P26583 · HMGB2_HUMAN
- ProteinHigh mobility group protein B2
- GeneHMGB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids209 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity (PubMed:11909973, PubMed:18413230, PubMed:19522541, PubMed:19965638, PubMed:20123072, PubMed:7797075).
Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (By similarity).
Proposed to be involved in the innate immune response to nucleic acids by acting as a promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (By similarity).
In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE (PubMed:19811285).
Has antimicrobial activity in gastrointestinal epithelial tissues (PubMed:23877675).
Involved in inflammatory response to antigenic stimulus coupled with pro-inflammatory activity (By similarity).
Involved in modulation of neurogenesis probably by regulation of neural stem proliferation (By similarity).
Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway (By similarity).
Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (By similarity).
Proposed to be involved in the innate immune response to nucleic acids by acting as a promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (By similarity).
In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE (PubMed:19811285).
Has antimicrobial activity in gastrointestinal epithelial tissues (PubMed:23877675).
Involved in inflammatory response to antigenic stimulus coupled with pro-inflammatory activity (By similarity).
Involved in modulation of neurogenesis probably by regulation of neural stem proliferation (By similarity).
Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway (By similarity).
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 9-79 | HMG box 1 | ||||
Sequence: PRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYV | ||||||
DNA binding | 95-163 | HMG box 2 | ||||
Sequence: PKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYR |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHigh mobility group protein B2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP26583
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In basal state predominantly nuclear.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 195 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000048534 | 1-209 | UniProt | High mobility group protein B2 | |||
Sequence: MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEDEDEEEEDEDEE | |||||||
Modified residue | 3 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 16 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 23 | UniProt | Cysteine sulfonic acid (-SO3H); alternate | ||||
Sequence: C | |||||||
Disulfide bond | 23↔45 | UniProt | In disulfide HMGB2; alternate | ||||
Sequence: CREEHKKKHPDSSVNFAEFSKKC | |||||||
Modified residue | 30 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 35 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 35 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 43 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 45 | UniProt | Cysteine sulfonic acid (-SO3H); alternate | ||||
Sequence: C | |||||||
Modified residue | 90 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 100 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 106 | UniProt | Cysteine sulfonic acid (-SO3H) | ||||
Sequence: C | |||||||
Modified residue | 114 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 141 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).
Acetylation enhances nucleosome binding and chromation remodeling activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in gastric and intestinal tissues (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with POU2F2, POU2F1 and POU3F1 (By similarity).
Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2 (By similarity).
Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET (PubMed:11909973).
Interacts with LEF1 (By similarity).
Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2 (By similarity).
Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET (PubMed:11909973).
Interacts with LEF1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P26583 | COMMD1 Q8N668 | 3 | EBI-1057009, EBI-1550112 | |
BINARY | P26583 | MIEN1 Q9BRT3 | 6 | EBI-1057009, EBI-6137472 | |
BINARY | P26583 | NOP53 Q9NZM5 | 4 | EBI-1057009, EBI-720156 | |
BINARY | P26583 | PKNOX1 P55347 | 4 | EBI-1057009, EBI-1373569 | |
BINARY | P26583 | PKNOX1 Q96I87 | 3 | EBI-1057009, EBI-10173774 | |
BINARY | P26583 | TSNAX Q99598 | 3 | EBI-1057009, EBI-21353855 | |
BINARY | P26583 | ZNF428 Q96B54 | 4 | EBI-1057009, EBI-9995882 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-95 | Basic and acidic residues | ||||
Sequence: MSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAP | ||||||
Region | 52-150 | Disordered | ||||
Sequence: MSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAK | ||||||
Compositional bias | 133-150 | Basic and acidic residues | ||||
Sequence: WSEQSAKDKQPYEQKAAK | ||||||
Region | 162-209 | Disordered | ||||
Sequence: YRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEDEDEEEEDEDEE | ||||||
Region | 165-180 | Required for chemotactic activity | ||||
Sequence: KGKSEAGKKGPGRPTG | ||||||
Compositional bias | 188-209 | Acidic residues | ||||
Sequence: EDEEEEEEEEDEDEEEEDEDEE |
Domain
Both, HMG box 1 and HMG box 2, show antimicrobial activity.
Sequence similarities
Belongs to the HMGB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length209
- Mass (Da)24,034
- Last updated2007-01-23 v2
- Checksum5E65292BC4AD8373
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D6R9A6 | D6R9A6_HUMAN | HMGB2 | 134 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-95 | Basic and acidic residues | ||||
Sequence: MSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAP | ||||||
Compositional bias | 133-150 | Basic and acidic residues | ||||
Sequence: WSEQSAKDKQPYEQKAAK | ||||||
Sequence conflict | 163 | in Ref. 7; CAA78938 | ||||
Sequence: R → G | ||||||
Compositional bias | 188-209 | Acidic residues | ||||
Sequence: EDEEEEEEEEDEDEEEEDEDEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M83665 EMBL· GenBank· DDBJ | AAA58659.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X62534 EMBL· GenBank· DDBJ | CAA44395.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019782 EMBL· GenBank· DDBJ | AAV38585.1 EMBL· GenBank· DDBJ | mRNA | ||
AK311864 EMBL· GenBank· DDBJ | BAG34805.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471056 EMBL· GenBank· DDBJ | EAX04758.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471056 EMBL· GenBank· DDBJ | EAX04759.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001063 EMBL· GenBank· DDBJ | AAH01063.1 EMBL· GenBank· DDBJ | mRNA | ||
BC100019 EMBL· GenBank· DDBJ | AAI00020.1 EMBL· GenBank· DDBJ | mRNA | ||
Z17240 EMBL· GenBank· DDBJ | CAA78938.1 EMBL· GenBank· DDBJ | mRNA |