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RASSF9

Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia

RASSF9
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Ras association domain-containing protein 9 (RASSF9), also known as PAM COOH-terminal interactor protein 1 (PCIP1) or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor (PAMCI) is a protein that in humans is encoded by the RASSF9 gene.[5]

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Function

RASSF9 the N-terminal RASSF family member Ras association (RalGDS/AF-6) domain family (N-terminal) member 9 12q21.31,[6][7] is one of two new wild type RASSF9 and RASSF10[7] proteins. Three proteins that interact with a fragment of the PAM cytosolic domain containing signaling switch I and II the RA1 and RA2ras complex.[8] RASSF7, the first member of the N-terminal RASSF family is required for mitosis.[7] RASSF9 is recently found to be involved in regulation of epidermal homeostasis.[9]

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Regulation

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The mutant proregion encoding PAM COOH-terminal interactor protein-1 (P-CIP1) is comparable to that of human band 4.1-like TF (blood plasma protein) as a recycling endosomal pathway[6] in microtubule locations, does NOT bind RasGTP.[10] Specificity of interaction may all be related to microtubule locations of the endosomal-lysosomal system localized within the centrosome with Transferrin and different Ras proteins or with that one (N-Ras), but on the other hand, it interacts with three[11] (Ha-Ras, Ki-Ras,[12] and Rap[13]) residues function,[14] blocked by a mutation that affects Ras effector function[15] is the critical product of the t (6:11) abnormality associated with some human leukemias.[12] Phosphatidylinositol-3-kinase make contacts with both (6:11) switch I and II[12] regions of ras[8] and yeast adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro.[16] Ras-interacting residues, are appreciably different from that of RalGDS-RBD[17] through their C-terminal Ras-binding domains (RBD).[18] Such outliers as afadin/AF-6 and Rin1[16] were found to inhibit the binding of Raf to Ras.[14] Adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro with the Ras-associating domain-RA,[16] not all RA domains bind RasGTP it is a primary Ras-binding site.

Interactions

  • PAM Peptidyl-glycine alpha-amidating monooxygenase precursor (PAM)
  • RASSF7 Ras association domain-containing protein 7 (HRAS1-related cluster protein 1)
  • BLOC1S2 Biogenesis of lysosome-related organelles complex-1 subunit 2 (BLOC subunit 2)
  • TF Serotransferrin precursor (Transferrin) (Beta-1-metal- binding globulin)
  • RAB11A Ras-related protein Rab-11A[19]

References

Further reading

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