN | acetylation | [2, 8] | 121 | LQDFFNGKELNKSIN | ubiquitination | [3, 5, 6, 7, 9] | 125 | FNGKELNKSINPDEA | ubiquitination | [3, 4, 6, 7, 9] | 187 | RNTTIPTKQTQTFTT | ubiquitination | [3, 4, 6, 7, 8, 9, 10] | 215 | EGERAMTKDNNLLGK | acetylation | [1, 8] | 215 | EGERAMTKDNNLLGK | ubiquitination | [3, 4, 6, 7, 8, 9, 10] | 222 | KDNNLLGKFELTGIP | ubiquitination | [3, 7, 8, 9] | 261 | AVDKSTGKENKITIT | ubiquitination | [6, 7, 8, 10] | 264 | KSTGKENKITITNDK | ubiquitination | [6, 7, 8, 9, 10] | 271 | KITITNDKGRLSKED | acetylation | [1, 2, 8] | 271 | KITITNDKGRLSKED | ubiquitination | [3, 4, 5, 6, 7, 8, 9, 10, 11, 12] | 276 | NDKGRLSKEDIERMV | acetylation | [1, 2, 8] | 276 | NDKGRLSKEDIERMV | ubiquitination | [3, 4, 5, 6, 7, 8, 9, 10, 11] | 288 | RMVQEAEKYKAEDEK | acetylation | [1, 8] | 288 | RMVQEAEKYKAEDEK | ubiquitination | [3, 4, 5, 6, 7, 8, 9, 10, 11, 12] | 290 | VQEAEKYKAEDEKQR | ubiquitination | [7, 8, 9, 10] | 295 | KYKAEDEKQRDKVSS | acetylation | [8] | 295 | KYKAEDEKQRDKVSS | ubiquitination | [5, 7, 9, 10] | 299 | EDEKQRDKVSSKNSL | ubiquitination | [5, 10] | 303 | QRDKVSSKNSLESYA | ubiquitination | [3, 6, 7, 8, 9, 10] | 314 | ESYAFNMKATVEDEK | ubiquitination | [4, 7, 9] | 321 | KATVEDEKLQGKIND | acetylation | [13] | 321 | KATVEDEKLQGKIND | methylation | [14] | 321 | KATVEDEKLQGKIND | ubiquitination | [6, 7, 8, 9, 10] | 325 | EDEKLQGKINDEDKQ | acetylation | [13] | 325 | EDEKLQGKINDEDKQ | methylation | [14] | 325 | EDEKLQGKINDEDKQ | ubiquitination | [9] | 331 | GKINDEDKQKILDKC | acetylation | [13] | 331 | GKINDEDKQKILDKC | methylation | [14] | 333 | INDEDKQKILDKCNE | acetylation | [13] | 333 | INDEDKQKILDKCNE | methylation | [14] | 337 | DKQKILDKCNEIINW | ubiquitination | [6, 8, 9] | 347 | EIINWLDKNQTAEKE | acetylation | [8] | 347 | EIINWLDKNQTAEKE | ubiquitination | [3, 5, 6, 7, 8, 9, 10] | 353 | DKNQTAEKEEFEHQQ | acetylation | [2, 8] | 353 | DKNQTAEKEEFEHQQ | ubiquitination | [7, 8, 9, 10] | 361 | EEFEHQQKELEKVCN | acetylation | [1, 8] | 361 | EEFEHQQKELEKVCN | ubiquitination | [3, 4, 6, 7, 8, 9, 10] | 365 | HQQKELEKVCNPIIT | acetylation | [1, 2, 8] | 365 | HQQKELEKVCNPIIT | ubiquitination | [3, 4, 6, 7, 8, 9, 10] | 373 | VCNPIITKLYQSAGG | ubiquitination | [7, 8, 10] |
| Reference | [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response. Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C. Mol Cell. 2012 Apr 27;46(2):212-25. [ PMID: 22424773] [2] 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] [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [ PMID: 21890473] [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin. Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI. J Proteome Res. 2012 Feb 3;11(2):796-807. [ PMID: 22053931] [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA. Mol Cell Proteomics. 2012 May;11(5):148-59. [ PMID: 22505724] [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Nature. 2013 Apr 18;496(7445):372-6. [ PMID: 23503661] [8] Integrated proteomic analysis of post-translational modifications by serial enrichment. Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA. Nat Methods. 2013 Jul;10(7):634-7. [ PMID: 23749302] [9] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] [10] Global identification of modular cullin-RING ligase substrates. Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ. Cell. 2011 Oct 14;147(2):459-74. [ PMID: 21963094] [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML. Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [ PMID: 21139048] [12] A data set of human endogenous protein ubiquitination sites. Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J. Mol Cell Proteomics. 2011 May;10(5):M110.002089. [ PMID: 20972266] [13] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis. Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A. Anal Chem. 2011 May 15;83(10):3623-6. [ PMID: 21466224] [14] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome. Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T. Mol Biosyst. 2013 Jul 30;9(9):2231-47. [ PMID: 23748837] | Functional Description | | Sequence Annotation | | Keyword | ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome. | Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL | Protein Length | 410 AA | Protein Sequence | MVNHFIAEFK RKHKKDISEN KRAVRRLRTA CERAKRTLSS STQASIEIDS LYEGIDFYTS 60 ITRARFEELN ADLFRGTLDP VEKALRDAKL DKSQIHDIVL VGGSTRIPKI QKLLQDFFNG 120 KELNKSINPD EAVAYGAAVQ AAILSGDKSE NVQDLLLLDV TPLSLGIETA GGVMTVLIKR 180 NTTIPTKQTQ TFTTYSDNQP GVLIQVYEGE RAMTKDNNLL GKFELTGIPP APRGVPQIEV 240 TFDIDANGIL NVSAVDKSTG KENKITITND KGRLSKEDIE RMVQEAEKYK AEDEKQRDKV 300 SSKNSLESYA FNMKATVEDE KLQGKINDED KQKILDKCNE IINWLDKNQT AEKEEFEHQQ 360 KELEKVCNPI ITKLYQSAGG MPGGMPGGFP GGGAPPSGGA SSGPTIEEVD 410 | Gene Ontology | GO:0005829; C:cytosol; IEA:Compara. GO:0070062; C:extracellular vesicular exosome; IEA:Compara. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0042623; F:ATPase activity, coupled; IEA:Compara. GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Compara. GO:0051726; P:regulation of cell cycle; IEA:Compara. | Interpro | | Pfam | | SMART | | PROSITE | | PRINTS | |
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