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: P06899 USC-OGP 2-DE database:  P06899 P06899 General information about the entry View entry in simple text format Entry name H2B1J_HUMAN Primary accession number P06899 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=Histone H2B type 1-J; AltName: Full=Histone H2B.1; AltName: Full=Histone H2B.r; Short=H2B/r;. Gene name Name=HIST1H2BJ Synonyms=H2BFR 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-1331: pI=5.13; Mw=16684 Cross-references UniProtKB/Swiss-Prot P06899; H2B1J_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 H2B1J_HUMAN Primary accession number P06899 Secondary accession number(s) B2R4J4 O60816 Sequence was last modified on  January 23, 2007 (version 3) Annotations were last modified on  March 15, 2017 (version 170) Name and origin of the protein Description RecName: Full=Histone H2B type 1-J; AltName: Full=Histone H2B.1; AltName: Full=Histone H2B.r; Short=H2B/r; Gene name Name=HIST1H2BJ Synonyms=H2BFR Encoded on Name=HIST1H2BJ; Synonyms=H2BFR Keywords 3D-structure; Acetylation; Antibiotic; Antimicrobial; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL X00088; CAA24950.1; -; Genomic_DNA EMBL AF531293; AAN06693.1; -; Genomic_DNA EMBL AK311849; BAG34791.1; -; mRNA EMBL AL021807; CAA16949.1; -; Genomic_DNA EMBL CH471081; EAX03080.1; -; Genomic_DNA CCDS CCDS4618.1; -; . PIR A26318; HSHUB1; . PIR S65409; S65409; . RefSeq NP_066402.2; NM_021058.3; . UniGene Hs.591807; -; . UniGene Hs.656567; -; . PDB 2RVQ; NMR; -; D=1-126 PDB 3A6N; X-ray; 2.70 A; D/H=1-126 PDB 3AFA; X-ray; 2.50 A; D/H=1-126 PDB 3AN2; X-ray; 3.60 A; D/H=1-126 PDB 3AV1; X-ray; 2.50 A; D/H=1-126 PDB 3AV2; X-ray; 2.80 A; D/H=1-126 PDB 3AYW; X-ray; 2.90 A; D/H=1-126 PDB 3AZE; X-ray; 3.00 A; D/H=1-126 PDB 3AZF; X-ray; 2.70 A; D/H=1-126 PDB 3AZG; X-ray; 2.40 A; D/H=1-126 PDB 3AZH; X-ray; 3.49 A; D/H=1-126 PDB 3AZI; X-ray; 2.70 A; D/H=1-126 PDB 3AZJ; X-ray; 2.89 A; D/H=1-126 PDB 3AZK; X-ray; 3.20 A; D/H=1-126 PDB 3AZL; X-ray; 2.70 A; D/H=1-126 PDB 3AZM; X-ray; 2.89 A; D/H=1-126 PDB 3AZN; X-ray; 3.00 A; D/H=1-126 PDB 3W96; X-ray; 3.00 A; D/H=1-126 PDB 3W97; X-ray; 3.20 A; D/H=26-126 PDB 3W98; X-ray; 3.42 A; D/H=1-126 PDB 3W99; X-ray; 3.00 A; D/H=1-126 PDB 3WA9; X-ray; 3.07 A; D/H=1-126 PDB 3WAA; X-ray; 3.20 A; D/H=1-126 PDB 3WTP; X-ray; 2.67 A; D/H=1-126 PDB 4CAY; X-ray; 1.48 A; B=31-126 PDB 4YM5; X-ray; 4.00 A; D/H=1-126 PDB 4YM6; X-ray; 3.51 A; D/H=1-126 PDB 4Z5T; X-ray; 2.80 A; D/H=1-126 PDB 5AV5; X-ray; 2.40 A; D/H=1-126 PDB 5AV6; X-ray; 2.20 A; D/H=1-126 PDB 5AV8; X-ray; 2.20 A; D/H=1-126 PDB 5AV9; X-ray; 2.20 A; D/H=1-126 PDB 5AVB; X-ray; 2.40 A; D/H=1-126 PDB 5AVC; X-ray; 2.40 A; D/H=1-126 PDB 5AY8; X-ray; 2.80 A; D/H=1-126 PDB 5B0Y; X-ray; 2.56 A; D/H=1-126 PDB 5B0Z; X-ray; 1.99 A; D/H=1-126 PDB 5B24; X-ray; 3.60 A; D/H=1-126 PDB 5B2I; X-ray; 3.00 A; D/H=1-126 PDB 5B2J; X-ray; 2.60 A; D/H=1-126 PDB 5B31; X-ray; 2.20 A; D/H=1-126 PDB 5B32; X-ray; 2.35 A; D/H=1-126 PDB 5B33; X-ray; 2.92 A; D/H=1-126 PDB 5B40; X-ray; 3.33 A; D/H=1-126 PDB 5CPI; X-ray; 2.90 A; D/H=1-126 PDB 5CPJ; X-ray; 3.15 A; D/H=1-126 PDB 5CPK; X-ray; 2.63 A; D/H=1-126 PDB 5FUG; X-ray; 2.70 A; B/E/H/K=31-126 PDBsum 2RVQ; -; . PDBsum 3A6N; -; . PDBsum 3AFA; -; . PDBsum 3AN2; -; . PDBsum 3AV1; -; . PDBsum 3AV2; -; . PDBsum 3AYW; -; . PDBsum 3AZE; -; . PDBsum 3AZF; -; . PDBsum 3AZG; -; . PDBsum 3AZH; -; . PDBsum 3AZI; -; . PDBsum 3AZJ; -; . PDBsum 3AZK; -; . PDBsum 3AZL; -; . PDBsum 3AZM; -; . PDBsum 3AZN; -; . PDBsum 3W96; -; . PDBsum 3W97; -; . PDBsum 3W98; -; . PDBsum 3W99; -; . PDBsum 3WA9; -; . PDBsum 3WAA; -; . PDBsum 3WTP; -; . PDBsum 4CAY; -; . PDBsum 4YM5; -; . PDBsum 4YM6; -; . PDBsum 4Z5T; -; . PDBsum 5AV5; -; . PDBsum 5AV6; -; . PDBsum 5AV8; -; . PDBsum 5AV9; -; . PDBsum 5AVB; -; . PDBsum 5AVC; -; . PDBsum 5AY8; -; . PDBsum 5B0Y; -; . PDBsum 5B0Z; -; . PDBsum 5B24; -; . PDBsum 5B2I; -; . PDBsum 5B2J; -; . PDBsum 5B31; -; . PDBsum 5B32; -; . PDBsum 5B33; -; . PDBsum 5B40; -; . PDBsum 5CPI; -; . PDBsum 5CPJ; -; . PDBsum 5CPK; -; . PDBsum 5FUG; -; . ProteinModelPortal P06899; -; . SMR P06899; -; . BioGrid 114460; 26; . DIP DIP-421N; -; . IntAct P06899; 7; . MINT MINT-4822927; -; . STRING 9606.ENSP00000342886; -; . iPTMnet P06899; -; . PhosphoSitePlus P06899; -; . SwissPalm P06899; -; . BioMuta HIST1H2BJ; -; . DMDM 7404367; -; . EPD P06899; -; . MaxQB P06899; -; . PaxDb P06899; -; . PeptideAtlas P06899; -; . PRIDE P06899; -; . TopDownProteomics P06899; -; . Ensembl ENST00000339812; ENSP00000342886; ENSG00000124635; . Ensembl ENST00000607124; ENSP00000476136; ENSG00000124635; . GeneID 8970; -; . KEGG hsa:8970; -; . UCSC uc003niv.4; human; . CTD 8970; -; . DisGeNET 8970; -; . GeneCards HIST1H2BJ; -; . HGNC HGNC:4761; HIST1H2BJ; . HPA HPA042205; -; . HPA HPA043013; -; . HPA HPA048671; -; . MIM 615044; gene; . neXtProt NX_P06899; -; . OpenTargets ENSG00000124635; -; . PharmGKB PA29136; -; . eggNOG KOG1744; Eukaryota; . eggNOG ENOG4111NV5; LUCA; . GeneTree ENSGT00870000136414; -; . HOGENOM HOG000231213; -; . HOVERGEN HBG007774; -; . InParanoid P06899; -; . KO K11252; -; . OMA CCHIYAS; -; . OrthoDB EOG091G0XGD; -; . PhylomeDB P06899; -; . TreeFam TF300212; -; . Reactome R-HSA-1221632; Meiotic synapsis; . Reactome R-HSA-171306; Packaging Of Telomere Ends; . Reactome R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex; . Reactome R-HSA-212300; PRC2 methylates histones and DNA; . Reactome R-HSA-2299718; Condensation of Prophase Chromosomes; . Reactome R-HSA-2559580; Oxidative Stress Induced Senescence; . Reactome R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP); . Reactome R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence; . Reactome R-HSA-3214815; HDACs deacetylate histones; . Reactome R-HSA-3214847; HATs acetylate histones; . Reactome R-HSA-427359; SIRT1 negatively regulates rRNA Expression; . Reactome R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression; . Reactome R-HSA-427413; NoRC negatively regulates rRNA expression; . Reactome R-HSA-5250924; B-WICH complex positively regulates rRNA expression; . Reactome R-HSA-5334118; DNA methylation; . Reactome R-HSA-5578749; Transcriptional regulation by small RNAs; . Reactome R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis; . Reactome R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3; . Reactome R-HSA-5689880; Ub-specific processing proteases; . Reactome R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; . Reactome R-HSA-5693571; Nonhomologous End-Joining (NHEJ); . Reactome R-HSA-5693607; Processing of DNA double-strand break ends; . Reactome R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere; . Reactome R-HSA-69473; G2/M DNA damage checkpoint; . Reactome R-HSA-73728; RNA Polymerase I Promoter Opening; . Reactome R-HSA-73777; RNA Polymerase I Chain Elongation; . Reactome R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins; . Reactome R-HSA-912446; Meiotic recombination; . Reactome R-HSA-977225; Amyloid fiber formation; . EvolutionaryTrace P06899; -; . GeneWiki HIST1H2BJ; -; . GenomeRNAi 8970; -; . PRO PR:P06899; -; . Proteomes UP000005640; Chromosome 6; . Bgee ENSG00000124635; -; . CleanEx HS_HIST1H2BJ; -; . ExpressionAtlas P06899; baseline and differential; . GO GO:0005829; C:cytosol; IDA:HPA; . GO GO:0005615; C:extracellular space; IDA:UniProtKB; . GO GO:0005654; C:nucleoplasm; IDA:HPA; . GO GO:0000786; C:nucleosome; NAS:UniProtKB; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0003677; F:DNA binding; NAS:UniProtKB; . GO GO:0019731; P:antibacterial humoral response; IDA:UniProtKB; . GO GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB; . GO GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB; . GO GO:0006334; P:nucleosome assembly; NAS:UniProtKB; . GO GO:0016567; P:protein ubiquitination; TAS:Reactome; . Gene3D 1.10.20.10; -; 1; . InterPro IPR009072; Histone-fold; . InterPro IPR007125; Histone_H2A/H2B/H3; . InterPro IPR000558; Histone_H2B; . PANTHER PTHR23428; PTHR23428; 1; . Pfam PF00125; Histone; 1; . PRINTS PR00621; HISTONEH2B; . SMART SM00427; H2B; 1; . SUPFAM SSF47113; SSF47113; 1; . PROSITE PS00357; HISTONE_H2B; 1; .

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