Q9VJJ0 (Q9VJJ0_DROME) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Proteasome subunit beta type RuleBase RU004203
EC=3.4.25.1 RuleBase RU004203

Gene names

ORF Names:

CG17331 EMBL AAM29637.1 FlyBase FBgn0032596, Dmel_CG17331 EMBL AAF53558.1

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity. RuleBase RU000694
Catalytic activity	Cleavage of peptide bonds with very broad specificity. RuleBase RU000694
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 By similarity. RuleBase RU004203
Subcellular location	Cytoplasm. Nucleus By similarity RuleBase RU000694.
Sequence similarities	Belongs to the peptidase T1B family. RuleBase RU004202

Ontologies

Keywords
Cellular component	Nucleus SAAS SAAS016050 Proteasome RuleBase RU000694
Molecular function	Hydrolase Protease Threonine protease RuleBase RU000694
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis involved in cellular protein catabolic process Inferred from electronic annotation. Source: InterPro response to DNA damage stimulus Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9VJJ0 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8C168626D0FA4AD8	FASTA	201	22,482
	10 20 30 40 50 60 METLLGIKGP DFVMLAADTT HARSIIVMKE DQNKIHKVSD SLLISTVGES GDTEQFTEFI 70 80 90 100 110 120 SKNIALYKMR NGYDLSPRES AHFTRKNLAE YLRSRTPYQV FMFVAGYDPN AGPELTFIDY 130 140 150 160 170 180 LANALPVNYA GHGYGAIFAS SIYDRYWHPN ITQAEAYDVF KKCIAEIQKR LVVNLKNFTV 190 200 AVVDKDGVRD LEPISAASLA A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: Berkeley.
[3]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Berkeley EMBL AAM29637.1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014134 Genomic DNA. Translation: AAF53558.1. AY113632 mRNA. Translation: AAM29637.1.
RefSeq	NP_609804.1. NM_135960.3.
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P22141.
ProteinModelPortal	Q9VJJ0.
SMR	Q9VJJ0. Positions 1-197.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VJJ0. 23 interactions.
MINT	MINT-289707.
STRING	Q9VJJ0.
Protein family/group databases
MEROPS	T01.984.
Proteomic databases
PRIDE	Q9VJJ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0080936; FBpp0080490; FBgn0032596.
GeneID	34999.
KEGG	dme:Dmel_CG17331.
NMPDR	fig|7227.3.peg.2664.
UCSC	CG17331-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0032596. CG17331.
Phylogenomic databases
eggNOG	inNOG09305.
GeneTree	EMGT00050000009405.
InParanoid	Q9VJJ0.
OMA	FVMLAAD.
OrthoDB	EOG47PVNZ.
PhylomeDB	Q9VJJ0.
Gene expression databases
Bgee	Q9VJJ0.
Family and domain databases
InterPro	IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
KO	K02734.
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	791321.

Entry information

Entry name

Q9VJJ0_DROME

Accession

Primary (citable) accession number: Q9VJJ0

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)