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Protein

26S proteasome non-ATPase regulatory subunit 3

Gene

Psmd3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Tumor antigen

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
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-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-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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 3
Alternative name(s):
26S proteasome regulatory subunit RPN3
26S proteasome regulatory subunit S3
Proteasome subunit p58
Transplantation antigen P91A
Tum-P91A antigen
Gene namesi
Name:Psmd3
Synonyms:P91a, Tstap91a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98858. Psmd3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • proteasome accessory complex Source: UniProtKB
  • proteasome complex Source: MGI
  • proteasome regulatory particle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 53053026S proteasome non-ATPase regulatory subunit 3PRO_0000173817Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei426 – 4261PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP14685.
MaxQBiP14685.
PaxDbiP14685.
PRIDEiP14685.

PTM databases

iPTMnetiP14685.
PhosphoSiteiP14685.
SwissPalmiP14685.

Expressioni

Gene expression databases

BgeeiP14685.
ExpressionAtlasiP14685. baseline and differential.
GenevisibleiP14685. MM.

Interactioni

Subunit structurei

The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively. Interacts with UBQLN1 (via ubiquitin-like domain) (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi204358. 4 interactions.
IntActiP14685. 4 interactions.
STRINGi10090.ENSMUSP00000017365.

Structurei

3D structure databases

ProteinModelPortaliP14685.
SMRiP14685. Positions 158-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini354 – 458105PCIAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi25 – 306Poly-Pro

Sequence similaritiesi

Belongs to the proteasome subunit S3 family.Curated
Contains 1 PCI domain.Curated

Phylogenomic databases

eggNOGiKOG2581. Eukaryota.
ENOG410XS40. LUCA.
GeneTreeiENSGT00490000043406.
HOGENOMiHOG000193909.
HOVERGENiHBG000703.
InParanoidiP14685.
KOiK03033.
OMAiEKKNQDV.
OrthoDBiEOG7JQBNM.
TreeFamiTF106110.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR013586. 26S_Psome_reg_C.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
PF08375. Rpn3_C. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

P14685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQEGSARRR GADKAKPPPG GEQEPPPPAP QDVEMKEEAA AGSGSTGEGD
60 70 80 90 100
GKAAATEHSQ RELDTVTLED IKEHVRQLEK AVSGKEPRFV LRALRMLPST
110 120 130 140 150
SRRLNHYVLY KAVHGFFTSN NATRDFLLPF LEEPMDTEAD LQFRPRTGKA
160 170 180 190 200
ASAPLLPEVE AYLQLLMVIF LMNSKRYKEA QKISDDLMQK ISTQNRRALD
210 220 230 240 250
LVAAKCYYYH ARVYEFLDKL DVVRSFLHAR LRTATLRHDA DGQATLLNLL
260 270 280 290 300
LRNYLHYSLY DQAEKLVSKS VFPEQANNNE WARYLYYTGR IKAIQLEYSE
310 320 330 340 350
ARRTMTNALR KAPQHTAVGF KQTVHKLLIV VELLLGEIPD RLQFRQPSLK
360 370 380 390 400
RSLMPYFLLT QAVRTGNLAK FNQVLDQFGE KFQTDGTYTL IIRLRHNVIK
410 420 430 440 450
TGVRMISLSY SRISLADIAQ KLQLDSPEDA EFIVAKAIRD GVIEASINHE
460 470 480 490 500
KGYVQSKEMI DIYSTREPQL AFHQRISFCL DIHNMSVKAM RFPPKSYNKD
510 520 530
LESAEERRER EQQDLEFAKE MAEDDDDSFP
Length:530
Mass (Da):60,718
Last modified:July 27, 2011 - v3
Checksum:iCAB9C9AA3A0EEC8D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 132AD → H in AAA37241 (PubMed:2568889).Curated
Sequence conflicti196 – 1961R → H in AAA37241 (PubMed:2568889).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25149 Genomic DNA. Translation: AAA37241.1.
AK145488 mRNA. Translation: BAE26466.1.
AK164593 mRNA. Translation: BAE37842.1.
AK165520 mRNA. Translation: BAE38235.1.
AK166683 mRNA. Translation: BAE38942.1.
AK166714 mRNA. Translation: BAE38965.1.
AK167285 mRNA. Translation: BAE39391.1.
AK169690 mRNA. Translation: BAE41307.1.
AL590963 Genomic DNA. Translation: CAM46197.1.
CH466556 Genomic DNA. Translation: EDL16159.1.
BC003197 mRNA. Translation: AAH03197.1.
CCDSiCCDS25359.1.
PIRiI49504.
RefSeqiNP_033465.1. NM_009439.1.
UniGeneiMm.12194.

Genome annotation databases

EnsembliENSMUST00000017365; ENSMUSP00000017365; ENSMUSG00000017221.
GeneIDi22123.
KEGGimmu:22123.
UCSCiuc007lgw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25149 Genomic DNA. Translation: AAA37241.1.
AK145488 mRNA. Translation: BAE26466.1.
AK164593 mRNA. Translation: BAE37842.1.
AK165520 mRNA. Translation: BAE38235.1.
AK166683 mRNA. Translation: BAE38942.1.
AK166714 mRNA. Translation: BAE38965.1.
AK167285 mRNA. Translation: BAE39391.1.
AK169690 mRNA. Translation: BAE41307.1.
AL590963 Genomic DNA. Translation: CAM46197.1.
CH466556 Genomic DNA. Translation: EDL16159.1.
BC003197 mRNA. Translation: AAH03197.1.
CCDSiCCDS25359.1.
PIRiI49504.
RefSeqiNP_033465.1. NM_009439.1.
UniGeneiMm.12194.

3D structure databases

ProteinModelPortaliP14685.
SMRiP14685. Positions 158-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204358. 4 interactions.
IntActiP14685. 4 interactions.
STRINGi10090.ENSMUSP00000017365.

PTM databases

iPTMnetiP14685.
PhosphoSiteiP14685.
SwissPalmiP14685.

Proteomic databases

EPDiP14685.
MaxQBiP14685.
PaxDbiP14685.
PRIDEiP14685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017365; ENSMUSP00000017365; ENSMUSG00000017221.
GeneIDi22123.
KEGGimmu:22123.
UCSCiuc007lgw.1. mouse.

Organism-specific databases

CTDi5709.
MGIiMGI:98858. Psmd3.

Phylogenomic databases

eggNOGiKOG2581. Eukaryota.
ENOG410XS40. LUCA.
GeneTreeiENSGT00490000043406.
HOGENOMiHOG000193909.
HOVERGENiHBG000703.
InParanoidiP14685.
KOiK03033.
OMAiEKKNQDV.
OrthoDBiEOG7JQBNM.
TreeFamiTF106110.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
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-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-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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPsmd3. mouse.
PROiP14685.
SOURCEiSearch...

Gene expression databases

BgeeiP14685.
ExpressionAtlasiP14685. baseline and differential.
GenevisibleiP14685. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR013586. 26S_Psome_reg_C.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
PF08375. Rpn3_C. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the gene of tum- transplantation antigen P91A: the mutated exon encodes a peptide recognized with Ld by cytolytic T cells."
    Lurquin C., van Pel A., Mariame B., de Plaen E., Szikora J.-P., Janssens C., Reddehase M.J., Lejeune J., Boon T.
    Cell 58:293-303(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Kidney, Lung and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPSMD3_MOUSE
AccessioniPrimary (citable) accession number: P14685
Secondary accession number(s): Q3TP95, Q99LL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 136 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.