dbPTM

TXNIP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TXNIP_HUMAN
UniProt AC	Q9H3M7
Protein Name	Thioredoxin-interacting protein
Gene Name	TXNIP
Organism	Homo sapiens (Human).
Sequence Length	391
Subcellular Localization	Cytoplasm.
Protein Description	May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1)..
Protein Sequence	MVMFKKIKSFEVVFNDPEKVYGSGEKVAGRVIVEVCEVTRVKAVRILACGVAKVLWMQGSQQCKQTSEYLRYEDTLLLEDQPTGENEMVIMRPGNKYEYKFGFELPQGPLGTSFKGKYGCVDYWVKAFLDRPSQPTQETKKNFEVVDLVDVNTPDLMAPVSAKKEKKVSCMFIPDGRVSVSARIDRKGFCEGDEISIHADFENTCSRIVVPKAAIVARHTYLANGQTKVLTQKLSSVRGNHIISGTCASWRGKSLRVQKIRPSILGCNILRVEYSLLIYVSVPGSKKVILDLPLVIGSRSGLSSRTSSMASRTSSEMSWVDLNIPDTPEAPPCYMDVIPEDHRLESPTTPLLDDMDGSQDSPIFMYAPEFKFMPPPTYTEVDPCILNNNVQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Sumoylation	MVMFKKIKSFEVVFN CCCCEECCEEEEEEC	58.95	-
8	Sumoylation	MVMFKKIKSFEVVFN CCCCEECCEEEEEEC	58.95	-
9	Phosphorylation	VMFKKIKSFEVVFND CCCEECCEEEEEECC	30.07	27499020
19	Sumoylation	VVFNDPEKVYGSGEK EEECCHHHHCCCCCE	46.26	-
19	Ubiquitination	VVFNDPEKVYGSGEK EEECCHHHHCCCCCE	46.26	29967540
19	Sumoylation	VVFNDPEKVYGSGEK EEECCHHHHCCCCCE	46.26	-
21	Phosphorylation	FNDPEKVYGSGEKVA ECCHHHHCCCCCEEC	19.35	23312004
23	Phosphorylation	DPEKVYGSGEKVAGR CHHHHCCCCCEECCE	26.54	23312004
26	Ubiquitination	KVYGSGEKVAGRVIV HHCCCCCEECCEEEE	40.69	23000965
41	Ubiquitination	EVCEVTRVKAVRILA EEEECCCCEEHHHHH	3.22	23503661
45	Ubiquitination	VTRVKAVRILACGVA CCCCEEHHHHHHHHH	24.06	23503661
53	Ubiquitination	ILACGVAKVLWMQGS HHHHHHHHHHHHCCC	35.14	-
60	Ubiquitination	KVLWMQGSQQCKQTS HHHHHCCCHHHHHHH	10.53	21890473
60	Phosphorylation	KVLWMQGSQQCKQTS HHHHHCCCHHHHHHH	10.53	-
60	Ubiquitination	KVLWMQGSQQCKQTS HHHHHCCCHHHHHHH	10.53	22817900
62	Ubiquitination	LWMQGSQQCKQTSEY HHHCCCHHHHHHHHH	37.76	22817900
64	Ubiquitination	MQGSQQCKQTSEYLR HCCCHHHHHHHHHHC	52.88	-
85	Ubiquitination	LEDQPTGENEMVIMR ECCCCCCCCEEEEEC	53.12	29967540
96	Ubiquitination	VIMRPGNKYEYKFGF EEECCCCEEEEEEEE	45.43	23503661
100	Sumoylation	PGNKYEYKFGFELPQ CCCEEEEEEEEECCC	27.37	-
100	Sumoylation	PGNKYEYKFGFELPQ CCCEEEEEEEEECCC	27.37	-
100	Ubiquitination	PGNKYEYKFGFELPQ CCCEEEEEEEEECCC	27.37	23503661
108	Ubiquitination	FGFELPQGPLGTSFK EEEECCCCCCCCCCC	19.91	32015554
109	Ubiquitination	GFELPQGPLGTSFKG EEECCCCCCCCCCCC	23.52	23503661
111	Ubiquitination	ELPQGPLGTSFKGKY ECCCCCCCCCCCCCC	23.58	23503661
112	Ubiquitination	LPQGPLGTSFKGKYG CCCCCCCCCCCCCCC	38.38	23503661
115	Sumoylation	GPLGTSFKGKYGCVD CCCCCCCCCCCCCHH	55.02	-
115	Ubiquitination	GPLGTSFKGKYGCVD CCCCCCCCCCCCCHH	55.02	21906983
115	Sumoylation	GPLGTSFKGKYGCVD CCCCCCCCCCCCCHH	55.02	-
117	Ubiquitination	LGTSFKGKYGCVDYW CCCCCCCCCCCHHHH	38.77	22817900
117	Sumoylation	LGTSFKGKYGCVDYW CCCCCCCCCCCHHHH	38.77	-
117	Sumoylation	LGTSFKGKYGCVDYW CCCCCCCCCCCHHHH	38.77	-
140	Ubiquitination	SQPTQETKKNFEVVD CCCCHHHHCCEEEEE	44.99	29967540
140	Sumoylation	SQPTQETKKNFEVVD CCCCHHHHCCEEEEE	44.99	-
140	Sumoylation	SQPTQETKKNFEVVD CCCCHHHHCCEEEEE	44.99	-
141	Ubiquitination	QPTQETKKNFEVVDL CCCHHHHCCEEEEEE	74.43	-
157	Ubiquitination	DVNTPDLMAPVSAKK ECCCCCCCCCCCCCC	5.30	21890473
157	Ubiquitination	DVNTPDLMAPVSAKK ECCCCCCCCCCCCCC	5.30	21890473
163	Ubiquitination	LMAPVSAKKEKKVSC CCCCCCCCCCCCEEE	54.69	32015554
163	Sumoylation	LMAPVSAKKEKKVSC CCCCCCCCCCCCEEE	54.69	-
163	Sumoylation	LMAPVSAKKEKKVSC CCCCCCCCCCCCEEE	54.69	-
164	Ubiquitination	MAPVSAKKEKKVSCM CCCCCCCCCCCEEEE	74.59	23503661
166	Ubiquitination	PVSAKKEKKVSCMFI CCCCCCCCCEEEEEE	68.31	23503661
167	Ubiquitination	VSAKKEKKVSCMFIP CCCCCCCCEEEEEEC	40.24	23503661
167	Sumoylation	VSAKKEKKVSCMFIP CCCCCCCCEEEEEEC	40.24	-
167	Sumoylation	VSAKKEKKVSCMFIP CCCCCCCCEEEEEEC	40.24	-
173	Ubiquitination	KKVSCMFIPDGRVSV CCEEEEEECCCCEEE	0.90	22817900
173	Ubiquitination	KKVSCMFIPDGRVSV CCEEEEEECCCCEEE	0.90	21890473
178	Ubiquitination	MFIPDGRVSVSARID EEECCCCEEEEEEEC	8.95	21890473
178	Ubiquitination	MFIPDGRVSVSARID EEECCCCEEEEEEEC	8.95	22817900
187	Ubiquitination	VSARIDRKGFCEGDE EEEEECCCCCCCCCE	53.22	-
206	Phosphorylation	ADFENTCSRIVVPKA ECCCCCCCCEEECHH	24.01	24719451
212	Sumoylation	CSRIVVPKAAIVARH CCCEEECHHHEEEEE	38.55	-
212	Sumoylation	CSRIVVPKAAIVARH CCCEEECHHHEEEEE	38.55	-
212	Ubiquitination	CSRIVVPKAAIVARH CCCEEECHHHEEEEE	38.55	22817900
228	Sumoylation	YLANGQTKVLTQKLS EECCCCEEEEEECHH	27.62	-
228	Sumoylation	YLANGQTKVLTQKLS EECCCCEEEEEECHH	27.62	-
228	Ubiquitination	YLANGQTKVLTQKLS EECCCCEEEEEECHH	27.62	21906983
231	Ubiquitination	NGQTKVLTQKLSSVR CCCEEEEEECHHHCC	27.01	22817900
232	Ubiquitination	GQTKVLTQKLSSVRG CCEEEEEECHHHCCC	40.30	21890473
232	Ubiquitination	GQTKVLTQKLSSVRG CCEEEEEECHHHCCC	40.30	21890473
233	Ubiquitination	QTKVLTQKLSSVRGN CEEEEEECHHHCCCC	45.13	22817900
233	Sumoylation	QTKVLTQKLSSVRGN CEEEEEECHHHCCCC	45.13	-
233	Sumoylation	QTKVLTQKLSSVRGN CEEEEEECHHHCCCC	45.13	-
233	Malonylation	QTKVLTQKLSSVRGN CEEEEEECHHHCCCC	45.13	26320211
235	Phosphorylation	KVLTQKLSSVRGNHI EEEEECHHHCCCCEE	33.55	24719451
249	Phosphorylation	IISGTCASWRGKSLR EEECCCCCCCCCCCE	21.32	28857561
259	Ubiquitination	GKSLRVQKIRPSILG CCCCEEEECCHHHHC	37.51	-
286	Ubiquitination	YVSVPGSKKVILDLP EEECCCCCEEEEECC	57.90	22817900
287	Sumoylation	VSVPGSKKVILDLPL EECCCCCEEEEECCE	35.88	-
287	Ubiquitination	VSVPGSKKVILDLPL EECCCCCEEEEECCE	35.88	21906983
287	Sumoylation	VSVPGSKKVILDLPL EECCCCCEEEEECCE	35.88	-
300	Phosphorylation	PLVIGSRSGLSSRTS CEEEECCCCCCHHCC	45.87	23090842
303	Phosphorylation	IGSRSGLSSRTSSMA EECCCCCCHHCCHHC	22.69	23090842
304	Phosphorylation	GSRSGLSSRTSSMAS ECCCCCCHHCCHHCC	44.62	23090842
306	Phosphorylation	RSGLSSRTSSMASRT CCCCCHHCCHHCCCC	27.40	23090842
307	Phosphorylation	SGLSSRTSSMASRTS CCCCHHCCHHCCCCC	19.60	23090842
308	Phosphorylation	GLSSRTSSMASRTSS CCCHHCCHHCCCCCC	20.11	23090842
311	Phosphorylation	SRTSSMASRTSSEMS HHCCHHCCCCCCCCC	27.70	23090842
313	Phosphorylation	TSSMASRTSSEMSWV CCHHCCCCCCCCCCC	33.82	27642862
314	Phosphorylation	SSMASRTSSEMSWVD CHHCCCCCCCCCCCC	24.16	26356563
315	Phosphorylation	SMASRTSSEMSWVDL HHCCCCCCCCCCCCC	36.38	22210691
318	Phosphorylation	SRTSSEMSWVDLNIP CCCCCCCCCCCCCCC	21.64	26356563
327	Phosphorylation	VDLNIPDTPEAPPCY CCCCCCCCCCCCCCE	20.06	27642862
334	Phosphorylation	TPEAPPCYMDVIPED CCCCCCCEEECCCCC	11.34	27642862
346	Phosphorylation	PEDHRLESPTTPLLD CCCCCCCCCCCCCCC	31.94	28450419
348	Phosphorylation	DHRLESPTTPLLDDM CCCCCCCCCCCCCCC	50.77	28450419
349	Phosphorylation	HRLESPTTPLLDDMD CCCCCCCCCCCCCCC	18.47	28102081
358	Phosphorylation	LLDDMDGSQDSPIFM CCCCCCCCCCCCEEE	26.92	28102081
361	Phosphorylation	DMDGSQDSPIFMYAP CCCCCCCCCEEEECC	16.56	20068034
366	Phosphorylation	QDSPIFMYAPEFKFM CCCCEEEECCCCCCC	14.30	28450419
377	Phosphorylation	FKFMPPPTYTEVDPC CCCCCCCCCCCCCCC	49.18	21945579
378	Phosphorylation	KFMPPPTYTEVDPCI CCCCCCCCCCCCCCC	13.48	21945579
379	Phosphorylation	FMPPPTYTEVDPCIL CCCCCCCCCCCCCCC	31.82	21945579

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
308	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
349	T	Phosphorylation	Kinase	ERK2	P28482	PSP
361	S	Phosphorylation	Kinase	P38A	Q16539	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:20068034

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBT32_HUMAN	ZBTB32	physical	12821938
ZBT16_HUMAN	ZBTB16	physical	12821938
HDAC1_HUMAN	HDAC1	physical	12821938
ITCH_HUMAN	ITCH	physical	20068034
THIO_HUMAN	TXN	physical	21705327
ECD_HUMAN	ECD	physical	23880345
THIO_HUMAN	TXN	physical	23880345
DDIT4_HUMAN	DDIT4	physical	21460850
THIO_HUMAN	TXN	physical	23519408
THIO_HUMAN	TXN	physical	17603038
THIO_HUMAN	TXN	physical	16269462
CSN5_HUMAN	COPS5	physical	18202760
CDN1B_HUMAN	CDKN1B	physical	18202760
HDAC1_HUMAN	HDAC1	physical	20826751
HDAC3_HUMAN	HDAC3	physical	20826751
TF65_HUMAN	RELA	physical	20826751
THIO_HUMAN	TXN	physical	21636804
VGFR2_HUMAN	KDR	physical	23393387
RAB5A_HUMAN	RAB5A	physical	23393387
AP2A2_MOUSE	Ap2a2	physical	23453806
CLH1_MOUSE	Cltc	physical	23453806
GTR1_HUMAN	SLC2A1	physical	23453806
THIO_HUMAN	TXN	physical	24389582
TXNIP_HUMAN	TXNIP	physical	24389582
RAD18_HUMAN	RAD18	physical	28514442
DCA16_HUMAN	DCAF16	physical	28514442
MYCB2_HUMAN	MYCBP2	physical	28514442
PER1_HUMAN	PER1	physical	28514442
MBD3_HUMAN	MBD3	physical	28514442
MTA1_HUMAN	MTA1	physical	28514442
KBTB7_HUMAN	KBTBD7	physical	28514442
F91A1_HUMAN	FAM91A1	physical	28514442
P66B_HUMAN	GATAD2B	physical	28514442
CRY2_HUMAN	CRY2	physical	28514442
THIOM_HUMAN	TXN2	physical	28514442
KBTB6_HUMAN	KBTBD6	physical	28514442
THIO_HUMAN	TXN	physical	28514442
WWP1_HUMAN	WWP1	physical	28514442
SRC8_HUMAN	CTTN	physical	27437069
FLNA_HUMAN	FLNA	physical	27437069
4F2_HUMAN	SLC3A2	physical	27437069
HS90B_HUMAN	HSP90AB1	physical	27437069
HSP13_HUMAN	HSPA13	physical	27437069
DNJC7_HUMAN	DNAJC7	physical	27437069
HSP7C_HUMAN	HSPA8	physical	27437069
STIP1_HUMAN	STIP1	physical	27437069
JHD2C_HUMAN	JMJD1C	physical	27437069
TOX4_HUMAN	TOX4	physical	27437069
YETS2_HUMAN	YEATS2	physical	27437069
MRE11_HUMAN	MRE11A	physical	27437069
PARP1_HUMAN	PARP1	physical	27437069
EP15R_HUMAN	EPS15L1	physical	27437069
NUMA1_HUMAN	NUMA1	physical	27437069
TPR_HUMAN	TPR	physical	27437069
ITCH_HUMAN	ITCH	physical	27437069
UBE2O_HUMAN	UBE2O	physical	27437069
TXNL1_HUMAN	TXNL1	physical	27437069
AHNK_HUMAN	AHNAK	physical	27437069
NOP58_HUMAN	NOP58	physical	27437069
SNUT1_HUMAN	SART1	physical	27437069
ADNP_HUMAN	ADNP	physical	27437069
S30BP_HUMAN	SAP30BP	physical	27437069
SCML2_HUMAN	SCML2	physical	27437069
TIF1B_HUMAN	TRIM28	physical	27437069
KAISO_HUMAN	ZBTB33	physical	27437069
IF5_HUMAN	EIF5	physical	27437069
CX056_HUMAN	CXorf56	physical	27437069

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 TXNIP_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 THR-349 AND SER-361, ANDMASS SPECTROMETRY.	18669648 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-212, AND MASSSPECTROMETRY.	18781797 [Abstract]