26S protease regulatory subunit S10B

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Reviewed, UniProtKB/Swiss-Prot P62333 (PRS10_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 S10B
Alternative name(s):
    Proteasome 26S subunit ATPase 6
    Proteasome subunit p42

Gene names

Name:	PSMC6
Synonyms:	SUG2

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	389 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	Found in the multi-protein complexes: the 26S proteasome (formed from the 20S proteasome and PA700), and the modulator. PA700 consists of 28 subunits arranged to form a cylinder-shaped complex by four stacked rings, each containing seven subunits. Interacts with PAAF1.
Subcellular location	CytoplasmBy similarity. NucleusBy similarity.
Sequence similarities	Belongs to the AAA ATPase family.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
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 Traceable author statement. Source: UniProtKB protein binding, bridging Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
PAAF1	Q9BRP4	1	EBI-357669,EBI-1056358
PSMD10	O75832	1	EBI-357669,EBI-752185
PSMD6	Q15008	1	EBI-357669,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 – 389

388

26S protease regulatory subunit S10B

PRO_0000084732

Regions

Nucleotide binding

174 – 181

ATP Potential

Amino acid modifications

Modified residue

N-acetylalanine

Modified residue

207

Phosphotyrosine

Experimental info

Sequence conflict

276

I → T in BAA11338. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P62333-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B26421295742CACD
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FASTA

389

44,173

        10         20         30         40         50         60 
MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV 

        70         80         90        100        110        120 
LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY 

       130        140        150        160        170        180 
NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK 

       190        200        210        220        230        240 
TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG 

       250        260        270        280        290        300 
RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH 

       310        320        330        340        350        360 
IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA GMFAIRADHD 

       370        380 
FVVQEDFMKA VRKVADSKKL ESKLDYKPV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of p42, a shared subunit of two proteasome regulatory proteins, reveals a novel member of the AAA protein family." Fujiwara T., Watanabe T.K., Tanaka K., Slaughter C.A., Demartino G.N. FEBS Lett. 387:184-188(1996) [PubMed: 8674546] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Aorta.
[2]	"Human SUG2." Li Y., Benezra R. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: Urinary bladder.
[6]	"Identification, purification, and characterization of a PA700-dependent activator of the proteasome." Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X., Hisamatsu H., Tanaka K., Slaughter C.A. J. Biol. Chem. 271:3112-3118(1996) [PubMed: 8621709] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[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]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207, MASS SPECTROMETRY.

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Cross-references

Sequence databases
	D78275 mRNA. Translation: BAA11338.1. AF006305 mRNA. Translation: AAB61616.1. BT006843 mRNA. Translation: AAP35489.1. CR456709 mRNA. Translation: CAG32990.1. BC005390 mRNA. Translation: AAH05390.1.
PIR	S71316.
RefSeq	NP_002797.3.
UniGene	Hs.156171
3D structure databases
HSSP	HSSP built from PDB template 1IM2 based on UniProtKB P43773.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62333.
PTM databases
PhosphoSite	P62333.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00021926.
Proteomic databases
PeptideAtlas	P62333.
Genome annotation databases
Ensembl	ENSG00000100519. Homo sapiens. [Contig view]
GeneID	5706.
KEGG	hsa:5706.
Organism-specific databases
H-InvDB	HIX0011661. HIX0034665.
HGNC	HGNC:9553. PSMC6.
MIM	602708. gene.
PharmGKB	PA33898.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P62333.
HOVERGEN	P62333.
Enzyme and pathway databases
Reactome	REACT_11045. Signaling by Wnt. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. 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
CleanEx	HS_PSMC6.
GermOnline	ENSG00000100519. 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
LinkHub	P62333.
NextBio	22170.
SOURCE	Search...

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Entry information

Entry name

PRS10_HUMAN

Accession

Primary (citable) accession number: P62333
Secondary accession number(s): P49719, Q6IBU3, Q92524

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel 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