TXD17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TXD17_HUMAN
• UniProt AC: Q9BRA2
• Protein Name: Thioredoxin domain-containing protein 17
• Gene Name: TXNDC17
• Organism: Homo sapiens (Human).
• Sequence Length: 123
• Subcellular Localization: Cytoplasm .
• Protein Description: Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide..
• Protein Sequence: MARYEEVSVSGFEEFHRAVEQHNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNNDFRKNLKVTAVPTLLKYGTPQKLVESECLQANLVEMLFSED

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
2	Acetylation	------MARYEEVSV ------CCCCEEEEC	23.82	19413330
8	Phosphorylation	MARYEEVSVSGFEEF CCCCEEEECCCHHHH	17.53	25849741
25	Succinylation	AVEQHNGKTIFAYFT HHHHHCCCEEEEEEE	43.71	23954790
25	Acetylation	AVEQHNGKTIFAYFT HHHHHCCCEEEEEEE	43.71	26051181
25	Ubiquitination	AVEQHNGKTIFAYFT HHHHHCCCEEEEEEE	43.71	21890473
26	Phosphorylation	VEQHNGKTIFAYFTG HHHHCCCEEEEEEEC	23.79	20068231
30	Phosphorylation	NGKTIFAYFTGSKDA CCCEEEEEEECCCCC	7.30	28152594
32	Phosphorylation	KTIFAYFTGSKDAGG CEEEEEEECCCCCCC	28.06	28152594
34	Phosphorylation	IFAYFTGSKDAGGKS EEEEEECCCCCCCCC	25.06	28152594
35	Ubiquitination	FAYFTGSKDAGGKSW EEEEECCCCCCCCCC	53.60	21890473
35	Acetylation	FAYFTGSKDAGGKSW EEEEECCCCCCCCCC	53.60	26051181
40	Acetylation	GSKDAGGKSWCPDCV CCCCCCCCCCCCCCC	39.61	23749302
40	Ubiquitination	GSKDAGGKSWCPDCV CCCCCCCCCCCCCCC	39.61	-
46	Glutathionylation	GKSWCPDCVQAEPVV CCCCCCCCCCCHHHH	1.15	22555962
74	Acetylation	IYCQVGEKPYWKDPN EEEEECCCCCCCCCC	37.16	27452117
78	Acetylation	VGEKPYWKDPNNDFR ECCCCCCCCCCCHHH	58.42	23954790
78	Ubiquitination	VGEKPYWKDPNNDFR ECCCCCCCCCCCHHH	58.42	21906983
89	Acetylation	NDFRKNLKVTAVPTL CHHHHHCCCCCCCCH	47.11	25953088
89	Ubiquitination	NDFRKNLKVTAVPTL CHHHHHCCCCCCCCH	47.11	21890473
91	Phosphorylation	FRKNLKVTAVPTLLK HHHHCCCCCCCCHHH	21.98	23911959
95	Phosphorylation	LKVTAVPTLLKYGTP CCCCCCCCHHHHCCC	37.82	27067055
98	Ubiquitination	TAVPTLLKYGTPQKL CCCCCHHHHCCCHHH	44.75	21890473
98	Acetylation	TAVPTLLKYGTPQKL CCCCCHHHHCCCHHH	44.75	25038526
104	Ubiquitination	LKYGTPQKLVESECL HHHCCCHHHHHHHHH	56.56	-

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

Oops, there are no upstream regulatory protein records of TXD17_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TXD17_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TXD17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
INS_HUMAN	INS	physical	14607844
NEU1_HUMAN	OXT	physical	14607844
NEU2_HUMAN	AVP	physical	14607844
DYL1_HUMAN	DYNLL1	physical	14607843
COF1_HUMAN	CFL1	physical	14607843
WDR1_HUMAN	WDR1	physical	22939629
TYSY_HUMAN	TYMS	physical	22939629
TXNL1_HUMAN	TXNL1	physical	22939629
VINEX_HUMAN	SORBS3	physical	22939629
UBP3_HUMAN	USP3	physical	22939629
UBE2H_HUMAN	UBE2H	physical	22939629
UBP5_HUMAN	USP5	physical	22939629
UBA3_HUMAN	UBA3	physical	22939629
UBE2N_HUMAN	UBE2N	physical	22939629
UBE2K_HUMAN	UBE2K	physical	22939629
VATA_HUMAN	ATP6V1A	physical	22939629
VATC1_HUMAN	ATP6V1C1	physical	22939629
WIPI3_HUMAN	WDR45B	physical	22939629
UPAR_HUMAN	PLAUR	physical	22939629
NALP5_HUMAN	NLRP5	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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-78, AND MASS SPECTROMETRY.
PubMed: 19608861