| Category | Summary |
|---|---|
| Identity/domains | • Verified target: **human SRP72 / signal recognition particle 72 kDa subunit**, a canonical component of mammalian SRP containing six proteins plus **7SL RNA** (pqac-00000010, pqac-00000021)  • Forms the **SRP68/72 heterodimer** within the **S-domain** of SRP; UniProt O76094 assignment is consistent with literature on human SRP72 (pqac-00000003, pqac-00000028) |
| Molecular function | • Functions in **co-translational targeting** of secretory and membrane proteins to the **ER** as part of SRP, which pauses elongation, targets the ribosome–nascent chain complex to the **SRP receptor**, and hands substrates to the **Sec61 translocon** (pqac-00000010, pqac-00000023, pqac-00000026)  • SRP68/72 is positioned on the **7SL S-domain** and is described as helping **control translocation** (pqac-00000025, pqac-00000028) |
| Key interactions | • **SRP72 + SRP68** form a stable heterodimer; GFP-SRP72 co-immunoprecipitates other SRP subunits, confirming assembly into mature SRP (pqac-00000003, pqac-00000009)  • Interactions between **Alu-domain proteins** and **S-domain proteins including SRP72** are strongly **RNase-sensitive**, supporting dependence on **7SL RNA** (pqac-00000001, pqac-00000009)  • Disease-associated frameshift SRP72 shows markedly reduced **7SL RNA co-precipitation** (pqac-00000014) |
| Subcellular localization/biogenesis | • Mature SRP72 is found in the **cytoplasm**, where SRP functions, but SRP72 also has a clear **nuclear/nucleolar biogenesis phase** (pqac-00000005, pqac-00000011)  • Five SRP proteins, including **SRP72**, assemble with 7SL in the **nucleolus** before **SRP54** joins in the cytoplasm (pqac-00000009, pqac-00000010)  • SRP72 localizes to the **PDFC region of the nucleolus** and to **Cajal bodies**, implying additional assembly steps there (pqac-00000009, pqac-00000011, pqac-00000018) |
| Disease genetics | • **Heterozygous germline SRP72 mutations** are linked to **autosomal-dominant familial aplasia / myelodysplasia** and bone-marrow failure phenotypes including **AA/MDS, pancytopenia, macrocytic anemia, thrombocytopenia** (pqac-00000013, pqac-00000015, pqac-00000017)  • Reported pathogenic variants include **p.Thr355Lysfs*19** and **p.Arg207His**; the frameshift removes the **7SL RNA-binding region** and impairs association with 7SL (pqac-00000013, pqac-00000014) |
| Recent non-canonical roles | • 2024 proteomics places SRP72 in a broader **nucleolar/ribosome-biogenesis network**, suggesting coordinated assembly of SRP and ribosomes (pqac-00000004, pqac-00000012)  • **Zika virus NS3** was reported to bind **SRP72** and other SRP machinery during ER-translation remodeling (pqac-00000030)  • In 2025 heat-shock work, **SRP72 depletion** altered stress-linked translation programs, implicating SRP72/SRP in acute thermal-stress responses beyond secretion (pqac-00000031) |
| Applications/implementations | • **Clinical genetics**: SRP72 is included in hereditary myeloid malignancy / inherited bone-marrow-failure evaluation frameworks and targeted-gene screening lists (pqac-00000017, pqac-00000029)  • **Cell biology/proteomics tool use**: inducible **GFP-SRP72** lines and **SILAC IP–MS** are being used to map SRP assembly and interactomes (pqac-00000007, pqac-00000011) |
| Quantitative highlights | • In U2OS cells, **~50% of analyzed Cajal bodies** were positive for SRP72; based on **45 GFP-SRP72-expressing cells** examined (pqac-00000001, pqac-00000009)  • SRP proteomics identified **~239 new SRP associations**, including **95 new nucleolar/ribosome-biogenesis proteins**, bringing the total such SRP interactors to **173** (pqac-00000012)  • SRP72 frameshift **p.Thr355Lysfs*19** retained only **~15% of wild-type 7SL RNA co-precipitation** (pqac-00000014)  • Heat-shock study reported **33 DEGs** and **4 SRP72-dependency clusters** upon SRP72 depletion (pqac-00000031) |
| Key references/URLs | • **Issa et al., 2024, Life Science Alliance** — nucleolar phase of SRP assembly — https://doi.org/10.26508/lsa.202402614 (pqac-00000010)  • **Kirwan et al., 2012, AJHG** — familial aplasia/myelodysplasia genetics — https://doi.org/10.1016/j.ajhg.2012.03.020 (pqac-00000013)  • **Karamysheva & Karamyshev, 2023, Front Cell Dev Biol** — SRP/RAPP overview — https://doi.org/10.3389/fcell.2023.1198184 (pqac-00000026)  • **Guarnizo et al., 2023, NAR Genom Bioinform** — pathogenic signal peptide variants/SRP pathway — https://doi.org/10.1093/nargab/lqad093 (pqac-00000027)  • **Wong et al., 2024, PLOS Pathogens** — viral remodeling with SRP72 interaction — https://doi.org/10.1371/journal.ppat.1012766 (pqac-00000030) |


*Table: This table condenses the most relevant verified findings on human SRP72 (UniProt O76094), covering identity, mechanism, localization, disease links, recent research, and practical clinical/research uses. It is useful as a citation-ready scaffold for the final research report.*