Search Results

Overview

Uniprot IDO76094
Protein NameSignal recognition particle subunit SRP72
Gene NameSRP72
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
112 NQQTDKLKELYGQVL
201 QAMKILQKAEDLCRR
383 KLTMAQLKISQGNIS
391 ISQGNISKACLILRS
544 VTGDSQPKEQGQGDL
569 LPKNYDPKVTPDPER
600 KKKDQIGKGTQGATA

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) in presence of SRP68 (PubMed:21073748, PubMed:27899666). Can bind 7SL RNA with low affinity (PubMed:21073748, PubMed:27899666). The SRP complex possibly participates in the elongation arrest function (By similarity)

Protein Sequence

10 MASGGSGGVS 20 VPALWSEVNR 30 YGQNGDFTRA 40 LKTVNKILQI 50 NKDDVTALHC 60 KVVCLIQNGS 70 FKEALNVINT 80 HTKVLANNSL 90 SFEKAYCEYR 100 LNRIENALKT 110 IESANQQTDK 120 LKELYGQVLY 130 RLERYDECLA 140 VYRDLVRNSQ 150 DDYDEERKTN 160 LSAVVAAQSN 170 WEKVVPENLG 180 LQEGTHELCY 190 NTACALIGQG 200 QLNQAMKILQ 210 KAEDLCRRSL 220 SEDTDGTEED 230 PQAELAIIHG 240 QMAYILQLQG 250 RTEEALQLYN 260 QIIKLKPTDV 270 GLLAVIANNI 280 ITINKDQNVF 290 DSKKKVKLTN 300 AEGVEFKLSK 310 KQLQAIEFNK 320 ALLAMYTNQA 330 EQCRKISASL 340 QSQSPEHLLP 350 VLIQAAQLCR 360 EKQHTKAIEL 370 LQEFSDQHPE 380 NAAEIKLTMA 390 QLKISQGNIS 400 KACLILRSIE 410 ELKHKPGMVS 420 ALVTMYSHEE 430 DIDSAIEVFT 440 QAIQWYQNHQ 450 PKSPAHLSLI 460 REAANFKLKY 470 GRKKEAISDL 480 QQLWKQNPKD 490 IHTLAQLISA 500 YSLVDPEKAK 510 ALSKHLPSSD 520 SMSLKVDVEA 530 LENSAGATYI 540 RKKGGKVTGD 550 SQPKEQGQGD 560 LKKKKKKKKG 570 KLPKNYDPKV 580 TPDPERWLPM 590 RERSYYRGRK 600 KGKKKDQIGK 610 GTQGATAGAS 620 SELDASKTVS 630 SPPTSPRPGS 640 AATVSASTSN 650 IIPPRHQKPA 660 GAPATKKKQQ 670 QKKKKGGKGG W

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005783 endoplasmic reticulum
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:0003723 RNA binding
Molecular Function GO:0005047 signal recognition particle binding
Molecular Function GO:0030911 TPR domain binding
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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[3] 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.