Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

26S proteasome non-ATPase regulatory subunit 6

Gene

Psmd6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.By similarity

GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-MMU-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174113 SCF-beta-TrCP mediated degradation of Emi1
R-MMU-174154 APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-202424 Downstream TCR signaling
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-350562 Regulation of ornithine decarboxylase (ODC)
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-MMU-4608870 Asymmetric localization of PCP proteins
R-MMU-4641257 Degradation of AXIN
R-MMU-4641258 Degradation of DVL
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome
R-MMU-5632684 Hedgehog 'on' state
R-MMU-5658442 Regulation of RAS by GAPs
R-MMU-5668541 TNFR2 non-canonical NF-kB pathway
R-MMU-5676590 NIK-->noncanonical NF-kB signaling
R-MMU-5687128 MAPK6/MAPK4 signaling
R-MMU-5689603 UCH proteinases
R-MMU-5689880 Ub-specific processing proteases
R-MMU-6798695 Neutrophil degranulation
R-MMU-68827 CDT1 association with the CDC6:ORC:origin complex
R-MMU-68949 Orc1 removal from chromatin
R-MMU-69017 CDK-mediated phosphorylation and removal of Cdc6
R-MMU-69229 Ubiquitin-dependent degradation of Cyclin D1
R-MMU-69481 G2/M Checkpoints
R-MMU-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8941858 Regulation of RUNX3 expression and activity
R-MMU-8948751 Regulation of PTEN stability and activity
R-MMU-9020702 Interleukin-1 signaling
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 6
Alternative name(s):
26S proteasome regulatory subunit RPN7
26S proteasome regulatory subunit S10
p42A
Gene namesi
Name:Psmd6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1913663 Psmd6

Subcellular locationi

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001738391 – 38926S proteasome non-ATPase regulatory subunit 6Add BLAST389

Proteomic databases

EPDiQ99JI4
MaxQBiQ99JI4
PaxDbiQ99JI4
PeptideAtlasiQ99JI4
PRIDEiQ99JI4

PTM databases

iPTMnetiQ99JI4
PhosphoSitePlusiQ99JI4
SwissPalmiQ99JI4

Expressioni

Gene expression databases

BgeeiENSMUSG00000021737
GenevisibleiQ99JI4 MM

Interactioni

Subunit structurei

Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD6, a base containing 6 ATPases and few additional components.By similarity1 Publication

Protein-protein interaction databases

BioGridi211457, 36 interactors
IntActiQ99JI4, 40 interactors
MINTiQ99JI4
STRINGi10090.ENSMUSP00000022256

Structurei

3D structure databases

ProteinModelPortaliQ99JI4
SMRiQ99JI4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini193 – 361PCIPROSITE-ProRule annotationAdd BLAST169

Sequence similaritiesi

Belongs to the proteasome subunit S10 family.Curated

Phylogenomic databases

eggNOGiKOG0687 Eukaryota
COG5187 LUCA
GeneTreeiENSGT00510000046608
HOGENOMiHOG000214998
HOVERGENiHBG023924
InParanoidiQ99JI4
KOiK03037
OMAiVDYIDQE
OrthoDBiEOG091G03SE
PhylomeDBiQ99JI4
TreeFamiTF313819

Family and domain databases

InterProiView protein in InterPro
IPR000717 PCI_dom
IPR035268 PSMD6
IPR019585 Rpn7/CSN1
IPR011990 TPR-like_helical_dom_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR14145:SF1 PTHR14145:SF1, 1 hit
PfamiView protein in Pfam
PF01399 PCI, 1 hit
PF10602 RPN7, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 1 hit

Sequencei

Sequence statusi: Complete.

Q99JI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLENLEEEG LPKNPDLRIA QLRFLLSLPE HRGDAAVREE LMAAVRENNM
60 70 80 90 100
APYYEALCKS LDWQMDVDLL SKMKKANEEE LKRLDEELED AEKNLGESEI
110 120 130 140 150
RDAMMAKAEY LCQIGDKEGA LTAFRKTYDK TVALGHRLDI VFYLLRIGLF
160 170 180 190 200
YMDNDLITRN TEKAKSLIEE GGDWDRRNRL KVYQGLYCVA IRDFKQAAEL
210 220 230 240 250
FLDTVSTFTS YELMDYKTFV TYTVYVSMIA LERPDLREKV IKGAEILEVL
260 270 280 290 300
HSLPAVRQYL FSLYECRYSV FFQSLAIVEQ EMKKDWLFAP HYRYYVREMR
310 320 330 340 350
IHAYSQLLES YRSLTLGYMA EAFGVGVDFI DQELSRFIAA GRLHCKIDKV
360 370 380
NEIVETNRPD SKNWQYQETI KKGDLLLNRV QKLSRVINM
Length:389
Mass (Da):45,536
Last modified:June 1, 2001 - v1
Checksum:iDC8C54144D2884B9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21 – 23QLR → DCV in BAB26823 (Ref. 1) Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ252147 mRNA Translation: CAC34579.1
AK010287 mRNA Translation: BAB26823.1
BC006869 mRNA Translation: AAH06869.1
CCDSiCCDS26824.1
RefSeqiNP_079826.2, NM_025550.2
UniGeneiMm.27591

Genome annotation databases

EnsembliENSMUST00000022256; ENSMUSP00000022256; ENSMUSG00000021737
GeneIDi66413
KEGGimmu:66413
UCSCiuc007sgj.1 mouse

Similar proteinsi

Entry informationi

Entry nameiPSMD6_MOUSE
AccessioniPrimary (citable) accession number: Q99JI4
Secondary accession number(s): Q9CWZ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: June 1, 2001
Last modified: May 23, 2018
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health