| Tag | Content |
|---|
| CPLM ID | CPLM-001220 |
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 |
|---|
| 149 | ARNIMLLKKKQARCQ | ubiquitination | [1] | | 246 | VIPKVPSKNQNDPLP | ubiquitination | [1] | | 665 | NYEVGDSKKLFFHVK | ubiquitination | [1] | | 727 | DRLVNRLKNITLDDA | ubiquitination | [1] |
|
Reference | [1] 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] |
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 NGQEVFYLTY TPEDVEGNVQ 120
LETGDKINFV IDNNKHTGAV SARNIMLLKK KQARCQGVVC AMKEAFGFIE RGDVVKEIFF 180
HYSEFKGDLE TLQPGDDVEF TIKDRNGKEV ATDVRLLPQG TVIFEDISIE HFEGTVTKVI 240
PKVPSKNQND PLPGRIKVDF VIPKELPFGD KDTKSKVTLL EGDHVRFNIS TDRRDKLERA 300
TNIEVLSNTF QFTNEAREMG VIAAMRDGFG FIKCVDRDVR MFFHFSEILD GNQLHIADEV 360
EFTVVPDMLS AQRNHAIRIK KLPKGTVSFH SHSDHRFLGT VEKEATFSNP KTTSPNKGKE 420
KEAEDGIIAY DDCGVKLTIA FQAKDVEGST SPQIGDKVEF SISDKQRPGQ QVATCVRLLG 480
RNSNSKRLLG YVATLKDNFG FIETANHDKE IFFHYSEFSG DVDSLELGDM VEYSLSKGKG 540
NKVSAEKVNK THSVNGITEE ADPTIYSGKV IRPLRSVDPT QTEYQGMIEI VEEGDMKGEV 600
YPFGIVGMAN KGDCLQKGES VKFQLCVLGQ NAQTMAYNIT PLRRATVECV KDQFGFINYE 660
VGDSKKLFFH VKEVQDGIEL QAGDEVEFSV ILNQRTGKCS ACNVWRVCEG PKAVAAPRPD 720
RLVNRLKNIT LDDASAPRLM VLRQPRGPDN SMGFGAERKI RQAGVID 767 |
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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |