Q3U1N2 · SRBP2_MOUSE
- ProteinSterol regulatory element-binding protein 2
- GeneSrebf2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1130 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Sterol regulatory element-binding protein 2
Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis (PubMed:16100574, PubMed:9616204).
Processed sterol regulatory element-binding protein 2
Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3') (By similarity).
Regulates transcription of genes related to cholesterol synthesis pathway (PubMed:9616204).
Activity regulation
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 457-458 | Cleavage; by caspase-3 and caspase-7 | ||||
Sequence: DS | ||||||
Site | 473-474 | Cleavage; by MBTPS2 | ||||
Sequence: LC | ||||||
Site | 511-512 | Cleavage; by MBTPS1 | ||||
Sequence: LS |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSterol regulatory element-binding protein 2
- Short namesSREBP-2
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3U1N2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed (By similarity).
Processed sterol regulatory element-binding protein 2
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-470 | Cytoplasmic | ||||
Sequence: MDESSELGVLETMETLTELGDELTLGDIDEMLQFVSNQVGEFPDLFSEQLCSSFPGGGSNGGSGNNSSGRGNNGGATDPAVQRSFSQVPLSTFSPSAASPQAPALQVKVSPTPPRATPVLQPRPQPQPQPPAQLQQQTVMITPTFSTAPQTRIIQQPLIYQNAATSFQVLQPQVQSLVTSPQVQPVTIQQQVQTVQAQRVLTQTANGTLQTLAPATVQTVAAPQVQQVPVLVQPQIIKTDSLVLTTLKTDGSPVMAAVQNPALTALTAPIQTAALQVPTLVGSNGTILTTMPVMMGQEKVPIKQVPGGVKQLDPPKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMVLKLANQKNKLLKGIDLGSLVDSDVDLKIDDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSR | ||||||
Transmembrane | 471-491 | Helical | ||||
Sequence: ILLCVLTFLGLSFNPLTSLLQ | ||||||
Topological domain | 492-522 | Lumenal | ||||
Sequence: WGGAHNTDQHPYSGSGRSVLSLESGAGGWFD | ||||||
Transmembrane | 523-543 | Helical | ||||
Sequence: WMVPTLLLWLVNGVIVLSVFV | ||||||
Topological domain | 544-1130 | Cytoplasmic | ||||
Sequence: KLLVHGEPVIRPHSRPSVTFWRHRKQADLDLAKGDFAAAAANLQTCLSVLGRALPTSRLDLACSLSWNVIRYSLQKLRLVRWLLKKVFQRWRATPATAAGFEDEAKSSARDAALAYHRLHQLHITGKLPAGSACSDVHMALCAVNLAECAEEKILPSTLIEIHLTAAMGLKTRCGGKLGFLASYFLNRAQSLCGPEHSTVPDSLRWLCHPLGQKFFMERSWSIKSAAKESLYCAQRSPADPIAQVHQAFCKNLLERAVESLVKPQAKKKAGDQEEESCEFSSALEYLKLLHSFVDSVGFVTSPFSSSSVLRSALGPDVICRWWTSAVTMAISWLQGDDAAVRSRFTEVERVPKALEVTESPLVKAVFYTCRAMHASLSGKADGQQNSFCHCERASGHLWSSLNVSGTTSDPSLNHVIQLFTCDLLLSLRTALWQKQASASQLLGETYHASGTELAGFQRDLGSLRRLAHSFRPAYRKVFLHEATVRLMAGASPTRTHQLLEHSLRRRPTQNTKHGEVDTWPGQRERATAILLACRHLPLSFLSSPGQRAVLLAEAARTLEKVGDRRSCSDCQQMIVKLGGGTAIAAS |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 369-383 | In L1.2.3A mutant; reduced affinity for importin-beta. | ||||
Sequence: LQQVNHKLRQENMVL → AQQVNHKARQENMVA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 52 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000317060 | 1-473 | Processed sterol regulatory element-binding protein 2 | |||
Sequence: MDESSELGVLETMETLTELGDELTLGDIDEMLQFVSNQVGEFPDLFSEQLCSSFPGGGSNGGSGNNSSGRGNNGGATDPAVQRSFSQVPLSTFSPSAASPQAPALQVKVSPTPPRATPVLQPRPQPQPQPPAQLQQQTVMITPTFSTAPQTRIIQQPLIYQNAATSFQVLQPQVQSLVTSPQVQPVTIQQQVQTVQAQRVLTQTANGTLQTLAPATVQTVAAPQVQQVPVLVQPQIIKTDSLVLTTLKTDGSPVMAAVQNPALTALTAPIQTAALQVPTLVGSNGTILTTMPVMMGQEKVPIKQVPGGVKQLDPPKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMVLKLANQKNKLLKGIDLGSLVDSDVDLKIDDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSRILL | ||||||
Chain | PRO_0000317059 | 1-1130 | Sterol regulatory element-binding protein 2 | |||
Sequence: MDESSELGVLETMETLTELGDELTLGDIDEMLQFVSNQVGEFPDLFSEQLCSSFPGGGSNGGSGNNSSGRGNNGGATDPAVQRSFSQVPLSTFSPSAASPQAPALQVKVSPTPPRATPVLQPRPQPQPQPPAQLQQQTVMITPTFSTAPQTRIIQQPLIYQNAATSFQVLQPQVQSLVTSPQVQPVTIQQQVQTVQAQRVLTQTANGTLQTLAPATVQTVAAPQVQQVPVLVQPQIIKTDSLVLTTLKTDGSPVMAAVQNPALTALTAPIQTAALQVPTLVGSNGTILTTMPVMMGQEKVPIKQVPGGVKQLDPPKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMVLKLANQKNKLLKGIDLGSLVDSDVDLKIDDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSRILLCVLTFLGLSFNPLTSLLQWGGAHNTDQHPYSGSGRSVLSLESGAGGWFDWMVPTLLLWLVNGVIVLSVFVKLLVHGEPVIRPHSRPSVTFWRHRKQADLDLAKGDFAAAAANLQTCLSVLGRALPTSRLDLACSLSWNVIRYSLQKLRLVRWLLKKVFQRWRATPATAAGFEDEAKSSARDAALAYHRLHQLHITGKLPAGSACSDVHMALCAVNLAECAEEKILPSTLIEIHLTAAMGLKTRCGGKLGFLASYFLNRAQSLCGPEHSTVPDSLRWLCHPLGQKFFMERSWSIKSAAKESLYCAQRSPADPIAQVHQAFCKNLLERAVESLVKPQAKKKAGDQEEESCEFSSALEYLKLLHSFVDSVGFVTSPFSSSSVLRSALGPDVICRWWTSAVTMAISWLQGDDAAVRSRFTEVERVPKALEVTESPLVKAVFYTCRAMHASLSGKADGQQNSFCHCERASGHLWSSLNVSGTTSDPSLNHVIQLFTCDLLLSLRTALWQKQASASQLLGETYHASGTELAGFQRDLGSLRRLAHSFRPAYRKVFLHEATVRLMAGASPTRTHQLLEHSLRRRPTQNTKHGEVDTWPGQRERATAILLACRHLPLSFLSSPGQRAVLLAEAARTLEKVGDRRSCSDCQQMIVKLGGGTAIAAS | ||||||
Cross-link | 453 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1087 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Sterol regulatory element-binding protein 2
Processed sterol regulatory element-binding protein 2
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Sterol regulatory element-binding protein 2
Processed sterol regulatory element-binding protein 2
Interacts with LMNA (PubMed:11929849).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q3U1N2 | Srf Q9JM73 | 3 | EBI-645275, EBI-493266 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-50 | Transcriptional activation (acidic) | ||||
Sequence: MDESSELGVLETMETLTELGDELTLGDIDEMLQFVSNQVGEFPDLFSEQL | ||||||
Compositional bias | 53-106 | Polar residues | ||||
Sequence: SFPGGGSNGGSGNNSSGRGNNGGATDPAVQRSFSQVPLSTFSPSAASPQAPALQ | ||||||
Region | 53-133 | Disordered | ||||
Sequence: SFPGGGSNGGSGNNSSGRGNNGGATDPAVQRSFSQVPLSTFSPSAASPQAPALQVKVSPTPPRATPVLQPRPQPQPQPPAQ | ||||||
Compositional bias | 115-131 | Pro residues | ||||
Sequence: RATPVLQPRPQPQPQPP | ||||||
Region | 226-480 | Interaction with LMNA | ||||
Sequence: QQVPVLVQPQIIKTDSLVLTTLKTDGSPVMAAVQNPALTALTAPIQTAALQVPTLVGSNGTILTTMPVMMGQEKVPIKQVPGGVKQLDPPKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMVLKLANQKNKLLKGIDLGSLVDSDVDLKIDDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSRILLCVLTFLG | ||||||
Domain | 319-369 | bHLH | ||||
Sequence: ERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYL | ||||||
Region | 369-390 | Leucine-zipper | ||||
Sequence: LQQVNHKLRQENMVLKLANQKN |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q3U1N2-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,130
- Mass (Da)122,911
- Last updated2008-02-05 v2
- Checksum052E858B0C3945F2
Q3U1N2-2
- Name2
- Differences from canonical
- 57-96: Missing
- 1105-1130: VGDRRSCSDCQQMIVKLGGGTAIAAS → SCEDEGKTDCSELLPAKAFGSFRASRTMGRAP
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8VHQ9 | A0A2R8VHQ9_MOUSE | Srebf2 | 247 | ||
A0A2R8VH82 | A0A2R8VH82_MOUSE | Srebf2 | 193 |
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 53-106 | Polar residues | ||||
Sequence: SFPGGGSNGGSGNNSSGRGNNGGATDPAVQRSFSQVPLSTFSPSAASPQAPALQ | ||||||
Alternative sequence | VSP_052658 | 57-96 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 115-131 | Pro residues | ||||
Sequence: RATPVLQPRPQPQPQPP | ||||||
Sequence conflict | 334 | in Ref. 3; AAK54763 | ||||
Sequence: S → F | ||||||
Sequence conflict | 621 | in Ref. 3; AAK54763 | ||||
Sequence: R → H | ||||||
Sequence conflict | 698 | in Ref. 3; AAK54763 | ||||
Sequence: L → P | ||||||
Sequence conflict | 899 | in Ref. 3; AAK54763 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_052659 | 1105-1130 | in isoform 2 | |||
Sequence: VGDRRSCSDCQQMIVKLGGGTAIAAS → SCEDEGKTDCSELLPAKAFGSFRASRTMGRAP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK155857 EMBL· GenBank· DDBJ | BAE33463.1 EMBL· GenBank· DDBJ | mRNA | ||
AC105358 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF374267 EMBL· GenBank· DDBJ | AAK54763.1 EMBL· GenBank· DDBJ | mRNA | ||
AF289715 EMBL· GenBank· DDBJ | AAG01859.2 EMBL· GenBank· DDBJ | mRNA |