CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014423
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription intermediary factor 1-beta 
Protein Synonyms/Alias
 TIF1-beta; E3 SUMO-protein ligase TRIM28; KRAB-A-interacting protein; KRIP-1; Tripartite motif-containing protein 28 
Gene Name
 Trim28 
Gene Synonyms/Alias
 Krip1; Tif1b 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
189HQRVKYTKDHTVRSTacetylation[1]
214TVYCNVHKHEPLVLFacetylation[2]
255DAVRNQRKLLASLVKubiquitination[3]
262KLLASLVKRLGDKHAubiquitination[3]
267LVKRLGDKHATLQKNacetylation[1]
305MAILQIMKELNKRGRacetylation[2]
305MAILQIMKELNKRGRubiquitination[3]
320VLVNDAQKVTEGQQEubiquitination[3]
367TALLLSKKLIYFQLHacetylation[2]
378FQLHRALKMIVDPVEacetylation[2]
378FQLHRALKMIVDPVEubiquitination[3]
408KSAEAFGKIVAERPGacetylation[2]
469EPHVSGMKRSRSGEGubiquitination[3]
750IRARLQEKLSPPYSSubiquitination[3]
770QDVGRMFKQFNKLTEubiquitination[3]
774RMFKQFNKLTEDKADubiquitination[3]
779FNKLTEDKADVQSIIacetylation[1, 4]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6 (By similarity). 
Sequence Annotation
 DOMAIN 697 801 Bromo.
 ZN_FING 66 122 RING-type.
 ZN_FING 149 196 B box-type 1.
 ZN_FING 205 246 B box-type 2.
 ZN_FING 625 672 PHD-type.
 REGION 247 377 Leucine zipper alpha helical coiled-coil
 REGION 248 377 Interaction with MAGEC2 (By similarity).
 REGION 367 371 Involved in binding PPP1CA (By
 REGION 476 513 HP1 box.
 MOTIF 481 494 PxVxL motif.
 MOD_RES 23 23 Phosphoserine.
 MOD_RES 51 51 Phosphoserine (By similarity).
 MOD_RES 305 305 N6-acetyllysine (By similarity).
 MOD_RES 341 341 N6-acetyllysine (By similarity).
 MOD_RES 378 378 N6-acetyllysine (By similarity).
 MOD_RES 440 440 Phosphoserine (By similarity).
 MOD_RES 471 471 Phosphoserine (By similarity).
 MOD_RES 473 473 Phosphoserine.
 MOD_RES 479 479 Phosphoserine (By similarity).
 MOD_RES 489 489 Phosphoserine (By similarity).
 MOD_RES 501 501 Phosphoserine.
 MOD_RES 594 594 Phosphoserine (By similarity).
 MOD_RES 683 683 Phosphoserine (By similarity).
 MOD_RES 697 697 Phosphoserine (By similarity).
 MOD_RES 752 752 Phosphoserine (By similarity).
 MOD_RES 757 757 Phosphoserine (By similarity).
 MOD_RES 770 770 N6-acetyllysine (By similarity).
 MOD_RES 774 774 N6-acetyllysine (By similarity).
 MOD_RES 824 824 Phosphoserine; by ATM and ATR and dsDNA
 CROSSLNK 554 554 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 804 804 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Alternative splicing; Bromodomain; Complete proteome; Isopeptide bond; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 834 AA 
Protein Sequence
MAASAAATAA ASAATAASAA SGSPGSGEGS AGGEKRPAAS SAAAASAAAS SPAGGGGEAQ 60
ELLEHCGVCR ERLRPERDPR LLPCLHSACS ACLGPATPAA ANNSGDGGSA GDGAMVDCPV 120
CKQQCYSKDI VENYFMRDSG SKASSDSQDA NQCCTSCEDN APATSYCVEC SEPLCETCVE 180
AHQRVKYTKD HTVRSTGPAK TRDGERTVYC NVHKHEPLVL FCESCDTLTC RDCQLNAHKD 240
HQYQFLEDAV RNQRKLLASL VKRLGDKHAT LQKNTKEVRS SIRQVSDVQK RVQVDVKMAI 300
LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA SWALESDNNT 360
ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT KSAEAFGKIV AERPGTNSTG 420
PGPMAPPRAP GPLSKQGSGS SQPMEVQEGY GFGSDDPYSS AEPHVSGMKR SRSGEGEVSG 480
LLRKVPRVSL ERLDLDLTSD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA AGQAGTVPPG 540
APGAPPLPGM AIVKEEETEA AIGAPPAAPE GPETKPVLMP LTEGPGAEGP RLASPSGSTS 600
SGLEVVAPEV TSAPVSGPGI LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP 660
GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL 720
HQLATDSTFS MEQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA 780
DVQSIIGLQR FFETRMNDAF GDTKFSAVLV EPPPLNLPSA GLSSQELSGP GDGP 834 
Gene Ontology
 GO:0005719; C:nuclear euchromatin; IDA:MGI.
 GO:0005720; C:nuclear heterochromatin; IDA:MGI.
 GO:0005654; C:nucleoplasm; IDA:MGI.
 GO:0003677; F:DNA binding; IEA:Compara.
 GO:0004672; F:protein kinase activity; IDA:MGI.
 GO:0003713; F:transcription coactivator activity; IDA:MGI.
 GO:0003714; F:transcription corepressor activity; IEA:Compara.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0060028; P:convergent extension involved in axis elongation; IMP:MGI.
 GO:0006281; P:DNA repair; IEA:Compara.
 GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
 GO:0001837; P:epithelial to mesenchymal transition; IDA:HGNC.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0045739; P:positive regulation of DNA repair; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:HGNC.
 GO:0046777; P:protein autophosphorylation; IDA:MGI.
 GO:0051259; P:protein oligomerization; IEA:Compara.
 GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR003649; Bbox_C.
 IPR001487; Bromodomain.
 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. 
Pfam
 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