Search Results

Overview

Uniprot IDQ9UHB9
Protein NameSignal recognition particle subunit SRP68
Gene NameSRP68
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
49 ERPSAGSKANKEFGD
504 NSDAGAFKNSLKDLP
587 GFQPIPCKPLFFDLA
612 DKLEQKTKSGLTGYI

Function

Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (PubMed:34020957). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (PubMed:34020957). Binds the signal recognition particle RNA (7SL RNA), SRP72 binds to this complex subsequently (PubMed:16672232, PubMed:27899666). The SRP complex possibly participates in the elongation arrest function (By similarity)

Protein Sequence

10 MAAEKQVPGG 20 GGGGGSGGGG 30 GSGGGGSGGG 40 RGAGGEENKE 50 NERPSAGSKA 60 NKEFGDSLSL 70 EILQIIKESQ 80 QQHGLRHGDF 90 QRYRGYCSRR 100 QRRLRKTLNF 110 KMGNRHKFTG 120 KKVTEELLTD 130 NRYLLLVLMD 140 AERAWSYAMQ 150 LKQEANTEPR 160 KRFHLLSRLR 170 KAVKHAEELE 180 RLCESNRVDA 190 KTKLEAQAYT 200 AYLSGMLRFE 210 HQEWKAAIEA 220 FNKCKTIYEK 230 LASAFTEEQA 240 VLYNQRVEEI 250 SPNIRYCAYN 260 IGDQSAINEL 270 MQMRLRSGGT 280 EGLLAEKLEA 290 LITQTRAKQA 300 ATMSEVEWRG 310 RTVPVKIDKV 320 RIFLLGLADN 330 EAAIVQAESE 340 ETKERLFESM 350 LSECRDAIQV 360 VREELKPDQK 370 QRDYILEGEP 380 GKVSNLQYLH 390 SYLTYIKLST 400 AIKRNENMAK 410 GLQRALLQQQ 420 PEDDSKRSPR 430 PQDLIRLYDI 440 ILQNLVELLQ 450 LPGLEEDKAF 460 QKEIGLKTLV 470 FKAYRCFFIA 480 QSYVLVKKWS 490 EALVLYDRVL 500 KYANEVNSDA 510 GAFKNSLKDL 520 PDVQELITQV 530 RSEKCSLQAA 540 AILDANDAHQ 550 TETSSSQVKD 560 NKPLVERFET 570 FCLDPSLVTK 580 QANLVHFPPG 590 FQPIPCKPLF 600 FDLALNHVAF 610 PPLEDKLEQK 620 TKSGLTGYIK GIFGFRS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005840 ribosome
Cellular Component GO:0048500 signal recognition particle
Cellular Component GO:0005786 signal recognition particle, endoplasmic reticulum targeting
Molecular Function GO:0008312 7S RNA binding
Molecular Function GO:0030942 endoplasmic reticulum signal peptide binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0005047 signal recognition particle binding
Biological Process GO:0009410 response to xenobiotic stimulus
Biological Process GO:0006614 SRP-dependent cotranslational protein targeting to membrane
Biological Process GO:0006617 SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition

Reference

[1] 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.

[2] 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.

[3] 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.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] 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.