Search Results

Overview

Uniprot IDO75534
Protein NameCold shock domain-containing protein E1
Gene NameCSDE1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
166 NFVIDNNKHTGAVSA
277 VIPKVPSKNQNDPLP
758 DRLVNRLKNITLDDA
91 AVKLVKIKQEILPEE

Function

RNA-binding protein involved in translationally coupled mRNA turnover (PubMed:11051545, PubMed:15314026). 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 (PubMed:11051545, PubMed:15314026). Required for efficient formation of stress granules (PubMed:29395067)

Protein Sequence

10 MSFDPNLLHN 20 NGHNGYPNGT 30 SAALRETGVI 40 EKLLTSYGFI 50 QCSERQARLF 60 FHCSQYNGNL 70 QDLKVGDDVE 80 FEVSSDRRTG 90 KPIAVKLVKI 100 KQEILPEERM 110 NGQVVCAVPH 120 NLESKSPAAP 130 GQSPTGSVCY 140 ERNGEVFYLT 150 YTPEDVEGNV 160 QLETGDKINF 170 VIDNNKHTGA 180 VSARNIMLLK 190 KKQARCQGVV 200 CAMKEAFGFI 210 ERGDVVKEIF 220 FHYSEFKGDL 230 ETLQPGDDVE 240 FTIKDRNGKE 250 VATDVRLLPQ 260 GTVIFEDISI 270 EHFEGTVTKV 280 IPKVPSKNQN 290 DPLPGRIKVD 300 FVIPKELPFG 310 DKDTKSKVTL 320 LEGDHVRFNI 330 STDRRDKLER 340 ATNIEVLSNT 350 FQFTNEAREM 360 GVIAAMRDGF 370 GFIKCVDRDV 380 RMFFHFSEIL 390 DGNQLHIADE 400 VEFTVVPDML 410 SAQRNHAIRI 420 KKLPKGTVSF 430 HSHSDHRFLG 440 TVEKEATFSN 450 PKTTSPNKGK 460 EKEAEDGIIA 470 YDDCGVKLTI 480 AFQAKDVEGS 490 TSPQIGDKVE 500 FSISDKQRPG 510 QQVATCVRLL 520 GRNSNSKRLL 530 GYVATLKDNF 540 GFIETANHDK 550 EIFFHYSEFS 560 GDVDSLELGD 570 MVEYSLSKGK 580 GNKVSAEKVN 590 KTHSVNGITE 600 EADPTIYSGK 610 VIRPLRSVDP 620 TQTEYQGMIE 630 IVEEGDMKGE 640 VYPFGIVGMA 650 NKGDCLQKGE 660 SVKFQLCVLG 670 QNAQTMAYNI 680 TPLRRATVEC 690 VKDQFGFINY 700 EVGDSKKLFF 710 HVKEVQDGIE 720 LQAGDEVEFS 730 VILNQRTGKC 740 SACNVWRVCE 750 GPKAVAAPRP 760 DRLVNRLKNI 770 TLDDASAPRL 780 MVLRQPRGPD 790 NSMGFGAERK IRQAGVID

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070937 CRD-mediated mRNA stability complex
Cellular Component GO:0010494 cytoplasmic stress granule
Cellular Component GO:0005829 cytosol
Cellular Component GO:0106002 mCRD-mediated mRNA stability complex
Cellular Component GO:0000932 P-body
Molecular Function GO:0106222 lncRNA binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0140517 protein-RNA adaptor activity
Molecular Function GO:1905172 RISC complex binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0035613 RNA stem-loop binding
Biological Process GO:0070934 CRD-mediated mRNA stabilization
Biological Process GO:0075522 IRES-dependent viral translational initiation
Biological Process GO:0008584 male gonad development
Biological Process GO:1900152 negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
Biological Process GO:0070966 nuclear-transcribed mRNA catabolic process, no-go decay
Biological Process GO:2000767 positive regulation of cytoplasmic translation
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:0006446 regulation of translational initiation
Biological Process GO:0034063 stress granule assembly

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.