P28072 (PSB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit beta type-6
EC=3.4.25.1

Alternative name(s):
Macropain delta chain
Multicatalytic endopeptidase complex delta chain
Proteasome delta chain
Proteasome subunit Y

Gene names

Name:	PSMB6
Synonyms:	LMPY, Y

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	239 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 proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. This subunit can be displaced by the equivalent immune-specific subunit PSMB9. Interacts with HIV-1 TAT protein. Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus.
Induction	Down-regulated by IFNG/IFN-gamma (at protein level). Up-regulated in anaplastic thyroid cancer cell lines. Ref.1 Ref.9
Sequence similarities	Belongs to the peptidase T1B family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein polyubiquitination Traceable author statement. Source: Reactome regulation of apoptotic process Traceable author statement. Source: Reactome regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome core complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	endopeptidase activity Non-traceable author statement Ref.1. Source: UniProtKB threonine-type endopeptidase activity 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
	Initiator methionine	1	1	Removed Ref.3
	Propeptide	2 – 34	33	Removed in mature form		PRO_0000026613
	Chain	35 – 239	205	Proteasome subunit beta type-6		PRO_0000026614
Sites
	Active site	35	1	Nucleophile By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3
Natural variations
	Natural variant	107	1	P → A. Corresponds to variant rs2304974 [ dbSNP | Ensembl ].		VAR_020030
Experimental info
	Sequence conflict	145	1	V → G in BAA06098. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P28072 [UniParc]. Last modified May 10, 2002. Version 4. Checksum: 7DF4081DC735930C	FASTA	239	25,358
	10 20 30 40 50 60 MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA DSRTTTGSYI 70 80 90 100 110 120 ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH SIELNEPPLV HTAASLFKEM 130 140 150 160 170 180 CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM GGMMVRQSFA IGGSGSSYIY GYVDATYREG 190 200 210 220 230 MTKEECLQFT ANALALAMER DGSSGGVIRL AAIAESGVER QVLLGDQIPK FAVATLPPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y." Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T., Akioka H., Nothwang H.G., Noda C., Tanaka K., Ichihara A. Science 265:1231-1234(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[3]	Bienvenut W.V., Zebisch A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-9; 54-63 AND 210-230, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[4]	"The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous." DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., Dawson P.A., Slaughter C.A. Biochim. Biophys. Acta 1079:29-38(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-239, PROTEIN SEQUENCE OF 35-75; 80-110 AND 210-233.
[5]	"Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)." Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A. Biochim. Biophys. Acta 1037:178-185(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-60.
[6]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 157-178, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[7]	"Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing." Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P., Hendil K.B., Tanaka K., Ichihara A. FEBS Lett. 343:85-88(1994) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[8]	"Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits." Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E. FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[9]	"Comprehensive gene expression profiling of anaplastic thyroid cancers with cDNA microarray of 25 344 genes." Onda M., Emi M., Yoshida A., Miyamoto S., Akaishi J., Asaka S., Mizutani K., Shimizu K., Nagahama M., Ito K., Tanaka T., Tsunoda T. Endocr. Relat. Cancer 11:843-854(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D29012 mRNA. Translation: BAA06098.1. BC000835 mRNA. Translation: AAH00835.1. X61971 mRNA. Translation: CAA43963.1.
IPI	IPI00000811.
PIR	B54589. S17522.
RefSeq	NP_002789.1. NM_002798.2.
UniGene	Hs.77060.
3D structure databases
ProteinModelPortal	P28072.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28072. 9 interactions.
MINT	MINT-5004163.
STRING	9606.ENSP00000270586.
Protein family/group databases
MEROPS	T01.010.
PTM databases
PhosphoSite	P28072.
Polymorphism databases
DMDM	20532407.
2D gel databases
OGP	P28072.
SWISS-2DPAGE	P28072.
Proteomic databases
PaxDb	P28072.
PeptideAtlas	P28072.
PRIDE	P28072.
Protocols and materials databases
DNASU	5694.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000270586; ENSP00000270586; ENSG00000142507.
GeneID	5694.
KEGG	hsa:5694.
UCSC	uc002fzb.3. human.
Organism-specific databases
CTD	5694.
GeneCards	GC17P004699.
HGNC	HGNC:9543. PSMB6.
HPA	HPA023312.
MIM	600307. gene.
neXtProt	NX_P28072.
PharmGKB	PA33888.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0638.
HOGENOM	HOG000091079.
HOVERGEN	HBG000123.
InParanoid	P28072.
KO	K02738.
OMA	NLGTSIM.
OrthoDB	EOG40CHHX.
PhylomeDB	P28072.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_115566. Cell Cycle. REACT_116125. Disease. REACT_13505. Proteasome mediated degradation of PAK-2p34. REACT_21257. Metabolism of RNA. REACT_21300. Mitotic M-M/G1 phases. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_6900. Immune System. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P28072.
Bgee	P28072.
CleanEx	HS_PSMB6.
Genevestigator	P28072.
GermOnline	ENSG00000142507. Homo sapiens.
Family and domain databases
InterPro	IPR000243. Pept_T1A_subB. IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PRINTS	PR00141. PROTEASOME.
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1944496.
ChiTaRS	PSMB6. human.
GenomeRNAi	5694.
NextBio	22118.
SOURCE	Search...

Entry information

Entry name

PSB6_HUMAN

Accession

Primary (citable) accession number: P28072
Secondary accession number(s): Q96J55

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	May 10, 2002
Last modified:	May 1, 2013
This is version 144 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.