P17741 (HMGB2_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 92.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: High mobility group protein B2 Alternative name(s): High mobility group protein 2 Short name=HMG-2 | ||||
| Gene names |
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| Organism | Sus scrofa (Pig) [Complete proteome] | ||||
| Taxonomic identifier | 9823 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 210 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. 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. |
| Subunit structure | Component of the SET complex, which also contains SET, ANP32A, APEX1 and NME1. Directly interacts with SET. Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2 By similarity. |
| Subcellular location | Nucleus By similarity. Chromosome By similarity. |
| Sequence similarities | Belongs to the HMGB family. Contains 2 HMG box DNA-binding domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosome Nucleus |
| Domain | Repeat |
| Ligand | DNA-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | DNA topological change Inferred from direct assay. Source: UniProtKB base-excision repair, DNA ligationInferred from sequence or structural similarity. Source: UniProtKB regulation of transcription from RNA polymerase II promoterInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | condensed chromosome Inferred from sequence or structural similarity. Source: UniProtKB nucleusInferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasmInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | DNA binding, bending Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | |||||||||||||||||||||||||||
| Chain | 2 – 210 | 209 | High mobility group protein B2 | PRO_0000048536 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| DNA binding | 9 – 79 | 71 | HMG box 1 | |||||||||||||||||||||||||||
| DNA binding | 95 – 163 | 69 | HMG box 2 | |||||||||||||||||||||||||||
| Compositional bias | 186 – 210 | 25 | Asp/Glu-rich (acidic) | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 30 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||
| Modified residue | 35 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||
| Modified residue | 59 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||
| Modified residue | 155 | 1 | Phosphotyrosine By similarity | |||||||||||||||||||||||||||
| Modified residue | 162 | 1 | Phosphotyrosine By similarity | |||||||||||||||||||||||||||
| Modified residue | 172 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||
| Modified residue | 173 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 6 – 8 | 3 | ||||||||||||||||||||||||||||
| Helix | 15 – 25 | 11 | ||||||||||||||||||||||||||||
| Helix | 28 – 30 | 3 | ||||||||||||||||||||||||||||
| Helix | 38 – 51 | 14 | ||||||||||||||||||||||||||||
| Helix | 54 – 70 | 17 | ||||||||||||||||||||||||||||
| Turn | 71 – 74 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 92 – 94 | 3 | ||||||||||||||||||||||||||||
| Helix | 102 – 116 | 15 | ||||||||||||||||||||||||||||
| Helix | 122 – 135 | 14 | ||||||||||||||||||||||||||||
| Helix | 147 – 149 | 3 | ||||||||||||||||||||||||||||
| Helix | 152 – 163 | 12 | ||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Primary structure of non-histone chromosomal protein HMG2 revealed by the nucleotide sequence." Shirakawa H., Tsuda K., Yoshida M. Biochemistry 29:4419-4423(1990) [PubMed: 2350545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | J02895 mRNA. Translation: AAA31051.1. | ||||||||||||||||||||||||
| PIR | A34719. | ||||||||||||||||||||||||
| RefSeq | NP_999228.1. NM_214063.1. | ||||||||||||||||||||||||
| UniGene | Ssc.226. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P17741. | ||||||||||||||||||||||||
| SMR | P17741. Positions 5-166. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| GeneID | 397130. | ||||||||||||||||||||||||
| KEGG | ssc:397130. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 3148. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| GeneTree | ENSGT00560000076717. | ||||||||||||||||||||||||
| HOVERGEN | HBG009000. | ||||||||||||||||||||||||
| OrthoDB | EOG4TTGK2. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR011989. ARM-like. IPR017967. HMG_boxA_CS. IPR000910. HMG_HMG1/HMG2. IPR000135. HMG_HMG1/HMG2_subgr. IPR009071. HMG_superfamily. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:1.25.10.10. ARM-like. 1 hit. G3DSA:1.10.30.10. HMG-box. 2 hits. | ||||||||||||||||||||||||
| KO | K11295. | ||||||||||||||||||||||||
| Pfam | PF00505. HMG_box. 2 hits. [Graphical view] | ||||||||||||||||||||||||
| PRINTS | PR00886. HIGHMOBLTY12. | ||||||||||||||||||||||||
| SMART | SM00398. HMG. 2 hits. [Graphical view] | ||||||||||||||||||||||||
| SUPFAM | SSF47095. HMG-box. 2 hits. | ||||||||||||||||||||||||
| PROSITE | PS00353. HMG_BOX_1. 1 hit. PS50118. HMG_BOX_2. 2 hits. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | HMGB2_PIG | ||||||||
| Accession | Primary (citable) accession number: P17741 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with