Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proteasome subunit beta type

Gene

PSMA4

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

GO - Molecular functioni

GO - Biological processi

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:PSMA4Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation
  • Nucleus SAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation, ProteasomeUniRule annotation

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33878.

PTM / Processingi

Proteomic databases

PaxDbiQ7Z474.
PRIDEiQ7Z474.

Expressioni

Gene expression databases

BgeeiQ7Z474.
GenevisibleiQ7Z474. HS.

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.UniRule annotation

Protein-protein interaction databases

IntActiQ7Z474. 2 interactions.
STRINGi9606.ENSP00000044462.

Structurei

3D structure databases

ProteinModelPortaliQ7Z474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili202 – 23736Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

eggNOGiKOG0178. Eukaryota.
COG0638. LUCA.
HOVERGENiHBG003005.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS51475. PROTEASOME_ALPHA_2. 1 hit.
PS00854. PROTEASOME_BETA_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7Z474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAIGHAGTC LGILANDGVL LAAERRNIHK LLDEVFFSEK IYKLNEDMAC
60 70 80 90 100
SVAGITSDAN VLTNELRLIA QRYLLQYQEP IPCEQLVTAL CDIKQAYTQF
110 120 130 140 150
GGKRPFGVSL LYIGWDKHYG FQLYQSDPSG NYGGWKATCI GNNSAAAVSM
160 170 180 190 200
LKQDYKEGEM TLKSALALAI KVLNKTMDVS KLSAEKVEIA TLTRENGKTV
210 220 230
IRVLKQKEVE QLIKKHEEEE AKAEREKKEK EQKEKDK
Length:237
Mass (Da):26,576
Last modified:October 1, 2003 - v1
Checksum:iEBC3E69EE3ABA658
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC056249 mRNA. Translation: AAH56249.1.
RefSeqiNP_002780.1. NM_002789.4.
UniGeneiHs.251531.

Genome annotation databases

GeneIDi5685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC056249 mRNA. Translation: AAH56249.1.
RefSeqiNP_002780.1. NM_002789.4.
UniGeneiHs.251531.

3D structure databases

ProteinModelPortaliQ7Z474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7Z474. 2 interactions.
STRINGi9606.ENSP00000044462.

Proteomic databases

PaxDbiQ7Z474.
PRIDEiQ7Z474.

Protocols and materials databases

DNASUi5685.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5685.

Organism-specific databases

CTDi5685.
PharmGKBiPA33878.

Phylogenomic databases

eggNOGiKOG0178. Eukaryota.
COG0638. LUCA.
HOVERGENiHBG003005.

Miscellaneous databases

ChiTaRSiPSMA4. human.
GenomeRNAii5685.
NextBioi22078.

Gene expression databases

BgeeiQ7Z474.
GenevisibleiQ7Z474. HS.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS51475. PROTEASOME_ALPHA_2. 1 hit.
PS00854. PROTEASOME_BETA_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported.

Entry informationi

Entry nameiQ7Z474_HUMAN
AccessioniPrimary (citable) accession number: Q7Z474
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2003
Last sequence update: October 1, 2003
Last modified: May 11, 2016
This is version 102 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.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.