RCBTB1 (13 q14.2), C-terminaalinen BTB , N- terminaalinen RCC1 domeeni

 https://www.ncbi.nlm.nih.gov/gene/55213

Official Symbol

RCBTB1provided by HGNC

Official Full Name

RCC1 and BTB domain containing protein 1provided by HGNC

Also known as

GLP; CLLD7; CLLL7; RDEOA

Summary

This gene encodes a protein with an N-terminal RCC1 domain and a C-terminal BTB (broad complex, tramtrack and bric-a-brac) domain. In rat, over-expression of this gene in vascular smooth muscle cells induced cellular hypertrophy. In rat, the C-terminus of RCBTB1 interacts with the angiotensin II receptor-1A. In humans, this gene maps to a region of chromosome 13q that is frequently deleted in B-cell chronic lymphocytic leukemia and other lymphoid malignancies. [provided by RefSeq, Jul 2008]

Expression

Ubiquitous expression in thyroid (RPKM 19.0), brain (RPKM 9.6) and 25 other tissues See more

Orthologs

mouse all

 

Preferred Names

RCC1 and BTB domain-containing protein 1

Names

CLL deletion region gene 7 protein

GDP/GTP exchange factor (GEF)-like protein

chronic lymphocytic leukemia deletion region gene 7 protein

regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 1

regulator of chromosome condensation and BTB domain-containing protein 1


Ref. 
The ubiquitin conjugating enzyme, UbcM2, engages in novel interactions with components of cullin-3 based E3 ligases.

Plafker KS¹, Singer JD, Plafker SM.

1

Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA. Abstract

The class III ubiquitin conjugating enzymes (E2s) are distinguished from other E2s by the presence of unique N-terminal domains, and the utilization of importin-11 for transport into the nucleus in an activation dependent fashion. To begin determining the physiological roles of these enzymes, we carried out a yeast two-hybrid screen with the class III E2, UbcM2. This screen retrieved RCBTB1, a putative substrate adaptor for a cullin3 (CUL3) E3 ligase. We initially established through biochemical studies that RCBTB1 has the properties of a CUL3 substrate adaptor. Further analysis of the UbcM2-RCBTB1 complex led to the discovery and characterization of the following novel interactions: (i) UbcM2 binds an N-terminal domain of CUL3 requiring the first 57 amino acids, the same domain that binds to RCBTB1 and other substrate adaptors; (ii) UbcM2 does not bind mutants of CUL3 that are deficient in substrate adaptor recruitment; (iii) UbcM2 interacts with CUL3 independent of a bridging RING-finger protein; and (iv) can engage the neddylated (i.e., activated) form of CUL3. We also present evidence that UbcM2 can bind to the N-terminal halves of multiple cullins, implying that this E2 is a general cofactor for this class of ligases. Together, these studies represent the first evidence that UbcM2, in concert with substrate adaptors, engages activated CUL3 ligases, thus suggesting that class III E2s are novel regulators of cullin ligases.

DOI:

10.1021/bi801971m