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Protein

26S proteasome non-ATPase regulatory subunit 14

Gene

Psmd14

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

Functioni

Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi113 – 1131Zinc; catalyticBy similarity
Metal bindingi115 – 1151Zinc; catalyticBy similarity
Metal bindingi126 – 1261Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

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-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiM67.A11.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 14 (EC:3.4.19.-)
Alternative name(s):
26S proteasome regulatory subunit RPN11
MAD1
Gene namesi
Name:Psmd14
Synonyms:Pad1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1913284. Psmd14.

Subcellular locationi

GO - Cellular componenti

  • cytosolic proteasome complex Source: Ensembl
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
  • proteasome accessory complex Source: UniProtKB
  • proteasome complex Source: MGI
  • proteasome regulatory particle, lid subcomplex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31031026S proteasome non-ATPase regulatory subunit 14PRO_0000213953Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei150 – 1501PhosphoserineBy similarity
Modified residuei224 – 2241PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO35593.
MaxQBiO35593.
PaxDbiO35593.
PRIDEiO35593.
TopDownProteomicsiO35593.

2D gel databases

REPRODUCTION-2DPAGEO35593.

PTM databases

iPTMnetiO35593.
PhosphoSiteiO35593.
SwissPalmiO35593.

Expressioni

Gene expression databases

BgeeiO35593.
GenevisibleiO35593. MM.

Interactioni

Subunit structurei

Component of the lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. Interacts with TXNL1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRM1Q161862EBI-772796,EBI-954387From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208496. 7 interactions.
IntActiO35593. 45 interactions.
MINTiMINT-4049993.
STRINGi10090.ENSMUSP00000028278.

Chemistry

BindingDBiO35593.

Structurei

3D structure databases

ProteinModelPortaliO35593.
SMRiO35593. Positions 27-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 139114MPNAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi113 – 12614JAMM motifAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M67A family. PSMD14 subfamily.Curated
Contains 1 MPN (JAB/Mov34) domain.Curated

Phylogenomic databases

eggNOGiKOG1555. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00730000111116.
HOGENOMiHOG000183690.
HOVERGENiHBG053742.
InParanoidiO35593.
KOiK03030.
OMAiTQQSFES.
OrthoDBiEOG7T7GTF.
PhylomeDBiO35593.
TreeFamiTF105748.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35593-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP
60 70 80 90 100
MEVMGLMLGE FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK
110 120 130 140 150
QTGRPEMVVG WYHSHPGFGC WLSGVDINTQ QSFEALSERA VAVVVDPIQS
160 170 180 190 200
VKGKVVIDAF RLINANMMVL GHEPRQTTSN LGHLNKPSIQ ALIHGLNRHY
210 220 230 240 250
YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH NESVVKEMLE
260 270 280 290 300
LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL
310
AAMLDTVVFK
Length:310
Mass (Da):34,577
Last modified:August 31, 2004 - v2
Checksum:i18ACE876C7682039
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 173GQG → AR in CAA73514 (PubMed:9727008).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13071 mRNA. Translation: CAA73514.1.
AK012013 mRNA. Translation: BAB27974.1.
AK151104 mRNA. Translation: BAE30114.1.
AK151733 mRNA. Translation: BAE30648.1.
BC003742 mRNA. Translation: AAH03742.1.
CCDSiCCDS38127.1.
RefSeqiNP_067501.2. NM_021526.2.
UniGeneiMm.218198.

Genome annotation databases

EnsembliENSMUST00000028278; ENSMUSP00000028278; ENSMUSG00000026914.
GeneIDi59029.
KEGGimmu:59029.
UCSCiuc008jvc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13071 mRNA. Translation: CAA73514.1.
AK012013 mRNA. Translation: BAB27974.1.
AK151104 mRNA. Translation: BAE30114.1.
AK151733 mRNA. Translation: BAE30648.1.
BC003742 mRNA. Translation: AAH03742.1.
CCDSiCCDS38127.1.
RefSeqiNP_067501.2. NM_021526.2.
UniGeneiMm.218198.

3D structure databases

ProteinModelPortaliO35593.
SMRiO35593. Positions 27-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208496. 7 interactions.
IntActiO35593. 45 interactions.
MINTiMINT-4049993.
STRINGi10090.ENSMUSP00000028278.

Chemistry

BindingDBiO35593.

Protein family/group databases

MEROPSiM67.A11.

PTM databases

iPTMnetiO35593.
PhosphoSiteiO35593.
SwissPalmiO35593.

2D gel databases

REPRODUCTION-2DPAGEO35593.

Proteomic databases

EPDiO35593.
MaxQBiO35593.
PaxDbiO35593.
PRIDEiO35593.
TopDownProteomicsiO35593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028278; ENSMUSP00000028278; ENSMUSG00000026914.
GeneIDi59029.
KEGGimmu:59029.
UCSCiuc008jvc.1. mouse.

Organism-specific databases

CTDi10213.
MGIiMGI:1913284. Psmd14.

Phylogenomic databases

eggNOGiKOG1555. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00730000111116.
HOGENOMiHOG000183690.
HOVERGENiHBG053742.
InParanoidiO35593.
KOiK03030.
OMAiTQQSFES.
OrthoDBiEOG7T7GTF.
PhylomeDBiO35593.
TreeFamiTF105748.

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-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPsmd14. mouse.
NextBioi314614.
PROiO35593.
SOURCEiSearch...

Gene expression databases

BgeeiO35593.
GenevisibleiO35593. MM.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Bone marrow.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 199-208.
    Tissue: Brain.
  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 nameiPSDE_MOUSE
AccessioniPrimary (citable) accession number: O35593
Secondary accession number(s): Q3UB50, Q9CZY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: March 16, 2016
This is version 131 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.