Srebf2
entrez
20788
canonical
uniprot
Q3U1N2
canonical
ensembl
ENSMUSG00000022463
resolver
ensp
ENSMUSP00000023100
resolver
genesymbol
Srebf2
resolver
genesymbol_syn
Srebp2
resolver
uniprot
Q925C2
resolver
uniprot
Q9ESZ4
resolver
uniprot_entry
SRBP2_MOUSE
resolver
uniprot_sec
Q925C2
resolver
uniprot_sec
Q9ESZ4
resolver
activity_regulation
ACTIVITY REGULATION: Activation by cleavage is down-regulated upon activation of SIRT3-dependent PRKAA1/AMPK-alpha signaling cascade which leads to inhibition of ATP-consuming lipogenesis to restore cellular energy balance. {ECO:0000269|PubMed:36804859}.
uniprot
proteins
amino_acid_sequence
MDESSELGVLETMETLTELGDELTLGDIDEMLQFVSNQVGEFPDLFSEQLCSSFPGGGSNGGSGNNSSGRGNNGGATDPAVQRSFSQVPLSTFSPSAASPQAPALQVKVSPTPPRATPVLQPRPQPQPQPPAQLQQQTVMITPTFSTAPQTRIIQQPLIYQNAATSFQVLQPQVQSLVTSPQVQPVTIQQQVQTVQAQRVLTQTANGTLQTLAPATVQTVAAPQVQQVPVLVQPQIIKTDSLVLTTLKTDGSPVMAAVQNPALTALTAPIQTAALQVPTLVGSNGTILTTMPVMMGQEKVPIKQVPGGVKQLDPPKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMVLKLANQKNKLLKGIDLGSLVDSDVDLKIDDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSRILLCVLTFLGLSFNPLTSLLQWGGAHNTDQHPYSGSGRSVLSLESGAGGWFDWMVPTLLLWLVNGVIVLSVFVKLLVHGEPVIRPHSRPSVTFWRHRKQADLDLAKGDFAAAAANLQTCLSVLGRALPTSRLDLACSLSWNVIRYSLQKLRLVRWLLKKVFQRWRATPATAAGFEDEAKSSARDAALAYHRLHQLHITGKLPAGSACSDVHMALCAVNLAECAEEKILPSTLIEIHLTAAMGLKTRCGGKLGFLASYFLNRAQSLCGPEHSTVPDSLRWLCHPLGQKFFMERSWSIKSAAKESLYCAQRSPADPIAQVHQAFCKNLLERAVESLVKPQAKKKAGDQEEESCEFSSALEYLKLLHSFVDSVGFVTSPFSSSSVLRSALGPDVICRWWTSAVTMAISWLQGDDAAVRSRFTEVERVPKALEVTESPLVKAVFYTCRAMHASLSGKADGQQNSFCHCERASGHLWSSLNVSGTTSDPSLNHVIQLFTCDLLLSLRTALWQKQASASQLLGETYHASGTELAGFQRDLGSLRRLAHSFRPAYRKVFLHEATVRLMAGASPTRTHQLLEHSLRRRPTQNTKHGEVDTWPGQRERATAILLACRHLPLSFLSSPGQRAVLLAEAARTLEKVGDRRSCSDCQQMIVKLGGGTAIAAS
uniprot
proteins
function
FUNCTION: [Sterol regulatory element-binding protein 2]: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 2), which is embedded in the endoplasmic reticulum membrane (By similarity). 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). {ECO:0000250|UniProtKB:Q12772, ECO:0000269|PubMed:16100574, ECO:0000269|PubMed:9616204}.; FUNCTION: [Processed sterol regulatory element-binding protein 2]: Key transcription factor that regulates expression of genes involved in cholesterol biosynthesis (PubMed:9616204, PubMed:36056653). 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). {ECO:0000250|UniProtKB:Q12772, ECO:0000269|PubMed:36056653, ECO:0000269|PubMed:9616204}.
uniprot
proteins
mass_dalton
122911
uniprot
proteins
mutagenesis
MUTAGEN 369..383; /note="LQQVNHKLRQENMVL->AQQVNHKARQENMVA: In L1.2.3A mutant; reduced affinity for importin-beta."; /evidence="ECO:0000269|PubMed:11283257
uniprot
proteins
post_translational_modification
PTM: [Sterol regulatory element-binding protein 2]: Processed in the Golgi apparatus, releasing the protein from the membrane. At low cholesterol the SCAP-SREBP complex is recruited into COPII vesicles for export from the endoplasmic reticulum. In the Golgi, complex SREBPs are cleaved sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain, releasing the transcription factor from the Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7. Cleavage and activation is induced by mediated cholesterol efflux. {ECO:0000250|UniProtKB:Q12772}.; PTM: Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression. {ECO:0000269|PubMed:21459323}.; PTM: [Sterol regulatory element-binding protein 2]: SCAP-free SREBF2 is ubiquitinated by the BCR(ARMC5) complex, leading to its degradation. {ECO:0000250|UniProtKB:Q12772}.; PTM: [Processed sterol regulatory element-binding protein 2]: Ubiquitinated; the nuclear form has a rapid turnover and is rapidly ubiquitinated and degraded by the proteasome in the nucleus. {ECO:0000250|UniProtKB:Q12772}.
uniprot
proteins
protein_family
SREBP family
uniprot
proteins
pubmed
10397761
uniprot
proteins
pubmed
11283257
uniprot
proteins
pubmed
11929849
uniprot
proteins
pubmed
11994399
uniprot
proteins
pubmed
12668174
uniprot
proteins
pubmed
16100574
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21459323
uniprot
proteins
pubmed
26311497
uniprot
proteins
pubmed
28849786
uniprot
proteins
pubmed
29068315
uniprot
proteins
pubmed
36056653
uniprot
proteins
pubmed
36804859
uniprot
proteins
pubmed
9616204
uniprot
proteins
sequence_length
1130
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000303|PubMed:28849786}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000303|PubMed:28849786}; Multi-pass membrane protein {ECO:0000255}. Note=At high sterol concentrations, the SCAP-SREBP is retained in the endoplasmic reticulum (By similarity). Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed (By similarity). {ECO:0000250|UniProtKB:Q12772}.; SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding protein 2]: Nucleus {ECO:0000269|PubMed:10397761, ECO:0000269|PubMed:11283257, ECO:0000269|PubMed:29068315}. Note=Transported into the nucleus with the help of importin-beta (PubMed:10397761, PubMed:11283257). Dimerization of the bHLH domain is a prerequisite for importin beta-dependent nuclear import (PubMed:10397761, PubMed:11283257). {ECO:0000269|PubMed:10397761, ECO:0000269|PubMed:11283257}.
uniprot
proteins
transmembrane_region
TRANSMEM 471..491; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 523..543; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins