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 13

Gene

Psmd13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

  • meiosis I Source: MGI
  • proteolysis Source: GOC
Complete GO annotation...

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 13
Alternative name(s):
26S proteasome regulatory subunit RPN9
26S proteasome regulatory subunit S11
26S proteasome regulatory subunit p40.5
Gene namesi
Name:Psmd13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1345192. Psmd13.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • membrane 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 – 37637626S proteasome non-ATPase regulatory subunit 13PRO_0000173868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei298 – 2981N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9WVJ2.
MaxQBiQ9WVJ2.
PaxDbiQ9WVJ2.
PRIDEiQ9WVJ2.

PTM databases

iPTMnetiQ9WVJ2.
PhosphoSiteiQ9WVJ2.
SwissPalmiQ9WVJ2.

Expressioni

Gene expression databases

BgeeiQ9WVJ2.
ExpressionAtlasiQ9WVJ2. baseline and differential.
GenevisibleiQ9WVJ2. MM.

Interactioni

Subunit structurei

Component of the PA700 complex.1 Publication

Protein-protein interaction databases

BioGridi204846. 1 interaction.
IntActiQ9WVJ2. 2 interactions.
MINTiMINT-4108941.
STRINGi10090.ENSMUSP00000026560.

Structurei

3D structure databases

ProteinModelPortaliQ9WVJ2.
SMRiQ9WVJ2. Positions 16-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini239 – 33597PCIAdd
BLAST

Sequence similaritiesi

Belongs to the proteasome subunit S11 family.Curated
Contains 1 PCI domain.Curated

Phylogenomic databases

eggNOGiKOG2908. Eukaryota.
ENOG410XPG9. LUCA.
GeneTreeiENSGT00390000001802.
HOGENOMiHOG000216633.
HOVERGENiHBG053740.
InParanoidiQ9WVJ2.
KOiK03039.
OMAiWCGDVKN.
OrthoDBiEOG7C5M8X.
PhylomeDBiQ9WVJ2.
TreeFamiTF105612.

Family and domain databases

InterProiIPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WVJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDVPAFLQQ SQSSGPGQAA VWHRLEELYT KKLWHQLTLE VLDFVQDPCF
60 70 80 90 100
AQGDGLIKLY ENFISEFEHR VNPLSLVEII LHVVRQMTDP NVALTFLEKT
110 120 130 140 150
REKVKSSDEA VILCKTAIGA LKLNIGDLQA TKETIEDVEE MLNNLPGVTS
160 170 180 190 200
VHSRFYDLSS KYYQTIGNHA SYYKDALRFL GCVDIKDLPV SEQQERAFTL
210 220 230 240 250
GLAGLLGEGV FNFGELLMHP VLESLRDTDR QWLIDTLYAF NSGAVDRFQT
260 270 280 290 300
LKCAWGQQPD LAANEAQLLR KIQLLCLMEM TFTRPANHRQ LTFEEIAKSA
310 320 330 340 350
KITVNKVELL VMKALSVGLV RGSIDEVDKR VHMTWVQPRV LDLQQIKGMK
360 370
DRLELWCTDV KSMEMLVEHQ AQDILT
Length:376
Mass (Da):42,809
Last modified:November 1, 1999 - v1
Checksum:i4728059FAD727E1F
GO

Sequence cautioni

The sequence BAE42495.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti358 – 3581T → A in BAE37156 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF107838 mRNA. Translation: AAD43443.1.
AK051078 mRNA. Translation: BAC34519.1.
AK075936 mRNA. Translation: BAC36066.1.
AK081160 mRNA. Translation: BAC38150.1.
AK145654 mRNA. Translation: BAE26568.1.
AK163017 mRNA. Translation: BAE37156.1.
AK167169 mRNA. Translation: BAE39307.1.
AK171504 mRNA. Translation: BAE42495.1. Sequence problems.
CCDSiCCDS21990.1.
RefSeqiNP_036005.1. NM_011875.4.
UniGeneiMm.29760.

Genome annotation databases

EnsembliENSMUST00000026560; ENSMUSP00000026560; ENSMUSG00000025487.
GeneIDi23997.
KEGGimmu:23997.
UCSCiuc009kim.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF107838 mRNA. Translation: AAD43443.1.
AK051078 mRNA. Translation: BAC34519.1.
AK075936 mRNA. Translation: BAC36066.1.
AK081160 mRNA. Translation: BAC38150.1.
AK145654 mRNA. Translation: BAE26568.1.
AK163017 mRNA. Translation: BAE37156.1.
AK167169 mRNA. Translation: BAE39307.1.
AK171504 mRNA. Translation: BAE42495.1. Sequence problems.
CCDSiCCDS21990.1.
RefSeqiNP_036005.1. NM_011875.4.
UniGeneiMm.29760.

3D structure databases

ProteinModelPortaliQ9WVJ2.
SMRiQ9WVJ2. Positions 16-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204846. 1 interaction.
IntActiQ9WVJ2. 2 interactions.
MINTiMINT-4108941.
STRINGi10090.ENSMUSP00000026560.

PTM databases

iPTMnetiQ9WVJ2.
PhosphoSiteiQ9WVJ2.
SwissPalmiQ9WVJ2.

Proteomic databases

EPDiQ9WVJ2.
MaxQBiQ9WVJ2.
PaxDbiQ9WVJ2.
PRIDEiQ9WVJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026560; ENSMUSP00000026560; ENSMUSG00000025487.
GeneIDi23997.
KEGGimmu:23997.
UCSCiuc009kim.1. mouse.

Organism-specific databases

CTDi5719.
MGIiMGI:1345192. Psmd13.

Phylogenomic databases

eggNOGiKOG2908. Eukaryota.
ENOG410XPG9. LUCA.
GeneTreeiENSGT00390000001802.
HOGENOMiHOG000216633.
HOVERGENiHBG053740.
InParanoidiQ9WVJ2.
KOiK03039.
OMAiWCGDVKN.
OrthoDBiEOG7C5M8X.
PhylomeDBiQ9WVJ2.
TreeFamiTF105612.

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

ChiTaRSiPsmd13. mouse.
PROiQ9WVJ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVJ2.
ExpressionAtlasiQ9WVJ2. baseline and differential.
GenevisibleiQ9WVJ2. MM.

Family and domain databases

InterProiIPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the mouse gene for the 26S proteasome subunit p40.5."
    Ting M.C., Chang L.Y.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  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.
    Tissue: Cerebellum and Thymus.
  3. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 59-70, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPSD13_MOUSE
AccessioniPrimary (citable) accession number: Q9WVJ2
Secondary accession number(s): Q3TB19, Q3TR74, Q542R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.