Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972262035 185 NLENLQKLRLLRLANSEYVDDWCIGRIGGLLPNLEMLDLSGCHrISSKGLMGL--KASKNLKFLRLEGLSGIRNLGKSAL 262
Cdd:cd09293   102 NCPKLQTINLGRHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELasGCSKSLERLSLNNCRNLTDQSIPAI 180

                          90
                  ....*....|..
gi 1972262035 263 ILEDLLPKLQIL 274
Cdd:cd09293   181 LASNYFPNLSVL 192

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972262035 185 NLENLQKLRLLRLANSEYVDDWCIGRIGGLLPNLEMLDLSGCHrISSKGLMGL--KASKNLKFLRLEGLSGIRNLGKSAL 262
Cdd:cd09293   102 NCPKLQTINLGRHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELasGCSKSLERLSLNNCRNLTDQSIPAI 180

                          90
                  ....*....|..
gi 1972262035 263 ILEDLLPKLQIL 274
Cdd:cd09293   181 LASNYFPNLSVL 192

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972262035 185 NLENLQKLRLLRLANSEYVDDWCIGRIGGLLPNLEMLDLSGCHrISSKGLMGL--KASKNLKFLRLEGLSGIRNLGKSAL 262
Cdd:cd09293   102 NCPKLQTINLGRHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELasGCSKSLERLSLNNCRNLTDQSIPAI 180

                          90
                  ....*....|..
gi 1972262035 263 ILEDLLPKLQIL 274
Cdd:cd09293   181 LASNYFPNLSVL 192

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972262035 181 EGLENLENLQKLRLL--RLANSEYVD-DWCIgrIGGLLPNLEMLDLSGChRISSkgLMGLKASKNLKFLRLEG 250
Cdd:cd21340    84 EGLENLTNLEELHIEnqRLPPGEKLTfDPRS--LAALSNSLRVLNISGN-NIDS--LEPLAPLRNLEQLDASN 151