dbPTM

TRI33_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRI33_HUMAN
UniProt AC	Q9UPN9
Protein Name	E3 ubiquitin-protein ligase TRIM33
Gene Name	TRIM33
Organism	Homo sapiens (Human).
Sequence Length	1127
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. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). 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)..
Protein Sequence	MAENKGGGEAESGGGGSGSAPVTAGAAGPAAQEAEPPLTAVLVEEEEEEGGRAGAEGGAAGPDDGGVAAASSGSAQAASSPAASVGTGVAGGAVSTPAPAPASAPAPGPSAGPPPGPPASLLDTCAVCQQSLQSRREAEPKLLPCLHSFCLRCLPEPERQLSVPIPGGSNGDIQQVGVIRCPVCRQECRQIDLVDNYFVKDTSEAPSSSDEKSEQVCTSCEDNASAVGFCVECGEWLCKTCIEAHQRVKFTKDHLIRKKEDVSESVGASGQRPVFCPVHKQEQLKLFCETCDRLTCRDCQLLEHKEHRYQFLEEAFQNQKGAIENLLAKLLEKKNYVHFAATQVQNRIKEVNETNKRVEQEIKVAIFTLINEINKKGKSLLQQLENVTKERQMKLLQQQNDITGLSRQVKHVMNFTNWAIASGSSTALLYSKRLITFQLRHILKARCDPVPAANGAIRFHCDPTFWAKNVVNLGNLVIESKPAPGYTPNVVVGQVPPGTNHISKTPGQINLAQLRLQHMQQQVYAQKHQQLQQMRMQQPPAPVPTTTTTTQQHPRQAAPQMLQQQPPRLISVQTMQRGNMNCGAFQAHQMRLAQNAARIPGIPRHSGPQYSMMQPHLQRQHSNPGHAGPFPVVSVHNTTINPTSPTTATMANANRGPTSPSVTAIELIPSVTNPENLPSLPDIPPIQLEDAGSSSLDNLLSRYISGSHLPPQPTSTMNPSPGPSALSPGSSGLSNSHTPVRPPSTSSTGSRGSCGSSGRTAEKTSLSFKSDQVKVKQEPGTEDEICSFSGGVKQEKTEDGRRSACMLSSPESSLTPPLSTNLHLESELDALASLENHVKIEPADMNESCKQSGLSSLVNGKSPIRSLMHRSARIGGDGNNKDDDPNEDWCAVCQNGGDLLCCEKCPKVFHLTCHVPTLLSFPSGDWICTFCRDIGKPEVEYDCDNLQHSKKGKTAQGLSPVDQRKCERLLLYLYCHELSIEFQEPVPASIPNYYKIIKKPMDLSTVKKKLQKKHSQHYQIPDDFVADVRLIFKNCERFNEMMKVVQVYADTQEINLKADSEVAQAGKAVALYFEDKLTEIYSDRTFAPLPEFEQEEDDGEVTEDSDEDFIQPRRKRLKSDERPVHIK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
148	Phosphorylation	KLLPCLHSFCLRCLP CHHHHHHHHHHHHCC	12.52	27080861
169	Phosphorylation	SVPIPGGSNGDIQQV ECCCCCCCCCCCCEE	43.48	27251275
197	Phosphorylation	QIDLVDNYFVKDTSE CCCCCCCEEECCCCC	12.80	-
202	Phosphorylation	DNYFVKDTSEAPSSS CCEEECCCCCCCCCC	23.81	30387612
252	Acetylation	HQRVKFTKDHLIRKK HHHHCCCHHHHCCCH	46.40	19608861
280	Acetylation	PVFCPVHKQEQLKLF CEECCCCCHHHHHHH	56.62	26051181
305	Ubiquitination	DCQLLEHKEHRYQFL CCCHHCCHHHHHHHH	45.93	-
320	Ubiquitination	EEAFQNQKGAIENLL HHHHHCCCHHHHHHH	58.83	-
329	Sumoylation	AIENLLAKLLEKKNY HHHHHHHHHHHHCCC	54.28	28112733
329	Ubiquitination	AIENLLAKLLEKKNY HHHHHHHHHHHHCCC	54.28	-
334	Sumoylation	LAKLLEKKNYVHFAA HHHHHHHCCCHHHHH	44.10	-
334	2-Hydroxyisobutyrylation	LAKLLEKKNYVHFAA HHHHHHHCCCHHHHH	44.10	-
334	Sumoylation	LAKLLEKKNYVHFAA HHHHHHHCCCHHHHH	44.10	25218447
334	Ubiquitination	LAKLLEKKNYVHFAA HHHHHHHCCCHHHHH	44.10	-
356	Ubiquitination	KEVNETNKRVEQEIK HHHHHHCHHHHHHHH	66.30	-
376	Ubiquitination	LINEINKKGKSLLQQ HHHHHHHHCHHHHHH	68.06	-
378	Ubiquitination	NEINKKGKSLLQQLE HHHHHHCHHHHHHHH	46.97	-
389	Ubiquitination	QQLENVTKERQMKLL HHHHHHHHHHHHHHH	46.76	-
394	Ubiquitination	VTKERQMKLLQQQND HHHHHHHHHHHHHHC	37.39	21890473
394 (in isoform 1)	Ubiquitination	-	37.39	21890473
394 (in isoform 2)	Ubiquitination	-	37.39	21890473
416	Phosphorylation	VKHVMNFTNWAIASG HHHHHHHCCHHHHCC	25.50	23532336
425	Phosphorylation	WAIASGSSTALLYSK HHHHCCCHHHHHHCH	22.64	23532336
440	Methylation	RLITFQLRHILKARC HHHHHHHHHHHHHCC	12.20	54560213
458	Methylation	PAANGAIRFHCDPTF CCCCCCEEEECCCCH	18.09	115918469
481	Sumoylation	GNLVIESKPAPGYTP CCEEEEECCCCCCCC	32.20	28112733
504	Sumoylation	PGTNHISKTPGQINL CCCCCCCCCCCCCCH	59.12	28112733
504	Ubiquitination	PGTNHISKTPGQINL CCCCCCCCCCCCCCH	59.12	-
505	Phosphorylation	GTNHISKTPGQINLA CCCCCCCCCCCCCHH	26.34	21815630
515	Asymmetric dimethylarginine	QINLAQLRLQHMQQQ CCCHHHHHHHHHHHH	21.88	-
515	Methylation	QINLAQLRLQHMQQQ CCCHHHHHHHHHHHH	21.88	24129315
524	Phosphorylation	QHMQQQVYAQKHQQL HHHHHHHHHHHHHHH	10.04	27642862
527	Sumoylation	QQQVYAQKHQQLQQM HHHHHHHHHHHHHHH	34.90	28112733
535	Methylation	HQQLQQMRMQQPPAP HHHHHHHHHCCCCCC	18.54	24129315
555	Methylation	TTTQQHPRQAAPQML CCCCCCHHHHHHHHH	36.32	115918473
577	Asymmetric dimethylarginine	ISVQTMQRGNMNCGA EEEEEECCCCCCCCH	27.86	-
577	Methylation	ISVQTMQRGNMNCGA EEEEEECCCCCCCCH	27.86	24129315
582	S-nitrosylation	MQRGNMNCGAFQAHQ ECCCCCCCCHHHHHH	2.64	22178444
591	Asymmetric dimethylarginine	AFQAHQMRLAQNAAR HHHHHHHHHHHHHHC	21.94	-
591	Methylation	AFQAHQMRLAQNAAR HHHHHHHHHHHHHHC	21.94	24129315
598	Asymmetric dimethylarginine	RLAQNAARIPGIPRH HHHHHHHCCCCCCCC	32.97	-
598	Methylation	RLAQNAARIPGIPRH HHHHHHHCCCCCCCC	32.97	24129315
604	Asymmetric dimethylarginine	ARIPGIPRHSGPQYS HCCCCCCCCCCCCCC	34.38	-
604	Methylation	ARIPGIPRHSGPQYS HCCCCCCCCCCCCCC	34.38	24129315
610	Phosphorylation	PRHSGPQYSMMQPHL CCCCCCCCCCCCHHH	11.15	-
611	Phosphorylation	RHSGPQYSMMQPHLQ CCCCCCCCCCCHHHH	11.52	23532336
622	Phosphorylation	PHLQRQHSNPGHAGP HHHHHCCCCCCCCCC	36.06	23401153
634	O-linked_Glycosylation	AGPFPVVSVHNTTIN CCCCCEEEEEECEEC	20.21	28510447
634	Phosphorylation	AGPFPVVSVHNTTIN CCCCCEEEEEECEEC	20.21	23401153
638	Phosphorylation	PVVSVHNTTINPTSP CEEEEEECEECCCCC	17.74	28348404
639	Phosphorylation	VVSVHNTTINPTSPT EEEEEECEECCCCCC	24.87	28348404
643	Phosphorylation	HNTTINPTSPTTATM EECEECCCCCCCCCC	42.73	28348404
644	Phosphorylation	NTTINPTSPTTATMA ECEECCCCCCCCCCC	22.85	28348404
646	Phosphorylation	TINPTSPTTATMANA EECCCCCCCCCCCCC	28.91	30177828
647	Phosphorylation	INPTSPTTATMANAN ECCCCCCCCCCCCCC	24.42	30177828
649	Phosphorylation	PTSPTTATMANANRG CCCCCCCCCCCCCCC	18.09	30177828
658	Phosphorylation	ANANRGPTSPSVTAI CCCCCCCCCCCEEEE	56.97	23663014
659	Phosphorylation	NANRGPTSPSVTAIE CCCCCCCCCCEEEEE	20.50	23663014
661	Phosphorylation	NRGPTSPSVTAIELI CCCCCCCCEEEEEEC	31.69	23663014
663	Phosphorylation	GPTSPSVTAIELIPS CCCCCCEEEEEECCC	26.67	23663014
670	Phosphorylation	TAIELIPSVTNPENL EEEEECCCCCCCCCC	34.28	23663014
672	Phosphorylation	IELIPSVTNPENLPS EEECCCCCCCCCCCC	49.77	23663014
679	Phosphorylation	TNPENLPSLPDIPPI CCCCCCCCCCCCCCC	56.55	23663014
720	Phosphorylation	PTSTMNPSPGPSALS CCCCCCCCCCCCCCC	37.17	27174698
724	Phosphorylation	MNPSPGPSALSPGSS CCCCCCCCCCCCCCC	47.99	27174698
727	Phosphorylation	SPGPSALSPGSSGLS CCCCCCCCCCCCCCC	27.25	27174698
730	Phosphorylation	PSALSPGSSGLSNSH CCCCCCCCCCCCCCC	25.31	27174698
731	Phosphorylation	SALSPGSSGLSNSHT CCCCCCCCCCCCCCC	50.06	27174698
734	Phosphorylation	SPGSSGLSNSHTPVR CCCCCCCCCCCCCCC	39.55	27174698
736	Phosphorylation	GSSGLSNSHTPVRPP CCCCCCCCCCCCCCC	25.92	27174698
738	Phosphorylation	SGLSNSHTPVRPPST CCCCCCCCCCCCCCC	24.25	27174698
744	Phosphorylation	HTPVRPPSTSSTGSR CCCCCCCCCCCCCCC	43.53	27174698
745	Phosphorylation	TPVRPPSTSSTGSRG CCCCCCCCCCCCCCC	32.25	27174698
746	Phosphorylation	PVRPPSTSSTGSRGS CCCCCCCCCCCCCCC	30.18	27174698
747	Phosphorylation	VRPPSTSSTGSRGSC CCCCCCCCCCCCCCC	36.55	27174698
748	Phosphorylation	RPPSTSSTGSRGSCG CCCCCCCCCCCCCCC	38.66	27174698
750	Phosphorylation	PSTSSTGSRGSCGSS CCCCCCCCCCCCCCC	33.29	27174698
763	Sumoylation	SSGRTAEKTSLSFKS CCCCCCCCEEEEEEC	40.73	-
763	Acetylation	SSGRTAEKTSLSFKS CCCCCCCCEEEEEEC	40.73	19608861
763	Sumoylation	SSGRTAEKTSLSFKS CCCCCCCCEEEEEEC	40.73	28112733
763	Ubiquitination	SSGRTAEKTSLSFKS CCCCCCCCEEEEEEC	40.73	19608861
765	Phosphorylation	GRTAEKTSLSFKSDQ CCCCCCEEEEEECCE	32.84	28348404
767	Phosphorylation	TAEKTSLSFKSDQVK CCCCEEEEEECCEEE	30.32	25159151
769	Sumoylation	EKTSLSFKSDQVKVK CCEEEEEECCEEEEE	50.15	-
769	Acetylation	EKTSLSFKSDQVKVK CCEEEEEECCEEEEE	50.15	19608861
769	Sumoylation	EKTSLSFKSDQVKVK CCEEEEEECCEEEEE	50.15	28112733
769	Ubiquitination	EKTSLSFKSDQVKVK CCEEEEEECCEEEEE	50.15	19608861
770	Phosphorylation	KTSLSFKSDQVKVKQ CEEEEEECCEEEEEC	31.12	28555341
774	Acetylation	SFKSDQVKVKQEPGT EEECCEEEEECCCCC	37.77	26051181
774	Sumoylation	SFKSDQVKVKQEPGT EEECCEEEEECCCCC	37.77	28112733
776	Sumoylation	KSDQVKVKQEPGTED ECCEEEEECCCCCCC	43.13	-
776	Acetylation	KSDQVKVKQEPGTED ECCEEEEECCCCCCC	43.13	26051181
776	Sumoylation	KSDQVKVKQEPGTED ECCEEEEECCCCCCC	43.13	25114211
781	Phosphorylation	KVKQEPGTEDEICSF EEECCCCCCCCCCCC	51.48	20873877
787	Phosphorylation	GTEDEICSFSGGVKQ CCCCCCCCCCCCCCE	28.27	30576142
789	Phosphorylation	EDEICSFSGGVKQEK CCCCCCCCCCCCEEE	20.53	21815630
793	Sumoylation	CSFSGGVKQEKTEDG CCCCCCCCEEECCCC	56.89	-
793	Acetylation	CSFSGGVKQEKTEDG CCCCCCCCEEECCCC	56.89	23749302
793	Sumoylation	CSFSGGVKQEKTEDG CCCCCCCCEEECCCC	56.89	25114211
793	Ubiquitination	CSFSGGVKQEKTEDG CCCCCCCCEEECCCC	56.89	-
796	Sumoylation	SGGVKQEKTEDGRRS CCCCCEEECCCCCCE	55.51	28112733
803	Phosphorylation	KTEDGRRSACMLSSP ECCCCCCEECCCCCC	25.18	28450419
808	Phosphorylation	RRSACMLSSPESSLT CCEECCCCCCHHHCC	19.57	28450419
809	Phosphorylation	RSACMLSSPESSLTP CEECCCCCCHHHCCC	28.82	29496963
812	Phosphorylation	CMLSSPESSLTPPLS CCCCCCHHHCCCCCC	33.75	28450419
813	Phosphorylation	MLSSPESSLTPPLST CCCCCHHHCCCCCCC	34.30	28450419
815	Phosphorylation	SSPESSLTPPLSTNL CCCHHHCCCCCCCCC	25.47	28450419
819	Phosphorylation	SSLTPPLSTNLHLES HHCCCCCCCCCCHHH	22.48	26074081
820	Phosphorylation	SLTPPLSTNLHLESE HCCCCCCCCCCHHHH	49.86	26074081
826	Phosphorylation	STNLHLESELDALAS CCCCCHHHHHHHHHH	50.23	27080861
839	Sumoylation	ASLENHVKIEPADMN HHHHHCCCCCCCCCC	33.53	-
850	Acetylation	ADMNESCKQSGLSSL CCCCHHHHHCCHHHH	57.70	26051181
852	Phosphorylation	MNESCKQSGLSSLVN CCHHHHHCCHHHHHC	27.48	23927012
855	Phosphorylation	SCKQSGLSSLVNGKS HHHHCCHHHHHCCCC	25.75	30278072
856	Phosphorylation	CKQSGLSSLVNGKSP HHHCCHHHHHCCCCH	41.18	30278072
861	Sumoylation	LSSLVNGKSPIRSLM HHHHHCCCCHHHHHH	48.10	-
861	Acetylation	LSSLVNGKSPIRSLM HHHHHCCCCHHHHHH	48.10	23954790
861	Sumoylation	LSSLVNGKSPIRSLM HHHHHCCCCHHHHHH	48.10	28112733
862	Phosphorylation	SSLVNGKSPIRSLMH HHHHCCCCHHHHHHH	27.27	25159151
866	Phosphorylation	NGKSPIRSLMHRSAR CCCCHHHHHHHHHCC	30.66	26074081
881	Acetylation	IGGDGNNKDDDPNED CCCCCCCCCCCCCCC	67.54	26051181
949	Phosphorylation	DCDNLQHSKKGKTAQ ECCCCCCCCCCCCCC	24.09	23663014
950	Acetylation	CDNLQHSKKGKTAQG CCCCCCCCCCCCCCC	64.52	25953088
951	Acetylation	DNLQHSKKGKTAQGL CCCCCCCCCCCCCCC	69.52	21466224
951	Ubiquitination	DNLQHSKKGKTAQGL CCCCCCCCCCCCCCC	69.52	-
953	Sumoylation	LQHSKKGKTAQGLSP CCCCCCCCCCCCCCH	49.95	-
953	Acetylation	LQHSKKGKTAQGLSP CCCCCCCCCCCCCCH	49.95	19608861
953	Sumoylation	LQHSKKGKTAQGLSP CCCCCCCCCCCCCCH	49.95	28112733
953	Ubiquitination	LQHSKKGKTAQGLSP CCCCCCCCCCCCCCH	49.95	19608861
959	Phosphorylation	GKTAQGLSPVDQRKC CCCCCCCCHHHHHHH	29.69	21815630
998	Ubiquitination	PNYYKIIKKPMDLST CCHHHHHCCCCCHHH	55.06	-
999	Ubiquitination	NYYKIIKKPMDLSTV CHHHHHCCCCCHHHH	34.86	-
1004	Phosphorylation	IKKPMDLSTVKKKLQ HCCCCCHHHHHHHHH	27.22	25627689
1005	Phosphorylation	KKPMDLSTVKKKLQK CCCCCHHHHHHHHHH	43.58	29083192
1007	Sumoylation	PMDLSTVKKKLQKKH CCCHHHHHHHHHHHH	44.25	-
1007	Sumoylation	PMDLSTVKKKLQKKH CCCHHHHHHHHHHHH	44.25	25218447
1007	Ubiquitination	PMDLSTVKKKLQKKH CCCHHHHHHHHHHHH	44.25	-
1015	Phosphorylation	KKLQKKHSQHYQIPD HHHHHHHHCCCCCCC	27.77	30108239
1018	Phosphorylation	QKKHSQHYQIPDDFV HHHHHCCCCCCCCHH	10.66	30108239
1033	Ubiquitination	ADVRLIFKNCERFNE HHHHHHHHCCHHHHH	54.41	-
1043	Sumoylation	ERFNEMMKVVQVYAD HHHHHHHHEEEHHCC	37.63	28112733
1043 (in isoform 2)	Phosphorylation	-	37.63	-
1048	Phosphorylation	MMKVVQVYADTQEIN HHHEEEHHCCCCEEE	5.01	28796482
1051	Phosphorylation	VVQVYADTQEINLKA EEEHHCCCCEEECCC	21.67	29978859
1057	Sumoylation	DTQEINLKADSEVAQ CCCEEECCCCHHHHH	45.73	-
1057	Acetylation	DTQEINLKADSEVAQ CCCEEECCCCHHHHH	45.73	26051181
1057	Sumoylation	DTQEINLKADSEVAQ CCCEEECCCCHHHHH	45.73	28112733
1057	Ubiquitination	DTQEINLKADSEVAQ CCCEEECCCCHHHHH	45.73	-
1067	Ubiquitination	SEVAQAGKAVALYFE HHHHHHCCEEEEEEH	42.58	-
1085	Phosphorylation	TEIYSDRTFAPLPEF HHHHCCCCCCCCCCC	29.19	23927012
1102	Phosphorylation	EEDDGEVTEDSDEDF CCCCCCCCCCCCCCC	29.76	23927012
1105	Phosphorylation	DGEVTEDSDEDFIQP CCCCCCCCCCCCCHH	36.35	23927012
1118	Sumoylation	QPRRKRLKSDERPVH HHHHHHCCCCCCCCC	60.95	-
1118	Acetylation	QPRRKRLKSDERPVH HHHHHHCCCCCCCCC	60.95	26051181
1118	Sumoylation	QPRRKRLKSDERPVH HHHHHHCCCCCCCCC	60.95	28112733
1119	Phosphorylation	PRRKRLKSDERPVHI HHHHHCCCCCCCCCC	49.66	29255136
1127	Acetylation	DERPVHIK------- CCCCCCCC-------	39.13	30583181

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
524	Y	Phosphorylation	Kinase	ABL	P00519	PSP
610	Y	Phosphorylation	Kinase	ABL	P00519	PSP
1048	Y	Phosphorylation	Kinase	ABL	P00519	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRI33_HUMAN !!

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 TRI33_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI33_HUMAN	TRIM33	physical	12096914
TIF1A_HUMAN	TRIM24	physical	12096914
TAL1_HUMAN	TAL1	physical	20603019
HTF4_HUMAN	TCF12	physical	20603019
TFE2_HUMAN	TCF3	physical	20603019
LDB1_HUMAN	LDB1	physical	20603019
MTG8_HUMAN	RUNX1T1	physical	20603019
MTG16_HUMAN	CBFA2T3	physical	20603019
SSBP2_HUMAN	SSBP2	physical	20603019
SSBP3_HUMAN	SSBP3	physical	20603019
SSBP4_HUMAN	SSBP4	physical	20603019
LYL1_HUMAN	LYL1	physical	20603019
ITF2_HUMAN	TCF4	physical	20603019
RUNX1_HUMAN	RUNX1	physical	20603019
SP16H_HUMAN	SUPT16H	physical	20603019
SSRP1_HUMAN	SSRP1	physical	20603019
TRI33_HUMAN	TRIM33	physical	20603019
CDK9_HUMAN	CDK9	physical	20603019
SMAD4_HUMAN	SMAD4	physical	21726812
SMAD2_HUMAN	SMAD2	physical	16751102
SMAD3_HUMAN	SMAD3	physical	16751102
SMAD2_HUMAN	SMAD2	physical	22196728
SMAD3_HUMAN	SMAD3	physical	22196728
H31_HUMAN	HIST1H3A	physical	22196728
LDB1_HUMAN	LDB1	physical	20447379
UB2D3_HUMAN	UBE2D3	physical	21726812
CDC27_HUMAN	CDC27	physical	23160376
APC5_HUMAN	ANAPC5	physical	23160376
CDC20_HUMAN	CDC20	physical	23160376
BUB1B_HUMAN	BUB1B	physical	23160376
CCNA2_HUMAN	CCNA2	physical	23160376
UBC9_HUMAN	UBE2I	physical	23788427
SMAD4_HUMAN	SMAD4	physical	23788427
CRYAB_HUMAN	CRYAB	physical	24307592
SMAD4_HUMAN	SMAD4	physical	24382352
CHD1L_HUMAN	CHD1L	physical	23926104
UBC9_HUMAN	UBE2I	physical	25059663
DHX33_HUMAN	DHX33	physical	25172487
UBE2N_HUMAN	UBE2N	physical	25172487
UB2E1_HUMAN	UBE2E1	physical	25172487
UB2D3_HUMAN	UBE2D3	physical	25172487
FIBA_HUMAN	FGA	physical	26496610
RIR1_HUMAN	RRM1	physical	26496610
LA_HUMAN	SSB	physical	26496610
VDAC2_HUMAN	VDAC2	physical	26496610
TIF1A_HUMAN	TRIM24	physical	26496610
CQ053_HUMAN	C17orf53	physical	26496610
CTNB1_HUMAN	CTNNB1	physical	25639486

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
188550	Thyroid papillary carcinoma (TPC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TRI33_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252; LYS-763; LYS-769 ANDLYS-953, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102; SER-1105AND SER-1119, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-505, AND MASSSPECTROMETRY.	18220336 [Abstract]