4a0c: Difference between revisions

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===STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX===

==Disease==

[[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[http://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref><ref>PMID:20002452</ref><ref>PMID:17236139</ref><ref>PMID:19377476</ref>

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==Function==

~~The line below this paragraph, {{ABSTRACT_PUBMED_22118460}}, adds the Publication Abstract~~ to the ~~page~~

[[http://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref><ref>PMID:12504025</ref><ref>PMID:12609982</ref> [[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref><ref>PMID:16322693</ref><ref>PMID:16678110</ref><ref>PMID:18593899</ref><ref>PMID:18235224</ref><ref>PMID:19801544</ref>

~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov)~~, ~~where 22118460 is~~ the ~~PubMed ID number~~.

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~~{{ABSTRACT_PUBMED_22118460}}~~

==About this Structure==

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==Reference==

[[Category: Homo sapiens]]

[[Category: Mus musculus]]

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-[[Image:4a0c.png|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_4a0c", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
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 {{STRUCTURE_4a0c|  PDB=4a0c  |  SCENE=  }}
 ===STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX===
+{{ABSTRACT_PUBMED_22118460}}
+==Disease==
+[[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[http://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref><ref>PMID:20002452</ref><ref>PMID:17236139</ref><ref>PMID:19377476</ref>
-<!--
+==Function==
-The line below this paragraph, {{ABSTRACT_PUBMED_22118460}}, adds the Publication Abstract to the page
+[[http://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref><ref>PMID:12504025</ref><ref>PMID:12609982</ref> [[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref><ref>PMID:16322693</ref><ref>PMID:16678110</ref><ref>PMID:18593899</ref><ref>PMID:18235224</ref><ref>PMID:19801544</ref>
-(as it appears on PubMed at http://www.pubmed.gov), where 22118460 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_22118460}}
 ==About this Structure==
@@ Line 22: / Line 13: @@
 ==Reference==
-<ref group="xtra">PMID:022118460</ref><references group="xtra"/>
+<ref group="xtra">PMID:022118460</ref><references group="xtra"/><references/>
 [[Category: Homo sapiens]]
 [[Category: Mus musculus]]