USC-OGP 2-DE database Two-dimensional polyacrylamide gel electrophoresis database

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Searching in 'USC-OGP 2-DE database' for entry matching: Q99436 USC-OGP 2-DE database:  Q99436 Q99436 General information about the entry View entry in simple text format Entry name PSB7_HUMAN Primary accession number Q99436 integrated into USC-OGP 2-DE database on  January 17, 2017 (release 1) 2D Annotations were last modified on January 17, 2017 (version 1) General Annotations were last modified on  April 5, 2017 (version 2) Name and origin of the protein Description RecName: Full=Proteasome subunit beta type-7; EC=3.4.25.1 {ECO:0000269|PubMed:27176742}; AltName: Full=Macropain chain Z; AltName: Full=Multicatalytic endopeptidase complex chain Z; AltName: Full=Proteasome subunit Z; Flags: Precursor;. Gene name Name=PSMB7 Synonyms=Z Annotated species Homo sapiens (Human) [TaxID: 9606] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. References [1]   2D GEL CHARACTERIZATION Author 1., Author 2. Submitted (Mar-2011) to Current 2D PAGE maps for identified proteins How to interpret a protein UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1266: pI=5.84; Mw=28952 Cross-references UniProtKB/Swiss-Prot Q99436; PSB7_HUMAN. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 0.0 Entry name PSB7_HUMAN Primary accession number Q99436 Secondary accession number(s) B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 Sequence was last modified on  May 1, 1997 (version 1) Annotations were last modified on  March 15, 2017 (version 175) Name and origin of the protein Description RecName: Full=Proteasome subunit beta type-7; EC=3.4.25.1 {ECO:0000269|PubMed:27176742}; AltName: Full=Macropain chain Z; AltName: Full=Multicatalytic endopeptidase complex chain Z; AltName: Full=Proteasome subunit Z; Flags: Precursor; Gene name Name=PSMB7 Synonyms=Z Encoded on Name=PSMB7; Synonyms=Z Keywords 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus; Polymorphism; Protease; Proteasome; Reference proteome; Threonine protease; Zymogen. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL D38048; BAA07238.1; -; mRNA EMBL AK303460; BAG64503.1; -; mRNA EMBL AL137846; CAI10873.1; -; Genomic_DNA EMBL CH471090; EAW87582.1; -; Genomic_DNA EMBL CH471090; EAW87583.1; -; Genomic_DNA EMBL BC000509; AAH00509.1; -; mRNA EMBL BC008414; -; NOT_ANNOTATED_CDS; mRNA EMBL BC017116; AAH17116.2; -; mRNA CCDS CCDS6855.1; -. [Q99436-1]; . RefSeq NP_002790.1; NM_002799.3. [Q99436-1]; . UniGene Hs.213470; -; . PDB 4R3O; X-ray; 2.60 A; I/W=44-263 PDB 4R67; X-ray; 2.89 A; I/W/k/y=44-263 PDB 5A0Q; EM; 3.50 A; I/W=44-277 PDB 5GJQ; EM; 4.50 A; b/p=1-277 PDB 5GJR; EM; 3.50 A; b/p=1-277 PDB 5L4G; EM; 4.02 A; 7/8=1-277 PDB 5LE5; X-ray; 1.80 A; H/V=44-277 PDB 5LEX; X-ray; 2.20 A; H/V=44-277 PDB 5LEY; X-ray; 1.90 A; H/V=44-277 PDB 5LEZ; X-ray; 2.19 A; H/V=44-277 PDB 5LF0; X-ray; 2.41 A; H/V=44-277 PDB 5LF1; X-ray; 2.00 A; H/V=44-277 PDB 5LF3; X-ray; 2.10 A; H/V=44-277 PDB 5LF4; X-ray; 1.99 A; H/V=44-277 PDB 5LF6; X-ray; 2.07 A; H/V=44-277 PDB 5LF7; X-ray; 2.00 A; H/V=44-277 PDB 5T0C; EM; 3.80 A; AO/BO=2-277 PDB 5T0G; EM; 4.40 A; O=2-277 PDB 5T0H; EM; 6.80 A; O=2-277 PDB 5T0I; EM; 8.00 A; O=2-277 PDB 5T0J; EM; 8.00 A; O=2-277 PDBsum 4R3O; -; . PDBsum 4R67; -; . PDBsum 5A0Q; -; . PDBsum 5GJQ; -; . PDBsum 5GJR; -; . PDBsum 5L4G; -; . PDBsum 5LE5; -; . PDBsum 5LEX; -; . PDBsum 5LEY; -; . PDBsum 5LEZ; -; . PDBsum 5LF0; -; . PDBsum 5LF1; -; . PDBsum 5LF3; -; . PDBsum 5LF4; -; . PDBsum 5LF6; -; . PDBsum 5LF7; -; . PDBsum 5T0C; -; . PDBsum 5T0G; -; . PDBsum 5T0H; -; . PDBsum 5T0I; -; . PDBsum 5T0J; -; . ProteinModelPortal Q99436; -; . SMR Q99436; -; . BioGrid 111668; 83; . DIP DIP-33843N; -; . IntAct Q99436; 31; . MINT MINT-1351242; -; . STRING 9606.ENSP00000259457; -; . BindingDB Q99436; -; . ChEMBL CHEMBL3347256; -; . MEROPS T01.011; -; . iPTMnet Q99436; -; . PhosphoSitePlus Q99436; -; . BioMuta PSMB7; -; . DMDM 17380263; -; . EPD Q99436; -; . MaxQB Q99436; -; . PaxDb Q99436; -; . PeptideAtlas Q99436; -; . PRIDE Q99436; -; . DNASU 5695; -; . Ensembl ENST00000259457; ENSP00000259457; ENSG00000136930. [Q99436-1]; . GeneID 5695; -; . KEGG hsa:5695; -; . UCSC uc004boj.5; human. [Q99436-1]; . CTD 5695; -; . DisGeNET 5695; -; . GeneCards PSMB7; -; . HGNC HGNC:9544; PSMB7; . HPA HPA052408; -; . HPA HPA054902; -; . MIM 604030; gene; . neXtProt NX_Q99436; -; . OpenTargets ENSG00000136930; -; . PharmGKB PA33889; -; . eggNOG KOG0173; Eukaryota; . eggNOG COG0638; LUCA; . GeneTree ENSGT00510000046533; -; . HOGENOM HOG000182856; -; . HOVERGEN HBG093416; -; . InParanoid Q99436; -; . KO K02739; -; . OMA PFSVPNK; -; . OrthoDB EOG091G0E5S; -; . PhylomeDB Q99436; -; . TreeFam TF106222; -; . Reactome R-HSA-1169091; Activation of NF-kappaB in B cells; . Reactome R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha; . Reactome R-HSA-1236974; ER-Phagosome pathway; . Reactome R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes); . Reactome R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C; . Reactome R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1; . Reactome R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin; . Reactome R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1; . Reactome R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A; . Reactome R-HSA-180534; Vpu mediated degradation of CD4; . Reactome R-HSA-180585; Vif-mediated degradation of APOBEC3G; . Reactome R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21; . Reactome R-HSA-195253; Degradation of beta-catenin by the destruction complex; . Reactome R-HSA-202424; Downstream TCR signaling; . Reactome R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation; . Reactome R-HSA-2467813; Separation of Sister Chromatids; . Reactome R-HSA-2871837; FCERI mediated NF-kB activation; . Reactome R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1; . Reactome R-HSA-350562; Regulation of ornithine decarboxylase (ODC); . Reactome R-HSA-382556; ABC-family proteins mediated transport; . Reactome R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA; . Reactome R-HSA-4608870; Asymmetric localization of PCP proteins; . Reactome R-HSA-4641257; Degradation of AXIN; . Reactome R-HSA-4641258; Degradation of DVL; . Reactome R-HSA-5358346; Hedgehog ligand biogenesis; . Reactome R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD; . Reactome R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling; . Reactome R-HSA-5607764; CLEC7A (Dectin-1) signaling; . Reactome R-HSA-5610780; Degradation of GLI1 by the proteasome; . Reactome R-HSA-5610783; Degradation of GLI2 by the proteasome; . Reactome R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome; . Reactome R-HSA-5632684; Hedgehog 'on' state; . Reactome R-HSA-5658442; Regulation of RAS by GAPs; . Reactome R-HSA-5668541; TNFR2 non-canonical NF-kB pathway; . Reactome R-HSA-5676590; NIK-->noncanonical NF-kB signaling; . Reactome R-HSA-5678895; Defective CFTR causes cystic fibrosis; . Reactome R-HSA-5687128; MAPK6/MAPK4 signaling; . Reactome R-HSA-5689603; UCH proteinases; . Reactome R-HSA-5689880; Ub-specific processing proteases; . Reactome R-HSA-6798695; Neutrophil degranulation; . Reactome R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex; . Reactome R-HSA-68949; Orc1 removal from chromatin; . Reactome R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6; . Reactome R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1; . Reactome R-HSA-69481; G2/M Checkpoints; . Reactome R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A; . Reactome R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint; . Reactome R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis; . Reactome R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation; . ChiTaRS PSMB7; human; . GeneWiki PSMB7; -; . GenomeRNAi 5695; -; . PRO PR:Q99436; -; . Proteomes UP000005640; Chromosome 9; . Bgee ENSG00000136930; -; . CleanEx HS_PSMB7; -; . ExpressionAtlas Q99436; baseline and differential; . Genevisible Q99436; HS; . GO GO:0005829; C:cytosol; IDA:HPA; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; . GO GO:0005654; C:nucleoplasm; IDA:HPA; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0000502; C:proteasome complex; IDA:UniProtKB; . GO GO:0005839; C:proteasome core complex; ISS:UniProtKB; . GO GO:0034774; C:secretory granule lumen; TAS:Reactome; . GO GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW; . GO GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome; . GO GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAP-dependent; TAS:Reactome GO GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome; . GO GO:0000165; P:MAPK cascade; TAS:Reactome; . GO GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome; . GO GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome; . GO GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome; . GO GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome; . GO GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL; . GO GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome; . GO GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome; . GO GO:0016579; P:protein deubiquitination; TAS:Reactome; . GO GO:0000209; P:protein polyubiquitination; TAS:Reactome; . GO GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome; . GO GO:0043488; P:regulation of mRNA stability; TAS:Reactome; . GO GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome; . GO GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome; . GO GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome; . GO GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome; . GO GO:0055085; P:transmembrane transport; TAS:Reactome; . GO GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome; . GO GO:0016032; P:viral process; IEA:UniProtKB-KW; . GO GO:0060071; P:Wnt signaling pathway; planar cell polarity pathway; TAS:Reactome Gene3D 3.60.20.10; -; 1; . InterPro IPR029055; Ntn_hydrolases_N; . InterPro IPR000243; Pept_T1A_subB; . InterPro IPR024689; Proteasome_bsu_C; . InterPro IPR016050; Proteasome_bsu_CS; . InterPro IPR001353; Proteasome_sua/b; . InterPro IPR023333; Proteasome_suB-type; . Pfam PF12465; Pr_beta_C; 1; . Pfam PF00227; Proteasome; 1; . PRINTS PR00141; PROTEASOME; . SUPFAM SSF56235; SSF56235; 1; . PROSITE PS00854; PROTEASOME_BETA_1; 1; . PROSITE PS51476; PROTEASOME_BETA_2; 1; .

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