Reviewed, UniProtKB/Swiss-Prot P62196 (PRS8_MOUSE)

Names and origin

Protein names

Recommended name:
    26S protease regulatory subunit 8
Alternative name(s):
    Proteasome 26S subunit ATPase 5
    Proteasome subunit p45
    p45/SUG
      Short name=mSUG1

Gene names

Name:	Psmc5
Synonyms:	Sug1

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	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
Subunit structure	Interacts with NDC80. Interacts with PAAF1 By similarity. Interacts, in vitro, with the thyroid hormone receptor (in a thyroid hormone T3-dependent manner) and with retinoid X receptor (RXR).
Subcellular location	Cytoplasm Potential. Nucleus Potential.
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Gene Ontology (GO)
Biological process	negative regulation of transcription Inferred from direct assay. Source: MGI proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from sequence or structural similarity. Source: UniProtKB proteasome complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro thyrotropin-releasing hormone receptor binding Inferred from sequence or structural similarity. Source: UniProtKB transcription factor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERCC3	P19447	5	EBI-357713,EBI-1183307	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 406	405	26S protease regulatory subunit 8		PRO_0000084722
Regions
	Nucleotide binding	190 – 197	8	ATP Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
Experimental info
	Sequence conflict	375	1	R → G in BAB26990. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P62196-1 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: 29C6410C4A85A7F7	FASTA	406	45,626
	10 20 30 40 50 60 MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR 70 80 90 100 110 120 EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS 130 140 150 160 170 180 YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI 190 200 210 220 230 240 AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE 250 260 270 280 290 300 HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI 310 320 330 340 350 360 LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK 370 380 390 400 GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1." Vom Baur E., Zechel C., Heery D., Heine M.J., Garnier J.-M., Vivat V., le Douarin B., Gronemeyer H., Chambon P., Losson R. EMBO J. 15:110-124(1996) [PubMed: 8598193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NUCLEAR RECEPTORS.
[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: Embryonic stem cell and Muellerian duct.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z54219 mRNA. Translation: CAA90961.1. AK010505 mRNA. Translation: BAB26990.1. AK135451 mRNA. Translation: BAE22539.1. AK145703 mRNA. Translation: BAE26599.1.
IPI	IPI00135640.
PIR	S61923.
RefSeq	NP_032976.1.
UniGene	Mm.272361
3D structure databases
HSSP	HSSP built from PDB template 1IY0 based on UniProtKB Q9LCZ4.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62196. 2 interactions.
PTM databases
PhosphoSite	P62196.
2-D gel databases
REPRODUCTION-2DPAGE	P62196.
Proteomic databases
PRIDE	P62196.
Genome annotation databases
Ensembl	ENSMUSG00000020708. Mus musculus. [Contig view]
GeneID	19184.
KEGG	mmu:19184.
Organism-specific databases
MGI	MGI:105047. Psmc5.
Phylogenomic databases
HOVERGEN	P62196.
OMA	P62196. LAVAKVM.
Gene expression databases
Bgee	P62196.
GermOnline	ENSMUSG00000020708. Mus musculus.
Family and domain databases
InterPro	IPR005937. 26S_Psome_P45. IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. [Graphical view]
Pfam	PF00004. AAA. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
TIGRFAMs	TIGR01242. 26Sp45. 1 hit.
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	295882.
SOURCE	Search...

Entry information

Entry name

PRS8_MOUSE

Accession

Primary (citable) accession number: P62196
Secondary accession number(s): O35051 , P47210, P52915, P52916, Q3UL51, Q9CWN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)