TRI33_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI33_MOUSE
• UniProt AC: Q99PP7
• Protein Name: E3 ubiquitin-protein ligase TRIM33
• Gene Name: Trim33
• Organism: Mus musculus (Mouse).
• Sequence Length: 1142
• Subcellular Localization: Nucleus . In discrete nuclear dots resembling nuclear bodies.
• Protein Description: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway (By similarity). May act as a transcriptional repressor (By similarity). Inhibits the transcriptional response to TGF-beta/BMP signaling cascade (By similarity). Plays a role in the control of cell proliferation (By similarity). Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor. Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade) (By similarity)..
• Protein Sequence: MAENKGGGEAESGGGGSGSAPVTAGAAGPTAQEAEPPLAAVLVEEEEEEGGRAGAEGGAAGPDDGGVAAASSSSAPAASVPAASVGSAVPGGAASTPAPAAAPAPAPAPAPAPAPAPAPAPAPGSSSGPPLGPPASLLDTCAVCQQSLQSRREAEPKLLPCLHSFCLRCLPEPERQLSVPIPGGSNGDVQQVGVIRCPVCRQECRQIDLVDNYFVKDTSEAPSSSDEKSEQVCTSCEDNASAVGFCVECGEWLCKTCIEAHQRVKFTKDHLIRKKEDVSESVGTSGQRPVFCPVHKQEQLKLFCETCDRLTCRDCQLLEHKEHRYQFLEEAFQNQKGAIENLLAKLLEKKNYVHFAATQVQNRIKEVNETNKRVEQEIKVAIFTLINEINKKGKSLLQQLENVTKERQMKLLQQQNDITGLSRQVKHVMNFTNWAIASGSSTALLYSKRLITFQLRHILKARCDPVPAANGAIRFHCDPTFWAKNVVNLGNLVIESKPAPGYTPNVVVGQVPPGTNHISKTPGQINLAQLRLQHMQQQVYAQKHQQLQQMRLQQPPAPIPTTTATTQQHPRQAAPQMLQQQPPRLISVQTMQRGNMNCGAFQAHQMRLAQNAARIPGIPRHSAPQYSMMQPHLQRQHSNPGHAGPFPVVSAHNPINPTSPTTATMANANRGPTSPSVTAIELIPSVTNPENLPSLPDIPPIQLEDAGSSSLDNLLSRYISGSHLPPQPTSTMNPSPGPSALSPGSSGLSNSHTPVRPPSTSSTGSRGSCGSSGRTAEKSAHSFKSDQVKVKQEPGTEEEICSFSGAVKQEKTEDGRRSACMLSSPESSLTPPLSTNLHLESELDTLTGLENHVKTEPTDISESCKQSGLSNLVNGKSPIRNLMHRSARIGGDGNSKDDDPNEDWCAVCQNGGDLLCCEKCPKVFHLTCHVPTLLSFPSGDWICTFCRDIGKPEVEYDCDNMQHSKKGKTAQGLSPVDQRKCERLLLYLYCHELSIEFQEPVPVSIPNYYKIIKKPMDLSTVKKKLQKKHSQHYQIPDDFVADVRLIFKNCERFNEMMKVVQVYADTQEINLKGDSEVAKAGKAVALYFEDKLSEIYSDRTFTPLPEFEQDEDDGEVTEDSDEDFIQPRRKRLKSDERPVHIK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
336	Ubiquitination	EEAFQNQKGAIENLL HHHHHCCCHHHHHHH	58.83	-
456	Dimethylation	RLITFQLRHILKARC HHHHHHHHHHHHHCC	12.20	-
456	Methylation	RLITFQLRHILKARC HHHHHHHHHHHHHCC	12.20	54560215
521	Phosphorylation	GTNHISKTPGQINLA CCCCCCCCCCCCCHH	26.34	28066266
531	Asymmetric dimethylarginine	QINLAQLRLQHMQQQ CCCHHHHHHHHHHHH	21.88	-
531	Methylation	QINLAQLRLQHMQQQ CCCHHHHHHHHHHHH	21.88	24129315
551	Methylation	HQQLQQMRLQQPPAP HHHHHHHHHCCCCCC	25.63	18600507
593	Asymmetric dimethylarginine	ISVQTMQRGNMNCGA EEEEEECCCCCCCCH	27.86	-
593	Methylation	ISVQTMQRGNMNCGA EEEEEECCCCCCCCH	27.86	24129315
607	Asymmetric dimethylarginine	AFQAHQMRLAQNAAR HHHHHHHHHHHHHHC	21.94	-
607	Methylation	AFQAHQMRLAQNAAR HHHHHHHHHHHHHHC	21.94	24129315
614	Methylation	RLAQNAARIPGIPRH HHHHHHHCCCCCCCC	32.97	24129315
614	Asymmetric dimethylarginine	RLAQNAARIPGIPRH HHHHHHHCCCCCCCC	32.97	-
620	Asymmetric dimethylarginine	ARIPGIPRHSAPQYS HCCCCCCCCCCCCHH	34.18	-
620	Methylation	ARIPGIPRHSAPQYS HCCCCCCCCCCCCHH	34.18	24129315
622	Phosphorylation	IPGIPRHSAPQYSMM CCCCCCCCCCCHHHC	42.81	-
626	Phosphorylation	PRHSAPQYSMMQPHL CCCCCCCHHHCHHHH	9.47	-
627	Phosphorylation	RHSAPQYSMMQPHLQ CCCCCCHHHCHHHHH	11.52	-
635	Dimethylation	MMQPHLQRQHSNPGH HCHHHHHHCCCCCCC	42.41	-
635	Methylation	MMQPHLQRQHSNPGH HCHHHHHHCCCCCCC	42.41	54541741
638	Phosphorylation	PHLQRQHSNPGHAGP HHHHHCCCCCCCCCC	36.06	25338131
650	O-linked_Glycosylation	AGPFPVVSAHNPINP CCCCCEEECCCCCCC	24.84	21606357
650	Phosphorylation	AGPFPVVSAHNPINP CCCCCEEECCCCCCC	24.84	25338131
658	Phosphorylation	AHNPINPTSPTTATM CCCCCCCCCCCCCCC	42.73	25338131
659	Phosphorylation	HNPINPTSPTTATMA CCCCCCCCCCCCCCC	22.85	25338131
673	Phosphorylation	ANANRGPTSPSVTAI CCCCCCCCCCCEEEE	56.97	25338131
676	Phosphorylation	NRGPTSPSVTAIELI CCCCCCCCEEEEEEC	31.69	23649490
685	Phosphorylation	TAIELIPSVTNPENL EEEEECCCCCCCCCC	34.28	23649490
694	Phosphorylation	TNPENLPSLPDIPPI CCCCCCCCCCCCCCC	56.55	23649490
778	Acetylation	SSGRTAEKSAHSFKS CCCCCCCCCCCCCCC	50.94	23806337
782	Phosphorylation	TAEKSAHSFKSDQVK CCCCCCCCCCCCCEE	33.80	29176673
784	Acetylation	EKSAHSFKSDQVKVK CCCCCCCCCCCEEEE	57.02	23806337
791	Acetylation	KSDQVKVKQEPGTEE CCCCEEEECCCCCHH	43.13	22826441
804	Phosphorylation	EEEICSFSGAVKQEK HHHHHHHCCCEEEEE	15.00	28507225
808	Acetylation	CSFSGAVKQEKTEDG HHHCCCEEEEECCCC	52.81	23806337
818	Phosphorylation	KTEDGRRSACMLSSP ECCCCCCEECCCCCC	25.18	26239621
823	Phosphorylation	RRSACMLSSPESSLT CCEECCCCCCHHHCC	19.57	26239621
824	Phosphorylation	RSACMLSSPESSLTP CEECCCCCCHHHCCC	28.82	26239621
827	Phosphorylation	CMLSSPESSLTPPLS CCCCCCHHHCCCCCC	33.75	26643407
828	Phosphorylation	MLSSPESSLTPPLST CCCCCHHHCCCCCCC	34.30	26643407
830	Phosphorylation	SSPESSLTPPLSTNL CCCHHHCCCCCCCCC	25.47	26239621
834	Phosphorylation	SSLTPPLSTNLHLES HHCCCCCCCCCEEHH	22.48	26643407
835	Phosphorylation	SLTPPLSTNLHLESE HCCCCCCCCCEEHHH	49.86	23984901
841	Phosphorylation	STNLHLESELDTLTG CCCCEEHHHHHHHHC	50.23	23984901
845	Phosphorylation	HLESELDTLTGLENH EEHHHHHHHHCHHHH	38.55	23984901
847	Phosphorylation	ESELDTLTGLENHVK HHHHHHHHCHHHHCC	41.64	23984901
867	Phosphorylation	ISESCKQSGLSNLVN HHHHHHHCCCHHHCC	27.48	25159016
870	Phosphorylation	SCKQSGLSNLVNGKS HHHHCCCHHHCCCCC	31.48	25159016
875	Phosphorylation	GLSNLVNGKSPIRNL CCHHHCCCCCHHHHH	25.08	24719451
877	Phosphorylation	SNLVNGKSPIRNLMH HHHCCCCCHHHHHHH	27.27	27087446
895	Phosphorylation	RIGGDGNSKDDDPNE CCCCCCCCCCCCCCC	42.88	26745281
966	Acetylation	DNMQHSKKGKTAQGL CCCCCCCCCCCCCCC	69.52	23806337
968	Acetylation	MQHSKKGKTAQGLSP CCCCCCCCCCCCCCH	49.95	23806337
969	Phosphorylation	QHSKKGKTAQGLSPV CCCCCCCCCCCCCHH	32.64	-
974	Phosphorylation	GKTAQGLSPVDQRKC CCCCCCCCHHHHHHH	29.69	-
1019	Phosphorylation	IKKPMDLSTVKKKLQ HCCCCCHHHHHHHHH	27.22	-
1033	Phosphorylation	QKKHSQHYQIPDDFV HHHHHCCCCCCCCHH	10.66	28285833
1063	Phosphorylation	MMKVVQVYADTQEIN HHHEEEEEECCCEEE	5.01	25159016
1066	Phosphorylation	VVQVYADTQEINLKG EEEEEECCCEEECCC	21.67	-
1093	Phosphorylation	LYFEDKLSEIYSDRT EEEEHHHHHHHCCCC	27.91	22324799
1096	Phosphorylation	EDKLSEIYSDRTFTP EHHHHHHHCCCCCCC	10.64	22324799
1097	Phosphorylation	DKLSEIYSDRTFTPL HHHHHHHCCCCCCCC	26.69	22324799
1100	Phosphorylation	SEIYSDRTFTPLPEF HHHHCCCCCCCCCCC	36.53	28833060
1102	Phosphorylation	IYSDRTFTPLPEFEQ HHCCCCCCCCCCCCC	24.25	28833060
1117	Phosphorylation	DEDDGEVTEDSDEDF CCCCCCCCCCCCCCC	29.76	24925903
1120	Phosphorylation	DGEVTEDSDEDFIQP CCCCCCCCCCCCCHH	36.35	24925903
1134	Phosphorylation	PRRKRLKSDERPVHI HHHHHCCCCCCCCCC	49.66	26824392

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

Oops, there are no upstream regulatory protein records of TRI33_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRI33_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TRI33_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAL1_MOUSE	Tal1	physical	21474105
SPI1_MOUSE	Spi1	physical	21474105

Drug and Disease Associations

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