CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037755
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Cold shock domain-containing protein E1 
Protein Synonyms/Alias
  
Gene Name
 CSDE1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36NFVIDNNKHTGAVSAubiquitination[1, 2, 3]
50ARNIMLLKKKQARCQubiquitination[2, 4]
51RNIMLLKKKQARCQGubiquitination[5]
64QGVVCAMKEAFGFIEubiquitination[5]
77IERGDVVKEIFFHYSubiquitination[1]
109TIKDRNGKEVATDVRacetylation[3]
109TIKDRNGKEVATDVRubiquitination[2, 3, 5]
147VIPKVPSKNQNDPLPubiquitination[2, 3, 4, 5, 6, 7]
158DPLPGRIKVDFVIPKubiquitination[2, 3, 5]
165KVDFVIPKELPFGDKubiquitination[1]
177GDKDTKSKVTLLEGDubiquitination[2, 5]
234RDGFGFIKCVDRDVRacetylation[3]
234RDGFGFIKCVDRDVRubiquitination[3, 5, 8]
451VSAEKVNKTHSVNGIubiquitination[5]
470DPTIYSGKVIRPLRSubiquitination[5]
518NKGDCLQKGESVKFQacetylation[3]
518NKGDCLQKGESVKFQubiquitination[2, 5]
552RATVECVKDQFGFINacetylation[3]
552RATVECVKDQFGFINubiquitination[5]
566NYEVGDSKKLFFHVKubiquitination[2, 4]
567YEVGDSKKLFFHVKEubiquitination[5]
599ILNQRTGKCSACNVWubiquitination[3, 5, 7, 8, 9]
613WRVCEGPKAVAAPRPubiquitination[3, 5]
628DRLVNRLKNITLDDAubiquitination[1, 2, 3, 4, 5, 7, 8, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 668 AA 
Protein Sequence
MNGQEVFYLT YTPEDVEGNV QLETGDKINF VIDNNKHTGA VSARNIMLLK KKQARCQGVV 60
CAMKEAFGFI ERGDVVKEIF FHYSEFKGDL ETLQPGDDVE FTIKDRNGKE VATDVRLLPQ 120
GTVIFEDISI EHFEGTVTKV IPKVPSKNQN DPLPGRIKVD FVIPKELPFG DKDTKSKVTL 180
LEGDHVRFNI STDRRDKLER ATNIEVLSNT FQFTNEAREM GVIAAMRDGF GFIKCVDRDV 240
RMFFHFSEIL DGNQLHIADE VEFTVVPDML SAQRNHAIRI KKLPKGTVSF HSHSDHRFLG 300
TVEKEATFSN PKTTSPNKGK EKEAEDGIIA YDDCGVKLTI AFQAKDVEGS TSPQIGDKVE 360
FSISDKQRPG QQVATCVRLL GRNSNSKRLL GYVATLKDNF GFIETANHDK EIFFHYSEFS 420
GDVDSLELGD MVEYSLSKGK GNKVSAEKVN KTHSVNGITE EADPTIYSGK VIRPLRSVDP 480
TQTEYQGMIE IVEEGDMKGE VYPFGIVGMA NKGDCLQKGE SVKFQLCVLG QNAQTMAYNI 540
TPLRRATVEC VKDQFGFINY EVGDSKKLFF HVKEVQDGIE LQAGDEVEFS VILNQRTGKC 600
SACNVWRVCE GPKAVAAPRP DRLVNRLKNI TLDDASAPRL MVLRQPRGPD NSMGFGAERK 660
IRQAGVID 668 
Gene Ontology
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR019844; Cold-shock_CS.
 IPR011129; Cold_shock_prot.
 IPR002059; CSP_DNA-bd.
 IPR012340; NA-bd_OB-fold.
 IPR024642; SUZ-C. 
Pfam
 PF00313; CSD
 PF12901; SUZ-C 
SMART
 SM00357; CSP 
PROSITE
 PS00352; COLD_SHOCK 
PRINTS