dbPTM

GT2D1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GT2D1_HUMAN
UniProt AC	Q9UHL9
Protein Name	General transcription factor II-I repeat domain-containing protein 1
Gene Name	GTF2IRD1
Organism	Homo sapiens (Human).
Sequence Length	959
Subcellular Localization	Nucleus.
Protein Description	May be a transcription regulator involved in cell-cycle progression and skeletal muscle differentiation. May repress GTF2I transcriptional functions, by preventing its nuclear residency, or by inhibiting its transcriptional activation. May contribute to slow-twitch fiber type specificity during myogenesis and in regenerating muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds specifically and with high affinity to the EFG sequences derived from the early enhancer of HOXC8 (By similarity)..
Protein Sequence	MALLGKRCDVPTNGCGPDRWNSAFTRKDEIITSLVSALDSMCSALSKLNAEVACVAVHDESAFVVGTEKGRMFLNARKELQSDFLRFCRGPPWKDPEAEHPKKVQRGEGGGRSLPRSSLEHGSDVYLLRKMVEEVFDVLYSEALGRASVVPLPYERLLREPGLLAVQGLPEGLAFRRPAEYDPKALMAILEHSHRIRFKLKRPLEDGGRDSKALVELNGVSLIPKGSRDCGLHGQAPKVPPQDLPPTATSSSMASFLYSTALPNHAIRELKQEAPSCPLAPSDLGLSRPMPEPKATGAQDFSDCCGQKPTGPGGPLIQNVHASKRILFSIVHDKSEKWDAFIKETEDINTLRECVQILFNSRYAEALGLDHMVPVPYRKIACDPEAVEIVGIPDKIPFKRPCTYGVPKLKRILEERHSIHFIIKRMFDERIFTGNKFTKDTTKLEPASPPEDTSAEVSRATVLDLAGNARSDKGSMSEDCGPGTSGELGGLRPIKIEPEDLDIIQVTVPDPSPTSEEMTDSMPGHLPSEDSGYGMEMLTDKGLSEDARPEERPVEDSHGDVIRPLRKQVELLFNTRYAKAIGISEPVKVPYSKFLMHPEELFVVGLPEGISLRRPNCFGIAKLRKILEASNSIQFVIKRPELLTEGVKEPIMDSQGTASSLGFSPPALPPERDSGDPLVDESLKRQGFQENYDARLSRIDIANTLREQVQDLFNKKYGEALGIKYPVQVPYKRIKSNPGSVIIEGLPPGIPFRKPCTFGSQNLERILAVADKIKFTVTRPFQGLIPKPDEDDANRLGEKVILREQVKELFNEKYGEALGLNRPVLVPYKLIRDSPDAVEVTGLPDDIPFRNPNTYDIHRLEKILKAREHVRMVIINQLQPFAEICNDAKVPAKDSSIPKRKRKRVSEGNSVSSSSSSSSSSSSNPDSVASANQISLVQWPMYMVDYAGLNVQLPGPLNY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
27	Sumoylation	WNSAFTRKDEIITSL HHCCCCCHHHHHHHH	57.57	28112733
94	Ubiquitination	FCRGPPWKDPEAEHP HHCCCCCCCCCCCCC	70.00	-
94	Sumoylation	FCRGPPWKDPEAEHP HHCCCCCCCCCCCCC	70.00	28112733
113	Phosphorylation	RGEGGGRSLPRSSLE CCCCCCCCCCHHHHC	46.10	25159151
117	Phosphorylation	GGRSLPRSSLEHGSD CCCCCCHHHHCCCCC	37.02	25159151
118	Phosphorylation	GRSLPRSSLEHGSDV CCCCCHHHHCCCCCH	38.77	25159151
123	Phosphorylation	RSSLEHGSDVYLLRK HHHHCCCCCHHHHHH	26.30	20860994
130	Ubiquitination	SDVYLLRKMVEEVFD CCHHHHHHHHHHHHH	47.47	20972266
130 (in isoform 2)	Ubiquitination	-	47.47	21890473
148	Phosphorylation	SEALGRASVVPLPYE HHHHCCCCCCCCCHH	23.45	23917254
150	Phosphorylation	ALGRASVVPLPYERL HHCCCCCCCCCHHHH	3.59	27251275
184	Sumoylation	RPAEYDPKALMAILE CCCCCCHHHHHHHHH	51.78	28112733
193	Phosphorylation	LMAILEHSHRIRFKL HHHHHHHHHHHEEEE	12.70	-
201	Ubiquitination	HRIRFKLKRPLEDGG HHHEEEECCCCCCCC	53.19	-
212	Sumoylation	EDGGRDSKALVELNG CCCCCCCCEEHEECC	50.45	-
212	Sumoylation	EDGGRDSKALVELNG CCCCCCCCEEHEECC	50.45	28112733
225	Sumoylation	NGVSLIPKGSRDCGL CCEEEECCCCCCCCC	63.63	-
225	Sumoylation	NGVSLIPKGSRDCGL CCEEEECCCCCCCCC	63.63	28112733
238	Sumoylation	GLHGQAPKVPPQDLP CCCCCCCCCCCCCCC	71.09	28112733
271	Sumoylation	NHAIRELKQEAPSCP HHHHHHHHHHCCCCC	41.14	-
271	Sumoylation	NHAIRELKQEAPSCP HHHHHHHHHHCCCCC	41.14	28112733
271	Ubiquitination	NHAIRELKQEAPSCP HHHHHHHHHHCCCCC	41.14	-
294	Sumoylation	SRPMPEPKATGAQDF CCCCCCCCCCCCCCH	57.84	28112733
308	Sumoylation	FSDCCGQKPTGPGGP HHHHCCCCCCCCCCC	29.81	-
308	Sumoylation	FSDCCGQKPTGPGGP HHHHCCCCCCCCCCC	29.81	28112733
308	Ubiquitination	FSDCCGQKPTGPGGP HHHHCCCCCCCCCCC	29.81	-
329	Phosphorylation	ASKRILFSIVHDKSE CCCCEEEEECCCCHH	21.91	24719451
337	Sumoylation	IVHDKSEKWDAFIKE ECCCCHHHHHHHHHH	58.42	-
337	Sumoylation	IVHDKSEKWDAFIKE ECCCCHHHHHHHHHH	58.42	28112733
337	Ubiquitination	IVHDKSEKWDAFIKE ECCCCHHHHHHHHHH	58.42	-
361	Phosphorylation	CVQILFNSRYAEALG HHHHHHCHHHHHHHC	21.23	24719451
379	Sumoylation	MVPVPYRKIACDPEA CCCCCCCCEECCHHH	28.89	-
379	Sumoylation	MVPVPYRKIACDPEA CCCCCCCCEECCHHH	28.89	-
379	Ubiquitination	MVPVPYRKIACDPEA CCCCCCCCEECCHHH	28.89	-
395	Ubiquitination	EIVGIPDKIPFKRPC EEECCCCCCCCCCCC	47.10	-
403	Phosphorylation	IPFKRPCTYGVPKLK CCCCCCCCCCCHHHH	26.45	29978859
404	Phosphorylation	PFKRPCTYGVPKLKR CCCCCCCCCCHHHHH	23.89	20068231
418	Phosphorylation	RILEERHSIHFIIKR HHHHHHHCHHHHHHH	24.79	21406692
436	Sumoylation	ERIFTGNKFTKDTTK CCCCCCCCCCCCCCC	56.61	-
436	Sumoylation	ERIFTGNKFTKDTTK CCCCCCCCCCCCCCC	56.61	28112733
436	Ubiquitination	ERIFTGNKFTKDTTK CCCCCCCCCCCCCCC	56.61	-
439	Sumoylation	FTGNKFTKDTTKLEP CCCCCCCCCCCCCCC	57.10	28112733
441	Phosphorylation	GNKFTKDTTKLEPAS CCCCCCCCCCCCCCC	27.64	27987026
442	Phosphorylation	NKFTKDTTKLEPASP CCCCCCCCCCCCCCC	43.71	27987026
443	Sumoylation	KFTKDTTKLEPASPP CCCCCCCCCCCCCCC	53.60	-
443	Sumoylation	KFTKDTTKLEPASPP CCCCCCCCCCCCCCC	53.60	28112733
443	Ubiquitination	KFTKDTTKLEPASPP CCCCCCCCCCCCCCC	53.60	-
448	Phosphorylation	TTKLEPASPPEDTSA CCCCCCCCCCCCCCC	52.26	29255136
453	Phosphorylation	PASPPEDTSAEVSRA CCCCCCCCCCHHHHH	28.33	23663014
454	Phosphorylation	ASPPEDTSAEVSRAT CCCCCCCCCHHHHHH	34.45	23403867
458	Phosphorylation	EDTSAEVSRATVLDL CCCCCHHHHHHHHHH	14.01	21406692
461	Phosphorylation	SAEVSRATVLDLAGN CCHHHHHHHHHHCCC	22.08	21406692
471	Phosphorylation	DLAGNARSDKGSMSE HHCCCCCCCCCCCCC	41.06	25159151
475	Phosphorylation	NARSDKGSMSEDCGP CCCCCCCCCCCCCCC	25.52	22817900
477	Phosphorylation	RSDKGSMSEDCGPGT CCCCCCCCCCCCCCC	31.79	25159151
480	Phosphorylation	KGSMSEDCGPGTSGE CCCCCCCCCCCCCCC	6.60	24719451
480	Phosphorylation	KGSMSEDCGPGTSGE CCCCCCCCCCCCCCC	6.60	17081983
495	Sumoylation	LGGLRPIKIEPEDLD CCCCCCCCCCHHHCC	43.64	-
495	Sumoylation	LGGLRPIKIEPEDLD CCCCCCCCCCHHHCC	43.64	-
567	Sumoylation	DVIRPLRKQVELLFN CCCHHHHHHHHHHHC	67.39	-
567	Sumoylation	DVIRPLRKQVELLFN CCCHHHHHHHHHHHC	67.39	28112733
577	Phosphorylation	ELLFNTRYAKAIGIS HHHHCCCHHHHHCCC	15.49	-
579	Sumoylation	LFNTRYAKAIGISEP HHCCCHHHHHCCCCC	31.44	-
579	Ubiquitination	LFNTRYAKAIGISEP HHCCCHHHHHCCCCC	31.44	2189047
579	Sumoylation	LFNTRYAKAIGISEP HHCCCHHHHHCCCCC	31.44	28112733
579 (in isoform 1)	Ubiquitination	-	31.44	21890473
579 (in isoform 2)	Ubiquitination	-	31.44	21890473
584	Phosphorylation	YAKAIGISEPVKVPY HHHHHCCCCCCCCCH	30.54	-
588	Sumoylation	IGISEPVKVPYSKFL HCCCCCCCCCHHHHC	48.48	28112733
611 (in isoform 3)	Ubiquitination	-	27.04	-
611	Ubiquitination	VGLPEGISLRRPNCF EECCCCCCCCCCCCC	27.04	21890473
622	Acetylation	PNCFGIAKLRKILEA CCCCHHHHHHHHHHH	47.07	26051181
622	Sumoylation	PNCFGIAKLRKILEA CCCCHHHHHHHHHHH	47.07	28112733
630	Phosphorylation	LRKILEASNSIQFVI HHHHHHHCCCEEEEE	23.02	24043423
632	Phosphorylation	KILEASNSIQFVIKR HHHHHCCCEEEEECC	18.44	24043423
638	Sumoylation	NSIQFVIKRPELLTE CCEEEEECCHHHHCC	57.51	-
638	Sumoylation	NSIQFVIKRPELLTE CCEEEEECCHHHHCC	57.51	28112733
644	Phosphorylation	IKRPELLTEGVKEPI ECCHHHHCCCCCCCC	43.23	24043423
654	Phosphorylation	VKEPIMDSQGTASSL CCCCCCCCCCCHHHC	17.09	17525332
654 (in isoform 2)	Phosphorylation	-	17.09	17525332
659 (in isoform 2)	Phosphorylation	-	26.40	25627689
684	Sumoylation	PLVDESLKRQGFQEN CCCCHHHHHCCCCCC	52.54	-
684	Sumoylation	PLVDESLKRQGFQEN CCCCHHHHHCCCCCC	52.54	28112733
684	Ubiquitination	PLVDESLKRQGFQEN CCCCHHHHHCCCCCC	52.54	-
686 (in isoform 3)	Phosphorylation	-	56.30	17525332
691 (in isoform 3)	Phosphorylation	-	29.24	25627689
697	Phosphorylation	ENYDARLSRIDIANT CCHHHHHHHHHHHHH	22.95	28555341
704	Phosphorylation	SRIDIANTLREQVQD HHHHHHHHHHHHHHH	20.40	24719451
715	Ubiquitination	QVQDLFNKKYGEALG HHHHHHHHHHHHHHC	39.78	-
716	Ubiquitination	VQDLFNKKYGEALGI HHHHHHHHHHHHHCC	60.64	-
717	Phosphorylation	QDLFNKKYGEALGIK HHHHHHHHHHHHCCC	23.08	21406692
721	Phosphorylation	NKKYGEALGIKYPVQ HHHHHHHHCCCCCEE	6.75	24719451
724	Sumoylation	YGEALGIKYPVQVPY HHHHHCCCCCEECCC	41.52	-
724	Sumoylation	YGEALGIKYPVQVPY HHHHHCCCCCEECCC	41.52	28112733
724	Ubiquitination	YGEALGIKYPVQVPY HHHHHCCCCCEECCC	41.52	-
732	Sumoylation	YPVQVPYKRIKSNPG CCEECCCHHCCCCCC	41.39	28112733
754	Ubiquitination	PPGIPFRKPCTFGSQ CCCCCCCCCCCCCCC	44.84	-
757	Phosphorylation	IPFRKPCTFGSQNLE CCCCCCCCCCCCCHH	39.29	25921289
760	Phosphorylation	RKPCTFGSQNLERIL CCCCCCCCCCHHHHH	16.23	25921289
772	Sumoylation	RILAVADKIKFTVTR HHHHHHHHCEEEECC	37.75	28112733
774	Sumoylation	LAVADKIKFTVTRPF HHHHHHCEEEECCCC	40.50	28112733
787	Sumoylation	PFQGLIPKPDEDDAN CCCCCCCCCCHHHHH	59.09	-
787	Sumoylation	PFQGLIPKPDEDDAN CCCCCCCCCCHHHHH	59.09	28112733
799	Ubiquitination	DANRLGEKVILREQV HHHHHCHHHHHHHHH	32.55	-
807	Ubiquitination	VILREQVKELFNEKY HHHHHHHHHHHHHHH	48.68	-
814	Phosphorylation	KELFNEKYGEALGLN HHHHHHHHHHHHCCC	17.64	-
828	Phosphorylation	NRPVLVPYKLIRDSP CCCEEEEHHHHCCCC	15.79	-
829	Sumoylation	RPVLVPYKLIRDSPD CCEEEEHHHHCCCCC	31.22	-
829	Sumoylation	RPVLVPYKLIRDSPD CCEEEEHHHHCCCCC	31.22	28112733
829	Ubiquitination	RPVLVPYKLIRDSPD CCEEEEHHHHCCCCC	31.22	-
829	Acetylation	RPVLVPYKLIRDSPD CCEEEEHHHHCCCCC	31.22	26051181
834	Phosphorylation	PYKLIRDSPDAVEVT EHHHHCCCCCCEEEC	18.16	20860994
846 (in isoform 3)	Ubiquitination	-	48.82	-
889	Sumoylation	AEICNDAKVPAKDSS HHHHCCCCCCCCCCC	52.17	28112733
893	Sumoylation	NDAKVPAKDSSIPKR CCCCCCCCCCCCCHH	52.66	28112733
906	Phosphorylation	KRKRKRVSEGNSVSS HHHCCCCCCCCCCCC	43.76	-
914	Phosphorylation	EGNSVSSSSSSSSSS CCCCCCCCCCCCCCC	27.08	-
915	Phosphorylation	GNSVSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
916	Phosphorylation	NSVSSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
917	Phosphorylation	SVSSSSSSSSSSSSN CCCCCCCCCCCCCCC	35.87	-

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
Oops, there are no upstream regulatory protein records of GT2D1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GT2D1_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 GT2D1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIZ2_YEAST	NFI1	physical	12193603
PIAS2_MOUSE	Pias2	physical	12193603
HDAC3_HUMAN	HDAC3	physical	16055724
CBX5_HUMAN	CBX5	physical	26275350
CBX1_HUMAN	CBX1	physical	26275350
CBX3_HUMAN	CBX3	physical	26275350
SP1_HUMAN	SP1	physical	26275350
AKIR2_MOUSE	Akirin2	physical	26275350
ALMS1_HUMAN	ALMS1	physical	26275350
ARMX5_MOUSE	Armcx5	physical	26275350
MCAF1_HUMAN	ATF7IP	physical	26275350
AT2C1_HUMAN	ATP2C1	physical	26275350
BBS4_MOUSE	Bbs4	physical	26275350
CSPP1_MOUSE	Cspp1	physical	26275350
ELF2_MOUSE	Elf2	physical	26275350
FHAD1_MOUSE	Fhad1	physical	26275350
HOMEZ_MOUSE	Homez	physical	26275350
HTRA4_HUMAN	HTRA4	physical	26275350
INT12_HUMAN	INTS12	physical	26275350
IMA5_HUMAN	KPNA1	physical	26275350
IMA4_HUMAN	KPNA3	physical	26275350
IMA3_HUMAN	KPNA4	physical	26275350
MB3L1_HUMAN	MBD3L1	physical	26275350
NP1L2_MOUSE	Nap1l2	physical	26275350
OPHN1_MOUSE	Ophn1	physical	26275350
PARI_MOUSE	Parpbp	physical	26275350
PIAS2_HUMAN	PIAS2	physical	26275350
PKP2_HUMAN	PKP2	physical	26275350
SCNM1_MOUSE	Scnm1	physical	26275350
SETD6_MOUSE	Setd6	physical	26275350
SPTC1_HUMAN	SPTLC1	physical	26275350
TAF1B_MOUSE	Taf1b	physical	26275350
PP4P2_HUMAN	TMEM55A	physical	26275350
UBP20_HUMAN	USP20	physical	26275350
UBP33_MOUSE	Usp33	physical	26275350
SELS_HUMAN	VIMP	physical	26275350
ZMYM2_MOUSE	Zmym2	physical	26275350
ZMYM3_MOUSE	Zmym3	physical	26275350
DCAF6_MOUSE	Dcaf6	physical	26275350
DCAF6_HUMAN	DCAF6	physical	26275350
IMA1_MOUSE	Kpna2	physical	26275350
IMA1_HUMAN	KPNA2	physical	26275350
PIAS1_MOUSE	Pias1	physical	26275350
PIAS1_HUMAN	PIAS1	physical	26275350
ZC4H2_MOUSE	Zc4h2	physical	26275350
ZC4H2_HUMAN	ZC4H2	physical	26275350
ZMYM5_MOUSE	Zmym5	physical	26275350
ZMYM5_HUMAN	ZMYM5	physical	26275350
PKP1_HUMAN	PKP1	physical	26275350
ZMYM2_HUMAN	ZMYM2	physical	26275350
ZMYM3_HUMAN	ZMYM3	physical	26275350

Drug and Disease Associations

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

Regulatory Network of GT2D1_HUMAN

Related Literatures of Post-Translational Modification

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-448, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND MASSSPECTROMETRY.	15302935 [Abstract]