CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014578
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; Tripartite motif-containing protein 24 
Gene Name
 Trim24 
Gene Synonyms/Alias
 Tif1; Tif1a 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
724MLEPIRIKQENSGPPsumoylation[1]
742DFPVVIVKQESDEESsumoylation[1]
Reference
 [1] Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification.
 Seeler JS, Marchio A, Losson R, Desterro JM, Hay RT, Chambon P, Dejean A.
 Mol Cell Biol. 2001 May;21(10):3314-24. [PMID: 11313457] 
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) (By similarity). 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 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, such as RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes. Required for normal transition from proliferating neonatal hepatocytes to quiescent adult hepatocytes. 
Sequence Annotation
 DOMAIN 933 988 Bromo.
 ZN_FING 52 77 RING-type.
 ZN_FING 158 211 B box-type 1.
 ZN_FING 218 259 B box-type 2.
 ZN_FING 827 874 PHD-type.
 REGION 755 780 Nuclear receptor binding site (NRBS).
 REGION 835 841 Interaction with histone H3 that is not
 MOTIF 892 908 Nuclear localization signal (Potential).
 MOD_RES 97 97 Phosphothreonine (By similarity).
 MOD_RES 110 110 Phosphoserine (By similarity).
 MOD_RES 668 668 Phosphoserine (By similarity).
 MOD_RES 745 745 Phosphoserine (By similarity).
 MOD_RES 769 769 Phosphoserine (By similarity).
 MOD_RES 809 809 Phosphoserine (By similarity).
 MOD_RES 812 812 Phosphoserine.
 MOD_RES 819 819 Phosphothreonine (By similarity).
 MOD_RES 1026 1026 Phosphoserine.
 MOD_RES 1029 1029 Phosphoserine.
 MOD_RES 1043 1043 Phosphoserine (By similarity).
 CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 742 742 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; Bromodomain; Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond; Ligase; Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene; 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
 1051 AA 
Protein Sequence
MEVAVEKAAA AAAPAGGPAA AAPSGENEAE SRQGPDSESG GEASRLNLLD TCAVCHQNIQ 60
SRVPKLLPCL HSFCQRCLPA PQRYLMLTAP ALGSAETPPP APAPAPAPGS PAGGPSPFAT 120
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV 180
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK 240
LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKYTGNQ IQNRIIEINQ 300
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM 360
HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NTTIQFHCDP SFWAQNIINL 420
GSLVIEDKES QPQMPKQNPV VEQSSQPPGG LPSNQLSKFP TQISLAQLRL QHIQQQVMAQ 480
RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ HPPPRLINFQ NHSPKPNGPV LPPYPQQLRY 540
SPSQNVPRQT TIKPNPLQMA FLAQQAIKQW QISSVQAPPT TASSSSSTPS SPTITSAAGY 600
DGKAFSSPMI DLSAPVGGSY NLPSLPDIDC SSTIMLDNIA RKDTGVDHAQ PRPPSNRTVQ 660
SPNSSVPSPG LAGPVTMTSV HPPIRSPSAS SVGSRGSSGS SSKPAGADST HKVPVVMLEP 720
IRIKQENSGP PENYDFPVVI VKQESDEESR PQNTNYPRSI LTSLLLNSSQ SSASEETVLR 780
SDAPDSTGDQ PGLHQENSSN GKSEWSDASQ KSPVHVGETR KEDDPNEDWC AVCQNGGELL 840
CCEKCPKVFH LTCHVPTLTN FPSGEWICTF CRDLSKPEVD YDCDVPSHHS EKRKSEGLTK 900
LTPIDKRKCE RLLLFLYCHE MSLAFQDPVP LTVPDYYKII KNPMDLSTIK KRLQEDYCMY 960
TKPEDFVADF RLIFQNCAEF NEPDSEVANA GIKLESYFEE LLKNLYPEKR FPKVEFRHEA 1020
EDCKFSDDSD DDFVQPRKKR LKSTEDRQLL K 1051 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005719; C:nuclear euchromatin; IDA:MGI.
 GO:0005726; C:perichromatin fibrils; IDA:MGI.
 GO:0003682; F:chromatin binding; IDA:MGI.
 GO:0034056; F:estrogen response element binding; ISS:UniProtKB.
 GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB.
 GO:0016922; F:ligand-dependent nuclear receptor binding; IDA:MGI.
 GO:0004672; F:protein kinase activity; IDA:MGI.
 GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0055074; P:calcium ion homeostasis; IMP:MGI.
 GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IGI:MGI.
 GO:0046777; P:protein autophosphorylation; IDA:MGI.
 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; IMP:MGI.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
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.