CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001219
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cold shock domain-containing protein E1 
Protein Synonyms/Alias
 N-ras upstream gene protein; Protein UNR 
Gene Name
 CSDE1 
Gene Synonyms/Alias
 D1S155E; KIAA0885; NRU; UNR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
81SSDRRTGKPIAVKLVacetylation[1]
81SSDRRTGKPIAVKLVubiquitination[2]
91AVKLVKIKQEILPEEubiquitination[2]
166NFVIDNNKHTGAVSAubiquitination[2]
180ARNIMLLKKKQARCQubiquitination[2]
181RNIMLLKKKQARCQGubiquitination[3, 4]
207IERGDVVKEIFFHYSubiquitination[3]
239TIKDRNGKEVATDVRubiquitination[2]
277VIPKVPSKNQNDPLPubiquitination[2, 5]
288DPLPGRIKVDFVIPKubiquitination[2]
295KVDFVIPKELPFGDKubiquitination[3]
307GDKDTKSKVTLLEGDubiquitination[2]
648NKGDCLQKGESVKFQubiquitination[2]
696NYEVGDSKKLFFHVKubiquitination[2]
758DRLVNRLKNITLDDAubiquitination[2, 3]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] 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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [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] 
Functional Description
 RNA-binding protein. Required for internal initiation of translation of human rhinovirus RNA. May be involved in translationally coupled mRNA turnover. Implicated with other RNA- binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding- region determinant of instability (mCRD) domain. 
Sequence Annotation
 DOMAIN 26 87 CSD 1.
 DOMAIN 136 179 CSD 2; truncated.
 DOMAIN 186 245 CSD 3.
 DOMAIN 297 337 CSD 4; truncated.
 DOMAIN 349 410 CSD 5.
 DOMAIN 447 507 CSD 6.
 DOMAIN 519 579 CSD 7.
 DOMAIN 610 670 CSD 8.
 DOMAIN 674 735 CSD 9.
 MOD_RES 81 81 N6-acetyllysine.
 MOD_RES 123 123 Phosphoserine.
 MOD_RES 514 514 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 798 AA 
Protein Sequence
MSFDPNLLHN NGHNGYPNGT SAALRETGVI EKLLTSYGFI QCSERQARLF FHCSQYNGNL 60
QDLKVGDDVE FEVSSDRRTG KPIAVKLVKI KQEILPEERM NGQVVCAVPH NLESKSPAAP 120
GQSPTGSVCY ERNGEVFYLT YTPEDVEGNV QLETGDKINF VIDNNKHTGA VSARNIMLLK 180
KKQARCQGVV CAMKEAFGFI ERGDVVKEIF FHYSEFKGDL ETLQPGDDVE FTIKDRNGKE 240
VATDVRLLPQ GTVIFEDISI EHFEGTVTKV IPKVPSKNQN DPLPGRIKVD FVIPKELPFG 300
DKDTKSKVTL LEGDHVRFNI STDRRDKLER ATNIEVLSNT FQFTNEAREM GVIAAMRDGF 360
GFIKCVDRDV RMFFHFSEIL DGNQLHIADE VEFTVVPDML SAQRNHAIRI KKLPKGTVSF 420
HSHSDHRFLG TVEKEATFSN PKTTSPNKGK EKEAEDGIIA YDDCGVKLTI AFQAKDVEGS 480
TSPQIGDKVE FSISDKQRPG QQVATCVRLL GRNSNSKRLL GYVATLKDNF GFIETANHDK 540
EIFFHYSEFS GDVDSLELGD MVEYSLSKGK GNKVSAEKVN KTHSVNGITE EADPTIYSGK 600
VIRPLRSVDP TQTEYQGMIE IVEEGDMKGE VYPFGIVGMA NKGDCLQKGE SVKFQLCVLG 660
QNAQTMAYNI TPLRRATVEC VKDQFGFINY EVGDSKKLFF HVKEVQDGIE LQAGDEVEFS 720
VILNQRTGKC SACNVWRVCE GPKAVAAPRP DRLVNRLKNI TLDDASAPRL MVLRQPRGPD 780
NSMGFGAERK IRQAGVID 798 
Gene Ontology
 GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008584; P:male gonad development; TAS:ProtInc.
 GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IMP:UniProtKB.
 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