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Q9WTN3 (SRBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sterol regulatory element-binding protein 1

Short name=SREBP-1
Alternative name(s):
Sterol regulatory element-binding transcription factor 1
Gene names
Name:Srebf1
Synonyms:Srebp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1134 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the fatty acid and to a lesser degree the cholesterol synthesis pathway. 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'). Isoform SREBP-1A is much more active than isoform SREBP-1C in stimulating transcription from SRE-1-containing promoters. Ref.7 Ref.8 Ref.10 Ref.11

Subunit structure

Forms a tight complex with SCAP in the ER membrane. Efficient DNA binding of the soluble transcription factor fragment requires dimerization with another bHLH protein. Interacts with LMNA. Ref.9

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cytoplasmic vesicleCOPII-coated vesicle membrane; Multi-pass membrane protein. Note: Moves from the endoplasmic reticulum to the Golgi in the absence of sterols. Ref.14

Processed sterol regulatory element-binding protein 1: Nucleus Ref.14.

Tissue specificity

Isoform SREBP-1C predominates in liver, adrenal gland, brain and adipose tissue, whereas isoform SREBP-1A predominates in spleen. Isoform SREBP-1A and isoform SREBP-1C are found in kidney, thymus, testis, muscle, jejunum, and ileum.

Induction

Isoform SREBP-1C is expressed in a circadian manner in the liver with a peak at ZT16. Ref.13

Post-translational modification

At low cholesterol the SCAP/SREBP complex is recruited into COPII vesicles for export from the ER. In the Golgi complex SREBPs are cleaved sequentially by site-1 and site-2 protease. 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 and releases the transcription factor from the Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7.

Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression. Phosphorylation at Ser-389 by SIK1 represses activity possibly by inhibiting DNA-binding. Ref.12 Ref.14

Disruption phenotype

Mice show high embryonic lethality around day 11 dpc. Surviving mice show a 2-3-fold increase in processed Srebpf2 protein in liver nuclei, 3-fold increase in cholesterol synthesis and 50% increase in cholesterol content of the liver. Mice lacking isoform SREBP-1C show a lack of up-regulation of several lipogenic enzymes in response to high insulin or LXR activation. Mice overexpressing processed isoform SREBP-1A in adipocytes show enlarged white and brown adipocytes, increased rate of fatty acid synthesis and secretion leading to a fatty liver. Mice overexpressing processed isoform SREBP-1C in adipocytes show inhibition of adipocyte differentiation leading to a syndrome similar to human lipodystrophy with loss of peripheral white adipose tissue, diabetes and fatty liver. Ref.7 Ref.10

Sequence similarities

Belongs to the SREBP family.

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid metabolism
Steroid metabolism
Sterol metabolism
Transcription
Transcription regulation
   Cellular componentCytoplasmic vesicle
Endoplasmic reticulum
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

cellular response to fatty acid

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from direct assay PubMed 16407292. Source: HGNC

cholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor signaling pathway

Inferred from direct assay PubMed 17074803. Source: MGI

lipid biosynthetic process

Inferred from direct assay Ref.14. Source: UniProtKB

lung development

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 16890542. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17074803. Source: MGI

positive regulation of cholesterol biosynthetic process

Inferred from mutant phenotype PubMed 16046411Ref.7. Source: MGI

positive regulation of fatty acid biosynthetic process

Traceable author statement PubMed 11090130. Source: BHF-UCL

positive regulation of histone deacetylation

Inferred from direct assay PubMed 17636037. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 14654692PubMed 16890542PubMed 17074803PubMed 18060044Ref.7. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11090130. Source: BHF-UCL

positive regulation of triglyceride biosynthetic process

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of fatty acid metabolic process

Inferred from mutant phenotype PubMed 19564420. Source: MGI

regulation of heart rate by chemical signal

Inferred from mutant phenotype PubMed 18060044. Source: MGI

regulation of insulin secretion

Inferred from mutant phenotype PubMed 18178930. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay Ref.14. Source: UniProtKB

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to food

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from mutant phenotype PubMed 18178930. Source: MGI

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentER to Golgi transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

cytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 11090130. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.14. Source: UniProtKB

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay Ref.12. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 15637161PubMed 17074803PubMed 19564420. Source: MGI

protein binding

Inferred from physical interaction PubMed 20817729. Source: IntAct

protein kinase binding

Inferred from physical interaction Ref.12Ref.14. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 14654692. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity PubMed 16407292. Source: HGNC

sterol response element binding

Inferred from sequence or structural similarity PubMed 16407292. Source: HGNC

transcription regulatory region DNA binding

Inferred from direct assay PubMed 11739104. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sirt1Q923E42EBI-5273743,EBI-1802585

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform SREBP-1A (identifier: Q9WTN3-1)

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.
Isoform SREBP-1A-W42 (identifier: Q9WTN3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     90-131: Missing.
Isoform SREBP-1C (identifier: Q9WTN3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MDELAFGEAALEQTLAEMCELDTAVLNDI → MDCTF
Isoform SREBP-1C-W42 (identifier: Q9WTN3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MDELAFGEAALEQTLAEMCELDTAVLNDI → MDCTF
     90-131: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11341134Sterol regulatory element-binding protein 1
PRO_0000127448
Chain1 – 480480Processed sterol regulatory element-binding protein 1
PRO_0000314030

Regions

Topological domain1 – 477477Cytoplasmic Potential
Transmembrane478 – 49821Helical; Potential
Topological domain499 – 53638Lumenal Potential
Transmembrane537 – 55721Helical; Potential
Topological domain558 – 1134577Cytoplasmic Potential
Domain317 – 36751bHLH
Region1 – 6060Transcriptional activation (acidic)
Region227 – 487261Interaction with LMNA
Region367 – 38822Leucine-zipper
Compositional bias61 – 175115Pro/Ser-rich
Compositional bias420 – 45334Gly/Pro/Ser-rich

Sites

Site451 – 4522Cleavage; by caspase-3 and caspase-7 By similarity
Site480 – 4812Cleavage; by S2P By similarity
Site519 – 5202Cleavage; by S1P By similarity

Amino acid modifications

Modified residue1151Phosphoserine By similarity
Modified residue3311Phosphoserine; by SIK1 Ref.12
Modified residue3321Phosphoserine; by SIK1 Ref.12
Modified residue3891Phosphoserine; by AMPK Ref.14
Modified residue3951Phosphoserine; by SIK1 Ref.12

Natural variations

Alternative sequence1 – 2929MDELA…VLNDI → MDCTF in isoform SREBP-1C and isoform SREBP-1C-W42.
VSP_002151
Alternative sequence90 – 13142Missing in isoform SREBP-1A-W42 and isoform SREBP-1C-W42.
VSP_002152

Experimental info

Mutagenesis3311S → A: Weakly affects phosphorylation by SIK1. Ref.12
Mutagenesis3321S → A: Weakly affects phosphorylation by SIK1. Ref.12
Mutagenesis3541S → A: Does not affect AMPK-mediated phosphorylation. Ref.14
Mutagenesis3891S → A: Abolishes AMPK-mediated phosphorylation. Ref.14
Mutagenesis3951S → A: Strongly impairs affects phosphorylation by SIK1. Ref.12
Sequence conflict272 – 2765Missing in BAE32576. Ref.1
Sequence conflict272 – 2765Missing in AAK54762. Ref.6
Sequence conflict7951R → P in BAE29268. Ref.1
Sequence conflict10031H → N in AAH06051. Ref.3
Sequence conflict10611T → A in AAH06051. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform SREBP-1A [UniParc].

Last modified July 24, 2007. Version 4.
Checksum: 3D7422406E07A376

FASTA1,134120,537
        10         20         30         40         50         60 
MDELAFGEAA LEQTLAEMCE LDTAVLNDIE DMLQLINNQD SDFPGLFDAP YAGGETGDTG 

        70         80         90        100        110        120 
PSSPGANSPE SFSSASLASS LEAFLGGPKV TPAPLSPPPS APAALKMYPS VSPFSPGPGI 

       130        140        150        160        170        180 
KEEPVPLTIL QPAAPQPSPG TLLPPSFPAP PVQLSPAPVL GYSSLPSGFS GTLPGNTQQP 

       190        200        210        220        230        240 
PSSLPLAPAP GVLPTPALHT QVQSLASQQP LPASAAPRTN TVTSQVQQVP VVLQPHFIKA 

       250        260        270        280        290        300 
DSLLLTAVKT DAGATVKTAG ISTLAPGTAV QAGPLQTLVS GGTILATVPL VVDTDKLPIH 

       310        320        330        340        350        360 
RLAAGSKALG SAQSRGEKRT AHNAIEKRYR SSINDKIVEL KDLVVGTEAK LNKSAVLRKA 

       370        380        390        400        410        420 
IDYIRFLQHS NQKLKQENLT LRSAHKSKSL KDLVSACGSG GGTDVSMEGM KPEVVETLTP 

       430        440        450        460        470        480 
PPSDAGSPSQ SSPLSFGSRA SSSGGSDSEP DSPAFEDSQV KAQRLPSHSR GMLDRSRLAL 

       490        500        510        520        530        540 
CVLAFLCLTC NPLASLFGWG ILTPSDATGT HRSSGRSMLE AESRDGSNWT QWLLPPLVWL 

       550        560        570        580        590        600 
ANGLLVLACL ALLFVYGEPV TRPHSGPAVH FWRHRKQADL DLARGDFPQA AQQLWLALQA 

       610        620        630        640        650        660 
LGRPLPTSNL DLACSLLWNL IRHLLQRLWV GRWLAGQAGG LLRDRGLRKD ARASARDAAV 

       670        680        690        700        710        720 
VYHKLHQLHA MGKYTGGHLA ASNLALSALN LAECAGDAIS MATLAEIYVA AALRVKTSLP 

       730        740        750        760        770        780 
RALHFLTRFF LSSARQACLA QSGSVPLAMQ WLCHPVGHRF FVDGDWAVHG APPESLYSVA 

       790        800        810        820        830        840 
GNPVDPLAQV TRLFREHLLE RALNCIAQPS PGAADGDREF SDALGYLQLL NSCSDAAGAP 

       850        860        870        880        890        900 
ACSFSVSSSM AATTGPDPVA KWWASLTAVV IHWLRRDEEA AERLYPLVEH IPQVLQDTER 

       910        920        930        940        950        960 
PLPRAALYSF KAARALLDHR KVESSPASLA ICEKASGYLR DSLASTPTGS SIDKAMQLLL 

       970        980        990       1000       1010       1020 
CDLLLVARTS LWQRQQSPAS VQVAHGTSNG PQASALELRG FQHDLSSLRR LAQSFRPAMR 

      1030       1040       1050       1060       1070       1080 
RVFLHEATAR LMAGASPART HQLLDRSLRR RAGSSGKGGT TAELEPRPTW REHTEALLLA 

      1090       1100       1110       1120       1130 
SCYLPPAFLS APGQRMSMLA EAARTVEKLG DHRLLLDCQQ MLLRLGGGTT VTSS 

« Hide

Isoform SREBP-1A-W42 [UniParc].

Checksum: 7AD020CB6E87C2E6
Show »

FASTA1,092116,275
Isoform SREBP-1C [UniParc].

Checksum: FC912A03CE5C785E
Show »

FASTA1,110117,996
Isoform SREBP-1C-W42 [UniParc].

Checksum: 9229327B581AAAD2
Show »

FASTA1,068113,734

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SREBP-1A).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Kidney and Thymus.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SREBP-1A).
Strain: C57BL/6 and Czech II.
Tissue: Brain and Mammary gland.
[4]"Differential expression of exons 1a and 1c in mRNAs for sterol regulatory element binding protein-1 in human and mouse organs and cultured cells."
Shimomura I., Shimano H., Horton J.D., Goldstein J.L., Brown M.S.
J. Clin. Invest. 99:838-845(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-41 (ISOFORMS SREBP-1A AND SREBP-1C).
Tissue: Liver.
[5]"A novel splicing isoform of mouse sterol regulatory element-binding protein-1 (SREBP-1)."
Inoue J., Sato R.
Biosci. Biotechnol. Biochem. 63:243-245(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-444 (ISOFORMS SREBP-1A-W42 AND SREBP-1C-W42).
[6]"Mouse Srebp1."
Lloyd D.J., Shackleton S., Trembath R.C.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-1134.
[7]"Elevated levels of SREBP-2 and cholesterol synthesis in livers of mice homozygous for a targeted disruption of the SREBP-1 gene."
Shimano H., Shimomura I., Hammer R.E., Herz J., Goldstein J.L., Brown M.S., Horton J.D.
J. Clin. Invest. 100:2115-2124(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]"Insulin resistance and diabetes mellitus in transgenic mice expressing nuclear SREBP-1c in adipose tissue: model for congenital generalized lipodystrophy."
Shimomura I., Hammer R.E., Richardson J.A., Ikemoto S., Bashmakov Y., Goldstein J.L., Brown M.S.
Genes Dev. 12:3182-3194(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies."
Lloyd D.J., Trembath R.C., Shackleton S.
Hum. Mol. Genet. 11:769-777(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LMNA.
[10]"Diminished hepatic response to fasting/refeeding and liver X receptor agonists in mice with selective deficiency of sterol regulatory element-binding protein-1c."
Liang G., Yang J., Horton J.D., Hammer R.E., Goldstein J.L., Brown M.S.
J. Biol. Chem. 277:9520-9528(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]"Overexpression of sterol regulatory element-binding protein-1a in mouse adipose tissue produces adipocyte hypertrophy, increased fatty acid secretion, and fatty liver."
Horton J.D., Shimomura I., Ikemoto S., Bashmakov Y., Hammer R.E.
J. Biol. Chem. 278:36652-36660(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Salt-inducible kinase regulates hepatic lipogenesis by controlling SREBP-1c phosphorylation."
Yoon Y.S., Seo W.Y., Lee M.W., Kim S.T., Koo S.H.
J. Biol. Chem. 284:10446-10452(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-331; SER-332 AND SER-395, MUTAGENESIS OF SER-331; SER-332 AND SER-395.
[13]"The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."
Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., Makishima M.
Mol. Pharmacol. 76:1360-1369(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice."
Li Y., Xu S., Mihaylova M.M., Zheng B., Hou X., Jiang B., Park O., Luo Z., Lefai E., Shyy J.Y., Gao B., Wierzbicki M., Verbeuren T.J., Shaw R.J., Cohen R.A., Zang M.
Cell Metab. 13:376-388(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-389, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-354 AND SER-389.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK052628 mRNA. Translation: BAC35068.1.
AK150052 mRNA. Translation: BAE29268.1.
AK154424 mRNA. Translation: BAE32576.1.
AK169607 mRNA. Translation: BAE41256.1.
AL669954 Genomic DNA. Translation: CAI25757.1.
AL669954 Genomic DNA. Translation: CAI25758.1.
BC006051 mRNA. Translation: AAH06051.1.
BC056922 mRNA. Translation: AAH56922.1.
AB017337 mRNA. Translation: BAA74795.1.
AF374266 mRNA. Translation: AAK54762.1.
CCDSCCDS24785.1. [Q9WTN3-1]
PIRPD0035.
RefSeqNP_035610.1. NM_011480.3. [Q9WTN3-1]
XP_006532778.1. XM_006532715.1. [Q9WTN3-3]
UniGeneMm.278701.

3D structure databases

ProteinModelPortalQ9WTN3.
SMRQ9WTN3. Positions 313-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203495. 5 interactions.
IntActQ9WTN3. 2 interactions.

PTM databases

PhosphoSiteQ9WTN3.

Proteomic databases

PRIDEQ9WTN3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020846; ENSMUSP00000020846; ENSMUSG00000020538. [Q9WTN3-1]
GeneID20787.
KEGGmmu:20787.
UCSCuc007jfn.1. mouse. [Q9WTN3-1]

Organism-specific databases

CTD6720.
MGIMGI:107606. Srebf1.

Phylogenomic databases

eggNOGNOG242942.
GeneTreeENSGT00390000017651.
HOGENOMHOG000007091.
HOVERGENHBG061592.
InParanoidQ9WTN3.
KOK07197.
OMAFDPPYAG.
PhylomeDBQ9WTN3.
TreeFamTF313894.

Enzyme and pathway databases

ReactomeREACT_188937. Metabolism.
REACT_200794. Mus musculus biological processes.

Gene expression databases

BgeeQ9WTN3.
GenevestigatorQ9WTN3.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSREBF1. mouse.
NextBio299515.
PROQ9WTN3.
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Entry information

Entry nameSRBP1_MOUSE
AccessionPrimary (citable) accession number: Q9WTN3
Secondary accession number(s): Q3U458 expand/collapse secondary AC list , Q3UDJ3, Q5SRX5, Q8C733, Q99JK7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 24, 2007
Last modified: July 9, 2014
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot