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Gene Review

SCPEP1  -  serine carboxypeptidase 1

Homo sapiens

Synonyms: HSCP1, MSTP034, RISC, Retinoid-inducible serine carboxypeptidase, SCP1, ...
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Disease relevance of SCPEP1


Psychiatry related information on SCPEP1

  • We studied the relationships between structure and schizotypal features (assessed using RISC and SIS) and verbal learning and memory (measured using RAVLT) in relatives at high risk of developing schizophrenia and normal controls [6].
  • The CD-RISC has sound psychometric properties and distinguishes between those with greater and lesser resilience [7].

High impact information on SCPEP1

  • We recently showed that Scp1 is an evolutionarily conserved regulator of neuronal gene silencing [8].
  • Moreover, these results provide a template for the design of specific inhibitors of Scp1 for the study of neuronal stem cell development [8].
  • Fcp1 and Scp1 belong to a family of Mg(2+)-dependent phosphoserine (P.Ser)/phosphothreonine (P.Thr)-specific phosphatases [8].
  • The fundamental engines of RNA silencing are RISC and RITS complexes, whose common components are 21-25 nt RNA and an Argonaute protein containing a PIWI domain of unknown function [9].
  • Endothelin-1 is a peptidic substrate in vitro of lysosomal protective protein/cathepsin A (PPCA) with serine carboxypeptidase activity [10].

Biological context of SCPEP1

  • Radiation hybrid mapping studies placed the rat RISC locus on chromosome 10q [11].
  • A near full-length rat RISC cDNA was cloned and found to have a 452-amino acid open reading frame containing an amino-terminal signal sequence, followed by several conserved domains comprising the catalytic triad common to members of the serine carboxypeptidase family [11].
  • Overexpression of SCP 1, 2, or 3 decreased linker phosphorylation of Smads 1, 2 and 3 [12].
  • Chemical modifications impairing the cleavage of the passenger strand also impair the cleavage of a target RNA in vitro as well as the silencing of a reporter gene in vivo, suggesting that passenger strand removal is facilitated by its cleavage during RISC assembly [13].
  • The RISC (Relationship between Insulin Sensitivity and Cardiovascular disease) Study is using the infrastructure of an extended European collaborative research group to study insulin resistance and CVD risk in 1500 healthy people aged 30 to 60 years from 20 centres in 13 countries [14].

Anatomical context of SCPEP1


Associations of SCPEP1 with chemical compounds


Other interactions of SCPEP1


Analytical, diagnostic and therapeutic context of SCPEP1


  1. Novel form of non-muscle tropomyosin in human fibroblasts. Talbot, K., MacLeod, A.R. J. Mol. Biol. (1983) [Pubmed]
  2. Differential expression of cancer testis genes in histological subtypes of non-Hodgkin's lymphomas. Xie, X., Wacker, H.H., Huang, S., Regitz, E., Preuss, K.D., Romeike, B., Parwaresch, R., Tiemann, M., Pfreundschuh, M. Clin. Cancer Res. (2003) [Pubmed]
  3. Off-target effects by siRNA can induce toxic phenotype. Fedorov, Y., Anderson, E.M., Birmingham, A., Reynolds, A., Karpilow, J., Robinson, K., Leake, D., Marshall, W.S., Khvorova, A. RNA (2006) [Pubmed]
  4. Very early risk stratification by electrocardiogram at rest in men with suspected unstable coronary heart disease. The RISC Study Group. Nyman, I., Areskog, M., Areskog, N.H., Swahn, E., Wallentin, L. J. Intern. Med. (1993) [Pubmed]
  5. Belactins A and B, new serine carboxypeptidase inhibitors produced by Actinomycete. II. Physico-chemical properties, structure determinations and enzymatic inhibitory activities compared with other beta-lactone containing inhibitors. Murakami, S., Takahashi, Y., Naganawa, H., Takeuchi, T., Aoyagi, T. J. Enzym. Inhib. (1995) [Pubmed]
  6. Brain-behaviour relationships in people at high genetic risk of schizophrenia. Lymer, G.K., Job, D.E., William, T., Moorhead, J., McIntosh, A.M., Owens, D.G., Johnstone, E.C., Lawrie, S.M. Neuroimage (2006) [Pubmed]
  7. Development of a new resilience scale: the Connor-Davidson Resilience Scale (CD-RISC). Connor, K.M., Davidson, J.R. Depression and anxiety. (2003) [Pubmed]
  8. Determinants for Dephosphorylation of the RNA Polymerase II C-Terminal Domain by Scp1. Zhang, Y., Kim, Y., Genoud, N., Gao, J., Kelly, J.W., Pfaff, S.L., Gill, G.N., Dixon, J.E., Noel, J.P. Mol. Cell (2006) [Pubmed]
  9. Crystal structure of a PIWI protein suggests mechanisms for siRNA recognition and slicer activity. Parker, J.S., Roe, S.M., Barford, D. EMBO J. (2004) [Pubmed]
  10. Endothelin-1 in the brain of patients with galactosialidosis: its abnormal increase and distribution pattern. Itoh, K., Oyanagi, K., Takahashi, H., Sato, T., Hashizume, Y., Shimmoto, M., Sakuraba, H. Ann. Neurol. (2000) [Pubmed]
  11. Cloning of a novel retinoid-inducible serine carboxypeptidase from vascular smooth muscle cells. Chen, J., Streb, J.W., Maltby, K.M., Kitchen, C.M., Miano, J.M. J. Biol. Chem. (2001) [Pubmed]
  12. Dephosphorylation of the Linker Regions of Smad1 and Smad2/3 by Small C-terminal Domain Phosphatases Has Distinct Outcomes for Bone Morphogenetic Protein and Transforming Growth Factor-beta Pathways. Sapkota, G., Knockaert, M., Alarc??n, C., Montalvo, E., Brivanlou, A.H., Massagu??, J. J. Biol. Chem. (2006) [Pubmed]
  13. Cleavage of the siRNA passenger strand during RISC assembly in human cells. Leuschner, P.J., Ameres, S.L., Kueng, S., Martinez, J. EMBO Rep. (2006) [Pubmed]
  14. The EGIR-RISC STUDY (The European group for the study of insulin resistance: relationship between insulin sensitivity and cardiovascular disease risk): I. Methodology and objectives. Hills, S.A., Balkau, B., Coppack, S.W., Dekker, J.M., Mari, A., Natali, A., Walker, M., Ferrannini, E. Diabetologia (2004) [Pubmed]
  15. The CH-domain of calponin does not determine the modes of calponin binding to F-actin. Galkin, V.E., Orlova, A., Fattoum, A., Walsh, M.P., Egelman, E.H. J. Mol. Biol. (2006) [Pubmed]
  16. Cloning and characterization of CPVL, a novel serine carboxypeptidase, from human macrophages. Mahoney, J.A., Ntolosi, B., DaSilva, R.P., Gordon, S., McKnight, A.J. Genomics (2001) [Pubmed]
  17. Expression of lysosomal protective protein/cathepsin A in a stably transformed human neuroblastoma cell line during bi-directional differentiation into neuronal and Schwannian cells. Itoh, K., Satoh, Y., Kadota, Y., Oheda, Y., Kuwahara, J., Shimmoto, M., Sakuraba, H. Neurochem. Int. (2004) [Pubmed]
  18. Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase. Liao, D.I., Remington, S.J. J. Biol. Chem. (1990) [Pubmed]
  19. Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families. Tan, F., Morris, P.W., Skidgel, R.A., Erdös, E.G. J. Biol. Chem. (1993) [Pubmed]
  20. Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity. Bullock, T.L., Breddam, K., Remington, S.J. J. Mol. Biol. (1996) [Pubmed]
  21. Structure of the complex of L-benzylsuccinate with wheat serine carboxypeptidase II at 2.0-A resolution. Bullock, T.L., Branchaud, B., Remington, S.J. Biochemistry (1994) [Pubmed]
  22. Lysosomal protective protein/cathepsin A. Role of the "linker" domain in catalytic activation. Bonten, E.J., Galjart, N.J., Willemsen, R., Usmany, M., Vlak, J.M., d'Azzo, A. J. Biol. Chem. (1995) [Pubmed]
  23. Molecular cloning and sequence analysis of the scpZ gene encoding the serine carboxypeptidase of Absidia zychae. Lee, B.R., Takeuchi, M., Kobayashi, Y. Curr. Genet. (1995) [Pubmed]
  24. Amidation of growth hormone releasing factor (1-29) by serine carboxypeptidase catalysed transpeptidation. Breddam, K., Widmer, F., Meldal, M. Int. J. Pept. Protein Res. (1991) [Pubmed]
  25. Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms. Holmquist, M. Curr. Protein Pept. Sci. (2000) [Pubmed]
  26. Apparent and Internal Validity of a Monte Carlo-Markov Model for Cardiovascular Disease in a Cohort Follow-up Study. Nijhuis, R.L., Stijnen, T., Peeters, A., Witteman, J.C., Hofman, A., Hunink, M.G. Medical decision making : an international journal of the Society for Medical Decision Making. (2006) [Pubmed]
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