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Q9WTN3

- SRBP1_MOUSE

UniProt

Q9WTN3 - SRBP1_MOUSE

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Protein

Sterol regulatory element-binding protein 1

Gene

Srebf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei451 – 4522Cleavage; by caspase-3 and caspase-7By similarity
Sitei480 – 4812Cleavage; by S2PBy similarity
Sitei519 – 5202Cleavage; by S1PBy similarity

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. sequence-specific DNA binding Source: MGI
  5. sequence-specific DNA binding transcription factor activity Source: HGNC
  6. sterol response element binding Source: HGNC
  7. transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  1. aging Source: Ensembl
  2. cellular response to fatty acid Source: Ensembl
  3. cellular response to starvation Source: HGNC
  4. cholesterol metabolic process Source: UniProtKB-KW
  5. circadian rhythm Source: UniProtKB
  6. insulin receptor signaling pathway Source: MGI
  7. lipid biosynthetic process Source: UniProtKB
  8. lung development Source: Ensembl
  9. negative regulation of insulin secretion Source: MGI
  10. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  11. positive regulation of cholesterol biosynthetic process Source: MGI
  12. positive regulation of fatty acid biosynthetic process Source: BHF-UCL
  13. positive regulation of histone deacetylation Source: MGI
  14. positive regulation of transcription, DNA-templated Source: BHF-UCL
  15. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  16. positive regulation of triglyceride biosynthetic process Source: UniProtKB
  17. regulation of fatty acid metabolic process Source: MGI
  18. regulation of heart rate by chemical signal Source: MGI
  19. regulation of insulin secretion Source: MGI
  20. regulation of transcription, DNA-templated Source: UniProtKB
  21. response to cAMP Source: Ensembl
  22. response to drug Source: Ensembl
  23. response to food Source: Ensembl
  24. response to glucagon Source: Ensembl
  25. response to glucose Source: MGI
  26. response to progesterone Source: Ensembl
  27. response to retinoic acid Source: Ensembl
  28. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118837. Rora activates circadian gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198602. PPARA activates gene expression.
REACT_198968. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_198969. Activation of gene expression by SREBF (SREBP).

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol regulatory element-binding protein 1
Short name:
SREBP-1
Alternative name(s):
Sterol regulatory element-binding transcription factor 1
Cleaved into the following chain:
Gene namesi
Name:Srebf1
Synonyms:Srebp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:107606. Srebf1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Golgi apparatus membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cytoplasmic vesicleCOPII-coated vesicle membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: Moves from the endoplasmic reticulum to the Golgi in the absence of sterols.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. Golgi membrane Source: Reactome
  5. integral component of membrane Source: UniProtKB-KW
  6. membrane Source: BHF-UCL
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
  9. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi331 – 3311S → A: Weakly affects phosphorylation by SIK1. 1 Publication
Mutagenesisi332 – 3321S → A: Weakly affects phosphorylation by SIK1. 1 Publication
Mutagenesisi354 – 3541S → A: Does not affect AMPK-mediated phosphorylation. 1 Publication
Mutagenesisi389 – 3891S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication
Mutagenesisi395 – 3951S → A: Strongly impairs affects phosphorylation by SIK1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11341134Sterol regulatory element-binding protein 1PRO_0000127448Add
BLAST
Chaini1 – 480480Processed sterol regulatory element-binding protein 1PRO_0000314030Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151PhosphoserineBy similarity
Modified residuei331 – 3311Phosphoserine; by SIK11 Publication
Modified residuei332 – 3321Phosphoserine; by SIK11 Publication
Modified residuei389 – 3891Phosphoserine; by AMPK1 Publication
Modified residuei395 – 3951Phosphoserine; by SIK11 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9WTN3.
PRIDEiQ9WTN3.

PTM databases

PhosphoSiteiQ9WTN3.

Expressioni

Tissue specificityi

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.

Inductioni

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

Gene expression databases

BgeeiQ9WTN3.
GenevestigatoriQ9WTN3.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Sirt1Q923E42EBI-5273743,EBI-1802585

Protein-protein interaction databases

BioGridi203495. 6 interactions.
IntActiQ9WTN3. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9WTN3.
SMRiQ9WTN3. Positions 313-393.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 477477CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini499 – 53638LumenalSequence AnalysisAdd
BLAST
Topological domaini558 – 1134577CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei478 – 49821HelicalSequence AnalysisAdd
BLAST
Transmembranei537 – 55721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini317 – 36751bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060Transcriptional activation (acidic)Add
BLAST
Regioni227 – 487261Interaction with LMNAAdd
BLAST
Regioni367 – 38822Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 175115Pro/Ser-richAdd
BLAST
Compositional biasi420 – 45334Gly/Pro/Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the SREBP family.Curated
Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG242942.
GeneTreeiENSGT00390000017651.
HOGENOMiHOG000007091.
HOVERGENiHBG061592.
InParanoidiQ9WTN3.
KOiK07197.
OMAiFDPPYAG.
PhylomeDBiQ9WTN3.
TreeFamiTF313894.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform SREBP-1A (identifier: Q9WTN3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDELAFGEAA LEQTLAEMCE LDTAVLNDIE DMLQLINNQD SDFPGLFDAP
60 70 80 90 100
YAGGETGDTG PSSPGANSPE SFSSASLASS LEAFLGGPKV TPAPLSPPPS
110 120 130 140 150
APAALKMYPS VSPFSPGPGI KEEPVPLTIL QPAAPQPSPG TLLPPSFPAP
160 170 180 190 200
PVQLSPAPVL GYSSLPSGFS GTLPGNTQQP PSSLPLAPAP GVLPTPALHT
210 220 230 240 250
QVQSLASQQP LPASAAPRTN TVTSQVQQVP VVLQPHFIKA DSLLLTAVKT
260 270 280 290 300
DAGATVKTAG ISTLAPGTAV QAGPLQTLVS GGTILATVPL VVDTDKLPIH
310 320 330 340 350
RLAAGSKALG SAQSRGEKRT AHNAIEKRYR SSINDKIVEL KDLVVGTEAK
360 370 380 390 400
LNKSAVLRKA IDYIRFLQHS NQKLKQENLT LRSAHKSKSL KDLVSACGSG
410 420 430 440 450
GGTDVSMEGM KPEVVETLTP PPSDAGSPSQ SSPLSFGSRA SSSGGSDSEP
460 470 480 490 500
DSPAFEDSQV KAQRLPSHSR GMLDRSRLAL CVLAFLCLTC NPLASLFGWG
510 520 530 540 550
ILTPSDATGT HRSSGRSMLE AESRDGSNWT QWLLPPLVWL ANGLLVLACL
560 570 580 590 600
ALLFVYGEPV TRPHSGPAVH FWRHRKQADL DLARGDFPQA AQQLWLALQA
610 620 630 640 650
LGRPLPTSNL DLACSLLWNL IRHLLQRLWV GRWLAGQAGG LLRDRGLRKD
660 670 680 690 700
ARASARDAAV VYHKLHQLHA MGKYTGGHLA ASNLALSALN LAECAGDAIS
710 720 730 740 750
MATLAEIYVA AALRVKTSLP RALHFLTRFF LSSARQACLA QSGSVPLAMQ
760 770 780 790 800
WLCHPVGHRF FVDGDWAVHG APPESLYSVA GNPVDPLAQV TRLFREHLLE
810 820 830 840 850
RALNCIAQPS PGAADGDREF SDALGYLQLL NSCSDAAGAP ACSFSVSSSM
860 870 880 890 900
AATTGPDPVA KWWASLTAVV IHWLRRDEEA AERLYPLVEH IPQVLQDTER
910 920 930 940 950
PLPRAALYSF KAARALLDHR KVESSPASLA ICEKASGYLR DSLASTPTGS
960 970 980 990 1000
SIDKAMQLLL CDLLLVARTS LWQRQQSPAS VQVAHGTSNG PQASALELRG
1010 1020 1030 1040 1050
FQHDLSSLRR LAQSFRPAMR RVFLHEATAR LMAGASPART HQLLDRSLRR
1060 1070 1080 1090 1100
RAGSSGKGGT TAELEPRPTW REHTEALLLA SCYLPPAFLS APGQRMSMLA
1110 1120 1130
EAARTVEKLG DHRLLLDCQQ MLLRLGGGTT VTSS
Length:1,134
Mass (Da):120,537
Last modified:July 24, 2007 - v4
Checksum:i3D7422406E07A376
GO
Isoform SREBP-1A-W42 (identifier: Q9WTN3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-131: Missing.

Show »
Length:1,092
Mass (Da):116,275
Checksum:i7AD020CB6E87C2E6
GO
Isoform SREBP-1C (identifier: Q9WTN3-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,110
Mass (Da):117,996
Checksum:iFC912A03CE5C785E
GO
Isoform SREBP-1C-W42 (identifier: Q9WTN3-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,068
Mass (Da):113,734
Checksum:i9229327B581AAAD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti272 – 2765Missing in BAE32576. (PubMed:16141072)Curated
Sequence conflicti272 – 2765Missing in AAK54762. 1 PublicationCurated
Sequence conflicti795 – 7951R → P in BAE29268. (PubMed:16141072)Curated
Sequence conflicti1003 – 10031H → N in AAH06051. (PubMed:15489334)Curated
Sequence conflicti1061 – 10611T → A in AAH06051. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929MDELA…VLNDI → MDCTF in isoform SREBP-1C and isoform SREBP-1C-W42. 2 PublicationsVSP_002151Add
BLAST
Alternative sequencei90 – 13142Missing in isoform SREBP-1A-W42 and isoform SREBP-1C-W42. 1 PublicationVSP_002152Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS24785.1. [Q9WTN3-1]
PIRiPD0035.
RefSeqiNP_035610.1. NM_011480.3. [Q9WTN3-1]
XP_006532778.1. XM_006532715.1. [Q9WTN3-3]
UniGeneiMm.278701.

Genome annotation databases

EnsembliENSMUST00000020846; ENSMUSP00000020846; ENSMUSG00000020538. [Q9WTN3-1]
GeneIDi20787.
KEGGimmu:20787.
UCSCiuc007jfn.1. mouse. [Q9WTN3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS24785.1. [Q9WTN3-1 ]
PIRi PD0035.
RefSeqi NP_035610.1. NM_011480.3. [Q9WTN3-1 ]
XP_006532778.1. XM_006532715.1. [Q9WTN3-3 ]
UniGenei Mm.278701.

3D structure databases

ProteinModelPortali Q9WTN3.
SMRi Q9WTN3. Positions 313-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203495. 6 interactions.
IntActi Q9WTN3. 2 interactions.

PTM databases

PhosphoSitei Q9WTN3.

Proteomic databases

MaxQBi Q9WTN3.
PRIDEi Q9WTN3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020846 ; ENSMUSP00000020846 ; ENSMUSG00000020538 . [Q9WTN3-1 ]
GeneIDi 20787.
KEGGi mmu:20787.
UCSCi uc007jfn.1. mouse. [Q9WTN3-1 ]

Organism-specific databases

CTDi 6720.
MGIi MGI:107606. Srebf1.

Phylogenomic databases

eggNOGi NOG242942.
GeneTreei ENSGT00390000017651.
HOGENOMi HOG000007091.
HOVERGENi HBG061592.
InParanoidi Q9WTN3.
KOi K07197.
OMAi FDPPYAG.
PhylomeDBi Q9WTN3.
TreeFami TF313894.

Enzyme and pathway databases

Reactomei REACT_118837. Rora activates circadian gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198602. PPARA activates gene expression.
REACT_198968. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_198969. Activation of gene expression by SREBF (SREBP).

Miscellaneous databases

ChiTaRSi SREBF1. mouse.
NextBioi 299515.
PROi Q9WTN3.
SOURCEi Search...

Gene expression databases

Bgeei Q9WTN3.
Genevestigatori Q9WTN3.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
[Graphical view ]
SMARTi SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSRBP1_MOUSE
AccessioniPrimary (citable) accession number: Q9WTN3
Secondary accession number(s): Q3U458
, Q3UDJ3, Q5SRX5, Q8C733, Q99JK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 24, 2007
Last modified: October 29, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3