Reviewed, UniProtKB/Swiss-Prot O35593 (PSDE_MOUSE)

Names and origin

Protein names

Recommended name:
    26S proteasome non-ATPase regulatory subunit 14
    EC=3.1.2.15
Alternative name(s):
    26S proteasome regulatory subunit rpn11
    MAD1

Gene names

Name:	Psmd14
Synonyms:	Pad1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
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 process	Ubl conjugation pathway
Cellular component	Proteasome
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	proteasome complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 310	310	26S proteasome non-ATPase regulatory subunit 14		PRO_0000213953
Regions
	Domain	26 – 139	114	MPN
	Motif	113 – 126	14	JAMM motif
Sites
	Metal binding	113	1	Zinc; catalytic By similarity
	Metal binding	115	1	Zinc; catalytic By similarity
	Metal binding	126	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	32	1	Phosphotyrosine By similarity
	Modified residue	150	1	Phosphoserine By similarity
	Modified residue	224	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	15 – 17	3	GQG → AR in CAA73514. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O35593-1 [UniParc]. Last modified August 31, 2004. Version 2. Checksum: 18ACE876C7682039	FASTA	310	34,577
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	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.
IPI	IPI00113262.
RefSeq	NP_067501.2.
UniGene	Mm.218198
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O35593.
PTM databases
PhosphoSite	O35593.
2-D gel databases
PMMA-2DPAGE	O35593.
REPRODUCTION-2DPAGE	O35593.
Proteomic databases
PRIDE	O35593.
Genome annotation databases
Ensembl	ENSMUST00000028278; ENSMUSP00000028278; ENSMUSG00000026914; Mus musculus. [Genome view]
GeneID	59029.
KEGG	mmu:59029.
UCSC	uc008jvc.1. mouse.
Organism-specific databases
CTD	59029.
MGI	MGI:1913284. Psmd14.
Phylogenomic databases
HOGENOM	O35593.
HOVERGEN	O35593.
OMA	QDPKKHL.
Gene expression databases
ArrayExpress	O35593.
Bgee	O35593.
Genevestigator	O35593.
GermOnline	ENSMUSG00000026914. Mus musculus.
Family and domain databases
InterPro	IPR000555. Mov34_MPN_PAD1. [Graphical view]
Pfam	PF01398. Mov34. 1 hit. [Graphical view]
ProDom	PD363422. Mov34-1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	314614.
SOURCE	Search...

Entry information

Entry name

PSDE_MOUSE

Accession

Primary (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 3, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)