CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000394
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription intermediary factor 1-alpha 
Protein Synonyms/Alias
 TIF1-alpha; E3 ubiquitin-protein ligase TRIM24; RING finger protein 82; Tripartite motif-containing protein 24 
Gene Name
 TRIM24 
Gene Synonyms/Alias
 RNF82; TIF1; TIF1A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
303IEVNQNQKQVEQDIKubiquitination[1]
325VEINKKGKALLHQLEubiquitination[2, 3]
341LAKDHRMKLMQQQQEubiquitination[2, 3]
458LSSNQLSKFPTQISLubiquitination[2, 3]
723MLEPIRIKQENSGPPsumoylation[4]
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] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634] 
Functional Description
 Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). 
Sequence Annotation
 DOMAIN 932 987 Bromo.
 ZN_FING 56 82 RING-type.
 ZN_FING 158 211 B box-type 1.
 ZN_FING 218 259 B box-type 2.
 ZN_FING 826 873 PHD-type.
 REGION 754 779 Nuclear receptor binding site (NRBS).
 REGION 834 840 Interaction with histone H3 that is not
 REGION 979 980 Interaction with histone H3 that is
 MOTIF 891 907 Nuclear localization signal (Potential).
 MOD_RES 101 101 Phosphothreonine.
 MOD_RES 110 110 Phosphoserine.
 MOD_RES 667 667 Phosphoserine.
 MOD_RES 744 744 Phosphoserine.
 MOD_RES 768 768 Phosphoserine.
 MOD_RES 808 808 Phosphoserine.
 MOD_RES 811 811 Phosphoserine.
 MOD_RES 818 818 Phosphothreonine.
 MOD_RES 1019 1019 Phosphoserine.
 MOD_RES 1025 1025 Phosphoserine.
 MOD_RES 1028 1028 Phosphoserine.
 MOD_RES 1042 1042 Phosphoserine.
 CROSSLNK 723 723 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 741 741 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Bromodomain; Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1050 AA 
Protein Sequence
MEVAVEKAVA AAAAASAAAS GGPSAAPSGE NEAESRQGPD SERGGEAARL NLLDTCAVCH 60
QNIQSRAPKL LPCLHSFCQR CLPAPQRYLM LPAPMLGSAE TPPPVPAPGS PVSGSSPFAT 120
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV 180
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK 240
LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKFTGNQ IQNRIIEVNQ 300
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM 360
HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NNTIQFHCDP SFWAQNIINL 420
GSLVIEDKES QPQMPKQNPV VEQNSQPPSG LSSNQLSKFP TQISLAQLRL QHMQQQVMAQ 480
RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ QPPPRLINFQ NHSPKPNGPV LPPHPQQLRY 540
PPNQNIPRQA IKPNPLQMAF LAQQAIKQWQ ISSGQGTPST TNSTSSTPSS PTITSAAGYD 600
GKAFGSPMID LSSPVGGSYN LPSLPDIDCS STIMLDNIVR KDTNIDHGQP RPPSNRTVQS 660
PNSSVPSPGL AGPVTMTSVH PPIRSPSASS VGSRGSSGSS SKPAGADSTH KVPVVMLEPI 720
RIKQENSGPP ENYDFPVVIV KQESDEESRP QNANYPRSIL TSLLLNSSQS STSEETVLRS 780
DAPDSTGDQP GLHQDNSSNG KSEWLDPSQK SPLHVGETRK EDDPNEDWCA VCQNGGELLC 840
CEKCPKVFHL SCHVPTLTNF PSGEWICTFC RDLSKPEVEY DCDAPSHNSE KKKTEGLVKL 900
TPIDKRKCER LLLFLYCHEM SLAFQDPVPL TVPDYYKIIK NPMDLSTIKK RLQEDYSMYS 960
KPEDFVADFR LIFQNCAEFN EPDSEVANAG IKLENYFEEL LKNLYPEKRF PKPEFRNESE 1020
DNKFSDDSDD DFVQPRKKRL KSIEERQLLK 1050 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005719; C:nuclear euchromatin; IEA:Compara.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005726; C:perichromatin fibrils; IEA:Compara.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0034056; F:estrogen response element binding; IDA:UniProtKB.
 GO:0070577; F:histone acetyl-lysine binding; IDA:UniProtKB.
 GO:0004672; F:protein kinase activity; IEA:Compara.
 GO:0005102; F:receptor binding; TAS:ProtInc.
 GO:0043565; F:sequence-specific DNA binding; IEA:Compara.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0055074; P:calcium ion homeostasis; IEA:Compara.
 GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0046777; P:protein autophosphorylation; IEA:Compara.
 GO:0030163; P:protein catabolic process; IMP:UniProtKB.
 GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
 GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
 GO:0070562; P:regulation of vitamin D receptor signaling pathway; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR003649; Bbox_C.
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR000315; Znf_B-box.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00439; Bromodomain
 PF00628; PHD
 PF00643; zf-B_box 
SMART
 SM00502; BBC
 SM00336; BBOX
 SM00297; BROMO
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50119; ZF_BBOX
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR00503; BROMODOMAIN.