26S protease regulatory subunit 8 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P62195 (PRS8_HUMAN)

Last modified November 25, 2008. Version 50. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
    Thyroid hormone receptor-interacting protein 1
      Short name=TRIP1

Gene names

Name:	PSMC5
Synonyms:	SUG1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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, in vitro, with the thyroid hormone receptor (in a thyroid hormone T3-dependent manner) and with retinoid X receptor (RXR) By similarity. Interacts with NDC80. Interacts with PAAF1.
Subcellular location	CytoplasmPotential. NucleusPotential.
Sequence similarities	Belongs to the AAA ATPase family.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of programmed cell death Non-traceable author statement. Source: UniProtKB negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of gene-specific transcription Non-traceable author statement. Source: UniProtKB positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: UniProtKB proteasome complex Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro ATPase activity Ref.1 Traceable author statement. Source: UniProtKB thyrotropin-releasing hormone receptor binding Inferred from physical interaction. Source: UniProtKB transcription cofactor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ERCC3	P19447	1	EBI-357745,EBI-1183307
PAAF1	Q9BRP4	1	EBI-357745,EBI-1056358
PSMC4	P43686	1	EBI-357745,EBI-743997
PSMD10	O75832	1	EBI-357745,EBI-752185
PSMD6	Q15008	1	EBI-357745,EBI-359701

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 406

405

26S protease regulatory subunit 8

PRO_0000084721

Regions

Nucleotide binding

190 – 197

ATP Potential

Amino acid modifications

Modified residue

N-acetylalanine

Natural variations

Natural variant

R → Q in a colorectal cancer sample; somatic mutation.

VAR_035901

Experimental info

Sequence conflict

E → R in BAA07919. Ref.1

Sequence conflict

127 – 128

LP → ML in AAB88187. Ref.4

Sequence conflict

266

D → S in AAC41735. Ref.2

Sequence conflict

272

T → Q in AAC41735. Ref.2

Sequence conflict

300

I → M in AAC41735. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P62195-1 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: 29C6410C4A85A7F7
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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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of a new putative ATPase subunit p45 of the human 26S proteasome, a homolog of yeast transcriptional factor Sug1p." Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N., Slaughter C.A., Noda C., Tanaka K. FEBS Lett. 363:151-156(1995) [PubMed: 7729537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Hepatoma.
[2]	"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor." Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D. Mol. Endocrinol. 9:243-254(1995) [PubMed: 7776974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]. Tissue: Lung carcinoma.
[4]	"Large-scale concatenation cDNA sequencing." Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A. Genome Res. 7:353-358(1997) [PubMed: 9110174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-406. Tissue: Brain.
[5]	"HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins." Chen Y., Sharp Z.D., Lee W.-H. J. Biol. Chem. 272:24081-24087(1997) [PubMed: 9295362] [Abstract] Cited for: INTERACTION WITH NDC80.
[6]	"Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins." Zheng L., Chen Y., Lee W.-H. Mol. Cell. Biol. 19:5417-5428(1999) [PubMed: 10409732] [Abstract] Cited for: INTERACTION WITH NDC80.
[7]	"Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases." Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B. Mol. Cell. Biol. 25:3842-3853(2005) [PubMed: 15831487] [Abstract] Cited for: INTERACTION WITH PAAF1.
[8]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed: 17323924] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[9]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-60.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D44467 mRNA. Translation: BAA07919.1. L38810 mRNA. Translation: AAC41735.1. BC001932 mRNA. Translation: AAH01932.1. BC002367 mRNA. Translation: AAH02367.3. AF035309 mRNA. Translation: AAB88187.1.
PIR	S60343. S65536.
RefSeq	NP_002796.4.
UniGene	Hs.79387
3D structure databases
HSSP	HSSP built from PDB template 1IY0 based on UniProtKB Q9LCZ4.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62195.
PTM databases
PhosphoSite	P62195.
Genome annotation databases
Ensembl	ENSG00000087191. Homo sapiens. [Contig view]
GeneID	5705.
KEGG	hsa:5705.
Organism-specific databases
HGNC	HGNC:9552. PSMC5.
HPA	HPA017871.
MIM	601681. gene.
PharmGKB	PA33897.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P62195.
HOVERGEN	P62195.
Gene expression databases
CleanEx	HS_PSMC5.
GermOnline	ENSG00000087191. Homo sapiens.
Family and domain databases
InterPro	IPR005937. 26S_Psome_P45. IPR003593. AAA+_ATPase_core. IPR003959. AAA_ATPase_core. IPR003960. AAA_ATPase_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	22166.
SOURCE	Search...

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Entry information

Entry name

PRS8_HUMAN

Accession

Primary (citable) accession number: P62195
Secondary accession number(s): O35051

P52916

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	November 25, 2008
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

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Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents