SRBP1_MOUSE - dbPTM
SRBP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRBP1_MOUSE
UniProt AC Q9WTN3
Protein Name Sterol regulatory element-binding protein 1
Gene Name Srebf1
Organism Mus musculus (Mouse).
Sequence Length 1134
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein . Cytoplasmic vesicle, COPII-coated vesicle membrane
Multi-pass membrane protein . Moves from the endoplasmic reticulum to the Gol
Protein Description 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..
Protein Sequence MDELAFGEAALEQTLAEMCELDTAVLNDIEDMLQLINNQDSDFPGLFDAPYAGGETGDTGPSSPGANSPESFSSASLASSLEAFLGGPKVTPAPLSPPPSAPAALKMYPSVSPFSPGPGIKEEPVPLTILQPAAPQPSPGTLLPPSFPAPPVQLSPAPVLGYSSLPSGFSGTLPGNTQQPPSSLPLAPAPGVLPTPALHTQVQSLASQQPLPASAAPRTNTVTSQVQQVPVVLQPHFIKADSLLLTAVKTDAGATVKTAGISTLAPGTAVQAGPLQTLVSGGTILATVPLVVDTDKLPIHRLAAGSKALGSAQSRGEKRTAHNAIEKRYRSSINDKIVELKDLVVGTEAKLNKSAVLRKAIDYIRFLQHSNQKLKQENLTLRSAHKSKSLKDLVSACGSGGGTDVSMEGMKPEVVETLTPPPSDAGSPSQSSPLSFGSRASSSGGSDSEPDSPAFEDSQVKAQRLPSHSRGMLDRSRLALCVLAFLCLTCNPLASLFGWGILTPSDATGTHRSSGRSMLEAESRDGSNWTQWLLPPLVWLANGLLVLACLALLFVYGEPVTRPHSGPAVHFWRHRKQADLDLARGDFPQAAQQLWLALQALGRPLPTSNLDLACSLLWNLIRHLLQRLWVGRWLAGQAGGLLRDRGLRKDARASARDAAVVYHKLHQLHAMGKYTGGHLAASNLALSALNLAECAGDAISMATLAEIYVAAALRVKTSLPRALHFLTRFFLSSARQACLAQSGSVPLAMQWLCHPVGHRFFVDGDWAVHGAPPESLYSVAGNPVDPLAQVTRLFREHLLERALNCIAQPSPGAADGDREFSDALGYLQLLNSCSDAAGAPACSFSVSSSMAATTGPDPVAKWWASLTAVVIHWLRRDEEAAERLYPLVEHIPQVLQDTERPLPRAALYSFKAARALLDHRKVESSPASLAICEKASGYLRDSLASTPTGSSIDKAMQLLLCDLLLVARTSLWQRQQSPASVQVAHGTSNGPQASALELRGFQHDLSSLRRLAQSFRPAMRRVFLHEATARLMAGASPARTHQLLDRSLRRRAGSSGKGGTTAELEPRPTWREHTEALLLASCYLPPAFLSAPGQRMSMLAEAARTVEKLGDHRLLLDCQQMLLRLGGGTTVTSS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
14PhosphorylationGEAALEQTLAEMCEL
HHHHHHHHHHHHHHC		20.68-
63PhosphorylationTGDTGPSSPGANSPE
CCCCCCCCCCCCCCH		30.4123384938
91PhosphorylationFLGGPKVTPAPLSPP
HHCCCCCCCCCCCCC		21.6225159016
96PhosphorylationKVTPAPLSPPPSAPA
CCCCCCCCCCCCCCH		34.0126824392
100PhosphorylationAPLSPPPSAPAALKM
CCCCCCCCCCHHHHC		53.2925159016
108PhosphorylationAPAALKMYPSVSPFS
CCHHHHCCCCCCCCC		7.2617203969
110PhosphorylationAALKMYPSVSPFSPG
HHHHCCCCCCCCCCC		20.1017203969
112PhosphorylationLKMYPSVSPFSPGPG
HHCCCCCCCCCCCCC		25.2717203969
115PhosphorylationYPSVSPFSPGPGIKE
CCCCCCCCCCCCCCC		32.1228066266
249UbiquitinationSLLLTAVKTDAGATV
EEEEEEEECCCCCEE		37.9222790023
276UbiquitinationAVQAGPLQTLVSGGT
EEECCCCEEEECCCE		35.6027667366
278UbiquitinationQAGPLQTLVSGGTIL
ECCCCEEEECCCEEE		1.5427667366
283UbiquitinationQTLVSGGTILATVPL
EEEECCCEEEEEEEE		19.1527667366
284UbiquitinationTLVSGGTILATVPLV
EEECCCEEEEEEEEE		2.5227667366
302UbiquitinationDKLPIHRLAAGSKAL
CCCCHHHHHHHHHHH		2.0727667366
307UbiquitinationHRLAAGSKALGSAQS
HHHHHHHHHHCCHHH		46.8722790023
331PhosphorylationAIEKRYRSSINDKIV
HHHHHHHHHHCHHHH		27.0019244231
332PhosphorylationIEKRYRSSINDKIVE
HHHHHHHHHCHHHHH		19.2019244231
336UbiquitinationYRSSINDKIVELKDL
HHHHHCHHHHHHHHH		44.1327667366
375UbiquitinationQHSNQKLKQENLTLR
HHHCHHHHHHCCCHH		63.7022790023
389PhosphorylationRSAHKSKSLKDLVSA
HHHHHCCCHHHHHHH		47.9821459323
395PhosphorylationKSLKDLVSACGSGGG
CCHHHHHHHHCCCCC		25.7419244231
419PhosphorylationPEVVETLTPPPSDAG
CHHEEECCCCCCCCC		40.96-
441PhosphorylationLSFGSRASSSGGSDS
CCCCCCCCCCCCCCC		24.7526643407
442PhosphorylationSFGSRASSSGGSDSE
CCCCCCCCCCCCCCC		31.8326643407
443PhosphorylationFGSRASSSGGSDSEP
CCCCCCCCCCCCCCC		44.6826643407
446PhosphorylationRASSSGGSDSEPDSP
CCCCCCCCCCCCCCC		41.3023684622
448PhosphorylationSSSGGSDSEPDSPAF
CCCCCCCCCCCCCCC		53.3723684622
452PhosphorylationGSDSEPDSPAFEDSQ
CCCCCCCCCCCCCHH		28.9228066266
461UbiquitinationAFEDSQVKAQRLPSH
CCCCHHHHHHHCCCC		31.0322790023
576UbiquitinationVHFWRHRKQADLDLA
CCCEECHHHHCHHHH		43.6522790023
911UbiquitinationRAALYSFKAARALLD
HHHHHHHHHHHHHHC		34.8822790023
980PhosphorylationQRQQSPASVQVAHGT
HHCCCCCCEEEEECC		19.2328059163
994PhosphorylationTSNGPQASALELRGF
CCCCCCCCHHHHHCC		28.3028059163
1006PhosphorylationRGFQHDLSSLRRLAQ
HCCCCCHHHHHHHHH		33.1225159016
1007PhosphorylationGFQHDLSSLRRLAQS
CCCCCHHHHHHHHHH		32.9423140645
1026UbiquitinationMRRVFLHEATARLMA
HHHHHHHHHHHHHHC		50.2727667366
1028UbiquitinationRVFLHEATARLMAGA
HHHHHHHHHHHHCCC		14.8827667366
1033UbiquitinationEATARLMAGASPART
HHHHHHHCCCCHHHH		18.2627667366
1034UbiquitinationATARLMAGASPARTH
HHHHHHCCCCHHHHH		16.7827667366
1036PhosphorylationARLMAGASPARTHQL
HHHHCCCCHHHHHHH		20.4128066266
1047PhosphorylationTHQLLDRSLRRRAGS
HHHHHHHHHHHHCCC		26.37-
1052UbiquitinationDRSLRRRAGSSGKGG
HHHHHHHCCCCCCCC		22.0227667366
1057UbiquitinationRRAGSSGKGGTTAEL
HHCCCCCCCCCCCCC		56.9927667366
1086UbiquitinationLASCYLPPAFLSAPG
HHHHCCCHHHHCCCC		32.8027667366
1108UbiquitinationEAARTVEKLGDHRLL
HHHHHHHHHCCCHHH		54.13-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
331SPhosphorylationKinaseSIK1Q60670
Uniprot
332SPhosphorylationKinaseSIK1Q60670
Uniprot
389SPhosphorylationKinaseAMPK-FAMILY-GPS
389SPhosphorylationKinaseAMPK-Uniprot
395SPhosphorylationKinaseSIK1Q60670
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
389SPhosphorylation

21459323
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SRBP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRGC2_MOUSEPpargc1bphysical
20211142
ZBT7C_MOUSEZbtb7cphysical
22331133
BRE1A_MOUSERnf20physical
24425205
NFIL3_MOUSENfil3physical
27252523
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRBP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"AMPK phosphorylates and inhibits SREBP activity to attenuate hepaticsteatosis and atherosclerosis in diet-induced insulin-resistantmice.";
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).
Cited for: PHOSPHORYLATION AT SER-389, SUBCELLULAR LOCATION, AND MUTAGENESIS OFSER-354 AND SER-389.
"Salt-inducible kinase regulates hepatic lipogenesis by controllingSREBP-1c phosphorylation.";
Yoon Y.S., Seo W.Y., Lee M.W., Kim S.T., Koo S.H.;
J. Biol. Chem. 284:10446-10452(2009).
Cited for: PHOSPHORYLATION AT SER-331; SER-332 AND SER-395, AND MUTAGENESIS OFSER-331; SER-332 AND SER-395.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108 AND SER-112, ANDMASS SPECTROMETRY.

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