dbPTM

TTHY_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTHY_HUMAN
UniProt AC	P02766
Protein Name	Transthyretin
Gene Name	TTR
Organism	Homo sapiens (Human).
Sequence Length	147
Subcellular Localization	Secreted. Cytoplasm.
Protein Description	Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain..
Protein Sequence	MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	S-nitrosocysteine	SHRLLLLCLAGLVFV HHHHHHHHHHHHHEE	2.17	-
10	S-nitrosylation	SHRLLLLCLAGLVFV HHHHHHHHHHHHHEE	2.17	22178444
23	Phosphorylation	FVSEAGPTGTGESKC EEECCCCCCCCCCCC	46.59	-
25	Phosphorylation	SEAGPTGTGESKCPL ECCCCCCCCCCCCCE	40.01	-
62	4-carboxyglutamate	KAADDTWEPFASGKT HHCCCCCCCCCCCCC	32.41	-
62	Gamma-carboxyglutamic_acid	KAADDTWEPFASGKT HHCCCCCCCCCCCCC	32.41	18221012
62	Gamma-carboxyglutamic_acid	KAADDTWEPFASGKT HHCCCCCCCCCCCCC	32.41	18221012
69	Phosphorylation	EPFASGKTSESGELH CCCCCCCCCCCCCCC	41.05	27130503
70	Phosphorylation	PFASGKTSESGELHG CCCCCCCCCCCCCCC	33.00	27130503
72	Phosphorylation	ASGKTSESGELHGLT CCCCCCCCCCCCCCC	37.02	26657352
79	Phosphorylation	SGELHGLTTEEEFVE CCCCCCCCCHHHHHC	36.43	27130503
80	Phosphorylation	GELHGLTTEEEFVEG CCCCCCCCHHHHHCC	46.58	28060719
96	Acetylation	YKVEIDTKSYWKALG EEEEECCHHHHHHHC	37.49	27178108
96	2-Hydroxyisobutyrylation	YKVEIDTKSYWKALG EEEEECCHHHHHHHC	37.49	-
118	N-linked_Glycosylation	AEVVFTANDSGPRRY EEEEEECCCCCCCEE	40.71	16335952
125	Phosphorylation	NDSGPRRYTIAALLS CCCCCCEEEEEEEEC	12.08	-
137	Phosphorylation	LLSPYSYSTTAVVTN EECCCCCEEEEEEEC	17.22	-
138	Phosphorylation	LSPYSYSTTAVVTNP ECCCCCEEEEEEECC	15.56	-

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 TTHY_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
38	G	Glycosylation	19167329
Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway.
118	N	Glycosylation	16335952
Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway.

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 TTHY_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FEZ1_HUMAN	FEZ1	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
SETB1_HUMAN	SETDB1	physical	16169070
VIME_HUMAN	VIM	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
ELP1_HUMAN	IKBKAP	physical	16169070
TTHY_HUMAN	TTR	physical	11243784
PGBM_HUMAN	HSPG2	physical	9307034
RET4_HUMAN	RBP4	physical	574085
TBA1A_HUMAN	TUBA1A	physical	21900206
F10A1_HUMAN	ST13	physical	21900206
A2MG_HUMAN	A2M	physical	21900206
TAF1C_HUMAN	TAF1C	physical	21900206
SP110_HUMAN	SP110	physical	21900206
FEZ1_HUMAN	FEZ1	physical	21900206
SUMO3_HUMAN	SUMO3	physical	21900206
RAI1_HUMAN	RAI1	physical	21900206
VIME_HUMAN	VIM	physical	21900206
CE126_HUMAN	KIAA1377	physical	21900206
ELP1_HUMAN	IKBKAP	physical	21900206
CPNE6_HUMAN	CPNE6	physical	21900206
TNR16_HUMAN	NGFR	physical	21900206
ZBED1_HUMAN	ZBED1	physical	21900206
CAB45_HUMAN	SDF4	physical	21900206
OTUB1_HUMAN	OTUB1	physical	21900206
INP5K_HUMAN	INPP5K	physical	21900206
ERG28_HUMAN	C14orf1	physical	21900206
CHD3_HUMAN	CHD3	physical	21900206
SYQ_HUMAN	QARS	physical	21900206
KPCI_HUMAN	PRKCI	physical	21900206
ACTB_HUMAN	ACTB	physical	21900206
TAF5L_HUMAN	TAF5L	physical	21900206
ASNA_HUMAN	ASNA1	physical	21900206
BAG6_HUMAN	BAG6	physical	21900206
CTND2_HUMAN	CTNND2	physical	21900206
SETB1_HUMAN	SETDB1	physical	21900206
CLUS_HUMAN	CLU	physical	19664600
TTHY_HUMAN	TTR	physical	19664600
MT3_HUMAN	MT3	physical	20646067
NECA2_HUMAN	NECAB2	physical	25416956
TTHY_HUMAN	TTR	physical	25478940
DERL1_HUMAN	DERL1	physical	26565908
DERL2_HUMAN	DERL2	physical	26565908
DERL3_HUMAN	DERL3	physical	26565908
BAG6_HUMAN	BAG6	physical	26565908
TERA_HUMAN	VCP	physical	26565908

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
105210	Amyloidosis, transthyretin-related (AMYL-TTR)
145680	Hyperthyroxinemia, dystransthyretinemic (DTTRH)
115430	Carpal tunnel syndrome 1 (CTS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00586	Diclofenac
DB00255	Diethylstilbestrol
DB00861	Diflunisal
DB01093	Dimethyl sulfoxide
DB00451	Levothyroxine
DB00279	Liothyronine
DB01583	Liotrix

Regulatory Network of TTHY_HUMAN

Related Literatures of Post-Translational Modification

Gamma-carboxyglutamic acid
Reference	PubMed
"Detection of a gamma-carboxy-glutamate as novel post-translationalmodification of human transthyretin."; Rueggeberg S., Horn P., Li X., Vajkoczy P., Franz T.; Protein Pept. Lett. 15:43-46(2008). Cited for: GAMMA-CARBOXYGLUTAMATION AT GLU-62, AND MASS SPECTROMETRY.	18221012 [Abstract]
N-linked Glycosylation
Reference	PubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118, AND MASSSPECTROMETRY.	16335952 [Abstract]

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