The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

SRP72  -  signal recognition particle 72kDa

Homo sapiens

Synonyms: BMFF, BMFS1, HEL103, Signal recognition particle 72 kDa protein, Signal recognition particle subunit SRP72
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of SRP72

  • The depletion of SRP72 and SRP68 induced sudden death, most probably as a result of toxicity due to the accumulation of the pre-SRP in the nucleolus [1].
  • Polypeptides corresponding to various regions of the entire human SRP72 sequence were expressed in Escherichia coli, purified, and partially proteolyzed [2].

High impact information on SRP72

  • SRP68 contacts the 7S RNA via its NH2-terminal half while COOH-terminal portions of SRP68 and SRP72 are in contact with each other in SRP [3].
  • The amino acid sequence deduced from the cDNA of SRP72 reveals a basic protein of 671 amino acids which shares no sequence similarity with any protein in the sequence data libraries [3].
  • As a large NH2-terminal domain of SRP72 is exposed on SRP it may be a site of contact to other molecules involved in the SRP cycle between the ribosome and the ER membrane [3].
  • In transfected rat fibroblasts, green fluorescent protein fusions of SRP19, SRP68, and SRP72 localized to the nucleolus, as well as to the cytoplasm, as expected [4].
  • Cleavage of SRP 72 produces a 66-kDa amino-terminal fragment and a 6-kDa carboxyl-terminal fragment that is selectively phosphorylated on serine residues [5].

Biological context of SRP72


Anatomical context of SRP72


Associations of SRP72 with chemical compounds

  • Sucrose gradient centrifugation and filter-binding analysis using mutant SRP RNAs showed that SRP72 bound to the moderately conserved portion of SRP RNA helix 5 [2].

Physical interactions of SRP72

  • Human SRP68 was purified from overexpressing Escherichia coli cells and was found to bind to recombinant SRP72 as well as in vitro-transcribed human SRP RNA [7].


  1. The Trypanosoma brucei signal recognition particle lacks the Alu-domain-binding proteins: purification and functional analysis of its binding proteins by RNAi. Lustig, Y., Goldshmidt, H., Uliel, S., Michaeli, S. J. Cell. Sci. (2005) [Pubmed]
  2. Identification of an RNA-binding domain in human SRP72. Iakhiaeva, E., Yin, J., Zwieb, C. J. Mol. Biol. (2005) [Pubmed]
  3. Assembly of the 68- and 72-kD proteins of signal recognition particle with 7S RNA. Lütcke, H., Prehn, S., Ashford, A.J., Remus, M., Frank, R., Dobberstein, B. J. Cell Biol. (1993) [Pubmed]
  4. Signal recognition particle components in the nucleolus. Politz, J.C., Yarovoi, S., Kilroy, S.M., Gowda, K., Zwieb, C., Pederson, T. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  5. The 72-kDa component of signal recognition particle is cleaved during apoptosis. Utz, P.J., Hottelet, M., Le, T.M., Kim, S.J., Geiger, M.E., van Venrooij, W.J., Anderson, P. J. Biol. Chem. (1998) [Pubmed]
  6. A truncated isoform of Ca2+/calmodulin-dependent protein kinase II expressed in human islets of Langerhans may result from trans-splicing. Breen, M.A., Ashcroft, S.J. FEBS Lett. (1997) [Pubmed]
  7. Protein SRP68 of human signal recognition particle: identification of the RNA and SRP72 binding domains. Iakhiaeva, E., Bhuiyan, S.H., Yin, J., Zwieb, C. Protein Sci. (2006) [Pubmed]
WikiGenes - Universities