CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031711
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Sterol regulatory element-binding protein 1 
Protein Synonyms/Alias
  
Gene Name
 SREBF1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
59NRLAAGSKAPASAQSubiquitination[1, 2]
88YRSSINDKIIELKDLubiquitination[2]
93NDKIIELKDLVVGTEubiquitination[1, 2, 3, 4]
102LVVGTEAKLNKSAVLubiquitination[1, 2, 4]
105GTEAKLNKSAVLRKAubiquitination[2, 5]
111NKSAVLRKAIDYIRFubiquitination[2]
125FLQHSNQKLKQENLSubiquitination[2]
127QHSNQKLKQENLSLRubiquitination[2, 5]
141RTAVHKSKSLKDLVSubiquitination[2]
144VHKSKSLKDLVSACGubiquitination[2]
214SPVFEDSKAKPEQRPubiquitination[3]
216VFEDSKAKPEQRPSLubiquitination[1, 2, 3]
333VYFWRHRKQADLDLAubiquitination[1, 2, 3, 4, 5, 6]
421DAALVYHKLHQLHTMubiquitination[1, 2, 3, 4]
473VAAALRVKTSLPRALubiquitination[2]
670RAALHSFKAARALLGubiquitination[1, 2, 3, 4, 5, 6]
680RALLGCAKAESGPASubiquitination[2, 3, 5, 6]
693ASLTICEKASGYLQDubiquitination[2, 3]
816RRAGPGGKGGAVAELubiquitination[1, 2, 4, 5, 6]
867EAARTLEKLGDRRLLubiquitination[1, 2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 893 AA 
Protein Sequence
MKTDGATVKA AGLSPLVSGT TVQTGPLPTL VSGGTILATV PLVVDAEKLP INRLAAGSKA 60
PASAQSRGEK RTAHNAIEKR YRSSINDKII ELKDLVVGTE AKLNKSAVLR KAIDYIRFLQ 120
HSNQKLKQEN LSLRTAVHKS KSLKDLVSAC GSGGNTDVLM EGVKTEVEDT LTPPPSDAGS 180
PFQSSPLSLG SRGSGSGGSG SDSEPDSPVF EDSKAKPEQR PSLHSRGMLD RSRLALCTLV 240
FLCLSCNPLA SLLGARGLPS PSDTTSVYHS PGRNVLGTES RDGPGWAQWL LPPVVWLLNG 300
LLVLVSLVLL FVYGEPVTRP HSGPAVYFWR HRKQADLDLA RGDFAQAAQQ LWLALRALGR 360
PLPTSHLDLA CSLLWNLIRH LLQRLWVGRW LAGRAGGLQQ DCALRVDASA SARDAALVYH 420
KLHQLHTMGK HTGGHLTATN LALSALNLAE CAGDAVSVAT LAEIYVAAAL RVKTSLPRAL 480
HFLTRFFLSS ARQACLAQSG SVPPAMQWLC HPVGHRFFVD GDWSVLSTPW ESLYSLAGNP 540
VDPLAQVTQL FREHLLERAL NCVTQPNPSP GSADGDKEFS DALGYLQLLN SCSDAAGAPA 600
YSFSISSSMA TTTGVDPVAK WWASLTAVVI HWLRRDEEAA ERLCPLVEHL PRVLQESERP 660
LPRAALHSFK AARALLGCAK AESGPASLTI CEKASGYLQD SLATTPASSS IDKAVQLFLC 720
DLLLVVRTSL WRQQQPPAPA PAAQGTSSRP QASALELRGF QRDLSSLRRL AQSFRPAMRR 780
VFLHEATARL MAGASPTRTH QLLDRSLRRR AGPGGKGGAV AELEPRPTRR EHAEALLLAS 840
CYLPPGFLSA PGQRVGMLAE AARTLEKLGD RRLLHDCQQM LMRLGGGTTV TSS 893 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0016020; C:membrane; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0043565; F:sequence-specific DNA binding; IEA:Compara.
 GO:0007568; P:aging; IEA:Compara.
 GO:0009267; P:cellular response to starvation; IEA:Compara.
 GO:0008203; P:cholesterol metabolic process; IEA:Compara.
 GO:0008286; P:insulin receptor signaling pathway; IEA:Compara.
 GO:0008610; P:lipid biosynthetic process; IEA:Compara.
 GO:0030324; P:lung development; IEA:Compara.
 GO:0046676; P:negative regulation of insulin secretion; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0045542; P:positive regulation of cholesterol biosynthetic process; IEA:Compara.
 GO:0031065; P:positive regulation of histone deacetylation; IEA:Compara.
 GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Compara.
 GO:0019217; P:regulation of fatty acid metabolic process; IEA:Compara.
 GO:0003062; P:regulation of heart rate by chemical signal; IEA:Compara.
 GO:0051591; P:response to cAMP; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0070542; P:response to fatty acid; IEA:Compara.
 GO:0032094; P:response to food; IEA:Compara.
 GO:0033762; P:response to glucagon stimulus; IEA:Compara.
 GO:0009749; P:response to glucose stimulus; IEA:Compara.
 GO:0032570; P:response to progesterone stimulus; IEA:Compara.
 GO:0032526; P:response to retinoic acid; IEA:Compara.
 GO:0032933; P:SREBP signaling pathway; IEA:Compara. 
Interpro
 IPR011598; bHLH_dom. 
Pfam
 PF00010; HLH 
SMART
 SM00353; HLH 
PROSITE
 PS50888; BHLH 
PRINTS