dbPTM

TIF1B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TIF1B_MOUSE
UniProt AC	Q62318
Protein Name	Transcription intermediary factor 1-beta
Gene Name	Trim28
Organism	Mus musculus (Mouse).
Sequence Length	834
Subcellular Localization	Nucleus . Associated with centromeric heterochromatin during cell differentiation through CBX1.
Protein 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. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (By similarity). Acts as a corepressor for ZFP568. [PubMed: 22110054]
Protein Sequence	MAASAAATAAASAATAASAASGSPGSGEGSAGGEKRPAASSAAAASAAASSPAGGGGEAQELLEHCGVCRERLRPERDPRLLPCLHSACSACLGPATPAAANNSGDGGSAGDGAMVDCPVCKQQCYSKDIVENYFMRDSGSKASSDSQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKTRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKNTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPGPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSDDPYSSAEPHVSGMKRSRSGEGEVSGLLRKVPRVSLERLDLDLTSDSQPPVFKVFPGSTTEDYNLIVIERGAAAAAAGQAGTVPPGAPGAPPLPGMAIVKEEETEAAIGAPPAAPEGPETKPVLMPLTEGPGAEGPRLASPSGSTSSGLEVVAPEVTSAPVSGPGILDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSMEQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNDAFGDTKFSAVLVEPPPLNLPSAGLSSQELSGPGDGP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAASAAATA ------CHHHHHHHH	15.32	19131326
4	Phosphorylation	----MAASAAATAAA ----CHHHHHHHHHH	14.65	25619855
8	Phosphorylation	MAASAAATAAASAAT CHHHHHHHHHHHHHH	16.47	20469934
12	Phosphorylation	AAATAAASAATAASA HHHHHHHHHHHHHHH	17.45	23684622
15	Phosphorylation	TAAASAATAASAASG HHHHHHHHHHHHHCC	23.60	23684622
18	Phosphorylation	ASAATAASAASGSPG HHHHHHHHHHCCCCC	23.15	20469934
21	Phosphorylation	ATAASAASGSPGSGE HHHHHHHCCCCCCCC	39.25	23375375
23	Phosphorylation	AASAASGSPGSGEGS HHHHHCCCCCCCCCC	24.48	23527152
26	Phosphorylation	AASGSPGSGEGSAGG HHCCCCCCCCCCCCC	36.74	26824392
30	Phosphorylation	SPGSGEGSAGGEKRP CCCCCCCCCCCCCCC	21.31	23684622
40	Phosphorylation	GEKRPAASSAAAASA CCCCCCHHHHHHHHH	23.71	25619855
41	Phosphorylation	EKRPAASSAAAASAA CCCCCHHHHHHHHHH	19.73	25619855
46	Phosphorylation	ASSAAAASAAASSPA HHHHHHHHHHHCCCC	17.45	24925903
50	Phosphorylation	AAASAAASSPAGGGG HHHHHHHCCCCCCCH	31.93	25521595
51	Phosphorylation	AASAAASSPAGGGGE HHHHHHCCCCCCCHH	17.65	24925903
87	Phosphorylation	RLLPCLHSACSACLG CHHHHHHHHHHHHHC	20.30	26745281
90	Phosphorylation	PCLHSACSACLGPAT HHHHHHHHHHHCCCC	23.02	26745281
97	Phosphorylation	SACLGPATPAAANNS HHHHCCCCHHHHCCC	19.32	26745281
104	Phosphorylation	TPAAANNSGDGGSAG CHHHHCCCCCCCCCC	37.76	24453211
109	Phosphorylation	NNSGDGGSAGDGAMV CCCCCCCCCCCCCEE	34.31	24453211
128	Ubiquitination	CKQQCYSKDIVENYF HCCEECCCHHHHHHC	25.62	-
134	Phosphorylation	SKDIVENYFMRDSGS CCHHHHHHCCCCCCC	5.80	28285833
139	Phosphorylation	ENYFMRDSGSKASSD HHHCCCCCCCCCCCC	34.30	22006019
141	Phosphorylation	YFMRDSGSKASSDSQ HCCCCCCCCCCCCCC	29.06	25338131
144	Phosphorylation	RDSGSKASSDSQDAN CCCCCCCCCCCCCHH	38.11	25293948
145	Phosphorylation	DSGSKASSDSQDANQ CCCCCCCCCCCCHHH	46.25	25293948
147	Phosphorylation	GSKASSDSQDANQCC CCCCCCCCCCHHHHC	31.72	23649490
155	Phosphorylation	QDANQCCTSCEDNAP CCHHHHCCCCCCCCC	44.00	25293948
156	Phosphorylation	DANQCCTSCEDNAPA CHHHHCCCCCCCCCC	11.12	25293948
189	Acetylation	HQRVKYTKDHTVRST HHHHCCCCCCCCEEC	44.41	23806337
210	Glutathionylation	DGERTVYCNVHKHEP CCCEEEEEEEECCCC	3.59	24333276
214	Acetylation	TVYCNVHKHEPLVLF EEEEEEECCCCEEEE	45.43	22826441
239	Ubiquitination	DCQLNAHKDHQYQFL CCCCCCCCCHHHHHH	55.27	-
255	Ubiquitination	DAVRNQRKLLASLVK HHHHHHHHHHHHHHH	37.78	-
259	Phosphorylation	NQRKLLASLVKRLGD HHHHHHHHHHHHHCH	33.39	29895711
262	Ubiquitination	KLLASLVKRLGDKHA HHHHHHHHHHCHHHH	47.39	-
267	Acetylation	LVKRLGDKHATLQKN HHHHHCHHHHHHHHC	33.08	23806337
267	Malonylation	LVKRLGDKHATLQKN HHHHHCHHHHHHHHC	33.08	26320211
273	Ubiquitination	DKHATLQKNTKEVRS HHHHHHHHCHHHHHH	70.47	-
286	Phosphorylation	RSSIRQVSDVQKRVQ HHHHHHHHHHHHHHH	24.59	-
305	Acetylation	MAILQIMKELNKRGR HHHHHHHHHHHHCCC	61.76	22826441
305	Ubiquitination	MAILQIMKELNKRGR HHHHHHHHHHHHCCC	61.76	-
320	Ubiquitination	VLVNDAQKVTEGQQE EEECCHHHCCHHHHH	53.50	-
341	Acetylation	WTMTKIQKHQEHILR CHHHHHHHHHHHHHH	51.21	-
367	Acetylation	TALLLSKKLIYFQLH HHHHHHHHHHHHHHH	36.42	22826441
370	Phosphorylation	LLSKKLIYFQLHRAL HHHHHHHHHHHHHHH	8.84	29514104
378	Acetylation	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	22826441
378	Malonylation	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	26320211
378	Ubiquitination	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	-
401	Ubiquitination	WDLNAWTKSAEAFGK EEHHHHHHHHHHHHH	36.65	-
408	Acetylation	KSAEAFGKIVAERPG HHHHHHHHHEEECCC	27.79	22826441
408	Ubiquitination	KSAEAFGKIVAERPG HHHHHHHHHEEECCC	27.79	-
416	Phosphorylation	IVAERPGTNSTGPGP HEEECCCCCCCCCCC	28.78	25338131
418	Phosphorylation	AERPGTNSTGPGPMA EECCCCCCCCCCCCC	34.28	25338131
434	Phosphorylation	PRAPGPLSKQGSGSS CCCCCCCCCCCCCCC	26.51	29514104
435	Ubiquitination	RAPGPLSKQGSGSSQ CCCCCCCCCCCCCCC	67.38	-
438	Phosphorylation	GPLSKQGSGSSQPME CCCCCCCCCCCCCCE	32.76	23375375
440	Phosphorylation	LSKQGSGSSQPMEVQ CCCCCCCCCCCCEEE	27.74	24704852
441	Phosphorylation	SKQGSGSSQPMEVQE CCCCCCCCCCCEEEC	41.66	24704852
450	Phosphorylation	PMEVQEGYGFGSDDP CCEEECCCCCCCCCC	14.45	21149613
454	Phosphorylation	QEGYGFGSDDPYSSA ECCCCCCCCCCCCCC	36.26	21149613
458	Phosphorylation	GFGSDDPYSSAEPHV CCCCCCCCCCCCCCC	23.42	21149613
459	Phosphorylation	FGSDDPYSSAEPHVS CCCCCCCCCCCCCCC	28.58	26643407
460	Phosphorylation	GSDDPYSSAEPHVSG CCCCCCCCCCCCCCC	30.70	26643407
466	Phosphorylation	SSAEPHVSGMKRSRS CCCCCCCCCCCCCCC	30.09	25777480
469	Acetylation	EPHVSGMKRSRSGEG CCCCCCCCCCCCCCC	51.23	15606783
469	Ubiquitination	EPHVSGMKRSRSGEG CCCCCCCCCCCCCCC	51.23	-
470	Citrullination	PHVSGMKRSRSGEGE CCCCCCCCCCCCCCC	28.54	-
470	Citrullination	PHVSGMKRSRSGEGE CCCCCCCCCCCCCCC	28.54	24463520
471	Phosphorylation	HVSGMKRSRSGEGEV CCCCCCCCCCCCCCH	25.86	27087446
472	Citrullination	VSGMKRSRSGEGEVS CCCCCCCCCCCCCHH	53.35	-
472	Citrullination	VSGMKRSRSGEGEVS CCCCCCCCCCCCCHH	53.35	24463520
473	Phosphorylation	SGMKRSRSGEGEVSG CCCCCCCCCCCCHHH	42.30	27087446
479	Phosphorylation	RSGEGEVSGLLRKVP CCCCCCHHHHHCCCC	21.30	27149854
489	Phosphorylation	LRKVPRVSLERLDLD HCCCCCCCEECCCCC	26.28	26824392
498	Phosphorylation	ERLDLDLTSDSQPPV ECCCCCCCCCCCCCE	30.10	26824392
499	Phosphorylation	RLDLDLTSDSQPPVF CCCCCCCCCCCCCEE	42.43	21082442
501	Phosphorylation	DLDLTSDSQPPVFKV CCCCCCCCCCCEEEE	44.33	27087446
507	Ubiquitination	DSQPPVFKVFPGSTT CCCCCEEEECCCCCC	43.11	-
514	Phosphorylation	KVFPGSTTEDYNLIV EECCCCCCCCCCEEE	28.67	25159016
517	Phosphorylation	PGSTTEDYNLIVIER CCCCCCCCCEEEEEH	12.97	26026062
554	Sumoylation	LPGMAIVKEEETEAA CCCEEEEEHHHHHHH	53.98	-
575	Sumoylation	APEGPETKPVLMPLT CCCCCCCCCCEEECC	31.31	-
594	Phosphorylation	AEGPRLASPSGSTSS CCCCCCCCCCCCCCC	24.96	25521595
596	Phosphorylation	GPRLASPSGSTSSGL CCCCCCCCCCCCCCE	42.77	27087446
598	Phosphorylation	RLASPSGSTSSGLEV CCCCCCCCCCCCEEE	29.47	27087446
599	Phosphorylation	LASPSGSTSSGLEVV CCCCCCCCCCCEEEE	30.36	21082442
600	Phosphorylation	ASPSGSTSSGLEVVA CCCCCCCCCCEEEEC	24.89	22942356
601	Phosphorylation	SPSGSTSSGLEVVAP CCCCCCCCCEEEECC	47.70	22942356
611	Phosphorylation	EVVAPEVTSAPVSGP EEECCCCCCCCCCCC	19.94	25619855
612	Phosphorylation	VVAPEVTSAPVSGPG EECCCCCCCCCCCCC	35.43	20469934
616	Phosphorylation	EVTSAPVSGPGILDD CCCCCCCCCCCCCCC	37.91	20469934
624	Phosphorylation	GPGILDDSATICRVC CCCCCCCCCEEHHHC	27.29	28973931
626	Phosphorylation	GILDDSATICRVCQK CCCCCCCEEHHHCCC	25.26	25619855
676	Sumoylation	CHVLPDLKEEDGSLS HHCCCCCCCCCCCEE	67.45	-
681	Phosphorylation	DLKEEDGSLSLDGAD CCCCCCCCEECCCCC	27.40	25619855
683	Phosphorylation	KEEDGSLSLDGADST CCCCCCEECCCCCCC	26.55	25619855
689	Phosphorylation	LSLDGADSTGVVAKL EECCCCCCCCCEEEC	26.91	25619855
690	Phosphorylation	SLDGADSTGVVAKLS ECCCCCCCCCEEECC	34.25	25619855
697	Phosphorylation	TGVVAKLSPANQRKC CCCEEECCHHHHHHH	22.66	27149854
750	Sumoylation	IRARLQEKLSPPYSS HHHHHHHHCCCCCCC	41.10	-
750	Ubiquitination	IRARLQEKLSPPYSS HHHHHHHHCCCCCCC	41.10	-
752	Phosphorylation	ARLQEKLSPPYSSPQ HHHHHHCCCCCCCHH	34.59	25521595
755	Phosphorylation	QEKLSPPYSSPQEFA HHHCCCCCCCHHHHH	25.76	27149854
756	Phosphorylation	EKLSPPYSSPQEFAQ HHCCCCCCCHHHHHH	41.12	25521595
757	Phosphorylation	KLSPPYSSPQEFAQD HCCCCCCCHHHHHHH	25.43	27087446
770	Acetylation	QDVGRMFKQFNKLTE HHHHHHHHHHHHHCC	44.64	-
770	Ubiquitination	QDVGRMFKQFNKLTE HHHHHHHHHHHHHCC	44.64	-
774	Acetylation	RMFKQFNKLTEDKAD HHHHHHHHHCCCHHH	59.06	-
774	Ubiquitination	RMFKQFNKLTEDKAD HHHHHHHHHCCCHHH	59.06	-
779	Sumoylation	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	-
779	Acetylation	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	23806337
779	Ubiquitination	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	-
784	Phosphorylation	EDKADVQSIIGLQRF CCHHHHHHHHHHHHH	18.93	22817900
804	Sumoylation	NDAFGDTKFSAVLVE HHCCCCCCEEEEEEC	41.90	-
806	Phosphorylation	AFGDTKFSAVLVEPP CCCCCCEEEEEECCC	21.01	25293948
819	Phosphorylation	PPPLNLPSAGLSSQE CCCCCCCCCCCCCCC	37.83	26745281
823	Phosphorylation	NLPSAGLSSQELSGP CCCCCCCCCCCCCCC	29.11	26745281
824	Phosphorylation	LPSAGLSSQELSGPG CCCCCCCCCCCCCCC	32.49	23984901
828	Phosphorylation	GLSSQELSGPGDGP- CCCCCCCCCCCCCC-	42.04	26745281

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
473	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
473	S	Phosphorylation	Kinase	RPS6KA5	O75582	GPS
824	S	Phosphorylation	Kinase	ATM	Q62388	Uniprot
824	S	Phosphorylation	Kinase	ATR	Q9JKK8	Uniprot
824	S	Phosphorylation	Kinase	DSDNA KINASE	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
554	K	Sumoylation	-
Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation.
779	K	Sumoylation	23806337
Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation.
804	K	Sumoylation	-
Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation.
824	S	Phosphorylation	-
ATM-induced phosphorylation on Ser-824 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress.
824	S	Phosphorylation	-
In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-824 prevents sumoylation and allows de-repression of CDKN1A/p21 (By similarity).
824	S	Phosphorylation	-
Represses and is repressed by Ser-824 phosphorylation.
824	S	Sumoylation	-
ATM-induced phosphorylation on Ser-824 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress.
824	S	Sumoylation	-
In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-824 prevents sumoylation and allows de-repression of CDKN1A/p21 (By similarity).

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TIF1B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZNF2_MOUSE	Zfp661	physical	20211142
CBX5_MOUSE	Cbx5	physical	15342492
CBX1_MOUSE	Cbx1	physical	15342492
MYB_MOUSE	Myb	physical	14761981
CBX1_MOUSE	Cbx1	physical	17381543
CBX5_MOUSE	Cbx5	physical	17381543
FRIH_HUMAN	FTH1	physical	20360068
C1QBP_HUMAN	C1QBP	physical	20360068
DDB1_HUMAN	DDB1	physical	20360068
RCN2_HUMAN	RCN2	physical	20360068
ZN331_HUMAN	ZNF331	physical	20360068
RBAK_HUMAN	RBAK	physical	20360068
CALU_HUMAN	CALU	physical	20360068
POGK_HUMAN	POGK	physical	20360068
IPO8_HUMAN	IPO8	physical	20360068
ZN124_HUMAN	ZNF124	physical	20360068
Z324A_HUMAN	ZNF324	physical	20360068
TIF1B_HUMAN	TRIM28	physical	20360068
ZFP1_HUMAN	ZFP1	physical	20360068
ZN566_HUMAN	ZNF566	physical	20360068
ZN552_HUMAN	ZNF552	physical	20360068
ZN250_HUMAN	ZNF250	physical	20360068
RCN1_HUMAN	RCN1	physical	20360068
ZNF8_HUMAN	ZNF8	physical	20360068
ZN460_HUMAN	ZNF460	physical	20360068
CBX5_MOUSE	Cbx5	physical	10562550
CBX1_MOUSE	Cbx1	physical	10562550
TIF1B_MOUSE	Trim28	physical	10562550
SRTD1_MOUSE	Sertad1	physical	11331592
SRTD2_HUMAN	SERTAD2	physical	11331592

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TIF1B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-473 AND SER-501,AND MASS SPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASSSPECTROMETRY.	19367708 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASSSPECTROMETRY.	17622165 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASSSPECTROMETRY.	14729942 [Abstract]

show

show

show

show

show

show

show

show