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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: H2AX_HUMAN




USC-OGP 2-DE database:  H2AX_HUMAN


H2AX_HUMAN


General information about the entry
View entry in simple text format
Entry nameH2AX_HUMAN
Primary accession numberP16104
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 H2AX; Short=H2a/x; AltName: Full=Histone H2A.X;.
Gene nameName=H2AFX
Synonyms=H2AX
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=4.59; Mw=16158
pI=5.02; Mw=16085
pI=5.13; Mw=15865
pI=5.68; Mw=15649

Cross-references
UniProtKB/Swiss-ProtP16104; H2AX_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 nameH2AX_HUMAN
Primary accession numberP16104
Secondary accession number(s) Q4ZGJ7 Q6IAS5
Sequence was last modified on January 23, 2007 (version 2)
Annotations were last modified on March 15, 2017 (version 181)
Name and origin of the protein
DescriptionRecName: Full=Histone H2AX; Short=H2a/x; AltName: Full=Histone H2A.X;
Gene nameName=H2AFX
Synonyms=H2AX
Encoded onName=H2AFX; Synonyms=H2AX
Keywords3D-structure; Acetylation; Cell cycle; Chromosome; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA-binding; Host-virus interaction; Isopeptide bond; Meiosis; 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
EMBLX14850; CAA32968.1; -; mRNA
EMBLCR457079; CAG33360.1; -; mRNA
EMBLDQ015918; AAY22178.1; -; Genomic_DNA
EMBLBC004915; AAH04915.1; -; mRNA
EMBLBC011694; AAH11694.1; -; mRNA
EMBLBC013416; AAH13416.1; -; mRNA
CCDSCCDS8410.1; -; .
PIRS07631; S07631; .
RefSeqNP_002096.1; NM_002105.2; .
UniGeneHs.477879; -; .
PDB1YDP; X-ray; 1.90 A; P=78-86
PDB2AZM; X-ray; 2.41 A; C/D=134-143
PDB2D31; X-ray; 3.20 A; C/F=78-86
PDB2DYP; X-ray; 2.50 A; C=78-86
PDB3SHV; X-ray; 2.10 A; C/D=134-143
PDB3SQD; X-ray; 2.15 A; C/D=134-143
PDB3SZM; X-ray; 2.63 A; I/J/K/L/M/N/O/P=134-143
PDB3U3Z; X-ray; 1.50 A; B=140-143
PDBsum1YDP; -; .
PDBsum2AZM; -; .
PDBsum2D31; -; .
PDBsum2DYP; -; .
PDBsum3SHV; -; .
PDBsum3SQD; -; .
PDBsum3SZM; -; .
PDBsum3U3Z; -; .
ProteinModelPortalP16104; -; .
SMRP16104; -; .
BioGrid109268; 293; .
DIPDIP-33604N; -; .
IntActP16104; 172; .
MINTMINT-1338182; -; .
STRING9606.ENSP00000364310; -; .
iPTMnetP16104; -; .
PhosphoSitePlusP16104; -; .
SwissPalmP16104; -; .
BioMutaH2AFX; -; .
DMDM121992; -; .
EPDP16104; -; .
MaxQBP16104; -; .
PaxDbP16104; -; .
PeptideAtlasP16104; -; .
PRIDEP16104; -; .
TopDownProteomicsP16104; -; .
EnsemblENST00000375167; ENSP00000364310; ENSG00000188486; .
EnsemblENST00000530167; ENSP00000434024; ENSG00000188486; .
GeneID3014; -; .
KEGGhsa:3014; -; .
UCSCuc001pvg.4; human; .
CTD3014; -; .
DisGeNET3014; -; .
GeneCardsH2AFX; -; .
HGNCHGNC:4739; H2AFX; .
HPACAB012264; -; .
HPAHPA041189; -; .
HPAHPA051647; -; .
MIM601772; gene; .
neXtProtNX_P16104; -; .
OpenTargetsENSG00000188486; -; .
PharmGKBPA29116; -; .
eggNOGKOG1756; Eukaryota; .
eggNOGCOG5262; LUCA; .
GeneTreeENSGT00760000118934; -; .
HOGENOMHOG000234652; -; .
HOVERGENHBG009342; -; .
InParanoidP16104; -; .
KOK11251; -; .
OMATVGPKTP; -; .
OrthoDBEOG091G0XGD; -; .
PhylomeDBP16104; -; .
TreeFamTF300137; -; .
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-3214858; RMTs methylate histone arginines; .
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-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; .
SIGNORP16104; -; .
ChiTaRSH2AFX; human; .
EvolutionaryTraceP16104; -; .
GeneWikiH2AFX; -; .
GenomeRNAi3014; -; .
PROPR:P16104; -; .
ProteomesUP000005640; Chromosome 11; .
BgeeENSG00000188486; -; .
CleanExHS_H2AFX; -; .
GenevisibleP16104; HS; .
GOGO:0000794; C:condensed nuclear chromosome; IEA:Ensembl; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0001673; C:male germ cell nucleus; IEA:Ensembl; .
GOGO:0000790; C:nuclear chromatin; IBA:GO_Central; .
GOGO:0016607; C:nuclear speck; IDA:HPA; .
GOGO:0005654; C:nucleoplasm; IDA:HPA; .
GOGO:0000786; C:nucleosome; IEA:UniProtKB-KW; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0005657; C:replication fork; IEA:Ensembl; .
GOGO:0035861; C:site of double-strand break; IDA:MGI; .
GOGO:0001741; C:XY body; IEA:Ensembl; .
GOGO:0003684; F:damaged DNA binding; IEA:Ensembl; .
GOGO:0003677; F:DNA binding; NAS:UniProtKB; .
GOGO:0019899; F:enzyme binding; IPI:UniProtKB; .
GOGO:0042393; F:histone binding; IPI:UniProtKB; .
GOGO:0006974; P:cellular response to DNA damage stimulus; IDA:BHF-UCL; .
GOGO:0071480; P:cellular response to gamma radiation; IEA:Ensembl; .
GOGO:0090398; P:cellular senescence; IEA:Ensembl; .
GOGO:0021987; P:cerebral cortex development; IEA:Ensembl; .
GOGO:0006342; P:chromatin silencing; IBA:GO_Central; .
GOGO:0000077; P:DNA damage checkpoint; IDA:UniProtKB; .
GOGO:0006302; P:double-strand break repair; NAS:UniProtKB; .
GOGO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl; .
GOGO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome; .
GOGO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW; .
GOGO:0006334; P:nucleosome assembly; NAS:UniProtKB; .
GOGO:0045739; P:positive regulation of DNA repair; NAS:UniProtKB; .
GOGO:0010212; P:response to ionizing radiation; NAS:UniProtKB; .
GOGO:0007283; P:spermatogenesis; IEA:Ensembl; .
GOGO:0016032; P:viral process; IEA:UniProtKB-KW; .
Gene3D1.10.20.10; -; 1; .
InterProIPR009072; Histone-fold; .
InterProIPR002119; Histone_H2A; .
InterProIPR007125; Histone_H2A/H2B/H3; .
InterProIPR032454; Histone_H2A_C; .
InterProIPR032458; Histone_H2A_CS; .
PfamPF00125; Histone; 1; .
PfamPF16211; Histone_H2A_C; 1; .
PRINTSPR00620; HISTONEH2A; .
SMARTSM00414; H2A; 1; .
SUPFAMSSF47113; SSF47113; 1; .
PROSITEPS00046; HISTONE_H2A; 1; .



USC-OGP 2-DE database image


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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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