HUMAN:TTHY

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TTR (synonyms: PALB)
Protein Name(s)	Transthyretin ATTR Prealbumin TBPA
External Links
UniProt	P02766
EMBL	K02091 M10605 M11518 M11844 X59498 D00096 M15517 M15515 M15516 U19780 AF162690 AK312051 BT007189 CR456908 CH471088 BC005310 BC020791 S63185 S72385 M11714 M63285
CCDS	CCDS11899.1
PIR	A91532
RefSeq	NP_000362.1
UniGene	Hs.427202
PDB	1BM7 1BMZ 1BZ8 1BZD 1BZE 1DVQ 1DVS 1DVT 1DVU 1DVX 1DVY 1DVZ 1E3F 1E4H 1E5A 1ETA 1ETB 1F41 1F64 1F86 1FH2 1FHN 1G1O 1GKO 1ICT 1III 1IIK 1IJN 1QAB 1QWH 1RLB 1SOK 1SOQ 1THA 1THC 1TLM 1TSH 1TT6 1TTA 1TTB 1TTC 1TTR 1TYR 1TZ8 1U21 1X7S 1X7T 1Y1D 1Z7J 1ZCR 1ZD6 2B14 2B15 2B16 2B77 2B9A 2F7I 2F8I 2FBR 2FLM 2G3X 2G3Z 2G4E 2G4G 2G5U 2G9K 2GAB 2H4E 2M5N 2NOY 2PAB 2QEL 2QGB 2QGC 2QGD 2QGE 2ROX 2ROY 2TRH 2TRY 2WQA 3A4D 3A4E 3A4F 3B56 3BSZ 3BT0 3CBR 3CFM 3CFN 3CFQ 3CFT 3CN0 3CN1 3CN2 3CN3 3CN4 3CXF 3D2T 3D7P 3DGD 3DID 3DJR 3DJS 3DJT 3DJZ 3DK0 3DK2 3DO4 3ESN 3ESO 3ESP 3FC8 3FCB 3GLZ 3GPS 3GRB 3GRG 3GS0 3GS4 3GS7 3HJ0 3I9A 3I9I 3I9P 3IMR 3IMS 3IMT 3IMU 3IMV 3IMW 3IPB 3IPE 3KGS 3KGT 3KGU 3M1O 3NEE 3NEO 3NES 3NEX 3NG5 3OZK 3OZL 3P3R 3P3S 3P3T 3P3U 3SSG 3TCT 3TFB 3U2I 3U2J 3W3B 4ABQ 4ABU 4ABV 4ABW 4AC2 4AC4 4ACT 4ANK 4DER 4DES 4DET 4DEU 4DEW 4FI6 4FI7 4FI8 4HIQ 4HIS 4HJS 4HJT 4HJU 4I85 4I87 4I89 4IIZ 4IK6 4IK7 4IKI 4IKJ 4IKK 4IKL 4KY2 4L1S 4L1T 4MAS 4MRB 4MRC 4N85 4N86 4N87 4PM1 4PME 4PMF 4PVL 4PVM 4PVN 5TTR
PDBsum	1BM7 1BMZ 1BZ8 1BZD 1BZE 1DVQ 1DVS 1DVT 1DVU 1DVX 1DVY 1DVZ 1E3F 1E4H 1E5A 1ETA 1ETB 1F41 1F64 1F86 1FH2 1FHN 1G1O 1GKO 1ICT 1III 1IIK 1IJN 1QAB 1QWH 1RLB 1SOK 1SOQ 1THA 1THC 1TLM 1TSH 1TT6 1TTA 1TTB 1TTC 1TTR 1TYR 1TZ8 1U21 1X7S 1X7T 1Y1D 1Z7J 1ZCR 1ZD6 2B14 2B15 2B16 2B77 2B9A 2F7I 2F8I 2FBR 2FLM 2G3X 2G3Z 2G4E 2G4G 2G5U 2G9K 2GAB 2H4E 2M5N 2NOY 2PAB 2QEL 2QGB 2QGC 2QGD 2QGE 2ROX 2ROY 2TRH 2TRY 2WQA 3A4D 3A4E 3A4F 3B56 3BSZ 3BT0 3CBR 3CFM 3CFN 3CFQ 3CFT 3CN0 3CN1 3CN2 3CN3 3CN4 3CXF 3D2T 3D7P 3DGD 3DID 3DJR 3DJS 3DJT 3DJZ 3DK0 3DK2 3DO4 3ESN 3ESO 3ESP 3FC8 3FCB 3GLZ 3GPS 3GRB 3GRG 3GS0 3GS4 3GS7 3HJ0 3I9A 3I9I 3I9P 3IMR 3IMS 3IMT 3IMU 3IMV 3IMW 3IPB 3IPE 3KGS 3KGT 3KGU 3M1O 3NEE 3NEO 3NES 3NEX 3NG5 3OZK 3OZL 3P3R 3P3S 3P3T 3P3U 3SSG 3TCT 3TFB 3U2I 3U2J 3W3B 4ABQ 4ABU 4ABV 4ABW 4AC2 4AC4 4ACT 4ANK 4DER 4DES 4DET 4DEU 4DEW 4FI6 4FI7 4FI8 4HIQ 4HIS 4HJS 4HJT 4HJU 4I85 4I87 4I89 4IIZ 4IK6 4IK7 4IKI 4IKJ 4IKK 4IKL 4KY2 4L1S 4L1T 4MAS 4MRB 4MRC 4N85 4N86 4N87 4PM1 4PME 4PMF 4PVL 4PVM 4PVN 5TTR
ProteinModelPortal	P02766
SMR	P02766
BioGrid	113127
DIP	DIP-1083N
IntAct	P02766
MINT	MINT-1374623
STRING	9606.ENSP00000237014
BindingDB	P02766
ChEMBL	CHEMBL3194
DrugBank	DB00586 DB00255 DB00861 DB01093 DB00451 DB00279 DB01583
PhosphoSite	P02766
DMDM	136464
DOSAC-COBS-2DPAGE	P02766
REPRODUCTION-2DPAGE	P02766
SWISS-2DPAGE	P02766
UCD-2DPAGE	P02766
MaxQB	P02766
PaxDb	P02766
PeptideAtlas	P02766
PRIDE	P02766
DNASU	7276
Ensembl	ENST00000237014
GeneID	7276
KEGG	hsa:7276
UCSC	uc002kwx.4
CTD	7276
GeneCards	GC18P029194
GeneReviews	TTR
HGNC	HGNC:12405
HPA	CAB002517 CAB062567 HPA002550
MIM	105210 115430 145680 176300
neXtProt	NX_P02766
Orphanet	85447 85451
PharmGKB	PA37069
eggNOG	NOG321124
GeneTree	ENSGT00390000005321
HOGENOM	HOG000251776
HOVERGEN	HBG000285
InParanoid	P02766
OMA	KAADETW
OrthoDB	EOG7S4X7V
PhylomeDB	P02766
TreeFam	TF300210
Reactome	REACT_160130 REACT_160156 REACT_163874 REACT_24968 REACT_75925
ChiTaRS	TTR
EvolutionaryTrace	P02766
GeneWiki	Transthyretin
GenomeRNAi	7276
NextBio	28455
PMAP-CutDB	P02766
PRO	PR:P02766
Proteomes	UP000005640
Bgee	P02766
CleanEx	HS_TTR
ExpressionAtlas	P02766
Genevestigator	P02766
GO	GO:0005737 GO:0005576 GO:0005615 GO:0070062 GO:0043234 GO:0042562 GO:0042802 GO:0030198 GO:0007603 GO:0001523 GO:0042572 GO:0006810
Gene3D	2.60.40.180
InterPro	IPR023418 IPR030178 IPR000895 IPR023416 IPR023419
PANTHER	PTHR10395:SF12
Pfam	PF00576
PRINTS	PR00189
SMART	SM00095
SUPFAM	SSF49472
PROSITE	PS00768 PS00769

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0070062	extracellular exosome	PMID:23533145^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:16502470^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001914)	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:14718574^[3]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0070324	thyroid hormone binding	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000044594 UniProtKB:P27731 UniProtKB:P50390	F		Seeded From UniProt	complete
involved_in	GO:0006144	purine nucleobase metabolic process	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000044586 ZFIN:ZDB-GENE-060825-253	P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000044594 RGD:3916 UniProtKB:P27731 UniProtKB:P50390	C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23850452^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02766	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23792159^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02766	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21777382^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02766	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21740906^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02766	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21422279^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02766	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19861125^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02766	F		Seeded From UniProt	complete
involved_in	GO:0010469	regulation of signaling receptor activity	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0005179	P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P02767 ensembl:ENSRNOP00000022113	F		Seeded From UniProt	complete
enables	GO:0042562	hormone binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P02767 ensembl:ENSRNOP00000022113	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P02767 ensembl:ENSRNOP00000022113	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P02767 ensembl:ENSRNOP00000022113	C		Seeded From UniProt	complete
involved_in	GO:0042572	retinol metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030178	P		Seeded From UniProt	complete
enables	GO:0070324	thyroid hormone binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030178	F		Seeded From UniProt	complete
involved_in	GO:0070327	thyroid hormone transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030178	P		Seeded From UniProt	complete
involved_in	GO:0044267	cellular protein metabolic process	Reactome:R-HSA-392499	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035578	azurophil granule lumen	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030198	extracellular matrix organization	Reactome:R-HSA-1474244	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-977136 Reactome:R-HSA-976734 Reactome:R-HSA-6798751 Reactome:R-HSA-2453876 Reactome:R-HSA-2453863 Reactome:R-HSA-2453818 Reactome:R-HSA-2404134 Reactome:R-HSA-2396337	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001523	retinoid metabolic process	Reactome:R-HSA-975634 Reactome:R-HSA-2453902	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0005179	hormone activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0372	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page
↑ Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Hall, Z et al. (2013) The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure 21 1325-37 PubMed GONUTS page
↑ Zanotti, G et al. (2013) Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitors. FEBS Lett. 587 2325-31 PubMed GONUTS page
↑ Leelawatwattana, L et al. (2011) Effect of the N-terminal sequence on the binding affinity of transthyretin for human retinol-binding protein. FEBS J. 278 3337-47 PubMed GONUTS page
↑ Ferreira, N et al. (2011) Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation. FEBS Lett. 585 2424-30 PubMed GONUTS page
↑ Noborn, F et al. (2011) Heparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein. Proc. Natl. Acad. Sci. U.S.A. 108 5584-9 PubMed GONUTS page
↑ Ferreira, N et al. (2009) Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity. FEBS Lett. 583 3569-76 PubMed GONUTS page

[PMID:23533145-1] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:16502470-2] Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page

[PMID:14718574-3] Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page

[PMID:21873635-4] 4.0 ^4.1 ^4.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:23850452-5] Hall, Z et al. (2013) The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure 21 1325-37 PubMed GONUTS page

[PMID:23792159-6] Zanotti, G et al. (2013) Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitors. FEBS Lett. 587 2325-31 PubMed GONUTS page

[PMID:21777382-7] Leelawatwattana, L et al. (2011) Effect of the N-terminal sequence on the binding affinity of transthyretin for human retinol-binding protein. FEBS J. 278 3337-47 PubMed GONUTS page

[PMID:21740906-8] Ferreira, N et al. (2011) Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation. FEBS Lett. 585 2424-30 PubMed GONUTS page

[PMID:21422279-9] Noborn, F et al. (2011) Heparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein. Proc. Natl. Acad. Sci. U.S.A. 108 5584-9 PubMed GONUTS page

[PMID:19861125-10] Ferreira, N et al. (2009) Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity. FEBS Lett. 583 3569-76 PubMed GONUTS page

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HUMAN:TTHY

Contents

Annotations

Notes

References

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