THA_HUMAN - dbPTM
THA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THA_HUMAN
UniProt AC P10827
Protein Name Thyroid hormone receptor alpha
Gene Name THRA
Organism Homo sapiens (Human).
Sequence Length 490
Subcellular Localization Nucleus.
Protein Description Isoform Alpha-1: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.; Isoform Alpha-2: Does not bind thyroid hormone and functions as a weak dominant negative inhibitor of thyroid hormone action..
Protein Sequence MEQKPSKVECGSDPEENSARSPDGKRKRKNGQCSLKTSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHIATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQAVLLMSTDRSGLLCVDKIEKSQEAYLLAFEHYVNHRKHNIPHFWPKLLMKEREVQSSILYKGAAAEGRPGGSLGVHPEGQQLLGMHVVQGPQVRQLEQQLGEAGSLQGPVLQHQSPKSPQQRLLELLHRSGILHARAVCGEDDSSEADSPSSSEEEPEVCEDLAGNAASP
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 Orthologous
Protein Cluster
7Acetylation-MEQKPSKVECGSDP
-CCCCCCCCCCCCCC		51.057684559
12PhosphorylationPSKVECGSDPEENSA
CCCCCCCCCCCCCCC		62.7525850435
18PhosphorylationGSDPEENSARSPDGK
CCCCCCCCCCCCCCC		28.4825159151
21PhosphorylationPEENSARSPDGKRKR
CCCCCCCCCCCCCCC		27.3625159151
25AcetylationSARSPDGKRKRKNGQ
CCCCCCCCCCCCCCC		63.237684575
37PhosphorylationNGQCSLKTSMSGYIP
CCCEECCCCCCCCCH		34.6525219547
38PhosphorylationGQCSLKTSMSGYIPS
CCEECCCCCCCCCHH		14.9025219547
40PhosphorylationCSLKTSMSGYIPSYL
EECCCCCCCCCHHHC		28.3625219547
42PhosphorylationLKTSMSGYIPSYLDK
CCCCCCCCCHHHCCC		11.4425219547
45PhosphorylationSMSGYIPSYLDKDEQ
CCCCCCHHHCCCCCC		28.8625219547
46PhosphorylationMSGYIPSYLDKDEQC
CCCCCHHHCCCCCCE		17.3625219547
130AcetylationDLVLDDSKRVAKRKL
HHHHCCHHHHHHHHH		58.8619819978
134AcetylationDDSKRVAKRKLIEQN
CCHHHHHHHHHHHHH		47.4019819978
136AcetylationSKRVAKRKLIEQNRE
HHHHHHHHHHHHHHH		53.7819819978
190UbiquitinationSHWKQRRKFLPDDIG
CHHHHHHHCCCCCCC		54.1418655026
199PhosphorylationLPDDIGQSPIVSMPD
CCCCCCCCCCEECCC		16.0425159151
283 (in isoform 2)Sumoylation-40.45-
288 (in isoform 2)Sumoylation-53.92-
304UbiquitinationDAIFELGKSLSAFNL
HHHHHHCCCCCCCCC		61.93-
389 (in isoform 2)Sumoylation-63.45-
435PhosphorylationGPVLQHQSPKSPQQR
CCCCCCCCCCCHHHH		31.9726329039
450PhosphorylationLLELLHRSGILHARA
HHHHHHHCCCCHHEC		21.31-
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
-KUbiquitinationE3 ubiquitin ligaseTRIM63Q969Q1
PMID:26862156
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THA_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 THA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCND1_HUMANCCND1physical
12048199
EP300_HUMANEP300physical
12371907
MEF2A_HUMANMEF2Aphysical
12371907
CENPR_HUMANITGB3BPphysical
11713274
NRIP1_HUMANNRIP1physical
9626662
MED12_HUMANMED12physical
10198638
MED16_HUMANMED16physical
10198638
MED6_HUMANMED6physical
10198638
MED24_HUMANMED24physical
10198638
CDK8_HUMANCDK8physical
10198638
MED21_HUMANMED21physical
10198638
CSN2_DROMEalienphysical
10207062
CSN2_HUMANCOPS2physical
10207062
TRIPB_HUMANTRIP11physical
9256431
CENPR_HUMANITGB3BPphysical
10490654
RXRA_HUMANRXRAphysical
1314167
MED1_HUMANMED1physical
9653119
HDAC3_HUMANHDAC3physical
11889044
NCOR1_HUMANNCOR1physical
11889044
ZBTB3_HUMANZBTB3physical
20211142
SUV91_HUMANSUV39H1physical
12138181
NCOA1_HUMANNCOA1physical
11117530
NCOA2_HUMANNCOA2physical
11117530
NCOA3_HUMANNCOA3physical
11117530
MED1_HUMANMED1physical
11117530
RXRA_HUMANRXRAphysical
11117530
TAF11_HUMANTAF11physical
10744685
MED1_HUMANMED1physical
10733574
TAF7_HUMANTAF7physical
10409738
GRIP1_HUMANGRIP1physical
10379889
NCOA1_HUMANNCOA1physical
10379889
NRIP1_HUMANNRIP1physical
10379889
MED1_HUMANMED1physical
10037764
NCOR1_HUMANNCOR1physical
9849963
GRIP1_HUMANGRIP1physical
9849963
NCOR2_HUMANNCOR2physical
9415406
PRKDC_HUMANPRKDCphysical
17242407
NCOR1_HUMANNCOR1physical
17242407
NCOR2_HUMANNCOR2physical
17242407
SMC1A_HUMANSMC1Aphysical
17242407
PARP1_HUMANPARP1physical
17242407
DNLI3_HUMANLIG3physical
17242407
XRCC5_HUMANXRCC5physical
17242407
XRCC6_HUMANXRCC6physical
17242407
HSP74_HUMANHSPA4physical
17242407
TBL1R_HUMANTBL1XR1physical
17242407
HDAC3_HUMANHDAC3physical
17242407
GPS2_HUMANGPS2physical
17242407
TBL1X_HUMANTBL1Xphysical
17242407
RXRA_HUMANRXRAphysical
15604093
CUL1_HUMANCUL1physical
15604093
RGN_HUMANRGNphysical
15604093
SEPP1_HUMANSEPP1physical
15604093
NCOR1_HUMANNCOR1physical
15604093
MED1_HUMANMED1physical
16799563
MED21_HUMANMED21physical
15249124
CDK7_HUMANCDK7physical
15249124
NRIP1_HUMANNRIP1physical
21868449
MED1_HUMANMED1physical
21868449
ARI5A_HUMANARID5Aphysical
15941852
TAT_HV1H2tatphysical
7609079
NCOR2_HUMANNCOR2physical
16219912
THA_HUMANTHRAphysical
19422879
RXRA_HUMANRXRAphysical
19422879
NCOR1_HUMANNCOR1physical
7566114
AMOL2_HUMANAMOTL2physical
25416956
LMBL3_HUMANL3MBTL3physical
25416956
CEP76_HUMANCEP76physical
21516116
TRI63_HUMANTRIM63physical
26862156
HUTH_HUMANHALphysical
28514442
CYTM_HUMANCST6physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614450Hypothyroidism, congenital, non-goitrous, 6 (CHNG6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00509Dextrothyroxine
DB00451Levothyroxine
DB00279Liothyronine
DB01583Liotrix
Regulatory Network of THA_HUMAN

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells.";
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
Proteomics 8:2885-2896(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-190, AND MASSSPECTROMETRY.

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