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Protein

26S proteasome non-ATPase regulatory subunit 12

Gene

Psmd12

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.

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 12
Alternative name(s):
26S proteasome regulatory subunit RPN5
26S proteasome regulatory subunit p55
Gene namesi
Name:Psmd12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1914247. Psmd12.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • membrane 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
Initiator methionineiRemoved1 Publication
Chaini2 – 45645526S proteasome non-ATPase regulatory subunit 12PRO_0000173862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei368 – 3681N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9D8W5.
MaxQBiQ9D8W5.
PaxDbiQ9D8W5.
PRIDEiQ9D8W5.

PTM databases

iPTMnetiQ9D8W5.
PhosphoSiteiQ9D8W5.
SwissPalmiQ9D8W5.

Expressioni

Gene expression databases

BgeeiQ9D8W5.
ExpressionAtlasiQ9D8W5. baseline and differential.
GenevisibleiQ9D8W5. MM.

Interactioni

Subunit structurei

Component of the PA700 complex.1 Publication

Protein-protein interaction databases

BioGridi211864. 2 interactions.
IntActiQ9D8W5. 1 interaction.
MINTiMINT-1869795.
STRINGi10090.ENSMUSP00000021063.

Structurei

3D structure databases

ProteinModelPortaliQ9D8W5.
SMRiQ9D8W5. Positions 44-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini237 – 417181PCIAdd
BLAST

Sequence similaritiesi

Belongs to the proteasome subunit p55 family.Curated
Contains 1 PCI domain.Curated

Phylogenomic databases

eggNOGiKOG1498. Eukaryota.
COG5071. LUCA.
GeneTreeiENSGT00730000111110.
HOGENOMiHOG000194265.
HOVERGENiHBG053739.
InParanoidiQ9D8W5.
KOiK03035.
OMAiVAIVKMC.
OrthoDBiEOG7SJD4B.
TreeFamiTF105721.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D8W5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGGSERAD GRIVKMEVDY SATVDQRLPE CEKLAKEGRL QEVIETLLSL
60 70 80 90 100
EKQTRTASDM VSTSRILVAV VKMCYEAKEW DLLNENIMLL SKRRSQLKQA
110 120 130 140 150
VAKMVQQCCT YVEEITDLPV KLRLIDTLRM VTEGKIYVEI ERARLTKTLA
160 170 180 190 200
TIKEQNGDVK EAASILQELQ VETYGSMEKK ERVEFILEQM RLCLAVKDYI
210 220 230 240 250
RTQIISKKIN TKFFQEENTE NLKLKYYNLM IQLDQHEGSY LSICKHYRAI
260 270 280 290 300
YDTPCIQAES DKWQQALKSV VLYVILAPFD NEQSDLVHRI SSDKKLEEIP
310 320 330 340 350
KYKDLLKLFT TMELMRWSTL VEDYGVELRK GSSETPATDV FSSTEEGEKR
360 370 380 390 400
WKDLKSRVVE HNIRIMAKYY TRITMKRMAQ LLDLSVDESE AFLSNLVVNK
410 420 430 440 450
TIFAKVDRLA GVINFQRPKD PNNLLNDWSQ KLNSLMSLVN KTTHLIAKEE

MIHNLQ
Length:456
Mass (Da):52,895
Last modified:July 27, 2011 - v4
Checksum:i5D2CD4B0D5FC283F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831L → H in BAB25140 (PubMed:16141072).Curated
Sequence conflicti207 – 2071K → R in BAB30969 (PubMed:16141072).Curated
Sequence conflicti214 – 2141F → S in BAB25140 (PubMed:16141072).Curated
Sequence conflicti222 – 2221L → M in BAB25140 (PubMed:16141072).Curated
Sequence conflicti377 – 3771R → G in BAB30969 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007619 mRNA. Translation: BAB25140.1.
AK007680 mRNA. Translation: BAB25184.1.
AK009969 mRNA. Translation: BAB26619.1.
AK017843 mRNA. Translation: BAB30969.1.
AK151242 mRNA. Translation: BAE30234.1.
AL683815, AL645687 Genomic DNA. Translation: CAM20679.1.
AL645687, AL683815 Genomic DNA. Translation: CAM25445.1.
CH466558 Genomic DNA. Translation: EDL34331.1.
BC004694 mRNA. Translation: AAH04694.1.
CCDSiCCDS25568.1.
RefSeqiNP_080170.1. NM_025894.2.
UniGeneiMm.491171.

Genome annotation databases

EnsembliENSMUST00000021063; ENSMUSP00000021063; ENSMUSG00000020720.
GeneIDi66997.
KEGGimmu:66997.
UCSCiuc007mar.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007619 mRNA. Translation: BAB25140.1.
AK007680 mRNA. Translation: BAB25184.1.
AK009969 mRNA. Translation: BAB26619.1.
AK017843 mRNA. Translation: BAB30969.1.
AK151242 mRNA. Translation: BAE30234.1.
AL683815, AL645687 Genomic DNA. Translation: CAM20679.1.
AL645687, AL683815 Genomic DNA. Translation: CAM25445.1.
CH466558 Genomic DNA. Translation: EDL34331.1.
BC004694 mRNA. Translation: AAH04694.1.
CCDSiCCDS25568.1.
RefSeqiNP_080170.1. NM_025894.2.
UniGeneiMm.491171.

3D structure databases

ProteinModelPortaliQ9D8W5.
SMRiQ9D8W5. Positions 44-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211864. 2 interactions.
IntActiQ9D8W5. 1 interaction.
MINTiMINT-1869795.
STRINGi10090.ENSMUSP00000021063.

PTM databases

iPTMnetiQ9D8W5.
PhosphoSiteiQ9D8W5.
SwissPalmiQ9D8W5.

Proteomic databases

EPDiQ9D8W5.
MaxQBiQ9D8W5.
PaxDbiQ9D8W5.
PRIDEiQ9D8W5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021063; ENSMUSP00000021063; ENSMUSG00000020720.
GeneIDi66997.
KEGGimmu:66997.
UCSCiuc007mar.1. mouse.

Organism-specific databases

CTDi5718.
MGIiMGI:1914247. Psmd12.

Phylogenomic databases

eggNOGiKOG1498. Eukaryota.
COG5071. LUCA.
GeneTreeiENSGT00730000111110.
HOGENOMiHOG000194265.
HOVERGENiHBG053739.
InParanoidiQ9D8W5.
KOiK03035.
OMAiVAIVKMC.
OrthoDBiEOG7SJD4B.
TreeFamiTF105721.

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

PROiQ9D8W5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8W5.
ExpressionAtlasiQ9D8W5. baseline and differential.
GenevisibleiQ9D8W5. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
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. "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, Embryo, Pancreas and Tongue.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. 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].
  4. "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.
  5. Cited for: IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, ACETYLATION AT ALA-2.
  6. 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 nameiPSD12_MOUSE
AccessioniPrimary (citable) accession number: Q9D8W5
Secondary accession number(s): Q9CQT4, Q9CYB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 107 of the entry and version 4 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.