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Q6IAT9

- Q6IAT9_HUMAN

UniProt

Q6IAT9 - Q6IAT9_HUMAN

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Protein

Proteasome subunit beta type

Gene

PSMB6

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli

Functioni

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.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine proteaseUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta typeUniRule annotation (EC:3.4.25.1UniRule annotation)
Gene namesi
Name:PSMB6Imported
ORF Names:hCG_32695Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation. Nucleus UniRule annotationSAAS annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation, ProteasomeUniRule annotationImported

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33888.

Expressioni

Gene expression databases

ExpressionAtlasiQ6IAT9. baseline and differential.

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ6IAT9.
SMRiQ6IAT9. Positions 35-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000046484.
HOVERGENiHBG000123.
KOiK02738.
OMAiTSIMAVQ.
PhylomeDBiQ6IAT9.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6IAT9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA
60 70 80 90 100
DSRTTTGSYI ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH
110 120 130 140 150
SIELNEPPLV HTAASLFKEM CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM
160 170 180 190 200
GGMMVRQSFA IGGSGSSYIY GYVDATYREG MTKEECLQFT ANALALAMER
210 220 230
DGSSGGVIRL AAIAESGVER QVLLGDQIPK FAVATLPPA
Length:239
Mass (Da):25,358
Last modified:May 10, 2005 - v1
Checksum:i7DF4081DC735930C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT009809 mRNA. Translation: AAP88811.1.
AK311768 mRNA. Translation: BAG34711.1.
CR457065 mRNA. Translation: CAG33346.1.
CH471108 Genomic DNA. Translation: EAW90407.1.
RefSeqiNP_002789.1. NM_002798.2.
UniGeneiHs.77060.

Genome annotation databases

GeneIDi5694.
KEGGihsa:5694.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT009809 mRNA. Translation: AAP88811.1 .
AK311768 mRNA. Translation: BAG34711.1 .
CR457065 mRNA. Translation: CAG33346.1 .
CH471108 Genomic DNA. Translation: EAW90407.1 .
RefSeqi NP_002789.1. NM_002798.2.
UniGenei Hs.77060.

3D structure databases

ProteinModelPortali Q6IAT9.
SMRi Q6IAT9. Positions 35-236.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

DNASUi 5694.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5694.
KEGGi hsa:5694.

Organism-specific databases

CTDi 5694.
PharmGKBi PA33888.

Phylogenomic databases

GeneTreei ENSGT00510000046484.
HOVERGENi HBG000123.
KOi K02738.
OMAi TSIMAVQ.
PhylomeDBi Q6IAT9.

Miscellaneous databases

ChiTaRSi PSMB6. human.
GenomeRNAii 5694.
NextBioi 22118.

Gene expression databases

ExpressionAtlasi Q6IAT9. baseline and differential.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE.
  3. "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.
  4. Cited for: NUCLEOTIDE SEQUENCE.
  5. "NEDO functional analysis of protein and research application project."
    Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: TongueImported.

Entry informationi

Entry nameiQ6IAT9_HUMAN
AccessioniPrimary (citable) accession number: Q6IAT9
Entry historyi
Integrated into UniProtKB/TrEMBL: May 10, 2005
Last sequence update: May 10, 2005
Last modified: October 29, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny 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.