Summary: Grap2 and cyclin-D-interacting
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GCIP, or Grap2 and cyclin-D-interacting protein, is found in eukaryotes, and in the protein O95273 residues 149-190 constitute a helix-loop-helix domain, residues 190-240 an acidic region, and 240-261 a leucine zipper domain. GCIP interacts with full-length Grap2 protein and with the COOH-terminal unique and SH3 domains (designated QC domain) of Grap2. It is potentially involved in the regulation of cell differentiation and proliferation through Grap2 and cyclin D-mediated signalling pathways . In mice, it is involved in G1/S-phase progression of hepatocytes, which in older animals is associated with the development of liver tumours. In vitro it acts as an inhibitory HLH protein, for example, blocking transcription of the HNF-4 promoter. In its function as a cyclin D1-binding protein it is able to reduce CDK4-mediated phosphorylation of the retinoblastoma protein and to inhibit E2F-mediated transcriptional activity . GCIP has also been shown to have interact physically with Rad (Ras associated with diabetes), Rad being important in regulating cellular senescence .
Xia C, Bao Z, Tabassam F, Ma W, Qiu M, Hua S, Liu M;, J Biol Chem. 2000;275:20942-20948. : GCIP, a novel human grap2 and cyclin D interacting protein, regulates E2F-mediated transcriptional activity. PUBMED:10801854 EPMC:10801854
Lee I, Yeom SY, Lee SJ, Kang WK, Park C;, Cancer Res. 2010;70:4357-4365.: A novel senescence-evasion mechanism involving Grap2 and Cyclin D interacting protein inactivation by Ras associated with diabetes in cancer cells under doxorubicin treatment. PUBMED:20460530 EPMC:20460530
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Curation and family details
|Seed source:||Pfam-B_2169 (release 24.0)|
|Author:||Mistry J, Aldam G|
|Number in seed:||12|
|Number in full:||246|
|Average length of the domain:||213.70 aa|
|Average identity of full alignment:||19 %|
|Average coverage of the sequence by the domain:||65.93 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||1|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GCIP domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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