PSMA8_HUMAN
ID PSMA8_HUMAN Reviewed; 256 AA.
AC Q8TAA3; B0YJ75; Q8IVP4; Q8TA98; Q8TAA2;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Proteasome subunit alpha-type 8;
DE AltName: Full=Proteasome alpha 4 subunit {ECO:0000250|UniProtKB:Q9CWH6};
DE Short=Alpha4s {ECO:0000250|UniProtKB:Q9CWH6};
DE AltName: Full=Proteasome subunit alpha-type 7-like;
GN Name=PSMA8; Synonyms=PSMA7L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Component of the spermatoproteasome, a proteasome
CC specifically found in testis that promotes acetylation-dependent
CC degradation of histones, thereby participating actively to the exchange
CC of histones during spermatogenesis. The proteasome is a protein complex
CC that degrades unneeded or damaged proteins by proteolysis, a chemical
CC reaction that breaks peptide bonds. Required for 20S core proteasome
CC assembly, essential for the degradation of meiotic proteins RAD51 and
CC RPA1 at late prophase I and the progression of meiosis I during
CC spermatogenesis. Localizes to the synaptonemal complex, a 'zipper'-like
CC structure that holds homologous chromosome pairs in synapsis during
CC meiotic prophase I. {ECO:0000250|UniProtKB:Q9CWH6}.
CC -!- SUBUNIT: Component of the outer alpha-ring of the 20S proteasome core
CC which is composed of 28 subunits that are arranged in four stacked
CC rings, resulting in a barrel-shaped structure. The catalytic chamber
CC with the active sites is on the inside of the barrel. Interacts with
CC canonical subunits of the spermatoproteasome, including proteasome
CC activators PSME4 (also called PA200) and PSME3 (also called PA28-
CC gamma). Interacts with proteasome-interacting proteins chaperones,
CC ubiquitin ligases and ubiquitin specific proteases. Interacts with
CC meiotic proteins cyclin dependent kinase CDK1 and the ATPase TRIP13 as
CC well as proteins of the synaptonemal complex SIX6OS1 and SYCE3.
CC {ECO:0000250|UniProtKB:Q9CWH6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CWH6}.
CC Note=Localizes to the central region of the synaptonemal complex.
CC {ECO:0000250|UniProtKB:Q9CWH6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q8TAA3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAA3-2; Sequence=VSP_005285;
CC Name=3;
CC IsoId=Q8TAA3-5; Sequence=VSP_018602;
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; EF445014; ACA06053.1; -; Genomic_DNA.
DR EMBL; AC091021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01214.1; -; Genomic_DNA.
DR EMBL; BC028371; AAH28371.1; -; mRNA.
DR EMBL; BC028686; AAH28686.1; -; mRNA.
DR EMBL; BC042820; AAH42820.1; -; mRNA.
DR CCDS; CCDS32808.1; -. [Q8TAA3-1]
DR CCDS; CCDS45842.1; -. [Q8TAA3-5]
DR CCDS; CCDS45843.1; -. [Q8TAA3-2]
DR RefSeq; NP_001020267.1; NM_001025096.1. [Q8TAA3-5]
DR RefSeq; NP_001020268.1; NM_001025097.1. [Q8TAA3-2]
DR RefSeq; NP_653263.2; NM_144662.2. [Q8TAA3-1]
DR AlphaFoldDB; Q8TAA3; -.
DR SMR; Q8TAA3; -.
DR BioGRID; 126804; 58.
DR IntAct; Q8TAA3; 7.
DR STRING; 9606.ENSP00000311121; -.
DR BindingDB; Q8TAA3; -.
DR ChEMBL; CHEMBL2364701; -.
DR ChEMBL; CHEMBL3831201; -.
DR MEROPS; T01.978; -.
DR iPTMnet; Q8TAA3; -.
DR PhosphoSitePlus; Q8TAA3; -.
DR BioMuta; PSMA8; -.
DR DMDM; 108936006; -.
DR EPD; Q8TAA3; -.
DR jPOST; Q8TAA3; -.
DR MassIVE; Q8TAA3; -.
DR MaxQB; Q8TAA3; -.
DR PaxDb; Q8TAA3; -.
DR PeptideAtlas; Q8TAA3; -.
DR PRIDE; Q8TAA3; -.
DR ProteomicsDB; 73844; -. [Q8TAA3-1]
DR ProteomicsDB; 73845; -. [Q8TAA3-2]
DR ProteomicsDB; 73846; -. [Q8TAA3-5]
DR Antibodypedia; 22107; 75 antibodies from 23 providers.
DR DNASU; 143471; -.
DR Ensembl; ENST00000308268.10; ENSP00000311121.6; ENSG00000154611.15. [Q8TAA3-1]
DR Ensembl; ENST00000343848.10; ENSP00000345584.6; ENSG00000154611.15. [Q8TAA3-2]
DR Ensembl; ENST00000415576.7; ENSP00000409284.2; ENSG00000154611.15. [Q8TAA3-5]
DR GeneID; 143471; -.
DR KEGG; hsa:143471; -.
DR MANE-Select; ENST00000415576.7; ENSP00000409284.2; NM_001025096.2; NP_001020267.1. [Q8TAA3-5]
DR UCSC; uc002kvo.4; human. [Q8TAA3-1]
DR CTD; 143471; -.
DR DisGeNET; 143471; -.
DR GeneCards; PSMA8; -.
DR HGNC; HGNC:22985; PSMA8.
DR HPA; ENSG00000154611; Tissue enriched (testis).
DR MIM; 617841; gene.
DR neXtProt; NX_Q8TAA3; -.
DR OpenTargets; ENSG00000154611; -.
DR PharmGKB; PA134969470; -.
DR VEuPathDB; HostDB:ENSG00000154611; -.
DR eggNOG; KOG0183; Eukaryota.
DR GeneTree; ENSGT00940000160354; -.
DR HOGENOM; CLU_035750_4_0_1; -.
DR InParanoid; Q8TAA3; -.
DR OMA; RLFHTEP; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; Q8TAA3; -.
DR TreeFam; TF106212; -.
DR PathwayCommons; Q8TAA3; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q8TAA3; -.
DR BioGRID-ORCS; 143471; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; PSMA8; human.
DR GenomeRNAi; 143471; -.
DR Pharos; Q8TAA3; Tdark.
DR PRO; PR:Q8TAA3; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q8TAA3; protein.
DR Bgee; ENSG00000154611; Expressed in right testis and 43 other tissues.
DR ExpressionAtlas; Q8TAA3; baseline and differential.
DR Genevisible; Q8TAA3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0060631; P:regulation of meiosis I; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Differentiation; Nucleus; Proteasome;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..256
FT /note="Proteasome subunit alpha-type 8"
FT /id="PRO_0000124149"
FT VAR_SEQ 40..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005285"
FT VAR_SEQ 77..82
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018602"
FT CONFLICT 212
FT /note="K -> R (in Ref. 4; AAH28371/AAH28686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 28530 MW; 6DD04535A98BE44A CRC64;
MASRYDRAIT VFSPDGHLFQ VEYAQEAVKK GSTAVGIRGT NIVVLGVEKK SVAKLQDERT
VRKICALDDH VCMAFAVLTI FIGLTADARV VINRARVECQ SHKLTVEDPV TVEYITRFIA
TLKQKYTQSN GRRPFGISAL IVGFDDDGIS RLYQTDPSGT YHAWKANAIG RSAKTVREFL
EKNYTEDAIA SDSEAIKLAI KALLEVVQSG GKNIELAIIR RNQPLKMFSA KEVELYVTEI
EKEKEEAEKK KSKKSV
