UniProtKB - P68431 (H31_HUMAN)
Functioni
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Miscellaneous
This histone is only present in mammals and is enriched in acetylation of Lys-15 and dimethylation of Lys-10 (H3K9me2).
Caution
The original paper reporting lysine deamination at Lys-5 by LOXL2 has been retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this modification was confirmed in a subsequent publication (PubMed:27735137).2 Publications1 Publication
GO - Molecular functioni
- cadherin binding Source: BHF-UCL
- DNA binding Source: UniProtKB-KW
- protein heterodimerization activity Source: InterPro
GO - Biological processi
- blood coagulation Source: Reactome
- cellular protein metabolic process Source: Reactome
- chromatin organization Source: Reactome
- DNA replication-dependent nucleosome assembly Source: UniProtKB
- interleukin-7-mediated signaling pathway Source: Reactome
- negative regulation of gene expression, epigenetic Source: Reactome
- nucleosome assembly Source: UniProtKB
- rDNA heterochromatin assembly Source: Reactome
- regulation of gene silencing Source: BHF-UCL
- regulation of gene silencing by miRNA Source: Reactome
- regulation of megakaryocyte differentiation Source: Reactome
- telomere organization Source: BHF-UCL
Keywordsi
Molecular function | DNA-binding |
Enzyme and pathway databases
PathwayCommonsi | P68431 |
Reactomei | R-HSA-1266695, Interleukin-7 signaling R-HSA-1912408, Pre-NOTCH Transcription and Translation R-HSA-201722, Formation of the beta-catenin:TCF transactivating complex R-HSA-212300, PRC2 methylates histones and DNA R-HSA-2299718, Condensation of Prophase Chromosomes R-HSA-2559580, Oxidative Stress Induced Senescence R-HSA-2559582, Senescence-Associated Secretory Phenotype (SASP) R-HSA-3214815, HDACs deacetylate histones R-HSA-3214841, PKMTs methylate histone lysines R-HSA-3214842, HDMs demethylate histones R-HSA-3214847, HATs acetylate histones R-HSA-3214858, RMTs methylate histone arginines R-HSA-3247509, Chromatin modifying enzymes R-HSA-427359, SIRT1 negatively regulates rRNA expression R-HSA-427389, ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression R-HSA-427413, NoRC negatively regulates rRNA expression R-HSA-5250924, B-WICH complex positively regulates rRNA expression R-HSA-5334118, DNA methylation R-HSA-5578749, Transcriptional regulation by small RNAs R-HSA-5617472, Activation of anterior HOX genes in hindbrain development during early embryogenesis R-HSA-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 R-HSA-73728, RNA Polymerase I Promoter Opening R-HSA-73772, RNA Polymerase I Promoter Escape R-HSA-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-HSA-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs R-HSA-9018519, Estrogen-dependent gene expression R-HSA-912446, Meiotic recombination R-HSA-9609690, HCMV Early Events R-HSA-9610379, HCMV Late Events R-HSA-9616222, Transcriptional regulation of granulopoiesis R-HSA-977225, Amyloid fiber formation R-HSA-983231, Factors involved in megakaryocyte development and platelet production |
SIGNORi | P68431 |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H3.1Alternative name(s): Histone H3/a Histone H3/b Histone H3/c Histone H3/d Histone H3/f Histone H3/h Histone H3/i Histone H3/j Histone H3/k Histone H3/l |
Gene namesi | AND AND AND AND AND AND AND AND AND |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000197153.4 HostDB:ENSG00000197409.7 HostDB:ENSG00000273983.1 HostDB:ENSG00000274267.1 HostDB:ENSG00000274750.2 HostDB:ENSG00000275379.1 HostDB:ENSG00000275714.1 HostDB:ENSG00000277775.1 HostDB:ENSG00000278272.1 HostDB:ENSG00000278828.1 |
HGNCi | HGNC:4766, H3C1 HGNC:4775, H3C10 HGNC:4771, H3C11 HGNC:4774, H3C12 HGNC:4776, H3C2 HGNC:4768, H3C3 HGNC:4767, H3C4 HGNC:4769, H3C6 HGNC:4773, H3C7 HGNC:4772, H3C8 |
MIMi | 602810, gene 602811, gene 602812, gene 602813, gene 602814, gene 602815, gene 602816, gene 602817, gene 602818, gene 602819, gene |
neXtProti | NX_P68431 |
Subcellular locationi
Nucleus
Other locations
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
- extracellular region Source: Reactome
Nucleus
- nuclear chromosome Source: UniProtKB
- nuclear nucleosome Source: UniProtKB
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
Other locations
- membrane Source: UniProtKB
- nucleosome Source: UniProtKB
- protein-containing complex Source: UniProtKB
Keywords - Cellular componenti
Chromosome, Nucleosome core, NucleusPathology & Biotechi
Involvement in diseasei
Glioma (GLM)1 Publication
The gene represented in this entry is involved in disease pathogenesis. HIST1H3B mutations affecting residue Lys-28 involved in post-translational modifications of histone H3.1 are recurrent in malignant, aggressive gliomas including pediatric non-brain stem glioblastoma and diffuse intrinsic pontine glioma (DIPG) (PubMed:22286216). The mechanism through which mutations lead to tumorigenesis involves altered histone methylation, impaired regulation of Polycomb repressive complex 2 (PRC2) activity, and aberrant epigenetic regulation of gene expression (PubMed:23603901).2 Publications
Disease descriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_079018 | 28 | K → M in GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels. 2 PublicationsCorresponds to variant dbSNP:rs1057519904EnsemblClinVar. | 1 |
HIST1H3B or HIST1H3C mutations affecting residue Lys-37 of histone H3.1 are involved in the pathogenesis of pediatric undifferentiated soft tissue sarcomas. The mechanism through which mutations lead to tumorigenesis involves altered histones methylation with gain of global H3K27 methylation, altered Polycomb repressive complex 1 (PRC1) activity, aberrant epigenetic regulation of gene expression and impaired differentiation of mesenchimal progenitor cells.1 Publication
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNETi | 8350 8351 8352 8353 8354 8355 8356 8357 8358 8968 |
MalaCardsi | H3C1 H3C2 |
MIMi | 137800, phenotype |
OpenTargetsi | ENSG00000197153 ENSG00000197409 ENSG00000273983 ENSG00000274750 ENSG00000275379 ENSG00000275714 ENSG00000277775 ENSG00000278828 |
PharmGKBi | PA29148 |
Miscellaneous databases
Pharosi | P68431, Tbio |
Polymorphism and mutation databases
BioMutai | HIST1H3A |
DMDMi | 55977055 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000221245 | 2 – 136 | Histone H3.1Add BLAST | 135 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 3 | Asymmetric dimethylarginine; by PRMT6; alternate3 Publications | 1 | |
Modified residuei | 3 | Citrulline; alternate1 Publication | 1 | |
Modified residuei | 4 | Phosphothreonine; by HASPIN2 Publications | 1 | |
Modified residuei | 5 | Allysine; alternate1 Publication | 1 | |
Modified residuei | 5 | N6,N6,N6-trimethyllysine; alternate3 Publications | 1 | |
Modified residuei | 5 | N6,N6-dimethyllysine; alternate3 Publications | 1 | |
Modified residuei | 5 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 5 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 5 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 5 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 5 | N6-methyllysine; alternate3 Publications | 1 | |
Modified residuei | 7 | Phosphothreonine; by PKC1 Publication | 1 | |
Modified residuei | 9 | Citrulline; alternate2 Publications | 1 | |
Modified residuei | 9 | Symmetric dimethylarginine; by PRMT5; alternateBy similarity | 1 | |
Modified residuei | 10 | N6,N6,N6-trimethyllysine; alternate5 Publications | 1 | |
Modified residuei | 10 | N6,N6-dimethyllysine; alternate5 Publications | 1 | |
Modified residuei | 10 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 10 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 10 | N6-acetyllysine; alternate6 Publications | 1 | |
Modified residuei | 10 | N6-butyryllysine; alternate1 Publication | 1 | |
Modified residuei | 10 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 10 | N6-methyllysine; alternate5 Publications | 1 | |
Modified residuei | 11 | ADP-ribosylserine; alternate2 Publications | 1 | |
Modified residuei | 11 | Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications | 1 | |
Modified residuei | 12 | Phosphothreonine; by PKC and CHEK13 Publications | 1 | |
Modified residuei | 15 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 15 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 15 | N6-acetyllysine; alternate6 Publications | 1 | |
Modified residuei | 15 | N6-glutaryllysine; alternate1 Publication | 1 | |
Modified residuei | 15 | N6-succinyllysine; alternate1 Publication | 1 | |
Modified residuei | 18 | Asymmetric dimethylarginine; by CARM1; alternate3 Publications | 1 | |
Modified residuei | 18 | Citrulline; alternate3 Publications | 1 | |
Modified residuei | 19 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 19 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 19 | N6-acetyllysine; alternate3 Publications | 1 | |
Modified residuei | 19 | N6-butyryllysine; alternate1 Publication | 1 | |
Modified residuei | 19 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 19 | N6-glutaryllysine; alternate1 Publication | 1 | |
Modified residuei | 19 | N6-methyllysine; alternate2 Publications | 1 | |
Modified residuei | 24 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 24 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 24 | N6-acetyllysine; alternate4 Publications | 1 | |
Modified residuei | 24 | N6-butyryllysine; alternate1 Publication | 1 | |
Modified residuei | 24 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 24 | N6-glutaryllysine; alternate1 Publication | 1 | |
Modified residuei | 24 | N6-methyllysine; alternate1 Publication | 1 | |
Modified residuei | 27 | Citrulline1 Publication | 1 | |
Modified residuei | 28 | N6,N6,N6-trimethyllysine; alternate4 Publications | 1 | |
Modified residuei | 28 | N6,N6-dimethyllysine; alternate4 Publications | 1 | |
Modified residuei | 28 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 28 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 28 | N6-acetyllysine; alternate2 Publications | 1 | |
Modified residuei | 28 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 28 | N6-glutaryllysine; alternate1 Publication | 1 | |
Modified residuei | 28 | N6-methyllysine; alternate4 Publications | 1 | |
Modified residuei | 29 | ADP-ribosylserine; alternate2 Publications | 1 | |
Modified residuei | 29 | Phosphoserine; alternate; by AURKB, AURKC and RPS6KA56 Publications | 1 | |
Modified residuei | 37 | N6,N6,N6-trimethyllysine; alternate5 Publications | 1 | |
Modified residuei | 37 | N6,N6-dimethyllysine; alternate5 Publications | 1 | |
Modified residuei | 37 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 37 | N6-acetyllysine; alternate2 Publications | 1 | |
Modified residuei | 37 | N6-methyllysine; alternate5 Publications | 1 | |
Modified residuei | 38 | N6-methyllysine1 Publication | 1 | |
Modified residuei | 42 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 57 | N6,N6,N6-trimethyllysine; alternate2 Publications | 1 | |
Modified residuei | 57 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 57 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 57 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 57 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 57 | N6-glutaryllysine; alternate1 Publication | 1 | |
Modified residuei | 57 | N6-methyllysine; by EHMT2; alternate2 Publications | 1 | |
Modified residuei | 57 | N6-succinyllysine; alternate1 Publication | 1 | |
Modified residuei | 58 | Phosphoserine1 Publication | 1 | |
Modified residuei | 65 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 65 | N6-methyllysine; alternate2 Publications | 1 | |
Modified residuei | 80 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6,N6-dimethyllysine; alternate4 Publications | 1 | |
Modified residuei | 80 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 80 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 80 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 80 | N6-glutaryllysine; alternate1 Publication | 1 | |
Modified residuei | 80 | N6-methyllysine; alternate4 Publications | 1 | |
Modified residuei | 80 | N6-succinyllysine; alternate2 Publications | 1 | |
Modified residuei | 81 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 87 | PhosphoserineBy similarity | 1 | |
Modified residuei | 108 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 116 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 116 | N6-glutaryllysine; alternate1 Publication | 1 | |
Modified residuei | 123 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 123 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 123 | N6-acetyllysine; alternate2 Publications | 1 | |
Modified residuei | 123 | N6-glutaryllysine; alternate1 Publication | 1 | |
Modified residuei | 123 | N6-methyllysine; alternate2 Publications | 1 | |
Modified residuei | 123 | N6-succinyllysine; alternate2 Publications | 1 |
Post-translational modificationi
Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.11 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.4 Publications
Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters.9 Publications
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.15 Publications
Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.17 Publications
Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination (By similarity). Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins.By similarity1 Publication
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression.1 Publication
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.By similarity
Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes (PubMed:29211711). It gives a specific tag for epigenetic transcription activation (PubMed:29211711). Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair (PubMed:27436229).2 Publications
Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:30257210). Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac) (PubMed:30257210).1 Publication
Keywords - PTMi
Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P68431 |
jPOSTi | P68431 |
MassIVEi | P68431 |
MaxQBi | P68431 |
PaxDbi | P68431 |
PeptideAtlasi | P68431 |
PRIDEi | P68431 |
ProteomicsDBi | 57541 |
TopDownProteomicsi | P68431 |
PTM databases
GlyConnecti | 2886, 1 O-Linked glycan (1 site) |
iPTMneti | P68431 |
MetOSitei | P68431 |
PhosphoSitePlusi | P68431 |
SwissPalmi | P68431 |
Expressioni
Developmental stagei
Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.
Gene expression databases
Bgeei | ENSG00000197153, Expressed in stomach and 64 other tissues |
Genevisiblei | P68431, HS |
Organism-specific databases
HPAi | ENSG00000197153, Tissue enriched (lymphoid) ENSG00000197409, Tissue enriched (lymphoid) ENSG00000273983, Tissue enriched (lymphoid) ENSG00000274267, Tissue enriched (lymphoid) ENSG00000274750, Tissue enhanced (lymphoid tissue, testis, tongue) ENSG00000275379, Tissue enriched (lymphoid) ENSG00000275714, Tissue enhanced (lymphoid tissue, testis) ENSG00000277775, Tissue enriched (lymphoid) ENSG00000278272, Tissue enriched (lymphoid) ENSG00000278828, Group enriched (blood, lymphoid tissue) |
Interactioni
Subunit structurei
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
2 PublicationsBinary interactionsi
Hide detailsP68431
GO - Molecular functioni
- cadherin binding Source: BHF-UCL
- protein heterodimerization activity Source: InterPro
Protein-protein interaction databases
BioGRIDi | 113946, 667 interactors 113947, 16 interactors 113948, 17 interactors 113949, 205 interactors 113950, 10 interactors 113951, 10 interactors 113952, 9 interactors 113953, 12 interactors 113954, 28 interactors 114458, 13 interactors |
CORUMi | P68431 |
DIPi | DIP-29371N |
ELMi | P68431 |
IntActi | P68431, 458 interactors |
MINTi | P68431 |
STRINGi | 9606.ENSP00000484841 |
Chemistry databases
BindingDBi | P68431 |
Miscellaneous databases
RNActi | P68431, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P68431 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P68431 |
Family & Domainsi
Sequence similaritiesi
Belongs to the histone H3 family.Curated
Phylogenomic databases
eggNOGi | KOG1745, Eukaryota |
GeneTreei | ENSGT01010000222292 |
HOGENOMi | CLU_078295_4_0_1 |
InParanoidi | P68431 |
OMAi | TEFANEM |
OrthoDBi | 1564596at2759 |
PhylomeDBi | P68431 |
TreeFami | TF314241 |
Family and domain databases
Gene3Di | 1.10.20.10, 1 hit |
IDEALi | IID00062 |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR007125, Histone_H2A/H2B/H3 IPR000164, Histone_H3/CENP-A |
PANTHERi | PTHR11426, PTHR11426, 1 hit |
Pfami | View protein in Pfam PF00125, Histone, 1 hit |
PRINTSi | PR00622, HISTONEH3 |
SMARTi | View protein in SMART SM00428, H3, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00322, HISTONE_H3_1, 1 hit PS00959, HISTONE_H3_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P68431-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 70 | R → C in AAH67493 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 100 | Y → T in CAB02546 (PubMed:9119399).Curated | 1 | |
Sequence conflicti | 122 | P → L in AAH66884 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 135 | Missing in AAA52651 (PubMed:3013246).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_079018 | 28 | K → M in GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels. 2 PublicationsCorresponds to variant dbSNP:rs1057519904EnsemblClinVar. | 1 | |
Natural variantiVAR_079019 | 37 | K → I Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels. 1 Publication | 1 | |
Natural variantiVAR_079020 | 37 | K → M Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels. 2 Publications | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X00090 Genomic DNA Translation: CAA24952.1 M26150 Genomic DNA Translation: AAA52651.1 M60746 Genomic DNA Translation: AAA63185.1 X57128 Genomic DNA Translation: CAA40407.1 Z46261 Genomic DNA Translation: CAA86403.1 X83550 Genomic DNA Translation: CAA58540.1 Z80784 Genomic DNA Translation: CAB02546.1 Z80785 Genomic DNA Translation: CAB02547.1 Z80786 Genomic DNA Translation: CAB02548.1 Z83735 Genomic DNA Translation: CAB06030.1 Z83737 Genomic DNA Translation: CAB06032.1 AF531274 Genomic DNA Translation: AAN10051.1 AF531275 Genomic DNA Translation: AAN10052.1 AF531276 Genomic DNA Translation: AAN10053.1 AF531277 Genomic DNA Translation: AAN10054.1 AF531278 Genomic DNA Translation: AAN10055.1 AF531279 Genomic DNA Translation: AAN10056.1 AF531280 Genomic DNA Translation: AAN10057.1 AF531281 Genomic DNA Translation: AAN10058.1 AF531282 Genomic DNA Translation: AAN10059.1 AF531283 Genomic DNA Translation: AAN10060.1 AK311991 mRNA Translation: BAG34929.1 AK313905 mRNA Translation: BAG36628.1 AK314142 mRNA Translation: BAG36832.1 AK316611 mRNA Translation: BAG38198.1 CR542014 mRNA Translation: CAG46811.1 CR542011 mRNA Translation: CAG46808.1 CR541983 mRNA Translation: CAG46780.1 CR541858 mRNA Translation: CAG46656.1 Z98744 Genomic DNA No translation available. AL009179 Genomic DNA No translation available. AL031777 Genomic DNA No translation available. BC031333 mRNA Translation: AAH31333.1 BC066245 mRNA Translation: AAH66245.1 BC066246 mRNA Translation: AAH66246.1 BC066247 mRNA Translation: AAH66247.1 BC066884 mRNA Translation: AAH66884.1 BC067490 mRNA Translation: AAH67490.1 BC067491 mRNA Translation: AAH67491.1 BC067492 mRNA Translation: AAH67492.1 BC067493 mRNA Translation: AAH67493.1 BC069133 mRNA Translation: AAH69133.1 BC069303 mRNA Translation: AAH69303.1 BC069305 mRNA Translation: AAH69305.2 BC069818 mRNA Translation: AAH69818.1 BC096128 mRNA Translation: AAH96128.1 BC096129 mRNA Translation: AAH96129.1 BC096130 mRNA Translation: AAH96130.1 BC096131 mRNA Translation: AAH96131.1 BC096132 mRNA Translation: AAH96132.1 BC096133 mRNA Translation: AAH96133.1 BC096134 mRNA Translation: AAH96134.1 BC099630 mRNA Translation: AAH99630.1 BC127610 mRNA Translation: AAI27611.1 BC143046 mRNA Translation: AAI43047.1 BC148243 mRNA Translation: AAI48244.1 BC148250 mRNA Translation: AAI48251.1 |
CCDSi | CCDS4570.1 CCDS4573.1 CCDS4576.1 CCDS4590.1 CCDS4596.1 CCDS4600.1 CCDS4602.1 CCDS4627.1 CCDS4636.1 CCDS4638.1 |
PIRi | I37446, HSHU3 |
RefSeqi | NP_003520.1, NM_003529.2 NP_003521.2, NM_003530.4 NP_003522.1, NM_003531.2 NP_003523.1, NM_003532.2 NP_003524.1, NM_003533.2 NP_003525.1, NM_003534.2 NP_003526.1, NM_003535.2 NP_003527.1, NM_003536.2 NP_003528.1, NM_003537.3 NP_066298.1, NM_021018.2 |
Genome annotation databases
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X00090 Genomic DNA Translation: CAA24952.1 M26150 Genomic DNA Translation: AAA52651.1 M60746 Genomic DNA Translation: AAA63185.1 X57128 Genomic DNA Translation: CAA40407.1 Z46261 Genomic DNA Translation: CAA86403.1 X83550 Genomic DNA Translation: CAA58540.1 Z80784 Genomic DNA Translation: CAB02546.1 Z80785 Genomic DNA Translation: CAB02547.1 Z80786 Genomic DNA Translation: CAB02548.1 Z83735 Genomic DNA Translation: CAB06030.1 Z83737 Genomic DNA Translation: CAB06032.1 AF531274 Genomic DNA Translation: AAN10051.1 AF531275 Genomic DNA Translation: AAN10052.1 AF531276 Genomic DNA Translation: AAN10053.1 AF531277 Genomic DNA Translation: AAN10054.1 AF531278 Genomic DNA Translation: AAN10055.1 AF531279 Genomic DNA Translation: AAN10056.1 AF531280 Genomic DNA Translation: AAN10057.1 AF531281 Genomic DNA Translation: AAN10058.1 AF531282 Genomic DNA Translation: AAN10059.1 AF531283 Genomic DNA Translation: AAN10060.1 AK311991 mRNA Translation: BAG34929.1 AK313905 mRNA Translation: BAG36628.1 AK314142 mRNA Translation: BAG36832.1 AK316611 mRNA Translation: BAG38198.1 CR542014 mRNA Translation: CAG46811.1 CR542011 mRNA Translation: CAG46808.1 CR541983 mRNA Translation: CAG46780.1 CR541858 mRNA Translation: CAG46656.1 Z98744 Genomic DNA No translation available. AL009179 Genomic DNA No translation available. AL031777 Genomic DNA No translation available. BC031333 mRNA Translation: AAH31333.1 BC066245 mRNA Translation: AAH66245.1 BC066246 mRNA Translation: AAH66246.1 BC066247 mRNA Translation: AAH66247.1 BC066884 mRNA Translation: AAH66884.1 BC067490 mRNA Translation: AAH67490.1 BC067491 mRNA Translation: AAH67491.1 BC067492 mRNA Translation: AAH67492.1 BC067493 mRNA Translation: AAH67493.1 BC069133 mRNA Translation: AAH69133.1 BC069303 mRNA Translation: AAH69303.1 BC069305 mRNA Translation: AAH69305.2 BC069818 mRNA Translation: AAH69818.1 BC096128 mRNA Translation: AAH96128.1 BC096129 mRNA Translation: AAH96129.1 BC096130 mRNA Translation: AAH96130.1 BC096131 mRNA Translation: AAH96131.1 BC096132 mRNA Translation: AAH96132.1 BC096133 mRNA Translation: AAH96133.1 BC096134 mRNA Translation: AAH96134.1 BC099630 mRNA Translation: AAH99630.1 BC127610 mRNA Translation: AAI27611.1 BC143046 mRNA Translation: AAI43047.1 BC148243 mRNA Translation: AAI48244.1 BC148250 mRNA Translation: AAI48251.1 |
CCDSi | CCDS4570.1 CCDS4573.1 CCDS4576.1 CCDS4590.1 CCDS4596.1 CCDS4600.1 CCDS4602.1 CCDS4627.1 CCDS4636.1 CCDS4638.1 |
PIRi | I37446, HSHU3 |
RefSeqi | NP_003520.1, NM_003529.2 NP_003521.2, NM_003530.4 NP_003522.1, NM_003531.2 NP_003523.1, NM_003532.2 NP_003524.1, NM_003533.2 NP_003525.1, NM_003534.2 NP_003526.1, NM_003535.2 NP_003527.1, NM_003536.2 NP_003528.1, NM_003537.3 NP_066298.1, NM_021018.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CS9 | NMR | - | A | 131-136 | [»] | |
1CT6 | NMR | - | A | 131-136 | [»] | |
1O9S | X-ray | 1.75 | K/L | 2-10 | [»] | |
1Q3L | X-ray | 1.64 | P | 2-16 | [»] | |
2B2T | X-ray | 2.45 | D | 2-20 | [»] | |
2B2U | X-ray | 2.95 | D | 2-16 | [»] | |
2B2V | X-ray | 2.65 | D | 2-16 | [»] | |
2B2W | X-ray | 2.40 | D | 2-20 | [»] | |
2C1J | X-ray | 2.60 | C/D | 8-15 | [»] | |
2C1N | X-ray | 2.00 | C/E | 8-15 | [»] | |
2CO0 | X-ray | 2.25 | B/D | 2-16 | [»] | |
2CV5 | X-ray | 2.50 | A/E | 1-136 | [»] | |
2FSA | X-ray | 1.90 | P | 2-16 | [»] | |
2KWJ | NMR | - | B | 2-21 | [»] | |
2KWK | NMR | - | B | 2-21 | [»] | |
2L75 | NMR | - | B | 2-14 | [»] | |
2LBM | NMR | - | C | 2-16 | [»] | |
2LGG | NMR | - | B | 2-13 | [»] | |
2M0O | NMR | - | B | 32-42 | [»] | |
2NDF | NMR | - | B | 13-25 | [»] | |
2NDG | NMR | - | B | 13-25 | [»] | |
2OQ6 | X-ray | 2.00 | C/D | 8-15 | [»] | |
2OT7 | X-ray | 2.14 | C/D | 8-15 | [»] | |
2OX0 | X-ray | 1.95 | C/D | 8-15 | [»] | |
2RI7 | X-ray | 1.45 | P | 2-10 | [»] | |
2RR4 | NMR | - | B | 2-11 | [»] | |
2UXN | X-ray | 2.72 | E | 2-22 | [»] | |
2V85 | X-ray | 2.00 | D/E | 2-13 | [»] | |
2V89 | X-ray | 1.10 | D/E | 2-10 | [»] | |
2VNF | X-ray | 1.76 | B/D | 2-11 | [»] | |
2VPG | X-ray | 1.60 | P/R | 2-19 | [»] | |
2X0L | X-ray | 3.00 | C | 6-17 | [»] | |
3A1B | X-ray | 2.29 | A | 2-21 | [»] | |
3AFA | X-ray | 2.50 | A/E | 1-136 | [»] | |
3AVR | X-ray | 1.80 | B | 18-39 | [»] | |
3AYW | X-ray | 2.90 | A/E | 1-136 | [»] | |
3AZE | X-ray | 3.00 | A/E | 1-136 | [»] | |
3AZF | X-ray | 2.70 | A/E | 1-136 | [»] | |
3AZG | X-ray | 2.40 | A/E | 1-136 | [»] | |
3AZH | X-ray | 3.49 | A/E | 1-136 | [»] | |
3AZI | X-ray | 2.70 | A/E | 1-136 | [»] | |
3AZJ | X-ray | 2.89 | A/E | 1-136 | [»] | |
3AZK | X-ray | 3.20 | A/E | 1-136 | [»] | |
3AZL | X-ray | 2.70 | A/E | 1-136 | [»] | |
3AZM | X-ray | 2.89 | A/E | 1-136 | [»] | |
3AZN | X-ray | 3.00 | A/E | 1-136 | [»] | |
3B95 | X-ray | 2.99 | P | 2-16 | [»] | |
3FDT | X-ray | 2.00 | T | 2-16 | [»] | |
3KMT | X-ray | 1.78 | G/H/I | 26-33 | [»] | |
3KQI | X-ray | 1.78 | B | 2-13 | [»] | |
3LQI | X-ray | 1.92 | R/S/T | 2-10 | [»] | |
3LQJ | X-ray | 1.90 | Q/T | 2-10 | [»] | |
3MP1 | X-ray | 2.60 | P | 2-6 | [»] | |
3O34 | X-ray | 1.90 | B | 14-33 | [»] | |
3O35 | X-ray | 1.76 | D/E | 24-32 | [»] | |
3O37 | X-ray | 2.00 | E/F/G/H | 2-11 | [»] | |
3QJ6 | X-ray | 2.30 | T | 74-84 | [»] | |
3RIG | X-ray | 2.00 | C/D | 5-16 | [»] | |
3RIY | X-ray | 1.55 | C/D | 5-16 | [»] | |
3SOU | X-ray | 1.80 | D/E | 2-10 | [»] | |
3SOW | X-ray | 1.95 | C/D | 2-10 | [»] | |
3U31 | X-ray | 2.20 | B | 5-14 | [»] | |
3U3D | X-ray | 2.40 | B | 5-14 | [»] | |
3U4S | X-ray | 2.15 | C/D | 8-15 | [»] | |
3U5N | X-ray | 1.95 | C/D | 2-21 | [»] | |
3U5O | X-ray | 2.70 | I/J/K/L/M/N/O/P | 2-23 | [»] | |
3U5P | X-ray | 2.80 | I/J/K/L/M/N/O/P | 2-29 | [»] | |
3UEE | X-ray | 2.61 | B/D | 2-13 | [»] | |
3UEF | X-ray | 2.45 | B/D | 2-13 | [»] | |
3UIG | X-ray | 2.40 | P/Q | 2-16 | [»] | |
3UII | X-ray | 2.60 | P/Q | 2-11 | [»] | |
3UIK | X-ray | 2.70 | P/Q | 2-11 | [»] | |
3V43 | X-ray | 1.47 | Q | 2-19 | [»] | |
3W96 | X-ray | 3.00 | A/E | 1-136 | [»] | |
3W97 | X-ray | 3.20 | A/E | 1-136 | [»] | |
3W98 | X-ray | 3.42 | A/E | 29-136 | [»] | |
3W99 | X-ray | 3.00 | A/E | 1-136 | [»] | |
3WA9 | X-ray | 3.07 | A/E | 1-136 | [»] | |
3WAA | X-ray | 3.20 | A/E | 1-136 | [»] | |
3WKJ | X-ray | 2.80 | A/E | 1-136 | [»] | |
3X1S | X-ray | 2.81 | A/E | 2-136 | [»] | |
3X1T | X-ray | 2.81 | A/E | 2-136 | [»] | |
3X1U | X-ray | 3.25 | A/E | 2-136 | [»] | |
3X1V | X-ray | 2.92 | A/E | 2-136 | [»] | |
3ZG6 | X-ray | 2.20 | F | 5-14 | [»] | |
3ZVY | X-ray | 1.95 | C/D | 2-9 | [»] | |
4A0J | X-ray | 2.80 | C/D | 2-7 | [»] | |
4A0N | X-ray | 2.74 | C | 2-7 | [»] | |
4A7J | X-ray | 1.90 | B | 1-16 | [»] | |
4BD3 | NMR | - | B | 32-42 | [»] | |
4C1Q | X-ray | 2.30 | C | 2-10 | [»] | |
4F4U | X-ray | 2.00 | C/D | 5-16 | [»] | |
4F56 | X-ray | 1.70 | C/D | 5-16 | [»] | |
4FWF | X-ray | 2.70 | E | 2-21 | [»] | |
4HON | X-ray | 1.80 | F/G | 7-16 | [»] | |
4I51 | X-ray | 1.90 | C/D | 4-12 | [»] | |
4L7X | X-ray | 1.35 | U | 2-13 | [»] | |
4LK9 | X-ray | 1.60 | B | 2-22 | [»] | |
4LKA | X-ray | 1.61 | B | 2-22 | [»] | |
4LLB | X-ray | 2.50 | C/D | 2-22 | [»] | |
4LXL | X-ray | 1.87 | D | 8-15 | [»] | |
4N4H | X-ray | 2.30 | B | 22-43 | [»] | |
4QBQ | X-ray | 2.41 | P | 2-9 | [»] | |
4QBR | X-ray | 1.90 | E/P | 2-8 | [»] | |
4QBS | X-ray | 1.80 | P | 2-8 | [»] | |
4TN7 | X-ray | 2.20 | E/F | 30-44 | [»] | |
4U68 | X-ray | 1.80 | D/E/F | 5-15 | [»] | |
4UP0 | X-ray | 1.28 | F | 2-16 | [»] | |
4UY4 | X-ray | 1.86 | C/D | 2-7 | [»] | |
4X3K | X-ray | 1.45 | C/D | 24-30 | [»] | |
4Y6L | X-ray | 1.60 | C/D | 7-13 | [»] | |
4YHP | X-ray | 2.53 | P/Q | 2-17 | [»] | |
4YHZ | X-ray | 2.30 | P | 2-13 | [»] | |
4YM5 | X-ray | 4.00 | A/E | 1-136 | [»] | |
4YM6 | X-ray | 3.51 | A/E | 1-136 | [»] | |
4Z0R | X-ray | 1.75 | D | 2-16 | [»] | |
4Z2M | X-ray | 2.98 | G/I | 35-136 | [»] | |
5AV5 | X-ray | 2.40 | A/E | 1-136 | [»] | |
5AV6 | X-ray | 2.20 | A/E | 1-136 | [»] | |
5AV8 | X-ray | 2.20 | A/E | 1-136 | [»] | |
5AV9 | X-ray | 2.20 | A/E | 1-136 | [»] | |
5AVB | X-ray | 2.40 | A/E | 1-136 | [»] | |
5AVC | X-ray | 2.40 | A/E | 1-136 | [»] | |
5B24 | X-ray | 3.60 | A/E | 1-136 | [»] | |
5B2I | X-ray | 3.00 | A/E | 1-136 | [»] | |
5B2J | X-ray | 2.60 | A/E | 1-136 | [»] | |
5B31 | X-ray | 2.20 | A/E | 1-136 | [»] | |
5C11 | X-ray | 2.80 | B | 2-11 | [»] | |
5C13 | X-ray | 2.10 | D/F/H/P | 2-11 | [»] | |
5C3I | X-ray | 3.50 | B/F/J/N/R/V | 1-136 | [»] | |
5CPI | X-ray | 2.90 | A/E | 1-136 | [»] | |
5CPJ | X-ray | 3.15 | A/E | 1-136 | [»] | |
5CPK | X-ray | 2.63 | A/E | 1-136 | [»] | |
5D6Y | X-ray | 2.29 | a/b/c/d | 20-29 | [»] | |
5DAH | X-ray | 2.61 | C/D | 20-30 | [»] | |
5FB0 | X-ray | 2.70 | D/F | 2-16 | [»] | |
5FB1 | X-ray | 2.10 | C | 2-16 | [»] | |
5FFV | X-ray | 1.30 | C/D | 10-20 | [»] | |
5GH9 | X-ray | 1.45 | B | 45-58 | [»] | |
5GSE | X-ray | 3.14 | A/E/K/O | 1-136 | [»] | |
5GSU | X-ray | 3.10 | A/E | 2-136 | [»] | |
5GT0 | X-ray | 2.82 | A/E | 2-136 | [»] | |
5GT3 | X-ray | 2.91 | A/E | 2-136 | [»] | |
5GTC | X-ray | 2.70 | A/E | 1-136 | [»] | |
5H6Q | X-ray | 2.53 | C | 2-21 | [»] | |
5H6R | X-ray | 2.60 | C | 2-21 | [»] | |
5HJB | X-ray | 2.70 | B | 4-9 | [»] | |
5HJC | X-ray | 2.60 | B | 16-24 | [»] | |
5HJD | X-ray | 2.81 | B/D/F/H/I/J/L/M | 15-21 | [»] | |
5HYN | X-ray | 2.95 | D/I/O/T | 22-34 | [»] | |
5IQL | X-ray | 2.10 | B | 25-32 | [»] | |
5J3V | X-ray | 3.05 | C/D | 12-28 | [»] | |
5J9S | X-ray | 2.70 | B | 16-40 | [»] | |
5JHN | X-ray | 1.67 | F/G | 4-14 | [»] | |
5JIN | X-ray | 1.85 | F/G | 4-14 | [»] | |
5JIY | X-ray | 1.48 | F/G | 4-14 | [»] | |
5JJ0 | X-ray | 1.72 | F/G | 4-14 | [»] | |
5JRG | X-ray | 2.50 | A/E | 1-136 | [»] | |
5KJH | X-ray | 2.27 | D | 23-33 | [»] | |
E | 19-38 | [»] | ||||
5KJI | X-ray | 2.71 | E | 19-38 | [»] | |
5KKL | X-ray | 2.94 | B | 23-27 | [»] | |
5LUG | X-ray | 1.70 | E/F/G/H | 2-11 | [»] | |
5M5G | X-ray | 2.27 | D | 23-33 | [»] | |
5MR8 | X-ray | 1.74 | C | 2-10 | [»] | |
5NNC | X-ray | 2.22 | C/D | 5-21 | [»] | |
5NND | X-ray | 1.82 | D/E | 5-21 | [»] | |
5OY3 | X-ray | 2.14 | B | 18-34 | [»] | |
5SVX | X-ray | 1.56 | B | 2-12 | [»] | |
5SVY | X-ray | 1.05 | B | 2-12 | [»] | |
5SZB | X-ray | 1.20 | H | 2-19 | [»] | |
5SZC | X-ray | 1.19 | H | 2-19 | [»] | |
5T0K | X-ray | 1.70 | P/Q | 2-16 | [»] | |
5T0M | X-ray | 1.90 | C/P | 2-16 | [»] | |
5T1G | X-ray | 1.90 | B | 39-53 | [»] | |
5T1I | X-ray | 1.60 | C | 39-53 | [»] | |
5T8R | X-ray | 2.40 | E/G | 2-11 | [»] | |
5TBN | NMR | - | C | 2-12 | [»] | |
5TDR | X-ray | 1.42 | B | 2-12 | [»] | |
5TDW | X-ray | 1.70 | B | 2-12 | [»] | |
5U2J | X-ray | 1.60 | C/D | 2-17 | [»] | |
5V21 | X-ray | 2.42 | B | 30-44 | [»] | |
5V22 | X-ray | 2.40 | B | 30-44 | [»] | |
5VA6 | X-ray | 2.40 | C/D | 20-37 | [»] | |
5VAB | X-ray | 1.70 | F | 2-11 | [»] | |
5VGE | X-ray | 2.60 | C | 41-49 | [»] | |
5VNB | X-ray | 2.40 | K | 22-31 | [»] | |
5WFC | X-ray | 2.28 | D | 23-33 | [»] | |
5WLE | X-ray | 1.95 | C | 2-13 | [»] | |
5WVO | X-ray | 2.00 | D | 2-37 | [»] | |
5WXG | X-ray | 1.70 | P | 2-8 | [»] | |
5WXH | X-ray | 1.30 | D/P | 2-8 | [»] | |
5WYI | X-ray | 2.00 | E | 120-127 | [»] | |
5X60 | X-ray | 2.69 | C | 2-21 | [»] | |
5XF3 | X-ray | 2.60 | A/E | 1-136 | [»] | |
5XF4 | X-ray | 2.87 | A/E | 1-136 | [»] | |
5XF5 | X-ray | 2.82 | A/E | 1-136 | [»] | |
5XFQ | X-ray | 2.40 | E/F | 30-42 | [»] | |
5XFR | X-ray | 2.25 | C/D | 34-41 | [»] | |
5XNV | X-ray | 2.70 | B | 25-32 | [»] | |
5XTZ | X-ray | 2.10 | E | 23-32 | [»] | |
5Y0C | X-ray | 2.09 | A/E | 1-136 | [»] | |
5Y0D | X-ray | 1.99 | A/E | 1-136 | [»] | |
5Y20 | X-ray | 2.41 | P | 2-8 | [»] | |
5Y2F | X-ray | 2.53 | C | 6-14 | [»] | |
5Z23 | X-ray | 2.73 | A/E | 1-75 | [»] | |
A/E | 116-136 | [»] | ||||
5Z30 | X-ray | 2.45 | A/E | 1-136 | [»] | |
6AXJ | X-ray | 2.38 | E/F/G/H | 22-32 | [»] | |
6AZE | X-ray | 2.45 | P | 2-7 | [»] | |
6BHD | X-ray | 1.25 | B | 4-20 | [»] | |
6BHE | X-ray | 1.35 | B | 4-20 | [»] | |
6BHG | X-ray | 1.45 | B | 4-20 | [»] | |
6BHH | X-ray | 1.85 | B | 4-20 | [»] | |
6BHI | X-ray | 1.40 | B | 5-20 | [»] | |
6D07 | X-ray | 2.10 | C/D | 2-16 | [»] | |
6D08 | X-ray | 2.10 | C/D | 2-16 | [»] | |
6E83 | NMR | - | A | 2-13 | [»] | |
6E86 | NMR | - | A | 2-9 | [»] | |
6F6D | X-ray | 1.82 | B | 18-34 | [»] | |
6HKT | X-ray | 9.70 | A/E/K/O/U/Y/a/e/k/o/u/y | 1-136 | [»] | |
6HTS | electron microscopy | 4.80 | I/M | 1-136 | [»] | |
6IEU | X-ray | 1.79 | C | 2-13 | [»] | |
6IIS | X-ray | 2.36 | E/F | 34-41 | [»] | |
6IIT | X-ray | 2.10 | E/F | 34-41 | [»] | |
6IPU | X-ray | 1.99 | A/E | 39-136 | [»] | |
6IQ4 | X-ray | 2.25 | A/E | 39-136 | [»] | |
6JOU | X-ray | 2.17 | A/E | 1-136 | [»] | |
6JR0 | X-ray | 2.50 | A/E | 1-136 | [»] | |
6JR1 | X-ray | 2.40 | A/E | 1-136 | [»] | |
6JXD | X-ray | 2.25 | A | 39-136 | [»] | |
E | 39-135 | [»] | ||||
6K1I | X-ray | 2.75 | A/E | 1-136 | [»] | |
6K1J | X-ray | 2.85 | A/E | 1-136 | [»] | |
6K1K | X-ray | 2.20 | A/E | 1-136 | [»] | |
6KE9 | X-ray | 2.22 | A/E | 41-136 | [»] | |
6KVD | X-ray | 2.21 | A/E | 1-136 | [»] | |
6L49 | electron microscopy | 18.90 | K/O/S/W | 1-136 | [»] | |
6L4A | electron microscopy | 12.30 | A/E/K/O/S/W | 1-136 | [»] | |
6L9H | X-ray | 2.60 | A/E | 41-136 | [»] | |
6LE9 | X-ray | 2.60 | A/E | 41-136 | [»] | |
6MIL | X-ray | 1.93 | B/D | 2-20 | [»] | |
6MIM | X-ray | 2.52 | B/D | 6-14 | [»] | |
6MIN | X-ray | 1.90 | B | 6-12 | [»] | |
6MIO | X-ray | 1.85 | B | 6-12 | [»] | |
6MIQ | X-ray | 1.75 | C | 6-12 | [»] | |
6R8Y | electron microscopy | 4.30 | A/E | 1-136 | [»] | |
6R8Z | electron microscopy | 3.90 | A/E | 1-136 | [»] | |
6R90 | electron microscopy | 4.50 | A/E | 1-136 | [»] | |
6R91 | electron microscopy | 4.10 | A/E | 1-136 | [»] | |
6R92 | electron microscopy | 4.80 | A/E | 1-136 | [»] | |
6R93 | electron microscopy | 4.00 | A/E | 1-136 | [»] | |
6R94 | electron microscopy | 3.50 | A/E | 1-136 | [»] | |
6T90 | electron microscopy | 3.05 | A | 1-136 | [»] | |
E | 1-134 | [»] | ||||
6T93 | electron microscopy | 3.49 | A/E | 1-136 | [»] | |
6UPK | electron microscopy | 4.90 | A/E | 1-136 | [»] | |
6UPL | electron microscopy | 7.40 | A/E | 1-136 | [»] | |
6V2H | X-ray | 2.60 | B/D/F/H/J/L | 22-33 | [»] | |
6V3N | X-ray | 2.70 | C/D | 20-33 | [»] | |
6V41 | X-ray | 1.60 | QQQ | 2-16 | [»] | |
6V92 | electron microscopy | 20.00 | a/e | 1-136 | [»] | |
6WAV | X-ray | 1.70 | E/F/G/H | 32-43 | [»] | |
6WW4 | X-ray | 2.25 | A/B | 2-7 | [»] | |
6YIF | X-ray | 1.81 | D | 2-13 | [»] | |
6YIH | X-ray | 2.55 | D | 2-13 | [»] | |
6YOV | electron microscopy | 3.42 | A | 1-136 | [»] | |
E | 1-134 | [»] | ||||
SMRi | P68431 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 113946, 667 interactors 113947, 16 interactors 113948, 17 interactors 113949, 205 interactors 113950, 10 interactors |