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O35593 (PSDE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
26S proteasome non-ATPase regulatory subunit 14
EC=3.4.19.-
Alternative name(s):
26S proteasome regulatory subunit RPN11
MAD1
Gene names
Name:Psmd14
Synonyms:Pad1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. The function of the 'Lys-63'-specific deubiquitination of the proteasome is unclear By similarity.

Subunit structure

Component of the 19S regulatory cap of the 26S proteasome.

Sequence similarities

Belongs to the peptidase M67A family. PSMD14 subfamily.

Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentProteasome
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentproteasome complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31031026S proteasome non-ATPase regulatory subunit 14
PRO_0000213953

Regions

Domain26 – 139114MPN
Motif113 – 12614JAMM motif

Sites

Metal binding1131Zinc; catalytic By similarity
Metal binding1151Zinc; catalytic By similarity
Metal binding1261Zinc; catalytic By similarity

Amino acid modifications

Modified residue321Phosphotyrosine By similarity
Modified residue1501Phosphoserine By similarity
Modified residue2241Phosphoserine By similarity

Experimental info

Sequence conflict15 – 173GQG → AR in CAA73514. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35593 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 18ACE876C7682039

FASTA31034,577
        10         20         30         40         50         60 
MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP MEVMGLMLGE 

        70         80         90        100        110        120 
FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK QTGRPEMVVG WYHSHPGFGC 

       130        140        150        160        170        180 
WLSGVDINTQ QSFEALSERA VAVVVDPIQS VKGKVVIDAF RLINANMMVL GHEPRQTTSN 

       190        200        210        220        230        240 
LGHLNKPSIQ ALIHGLNRHY YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH 

       250        260        270        280        290        300 
NESVVKEMLE LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL 

       310 
AAMLDTVVFK

« Hide

References

« Hide 'large scale' references
[1]"The pad1+ gene encodes a subunit of the 26 S proteasome in fission yeast."
Penney M., Wilkinson C., Wallace M., Javerzat J.-P., Ferrell K., Seeger M., Dubiel W., McKay S., Allshire R., Gordon C.
J. Biol. Chem. 273:23938-23945(1998) [PubMed: 9727008] [Abstract]
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. expand/collapse author list , 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: 16141072] [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: 15489334] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00113262.
RefSeqNP_067501.2. NM_021526.2.
UniGeneMm.218198.

3D structure databases

ProteinModelPortalO35593.
SMRO35593. Positions 31-165.
ModBaseSearch...

Protein-protein interaction databases

IntActO35593. 2 interactions.
MINTMINT-4049993.
STRINGO35593.

Protein family/group databases

MEROPSM67.001.

PTM databases

PhosphoSiteO35593.

2D gel databases

PMMA-2DPAGEO35593.
REPRODUCTION-2DPAGEO35593.

Proteomic databases

PRIDEO35593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028278; ENSMUSP00000028278; ENSMUSG00000026914.
ENSMUST00000163857; ENSMUSP00000128069; ENSMUSG00000026914.
GeneID59029.
KEGGmmu:59029.

Organism-specific databases

CTD10213.
MGIMGI:1913284. Psmd14.

Phylogenomic databases

HOGENOMHBG499867.
HOVERGENHBG053742.
InParanoidO35593.
OMAQDPKKHL.
OrthoDBEOG4R23V7.
PhylomeDBO35593.

Gene expression databases

ArrayExpressO35593.
BgeeO35593.
GenevestigatorO35593.
GermOnlineENSMUSG00000026914. Mus musculus.

Family and domain databases

InterProIPR000555. Mov34_MPN_PAD1.
[Graphical view]
KOK03030.
PfamPF01398. Mov34. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio314614.
SOURCESearch...

Entry information

Entry namePSDE_MOUSE
AccessionPrimary (citable) accession number: O35593
Secondary accession number(s): Q3UB50, Q9CZY6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: November 16, 2011
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents