Primary Information
BoMiProt ID	Bomi3470
Protein Name	26S proteasome regulatory subunit 10B/26S proteasome AAA-ATPase subunit RPT4/Proteasome 26S subunit ATPase 6
Organism	Bos taurus
Uniprot ID	Q2KIW6
Milk Fraction	Whey
Ref Sequence ID	NP_001039705.1
Aminoacid Length	389
Molecular Weight	44074
FASTA Sequence	Download
Gene Name	PSMC6
Gene ID	518637
Protein Existence Status	reviewed
Secondary Information
Protein Function	Responsible for ~70% of intracellular proteolysis,[15] proteasome complex (26S proteasome) plays a critical roles in maintaining the homeostasis of cellular proteome.
Biochemical Properties	The 26S proteasome is the most downstream element of the ubiquitin-proteasome pathway of protein degradation. It is composed of the 20S core particle (CP) and the 19S regulatory particle (RP). The RP consists of 6 AAA-ATPases and at least 13 non-ATPase subunits.
PTMs	N6-Acetylation at Lys,Phosphorylation at Ser
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation	>sp|Q2KIW6|PRS10_BOVIN 26S proteasome regulatory subunit 10B OS=Bos taurus OX=9913 GN=PSMC6 PE=2 SV=1 MADPRDKALQDYRKKLLEHKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEV LKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVY NMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGK TLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGG RRFS*244EGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIH IDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLGNVCTEAGMFAIRADHD FVVQEDFMKAVRKVADSKKLESKLDYKPV
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	When the mammalian 26S proteasome 19S RP ATPase subunit Rpt6 was phosphorylated, the activity of proteasome was regulated by cAMP-dependent protein kinase (PKA).
Additional Comments	The base consists of a ring of six AAA ATPases (Subunit Rpt1-6, systematic nomenclature) and four non-ATPase subunits (Rpn1, Rpn2, Rpn10, and Rpn13). Thus, 26S protease regulatory subunit 4 (Rpt2) is an essential component of forming the base subcomplex of 19S regulatory particle.
Bibliography	1.Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL (Sep 1994). "Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules". Cell. 78 (5): 761–71. doi:10.1016/s0092-8674(94)90462-6. PMID 8087844. 2.Funakoshi M, Tomko RJ, Kobayashi H, Hochstrasser M (May 2009). "Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base". Cell. 137 (5): 887–99. doi:10.1016/j.cell.2009.04.061. PMC 2718848. PMID 19446322. 3.Park S, Roelofs J, Kim W, Robert J, Schmidt M, Gygi SP, Finley D (Jun 2009). "Hexameric assembly of the proteasomal ATPases is templated through their C termini". Nature. 459 (7248): 866–70. Bibcode:2009Natur.459..866P. doi:10.1038/nature08065. PMC 2722381. PMID 19412160. 4.Förster F, Lasker K, Beck F, Nickell S, Sali A, Baumeister W. An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome. Biochem Biophys Res Commun. 2009 Oct 16;388(2):228-33. doi: 10.1016/j.bbrc.2009.07.145. Epub 2009 Aug 3. PMID: 19653995; PMCID: PMC2771176. 5.Lu, H.; Zong, C.; Wang, Y.; Young, G. W.; Deng, N.; Souda, P.; Li, X.; Whitelegge, J.; Drews, O.; Yang, P.-Y.; Ping, P. (2008). Revealing the Dynamics of the 20 S Proteasome Phosphoproteome: A Combined CID and Electron Transfer Dissociation Approach. Molecular & Cellular Proteomics, 7(11), 2073–2089. doi:10.1074/mcp.M800064MCP200.