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USC-OGP 2-DE database

Two-dimensional polyacrylamide gel electrophoresis database


USC-OGP 2-DE database 
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Searching in 'USC-OGP 2-DE database' for entry matching: Q16778




USC-OGP 2-DE database:  Q16778


Q16778


General information about the entry
View entry in simple text format
Entry nameH2B2E_HUMAN
Primary accession numberQ16778
integrated into USC-OGP 2-DE database on January 17, 2017 (release 1)
2D Annotations were last modified onJanuary 17, 2017 (version 1)
General Annotations were last modified on April 5, 2017 (version 2)
Name and origin of the protein
DescriptionRecName: Full=Histone H2B type 2-E; AltName: Full=Histone H2B-GL105; AltName: Full=Histone H2B.q; Short=H2B/q;.
Gene nameName=HIST2H2BE
Synonyms=H2BFQ
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; 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)
UVEAL_MELANOMA_3-10
  map experimental info
 
UVEAL_MELANOMA_3-10

MAP LOCATIONS:
pI=5.13; Mw=16684

Cross-references
UniProtKB/Swiss-ProtQ16778; H2B2E_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 nameH2B2E_HUMAN
Primary accession numberQ16778
Secondary accession number(s) A3KMC7 A8K110 Q4KMY1 Q5QNX0 Q9UE88
Sequence was last modified on January 23, 2007 (version 3)
Annotations were last modified on March 15, 2017 (version 168)
Name and origin of the protein
DescriptionRecName: Full=Histone H2B type 2-E; AltName: Full=Histone H2B-GL105; AltName: Full=Histone H2B.q; Short=H2B/q;
Gene nameName=HIST2H2BE
Synonyms=H2BFQ
Encoded onName=HIST2H2BE; Synonyms=H2BFQ
Keywords3D-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
EMBLX57985; CAA41051.1; -; Genomic_DNA
EMBLAY131979; AAN59961.1; -; Genomic_DNA
EMBLCR541895; CAG46693.1; -; mRNA
EMBLAK289725; BAF82414.1; -; mRNA
EMBLAL591493; CAI12568.1; -; Genomic_DNA
EMBLCH471121; EAW53605.1; -; Genomic_DNA
EMBLBC005827; AAH05827.1; -; mRNA
EMBLBC069193; AAH69193.1; -; mRNA
EMBLBC096121; AAH96121.1; -; mRNA
EMBLBC098112; AAH98112.1; -; mRNA
EMBLBC098289; AAH98289.1; -; mRNA
EMBLBC107084; AAI07085.1; -; mRNA
EMBLBC107085; AAI07086.1; -; mRNA
EMBLM60756; AAA63192.1; -; mRNA
CCDSCCDS936.1; -; .
PIRI37467; I37467; .
PIRS65409; S65409; .
RefSeqNP_003519.1; NM_003528.2; .
UniGeneHs.2178; -; .
PDB4NFT; X-ray; 2.61 A; A/B/C/D=34-126
PDBsum4NFT; -; .
ProteinModelPortalQ16778; -; .
SMRQ16778; -; .
BioGrid113945; 122; .
DIPDIP-39324N; -; .
IntActQ16778; 16; .
MINTMINT-1461208; -; .
STRING9606.ENSP00000358151; -; .
iPTMnetQ16778; -; .
PhosphoSitePlusQ16778; -; .
SwissPalmQ16778; -; .
BioMutaHIST2H2BE; -; .
DMDM7387736; -; .
EPDQ16778; -; .
MaxQBQ16778; -; .
PaxDbQ16778; -; .
PeptideAtlasQ16778; -; .
PRIDEQ16778; -; .
TopDownProteomicsQ16778; -; .
DNASU8349; -; .
EnsemblENST00000369155; ENSP00000358151; ENSG00000184678; .
GeneID8349; -; .
KEGGhsa:8349; -; .
UCSCuc001etc.4; human; .
CTD8349; -; .
GeneCardsHIST2H2BE; -; .
H-InvDBHIX0029389; -; .
HGNCHGNC:4760; HIST2H2BE; .
HPAHPA042205; -; .
HPAHPA043013; -; .
HPAHPA048671; -; .
MIM601831; gene; .
neXtProtNX_Q16778; -; .
OpenTargetsENSG00000184678; -; .
PharmGKBPA29135; -; .
eggNOGKOG1744; Eukaryota; .
eggNOGENOG4111NV5; LUCA; .
GeneTreeENSGT00760000118976; -; .
HOGENOMHOG000231213; -; .
HOVERGENHBG007774; -; .
InParanoidQ16778; -; .
KOK11252; -; .
OMANESENHF; -; .
OrthoDBEOG091G0XGD; -; .
PhylomeDBQ16778; -; .
TreeFamTF300212; -; .
ReactomeR-HSA-1221632; Meiotic synapsis; .
ReactomeR-HSA-171306; Packaging Of Telomere Ends; .
ReactomeR-HSA-201722; Formation of the beta-catenin:TCF transactivating complex; .
ReactomeR-HSA-212300; PRC2 methylates histones and DNA; .
ReactomeR-HSA-2299718; Condensation of Prophase Chromosomes; .
ReactomeR-HSA-2559580; Oxidative Stress Induced Senescence; .
ReactomeR-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP); .
ReactomeR-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence; .
ReactomeR-HSA-3214815; HDACs deacetylate histones; .
ReactomeR-HSA-3214847; HATs acetylate histones; .
ReactomeR-HSA-427359; SIRT1 negatively regulates rRNA Expression; .
ReactomeR-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression; .
ReactomeR-HSA-427413; NoRC negatively regulates rRNA expression; .
ReactomeR-HSA-5250924; B-WICH complex positively regulates rRNA expression; .
ReactomeR-HSA-5334118; DNA methylation; .
ReactomeR-HSA-5578749; Transcriptional regulation by small RNAs; .
ReactomeR-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis; .
ReactomeR-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3; .
ReactomeR-HSA-5689880; Ub-specific processing proteases; .
ReactomeR-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; .
ReactomeR-HSA-5693571; Nonhomologous End-Joining (NHEJ); .
ReactomeR-HSA-5693607; Processing of DNA double-strand break ends; .
ReactomeR-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere; .
ReactomeR-HSA-69473; G2/M DNA damage checkpoint; .
ReactomeR-HSA-73728; RNA Polymerase I Promoter Opening; .
ReactomeR-HSA-73777; RNA Polymerase I Chain Elongation; .
ReactomeR-HSA-912446; Meiotic recombination; .
ReactomeR-HSA-977225; Amyloid fiber formation; .
ChiTaRSHIST2H2BE; human; .
GeneWikiHIST2H2BE; -; .
GenomeRNAi8349; -; .
PROPR:Q16778; -; .
ProteomesUP000005640; Chromosome 1; .
BgeeENSG00000184678; -; .
CleanExHS_HIST2H2BE; -; .
GenevisibleQ16778; HS; .
GOGO:0005829; C:cytosol; IDA:HPA; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0005615; C:extracellular space; IDA:UniProtKB; .
GOGO:0005654; C:nucleoplasm; IDA:HPA; .
GOGO:0000786; C:nucleosome; NAS:UniProtKB; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0003677; F:DNA binding; NAS:UniProtKB; .
GOGO:0019731; P:antibacterial humoral response; IDA:UniProtKB; .
GOGO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB; .
GOGO:0002227; P:innate immune response in mucosa; IDA:UniProtKB; .
GOGO:0006334; P:nucleosome assembly; NAS:UniProtKB; .
Gene3D1.10.20.10; -; 1; .
InterProIPR009072; Histone-fold; .
InterProIPR007125; Histone_H2A/H2B/H3; .
InterProIPR000558; Histone_H2B; .
PANTHERPTHR23428; PTHR23428; 1; .
PfamPF00125; Histone; 1; .
PRINTSPR00621; HISTONEH2B; .
SMARTSM00427; H2B; 1; .
SUPFAMSSF47113; SSF47113; 1; .
PROSITEPS00357; HISTONE_H2B; 1; .



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Database constructed and maintained by Angel Garcia, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server

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