CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013972
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ligand-dependent nuclear receptor-interacting factor 1 
Protein Synonyms/Alias
 Receptor-interacting factor 1 
Gene Name
 LRIF1 
Gene Synonyms/Alias
 C1orf103; RIF1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11NLRRVFLKPAEENSGubiquitination[1, 2, 3, 4, 5, 6]
50LQLLPIPKSSGNLIPubiquitination[5]
69SVMSDALKGNTGKPVubiquitination[1]
134NFSSSVSKVQSHGVKubiquitination[4, 5, 6]
175QSLPVTVKSPVLPSGubiquitination[5]
252NFQNIYPKPVTEIAKubiquitination[5]
259KPVTEIAKPVILNTTubiquitination[5, 6]
279VATETQLKGGQHSQAubiquitination[1, 2, 5, 6]
290HSQAAPVKWIFQDNLacetylation[7]
290HSQAAPVKWIFQDNLubiquitination[4, 5, 6]
308TPSLVPVKSSNNVASubiquitination[2, 5]
316SSNNVASKILKTFVDubiquitination[5]
319NVASKILKTFVDRKNubiquitination[5, 6]
325LKTFVDRKNLGDNTIubiquitination[4, 5]
348DPSGTRSKNMPIKDNubiquitination[5]
353RSKNMPIKDNALVMFubiquitination[5, 6]
369GKVYLLAKKGTDVLPubiquitination[2]
370KVYLLAKKGTDVLPSubiquitination[5, 6]
393SPDTPVRKDTLQTVSubiquitination[4, 5, 6]
418VVNIVLAKSKSSQMEubiquitination[5]
427KSSQMETKSLSNTQLubiquitination[5, 6]
446NLRAEKNKVEKPSPSubiquitination[2, 5]
449AEKNKVEKPSPSTTNubiquitination[5]
470SNYLKQSKTLFTNPIubiquitination[2, 5]
491TGHNAPRKVTAVIYAubiquitination[5]
500TAVIYARKGSVLQSIubiquitination[5]
532VFRDQEPKIHNEMASubiquitination[5]
543EMASTSDKGAQGRNDubiquitination[1, 2, 3, 5]
565SNKALHLKSDAEFKKubiquitination[5, 6]
578KKIFGLTKDLRVCLTubiquitination[5]
605DSFSSLVKSGTYKETubiquitination[1, 2, 5, 6]
610LVKSGTYKETEFMVKubiquitination[5, 6]
617KETEFMVKEGERKQQubiquitination[6]
705YTHEKQEKGTLNSNAubiquitination[5]
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] 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]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Represses the ligand-induced transcriptional activity of retinoic acid receptor alpha (RARA). This repression may occur through direct recruitment of histone deacetylases. 
Sequence Annotation
 MOTIF 628 631 Nuclear localization signal.
 MOTIF 642 645 Nuclear localization signal.
 MOD_RES 402 402 Phosphoserine.
 MOD_RES 599 599 Phosphoserine.
 MOD_RES 732 732 Phosphothreonine.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 769 AA 
Protein Sequence
MSNNLRRVFL KPAEENSGNA SRCVSGCMYQ VVQTIGSDGK NLLQLLPIPK SSGNLIPLVQ 60
SSVMSDALKG NTGKPVQVTF QTQISSSSTS ASVQLPIFQP ASSSNYFLTR TVDTSEKGRV 120
TSVGTGNFSS SVSKVQSHGV KIDGLTMQTF AVPPSTQKDS SFIVVNTQSL PVTVKSPVLP 180
SGHHLQIPAH AEVKSVPASS LPPSVQQKIL ATATTSTSGM VEASQMPTVI YVSPVNTVKN 240
VVTKNFQNIY PKPVTEIAKP VILNTTQIPK NVATETQLKG GQHSQAAPVK WIFQDNLQPF 300
TPSLVPVKSS NNVASKILKT FVDRKNLGDN TINMPPLSTI DPSGTRSKNM PIKDNALVMF 360
NGKVYLLAKK GTDVLPSQID QQNSVSPDTP VRKDTLQTVS SSPVTEISRE VVNIVLAKSK 420
SSQMETKSLS NTQLASMANL RAEKNKVEKP SPSTTNPHMN QSSNYLKQSK TLFTNPIFPV 480
GFSTGHNAPR KVTAVIYARK GSVLQSIEKI SSSVDATTVT SQQCVFRDQE PKIHNEMAST 540
SDKGAQGRND KKDSQGRSNK ALHLKSDAEF KKIFGLTKDL RVCLTRIPDH LTSGEGFDSF 600
SSLVKSGTYK ETEFMVKEGE RKQQNFDKKR KAKTNKKMDH IKKRKTENAY NAIINGEANV 660
TGSQLLSSIL PTSDVSQHNI LTSHSKTRQE KRTEMEYYTH EKQEKGTLNS NAAYEQSHFF 720
NKNYTEDIFP VTPPELEETI RDEKIRRLKQ VLREKEAALE EMRKKMHQK 769 
Gene Ontology
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR026191; LRIF1. 
Pfam
  
SMART
  
PROSITE
  
PRINTS