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Overview

Uniprot IDQ9BXP5
Protein NameSerrate RNA effector molecule homolog
Gene NameSRRT
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
279 EEEEQAGKPGEPSKK
285 GKPGEPSKKEEGRAG
286 KPGEPSKKEEGRAGA
723 PLSGKKFKGPEFVRK

Function

Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription (By similarity)

Protein Sequence

10 MGDSDDEYDR 20 RRRDKFRRER 30 SDYDRSRERD 40 ERRRGDDWND 50 REWDRGRERR 60 SRGEYRDYDR 70 NRRERFSPPR 80 HELSPPQKRM 90 RRDWDEHSSD 100 PYHSGYEMPY 110 AGGGGGPTYG 120 PPQPWGHPDV 130 HIMQHHVLPI 140 QARLGSIAEI 150 DLGVPPPVMK 160 TFKEFLLSLD 170 DSVDETEAVK 180 RYNDYKLDFR 190 RQQMQDFFLA 200 HKDEEWFRSK 210 YHPDEVGKRR 220 QEARGALQNR 230 LRVFLSLMET 240 GWFDNLLLDI 250 DKADAIVKML 260 DAAVIKMEGG 270 TENDLRILEQ 280 EEEEEQAGKP 290 GEPSKKEEGR 300 AGAGLGDGER 310 KTNDKDEKKE 320 DGKQAENDSS 330 NDDKTKKSEG 340 DGDKEEKKED 350 SEKEAKKSSK 360 KRNRKHSGDD 370 SFDEGSVSES 380 ESESESGQAE 390 EEKEEAEEAL 400 KEKEKPKEEE 410 WEKPKDAAGL 420 ECKPRPLHKT 430 CSLFMRNIAP 440 NISRAEIISL 450 CKRYPGFMRV 460 ALSEPQPERR 470 FFRRGWVTFD 480 RSVNIKEICW 490 NLQNIRLREC 500 ELSPGVNRDL 510 TRRVRNINGI 520 TQHKQIVRND 530 IKLAAKLIHT 540 LDDRTQLWAS 550 EPGTPPLPTS 560 LPSQNPILKN 570 ITDYLIEEVS 580 AEEEELLGSS 590 GGAPPEEPPK 600 EGNPAEINVE 610 RDEKLIKVLD 620 KLLLYLRIVH 630 SLDYYNTCEY 640 PNEDEMPNRC 650 GIIHVRGPMP 660 PNRISHGEVL 670 EWQKTFEEKL 680 TPLLSVRESL 690 SEEEAQKMGR 700 KDPEQEVEKF 710 VTSNTQELGK 720 DKWLCPLSGK 730 KFKGPEFVRK 740 HIFNKHAEKI 750 EEVKKEVAFF 760 NNFLTDAKRP 770 ALPEIKPAQP 780 PGPAQILPPG 790 LTPGLPYPHQ 800 TPQGLMPYGQ 810 PRPPILGYGA 820 GAVRPAVPTG 830 GPPYPHAPYG 840 AGRGNYDAFR 850 GQGGYPGKPR 860 NRMVRGDPRA 870 IVEYRDLDAP DDVDFF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0140262 mRNA cap binding complex binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0097150 neuronal stem cell population maintenance
Biological Process GO:0050769 positive regulation of neurogenesis
Biological Process GO:0031053 primary miRNA processing
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0046685 response to arsenic-containing substance

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[2] 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.