dbPTM

TIF1B_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TIF1B_RAT
UniProt AC	O08629
Protein Name	Transcription intermediary factor 1-beta
Gene Name	Trim28
Organism	Rattus norvegicus (Rat).
Sequence Length	835
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. Also 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. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg). 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 genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions. Acts as a corepressor for ZFP568..
Protein Sequence	MAASAAAATAAASAATAASAASGSPGSGEGSAGGEKRPAASSAAAASASASSPAGGGGEAQELLEHCGVCRERLRPERDPRLLPCLHSACSACLGPATPAAANNSGDGGSAGDGAMVDCPVCKQQCYSKDIVENYFMRDSGSKASSDSQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKTRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKNTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPGPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGTDDPYSSAEPHVSGMKRSRSGEGEVSGLMRKVPRVSLERLDLDLTSDSQPPVFKVFPGSTTEDYNLIVIERGAAAAAAGQAGTVPPGAPGAPPLPGMAIVKEEETEAAIGAPPAAPEGPETKPVLMALTEGPGAEGPRLASPSGSTSSGLEVVAPEVTSAPVSGPGILDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPSLQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSMEQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNDAFGDTKFSAVLVEPPPLNLPSAGLSSQELSGPGDGP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	AASAAAATAAASAAT HHHHHHHHHHHHHHH	16.47	23984901
13	Phosphorylation	AAATAAASAATAASA HHHHHHHHHHHHHHH	17.45	23984901
16	Phosphorylation	TAAASAATAASAASG HHHHHHHHHHHHHCC	23.60	27097102
19	Phosphorylation	ASAATAASAASGSPG HHHHHHHHHHCCCCC	23.15	27097102
22	Phosphorylation	ATAASAASGSPGSGE HHHHHHHCCCCCCCC	39.25	27097102
24	Phosphorylation	AASAASGSPGSGEGS HHHHHCCCCCCCCCC	24.48	27097102
27	Phosphorylation	AASGSPGSGEGSAGG HHCCCCCCCCCCCCC	36.74	27097102
31	Phosphorylation	SPGSGEGSAGGEKRP CCCCCCCCCCCCCCC	21.31	27097102
41	Phosphorylation	GEKRPAASSAAAASA CCCCCCHHHHHHHHH	23.71	27097102
42	Phosphorylation	EKRPAASSAAAASAS CCCCCHHHHHHHHHH	19.73	27097102
47	Phosphorylation	ASSAAAASASASSPA HHHHHHHHHHCCCCC	20.31	27097102
49	Phosphorylation	SAAAASASASSPAGG HHHHHHHHCCCCCCC	26.62	21738781
51	Phosphorylation	AAASASASSPAGGGG HHHHHHCCCCCCCCH	34.07	21738781
52	Phosphorylation	AASASASSPAGGGGE HHHHHCCCCCCCCHH	20.63	23712012
98	Phosphorylation	SACLGPATPAAANNS HHHHCCCCHHHHCCC	19.32	27097102
105	Phosphorylation	TPAAANNSGDGGSAG CHHHHCCCCCCCCCC	37.76	27097102
110	Phosphorylation	NNSGDGGSAGDGAMV CCCCCCCCCCCCCEE	34.31	27097102
140	Phosphorylation	ENYFMRDSGSKASSD HHHCCCCCCCCCCCC	34.30	-
148	Phosphorylation	GSKASSDSQDANQCC CCCCCCCCCCHHHHC	31.72	21630457
157	Phosphorylation	DANQCCTSCEDNAPA CHHHHCCCCCCCCCC	11.12	21630457
167	Phosphorylation	DNAPATSYCVECSEP CCCCCCEEEEECCCC	9.00	22668510
190	Acetylation	HQRVKYTKDHTVRST HHHHCCCCCCCCEEC	44.41	22902405
225	Phosphorylation	PLVLFCESCDTLTCR CEEEEECCCCCEEEC	20.62	23984901
228	Phosphorylation	LFCESCDTLTCRDCQ EEECCCCCEEECCCC	28.44	23984901
230	Phosphorylation	CESCDTLTCRDCQLN ECCCCCEEECCCCCC	13.95	23984901
263	Acetylation	KLLASLVKRLGDKHA HHHHHHHHHHCHHHH	47.39	22902405
268	Acetylation	LVKRLGDKHATLQKN HHHHHCHHHHHHHHC	33.08	-
281	Phosphorylation	KNTKEVRSSIRQVSD HCHHHHHHHHHHHHH	34.98	23984901
282	Phosphorylation	NTKEVRSSIRQVSDV CHHHHHHHHHHHHHH	15.95	23984901
287	Phosphorylation	RSSIRQVSDVQKRVQ HHHHHHHHHHHHHHH	24.59	23984901
306	Acetylation	MAILQIMKELNKRGR HHHHHHHHHHHHCCC	61.76	-
321	Ubiquitination	VLVNDAQKVTEGQQE EEECCHHHCCHHHHH	53.50	-
339	Acetylation	RQHWTMTKIQKHQEH HHHCHHHHHHHHHHH	32.11	22902405
342	Acetylation	WTMTKIQKHQEHILR CHHHHHHHHHHHHHH	51.21	22902405
379	Acetylation	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	22902405
417	Phosphorylation	IVAERPGTNSTGPGP HEEECCCCCCCCCCC	28.78	23984901
419	Phosphorylation	AERPGTNSTGPGPMA EECCCCCCCCCCCCC	34.28	23984901
420	Phosphorylation	ERPGTNSTGPGPMAP ECCCCCCCCCCCCCC	49.84	23984901
439	Phosphorylation	GPLSKQGSGSSQPME CCCCCCCCCCCCCCE	32.76	27097102
441	Phosphorylation	LSKQGSGSSQPMEVQ CCCCCCCCCCCCEEE	27.74	27097102
442	Phosphorylation	SKQGSGSSQPMEVQE CCCCCCCCCCCEEEC	41.66	27097102
451	Phosphorylation	PMEVQEGYGFGTDDP CCEEECCCCCCCCCC	14.45	28432305
455	Phosphorylation	QEGYGFGTDDPYSSA ECCCCCCCCCCCCCC	34.66	25575281
461	Phosphorylation	GTDDPYSSAEPHVSG CCCCCCCCCCCCCCC	30.70	26022182
467	Phosphorylation	SSAEPHVSGMKRSRS CCCCCCCCCCCCCCC	30.09	26022182
471	Citrullination	PHVSGMKRSRSGEGE CCCCCCCCCCCCCCC	28.54	-
471	Citrullination	PHVSGMKRSRSGEGE CCCCCCCCCCCCCCC	28.54	-
472	Phosphorylation	HVSGMKRSRSGEGEV CCCCCCCCCCCCCCH	25.86	23712012
473	Citrullination	VSGMKRSRSGEGEVS CCCCCCCCCCCCCHH	53.35	-
473	Citrullination	VSGMKRSRSGEGEVS CCCCCCCCCCCCCHH	53.35	-
474	Phosphorylation	SGMKRSRSGEGEVSG CCCCCCCCCCCCHHH	42.30	23712012
480	Phosphorylation	RSGEGEVSGLMRKVP CCCCCCHHHHHCCCC	23.16	25403869
490	Phosphorylation	MRKVPRVSLERLDLD HCCCCCCCEECCCCC	26.28	22108457
499	Phosphorylation	ERLDLDLTSDSQPPV ECCCCCCCCCCCCCE	30.10	27097102
500	Phosphorylation	RLDLDLTSDSQPPVF CCCCCCCCCCCCCEE	42.43	27097102
502	Phosphorylation	DLDLTSDSQPPVFKV CCCCCCCCCCCEEEE	44.33	27097102
595	Phosphorylation	AEGPRLASPSGSTSS CCCCCCCCCCCCCCC	24.96	23712012
597	Phosphorylation	GPRLASPSGSTSSGL CCCCCCCCCCCCCCE	42.77	27097102
599	Phosphorylation	RLASPSGSTSSGLEV CCCCCCCCCCCCEEE	29.47	27097102
600	Phosphorylation	LASPSGSTSSGLEVV CCCCCCCCCCCEEEE	30.36	27097102
601	Phosphorylation	ASPSGSTSSGLEVVA CCCCCCCCCCEEEEC	24.89	27097102
602	Phosphorylation	SPSGSTSSGLEVVAP CCCCCCCCCEEEECC	47.70	27097102
612	Phosphorylation	EVVAPEVTSAPVSGP EEECCCCCCCCCCCC	19.94	28551015
613	Phosphorylation	VVAPEVTSAPVSGPG EECCCCCCCCCCCCC	35.43	28551015
617	Phosphorylation	EVTSAPVSGPGILDD CCCCCCCCCCCCCCC	37.91	28551015
625	Phosphorylation	GPGILDDSATICRVC CCCCCCCCCEEHHHC	27.29	27097102
627	Phosphorylation	GILDDSATICRVCQK CCCCCCCEEHHHCCC	25.26	28551015
682	Phosphorylation	DLKEEDGSLSLDGAD CCCCCCCCEECCCCC	27.40	28432305
684	Phosphorylation	KEEDGSLSLDGADST CCCCCCEECCCCCCC	26.55	27097102
690	Phosphorylation	LSLDGADSTGVVAKL EECCCCCCCCCEEEC	26.91	28432305
691	Phosphorylation	SLDGADSTGVVAKLS ECCCCCCCCCEEECC	34.25	16641100
698	Phosphorylation	TGVVAKLSPANQRKC CCCEEECCHHHHHHH	22.66	16641100
753	Phosphorylation	ARLQEKLSPPYSSPQ HHHHHHCCCCCCCHH	34.59	27097102
756	Phosphorylation	QEKLSPPYSSPQEFA HHHCCCCCCCHHHHH	25.76	26437020
757	Phosphorylation	EKLSPPYSSPQEFAQ HHCCCCCCCHHHHHH	41.12	27097102
758	Phosphorylation	KLSPPYSSPQEFAQD HCCCCCCCHHHHHHH	25.43	27097102
771	Acetylation	QDVGRMFKQFNKLTE HHHHHHHHHHHHHCC	44.64	22902405
775	Acetylation	RMFKQFNKLTEDKAD HHHHHHHHHCCCHHH	59.06	-
780	Acetylation	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	22902405
785	Phosphorylation	EDKADVQSIIGLQRF CCHHHHHHHHHHHHH	18.93	23984901
820	Phosphorylation	PPPLNLPSAGLSSQE CCCCCCCCCCCCCCC	37.83	27097102
824	Phosphorylation	NLPSAGLSSQELSGP CCCCCCCCCCCCCCC	29.11	27097102
825	Phosphorylation	LPSAGLSSQELSGPG CCCCCCCCCCCCCCC	32.49	27097102
829	Phosphorylation	GLSSQELSGPGDGP- CCCCCCCCCCCCCC-	42.04	23984901

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
825	S	Phosphorylation	Kinase	DSDNA KINASE	-	Uniprot
825	S	Phosphorylation	Kinase	ATM	-	Uniprot
825	S	Phosphorylation	Kinase	ATR	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
555	K	Sumoylation	-
Lys-555, Lys-780 and Lys-805 are the major sites of sumoylation.
780	K	Sumoylation	-
Lys-555, Lys-780 and Lys-805 are the major sites of sumoylation.
805	K	Sumoylation	-
Lys-555, Lys-780 and Lys-805 are the major sites of sumoylation.
824	S	Phosphorylation	-
Represses and is repressed by Ser-824 phosphorylation.
825	S	Phosphorylation	-
ATM-induced phosphorylation on Ser-825 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.
825	S	Phosphorylation	-
In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-825 prevents sumoylation and allows de-repression of CDKN1A/p21 (By similarity).
825	S	Sumoylation	-
ATM-induced phosphorylation on Ser-825 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.
825	S	Sumoylation	-
In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-825 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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TIF1B_RAT !!

Drug and Disease Associations

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

Regulatory Network of TIF1B_RAT

Related Literatures of Post-Translational Modification

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