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

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) [Complete proteome]

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. Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm Potential. Nucleus Potential.
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
Technical term	3D-structure Complete proteome
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	cytoplasm Inferred from direct assay. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB proteasome complex Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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	2	EBI-357745,EBI-1056358
PSMC4	P43686	2	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

1

Removed

Chain

2 – 406

405

26S protease regulatory subunit 8

PRO_0000084721

Regions

Nucleotide binding

190 – 197

8

ATP Potential

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10 Ref.12

Modified residue

222

1

N6-acetyllysine Ref.13

Natural variations

Natural variant

60

1

R → Q in a colorectal cancer sample; somatic mutation. Ref.14

VAR_035901

Natural variant

258

1

R → W: dbSNP rs11543211.

VAR_048119

Experimental info

Sequence conflict

61

1

E → R in BAA07919. Ref.1

Sequence conflict

127 – 128

2

LP → ML in AAB88187. Ref.6

Sequence conflict

266

1

D → S in AAC41735. Ref.2

Sequence conflict

272

1

T → Q in AAC41735. Ref.2

Sequence conflict

300

1

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]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skeletal muscle.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, MASS SPECTROMETRY.
[14]	"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

EMBL
GenBank
DDBJ

D44467 mRNA. Translation: BAA07919.1.
L38810 mRNA. Translation: AAC41735.1.
AK291878 mRNA. Translation: BAF84567.1.
CH471109 Genomic DNA. Translation: EAW94272.1.
BC001932 mRNA. Translation: AAH01932.1.
BC002367 mRNA. Translation: AAH02367.3.
AF035309 mRNA. Translation: AAB88187.1.

IPI

IPI00023919.

PIR

S60343.
S65536.

RefSeq

NP_002796.4.

UniGene

Hs.79387

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KW6	X-ray	2.10	A	318-395	[»]

SMR

P62195. Positions 142-388.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62195. 26 interactions.

STRING

P62195.

PTM databases

PhosphoSite

P62195.

Proteomic databases

PRIDE

P62195.

Genome annotation databases

Ensembl

ENST00000310144; ENSP00000310572; ENSG00000087191; Homo sapiens. [Genome view]

GeneID

5705.

KEGG

hsa:5705.

UCSC

uc002jcb.1. human.

Organism-specific databases

CTD

5705.

GeneCards

GC17P059258.

HGNC

HGNC:9552. PSMC5.

HPA

HPA017871.

MIM

601681. gene.

PharmGKB

PA33897.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06568.

HOGENOM

HBG724153.

HOVERGEN

P62195.

InParanoid

P62195.

OMA

VSLMKVE.

PhylomeDB

P62195.

Enzyme and pathway databases

Reactome

REACT_11045. Signaling by Wnt.
REACT_13. Metabolism of amino acids.
REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6185. HIV Infection.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.

Gene expression databases

ArrayExpress

P62195.

Bgee

P62195.

CleanEx

HS_PSMC5.

Genevestigator

P62195.

GermOnline

ENSG00000087191. Homo sapiens.

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

22166.

SOURCE

Search...

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Entry information

Entry name

PRS8_HUMAN

Accession

Primary (citable) accession number: P62195
Secondary accession number(s): A8K763

P52916

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	February 9, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents