Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Hepatocyte nuclear factor 4-alpha  

UniProtKB / Swiss-Prot ID :  HNF4A_HUMAN

Gene Name (Synonyms) : 
HNF4A, HNF4, NR2A1, TCF14  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Transcriptionally controlled transcription factor. Binds to DNA sites required for the transcription of alpha 1- antitrypsin, apolipoprotein CIII, transthyretin genes and HNF1- alpha. May be essential for development of the liver, kidney and intestine. 

Protein Sequence MRLSKTLVDMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGTNLNAPNSLGVSALCAICGDRATGK...
Predicted Secondary Structure CCCCHHCCCHHHHHCCCCCCCCCCCCCCCCCEECCCCCCCCCCCCCCCCCCCCCCCCCCCEEECCCCCCC...
Protein Variant
LocationDescription
136R -> W (in MODY1). VAR_004668
139T -> I (in dbSNP:rs1800961). VAR_004669
264V -> M (in late-onset NIDDM). VAR_010600
285E -> Q (in MODY1). VAR_010601
402V -> I (in MODY1; reduced transactivationactivity).
445P -> S (in dbSNP:rs1063239). VAR_011785
453V -> I. VAR_062267
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
23PhosphotyrosineLDPAYTTLE
CCCCCCCCC
12.97Phosphositeplus
Link-
106N6-acetyllysineCVVDKDKRN
CEECHHHHH
54.24Phosphositeplus
Link-
108N6-acetyllysineVDKDKRNQC
ECHHHHHHH
60.01Phosphositeplus
Link-
126N6-acetyllysineRAGMKKEAV
HHHCCCCCC
46.69Phosphositeplus
Link-
127N6-acetyllysineAGMKKEAVQ
HHCCCCCCC
41.85Phosphositeplus
Link-
138PhosphoserineRDRISTRRS
HHHHCCCCC
19.43Phosphositeplus
Link
142PhosphoserineSTRRSSYED
CCCCCCCCC
33.70PhosphoELM
Link
142PhosphoserineSTRRSSYED
CCCCCCCCC
33.70Phosphositeplus
Link
142Phosphoserine.STRRSSYED
CCCCCCCCC
33.70UniProtKB
Link
143PhosphoserineTRRSSYEDS
CCCCCCCCC
30.63PhosphoELM
Link
143PhosphoserineTRRSSYEDS
CCCCCCCCC
30.63Phosphositeplus
Link
147PhosphoserineSYEDSSLPS
CCCCCCCCH
23.10Phosphositeplus
Link
151PhosphoserineSSLPSINAL
CCCCHHHHH
33.49Phosphositeplus
Link
166PhosphothreonineSRQITSPVS
HHHHCCCCC
20.74Phosphositeplus
Link
166Phosphothreonine.SRQITSPVS
HHHHCCCCC
20.74UniProtKB
Link
167PhosphoserineRQITSPVSG
HHHCCCCCC
25.57Phosphositeplus
Link
167Phosphoserine (MAPK11)RQITSPVSG
HHHCCCCCC
25.57PhosphoELM
Link
167Phosphoserine (MAPK14)RQITSPVSG
HHHCCCCCC
25.57HPRD
Link
167Phosphoserine.RQITSPVSG
HHHCCCCCC
25.57UniProtKB
Link
190PhosphoserineDVCESMKEQ
HHHHHHHHH
29.99PhosphoELM
Link
190PhosphoserineDVCESMKEQ
HHHHHHHHH
29.99Phosphositeplus
Link
234Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LGATKRSMV
HHHHHHHCC
41.77Phosphositeplus
Link
234Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).LGATKRSMV
HHHHHHHCC
41.77UniProtKB
Link
286PhosphotyrosineDDNEYAYLK
CHHHHHHHH
13.55Phosphositeplus
Link
288PhosphotyrosineNEYAYLKAI
HHHHHHHHH
14.08Phosphositeplus
Link
303PhosphoserineAKGLSDPGK
CCCCCCHHH
50.88Phosphositeplus
Link
307Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SDPGKIKRL
CCHHHHHHH
50.90Phosphositeplus
Link
307Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).SDPGKIKRL
CCHHHHHHH
50.90UniProtKB
Link
313PhosphoserineKRLRSQVQV
HHHHHHHHH
39.02Phosphositeplus
Link
313Phosphoserine (AMPK_group)KRLRSQVQV
HHHHHHHHH
39.02PhosphoELM
Link
313Phosphoserine (PRKAA2)KRLRSQVQV
HHHHHHHHH
39.02HPRD
Link
313Phosphoserine; by AMPK.KRLRSQVQV
HHHHHHHHH
39.02UniProtKB
Link
318PhosphoserineQVQVSLEDY
HHHHHHHHH
14.67Phosphositeplus
Link
378PhosphoserineLLGGSPSDA
HCCCCCCCC
21.31Phosphositeplus
Link-
432PhosphothreonineATPETPQPS
CCCCCCCCC
28.55Phosphositeplus
Link-
432Phosphothreonine.ATPETPQPS
CCCCCCCCC
28.55UniProtKB
Link-
436PhosphoserineTPQPSPPGG
CCCCCCCCC
38.18Phosphositeplus
Link-
436Phosphoserine.TPQPSPPGG
CCCCCCCCC
38.18UniProtKB
Link-
443PhosphoserineGGSGSEPYK
CCCCCCCCC
36.78Phosphositeplus
Link-
455PhosphothreonineGAVATIVKP
HHHHHHCCC
21.50Phosphositeplus
Link-
458N6-acetyllysineATIVKPLSA
HHHCCCCCC
36.07Phosphositeplus
Link-
458N6-acetyllysine.ATIVKPLSA
HHHCCCCCC
36.07UniProtKB
Link-
469PhosphothreonineQPTITKQEV
CCHHHHHHC
29.20PhosphoELM
Link-
469PhosphothreonineQPTITKQEV
CCHHHHHHC
29.20Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SRBP2_HUMANphysical interactionMINT-16697MINT12855700
SRBP2_HUMANphysical interactionMINT-16696MINT12855700
SYUG_HUMANphysical interactionEBI-1062596
intact17353931
PABP4_HUMANphysical interactionEBI-1063555
intact17353931
STK16_HUMANphysical interactionEBI-1071104
intact17353931
RAD50_HUMANphysical interactionEBI-1071352
intact17353931
EXT2_HUMANphysical interactionEBI-1072755
intact17353931
COT1_HUMANin vitroHPRD:02612HPRD10652338
FOXO1_HUMANin vitroHPRD:02612HPRD12519792
HNF1A_HUMANin vitroHPRD:02612HPRD9792724
P53_HUMANin vitroHPRD:02612HPRD11818510
MED14_HUMANin vitroHPRD:02612HPRD12101254
CBP_HUMANin vitro
yeast 2-hybrid
HPRD:02612HPRD9434765
10085149
HNF4A_HUMANyeast 2-hybridHPRD:02612HPRD9795230
PRGC1_HUMANin vitroHPRD:02612HPRD15826954
NCOA1_HUMANyeast 2-hybridHPRD:02612HPRD9812974
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Disease Reference
Kegg disease
OMIM disease
125850Maturity-onset diabetes of the young 1 (MODY1)
125853Diabetes mellitus, non-insulin-dependent (NIDDM)
616026Fanconi renotubular syndrome 4 with maturity-onset diabetes of the young (FRTS4)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Multiple post-translational modifications in hepatocyte nuclearfactor 4alpha.";
Yokoyama A., Katsura S., Ito R., Hashiba W., Sekine H., Fujiki R.,Kato S.;
Biochem. Biophys. Res. Commun. 410:749-753(2011).
Cited for: PHOSPHORYLATION AT SER-142; THR-166; SER-167; THR-432 AND SER-436,UBIQUITINATION AT LYS-234 AND LYS-307, AND ACETYLATION AT LYS-458.
Phosphorylation
ReferencePubMed
"AMP-activated protein kinase regulates HNF4alpha transcriptionalactivity by inhibiting dimer formation and decreasing proteinstability.";
Hong Y.H., Varanasi U.S., Yang W., Leff T.;
J. Biol. Chem. 278:27495-27501(2003).
Cited for: PHOSPHORYLATION AT SER-313, AND MUTAGENESIS OF SER-313.
"Multiple post-translational modifications in hepatocyte nuclearfactor 4alpha.";
Yokoyama A., Katsura S., Ito R., Hashiba W., Sekine H., Fujiki R.,Kato S.;
Biochem. Biophys. Res. Commun. 410:749-753(2011).
Cited for: PHOSPHORYLATION AT SER-142; THR-166; SER-167; THR-432 AND SER-436,UBIQUITINATION AT LYS-234 AND LYS-307, AND ACETYLATION AT LYS-458.
Ubiquitylation
ReferencePubMed
"Multiple post-translational modifications in hepatocyte nuclearfactor 4alpha.";
Yokoyama A., Katsura S., Ito R., Hashiba W., Sekine H., Fujiki R.,Kato S.;
Biochem. Biophys. Res. Commun. 410:749-753(2011).
Cited for: PHOSPHORYLATION AT SER-142; THR-166; SER-167; THR-432 AND SER-436,UBIQUITINATION AT LYS-234 AND LYS-307, AND ACETYLATION AT LYS-458.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures