dbPTM

THIO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THIO_HUMAN
UniProt AC	P10599
Protein Name	Thioredoxin
Gene Name	TXN
Organism	Homo sapiens (Human).
Sequence Length	105
Subcellular Localization	Nucleus . Cytoplasm . Secreted . Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA) (PubMed:9108029). Predominantly in the cytoplasm in non irradiated cells (PubMed:11118054). Radiation induces tran
Protein Description	Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.; ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55)..
Protein Sequence	MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	2-Hydroxyisobutyrylation	-----MVKQIESKTA -----CCCCHHCHHH	44.23	-
3	Ubiquitination	-----MVKQIESKTA -----CCCCHHCHHH	44.23	19608861
3	Acetylation	-----MVKQIESKTA -----CCCCHHCHHH	44.23	19608861
8	Methylation	MVKQIESKTAFQEAL CCCCHHCHHHHHHHH	30.96	55170643
8	Acetylation	MVKQIESKTAFQEAL CCCCHHCHHHHHHHH	30.96	25825284
8	Succinylation	MVKQIESKTAFQEAL CCCCHHCHHHHHHHH	30.96	-
8	Ubiquitination	MVKQIESKTAFQEAL CCCCHHCHHHHHHHH	30.96	-
8	Succinylation	MVKQIESKTAFQEAL CCCCHHCHHHHHHHH	30.96	23954790
8	2-Hydroxyisobutyrylation	MVKQIESKTAFQEAL CCCCHHCHHHHHHHH	30.96	-
9	Phosphorylation	VKQIESKTAFQEALD CCCHHCHHHHHHHHH	41.82	21815630
28	Phosphorylation	KLVVVDFSATWCGPC EEEEEECCCCEECCH	21.96	30301811
30	Phosphorylation	VVVDFSATWCGPCKM EEEECCCCEECCHHH	21.79	30301811
37	Sulfoxidation	TWCGPCKMIKPFFHS CEECCHHHHHHHHHH	6.41	30846556
39	2-Hydroxyisobutyrylation	CGPCKMIKPFFHSLS ECCHHHHHHHHHHHH	32.07	-
39	Malonylation	CGPCKMIKPFFHSLS ECCHHHHHHHHHHHH	32.07	26320211
39	Ubiquitination	CGPCKMIKPFFHSLS ECCHHHHHHHHHHHH	32.07	21890473
39	Ubiquitination	CGPCKMIKPFFHSLS ECCHHHHHHHHHHHH	32.07	21890473
39	Acetylation	CGPCKMIKPFFHSLS ECCHHHHHHHHHHHH	32.07	19608861
44	Phosphorylation	MIKPFFHSLSEKYSN HHHHHHHHHHHHCCC	28.56	28450419
46	Phosphorylation	KPFFHSLSEKYSNVI HHHHHHHHHHCCCEE	34.75	28450419
48	Methylation	FFHSLSEKYSNVIFL HHHHHHHHCCCEEEE	51.07	115979325
49	Phosphorylation	FHSLSEKYSNVIFLE HHHHHHHCCCEEEEE	11.04	24275569
49	Nitration	FHSLSEKYSNVIFLE HHHHHHHCCCEEEEE	11.04	-
50	Phosphorylation	HSLSEKYSNVIFLEV HHHHHHCCCEEEEEE	35.37	22468782
62	S-nitrosylation	LEVDVDDCQDVASEC EEEEHHCHHHHHHHC	3.01	17260951
62	S-palmitoylation	LEVDVDDCQDVASEC EEEEHHCHHHHHHHC	3.01	25576832
62	S-nitrosocysteine	LEVDVDDCQDVASEC EEEEHHCHHHHHHHC	3.01	-
67	Phosphorylation	DDCQDVASECEVKCM HCHHHHHHHCCEEEE	42.50	24275569
69	S-nitrosylation	CQDVASECEVKCMPT HHHHHHHCCEEEECC	7.25	17260951
69	S-palmitoylation	CQDVASECEVKCMPT HHHHHHHCCEEEECC	7.25	25576832
69	S-nitrosocysteine	CQDVASECEVKCMPT HHHHHHHCCEEEECC	7.25	-
73	S-nitrosylation	ASECEVKCMPTFQFF HHHCCEEEECCEEEE	4.82	17606900
73	S-glutathionyl cysteine	ASECEVKCMPTFQFF HHHCCEEEECCEEEE	4.82	-
73	S-palmitoylation	ASECEVKCMPTFQFF HHHCCEEEECCEEEE	4.82	25839660
73	Glutathionylation	ASECEVKCMPTFQFF HHHCCEEEECCEEEE	4.82	12119401
76	Phosphorylation	CEVKCMPTFQFFKKG CCEEEECCEEEECCC	11.82	21712546
81	Acetylation	MPTFQFFKKGQKVGE ECCEEEECCCCEEEC	58.23	25953088
81	2-Hydroxyisobutyrylation	MPTFQFFKKGQKVGE ECCEEEECCCCEEEC	58.23	-
85	Ubiquitination	QFFKKGQKVGEFSGA EEECCCCEEECCCCC	61.96	-
85	Acetylation	QFFKKGQKVGEFSGA EEECCCCEEECCCCC	61.96	25953088
85	Succinylation	QFFKKGQKVGEFSGA EEECCCCEEECCCCC	61.96	23954790
90	Phosphorylation	GQKVGEFSGANKEKL CCEEECCCCCCHHHH	32.47	29978859
94	Ubiquitination	GEFSGANKEKLEATI ECCCCCCHHHHHHHH	56.54	21906983
94	Malonylation	GEFSGANKEKLEATI ECCCCCCHHHHHHHH	56.54	26320211
94	Succinylation	GEFSGANKEKLEATI ECCCCCCHHHHHHHH	56.54	-
94	Acetylation	GEFSGANKEKLEATI ECCCCCCHHHHHHHH	56.54	16916647
94	Succinylation	GEFSGANKEKLEATI ECCCCCCHHHHHHHH	56.54	-
96	Acetylation	FSGANKEKLEATINE CCCCCHHHHHHHHHH	53.92	25953088
96	2-Hydroxyisobutyrylation	FSGANKEKLEATINE CCCCCHHHHHHHHHH	53.92	-
96	Ubiquitination	FSGANKEKLEATINE CCCCCHHHHHHHHHH	53.92	21906983
100	Phosphorylation	NKEKLEATINELV-- CHHHHHHHHHHHC--	18.24	16097034

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
76	T	Phosphorylation	Kinase	MELK	Q61846	PSP
100	T	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CO1A1_HUMAN	COL1A1	physical	12099690
NCF4_HUMAN	NCF4	physical	10397171
GCR_HUMAN	NR3C1	physical	9915858
FST_HUMAN	FST	physical	12099690
VIME_HUMAN	VIM	physical	12099690
TXNIP_HUMAN	TXNIP	physical	10419473
M3K5_HUMAN	MAP3K5	physical	12089063
NFKB1_HUMAN	NFKB1	physical	7788295
M3K5_HUMAN	MAP3K5	physical	11689443
M3K5_HUMAN	MAP3K5	physical	9564042
P53_HUMAN	TP53	physical	19681600
TXNIP_HUMAN	TXNIP	physical	21705327
CSN5_HUMAN	COPS5	physical	15480426
M3K5_HUMAN	MAP3K5	physical	17724081
PTN6_HUMAN	PTPN6	physical	19561639
M3K5_HUMAN	MAP3K5	physical	20385180
WDR1_HUMAN	WDR1	physical	22939629
UBQL4_HUMAN	UBQLN4	physical	22939629
UB2V1_HUMAN	UBE2V1	physical	22939629
VATF_HUMAN	ATP6V1F	physical	22939629
UBL5_HUMAN	UBL5	physical	22939629
UB2D2_HUMAN	UBE2D2	physical	22939629
UBE2K_HUMAN	UBE2K	physical	22939629
TX1B3_HUMAN	TAX1BP3	physical	22939629
TXNIP_MOUSE	Txnip	physical	10843682
M3K5_HUMAN	MAP3K5	physical	10843682
PRDX1_HUMAN	PRDX1	physical	10843682
MELK_MOUSE	Melk	physical	23747528
APEX1_HUMAN	APEX1	physical	22863883
SRP09_HUMAN	SRP9	physical	22863883
GCR_HUMAN	NR3C1	physical	19570036
TXNIP_HUMAN	TXNIP	physical	10814541
TXNIP_HUMAN	TXNIP	physical	16766796
TXNIP_MOUSE	Txnip	physical	16766796
TXNIP_HUMAN	TXNIP	physical	17603038
TXNIP_HUMAN	TXNIP	physical	24198286
TXNIP_HUMAN	TXNIP	physical	16269462
M3K5_HUMAN	MAP3K5	physical	19018770
TXNIP_HUMAN	TXNIP	physical	19018770
TXNIP_HUMAN	TXNIP	physical	19605364
ARK72_HUMAN	AKR7A2	physical	26344197
GDIR1_HUMAN	ARHGDIA	physical	26344197
CCS_HUMAN	CCS	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
4EBP2_HUMAN	EIF4EBP2	physical	26344197
GLOD4_HUMAN	GLOD4	physical	26344197
GSTO1_HUMAN	GSTO1	physical	26344197
HINT1_HUMAN	HINT1	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
SODC_HUMAN	SOD1	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TAGL3_HUMAN	TAGLN3	physical	26344197
TYSY_HUMAN	TYMS	physical	26344197

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 THIO_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-3 AND LYS-39, AND MASSSPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100, AND MASSSPECTROMETRY.	16097034 [Abstract]
S-nitrosylation
Reference	PubMed
"Buried S-nitrosocysteine revealed in crystal structures of humanthioredoxin."; Weichsel A., Brailey J.L., Montfort W.R.; Biochemistry 46:1219-1227(2007). Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, DISULFIDE BONDS, ANDS-NITROSYLATION AT CYS-62 AND CYS-69.	17260951 [Abstract]
"Thioredoxin is required for S-nitrosation of procaspase-3 and theinhibition of apoptosis in Jurkat cells."; Mitchell D.A., Morton S.U., Fernhoff N.B., Marletta M.A.; Proc. Natl. Acad. Sci. U.S.A. 104:11609-11614(2007). Cited for: FUNCTION, MUTAGENESIS OF CYS-69; GLU-70; LYS-72 AND CYS-73, ANDS-NITROSYLATION AT CYS-73 IN RESPONSE TO NITRIC OXIDE.	17606900 [Abstract]
"Thioredoxin catalyzes the S-nitrosation of the caspase-3 active sitecysteine."; Mitchell D.A., Marletta M.A.; Nat. Chem. Biol. 1:154-158(2005). Cited for: FUNCTION, MUTAGENESIS OF CYS-73, AND S-NITROSYLATION AT CYS-73.	16408020 [Abstract]