HNF4A_MOUSE - dbPTM
HNF4A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNF4A_MOUSE
UniProt AC P49698
Protein Name Hepatocyte nuclear factor 4-alpha
Gene Name Hnf4a
Organism Mus musculus (Mouse).
Sequence Length 474
Subcellular Localization Nucleus.
Protein Description 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 MRLSKTLAGMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGANLNSSNSLGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFSRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINALLQAEVLSQQITSPISGINGDIRAKKIANITDVCESMKEQLLVLVEWAKYIPAFCELLLDDQVALLRAHAGEHLLLGATKRSMVFKDVLLLGNDYIVPRHCPELAEMSRVSIRILDELVLPFQELQIDDNEYACLKAIIFFDPDAKGLSDPGKIKRLRSQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFIKLFGMAKIDNLLQEMLLGGSASDAPHTHHPLHPHLMQEHMGTNVIVANTMPSHLSNGQMCEWPRPRGQAATPETPQPSPPSGSGSESYKLLPGAITTIVKPPSAIPQPTITKQEAI
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
139PhosphorylationNERDRISTRRSSYED
CHHHHHHHCHHHCCC
27.94-
142PhosphorylationDRISTRRSSYEDSSL
HHHHHCHHHCCCCCC
33.7022817900
143PhosphorylationRISTRRSSYEDSSLP
HHHHCHHHCCCCCCH
30.6322817900
144PhosphorylationISTRRSSYEDSSLPS
HHHCHHHCCCCCCHH
25.63-
147PhosphorylationRRSSYEDSSLPSINA
CHHHCCCCCCHHHHH
23.1023984901
148PhosphorylationRSSYEDSSLPSINAL
HHHCCCCCCHHHHHH
57.5323984901
151PhosphorylationYEDSSLPSINALLQA
CCCCCCHHHHHHHHH
33.4923984901
162PhosphorylationLLQAEVLSQQITSPI
HHHHHHHHHHCCCCC
25.8023984901
166PhosphorylationEVLSQQITSPISGIN
HHHHHHCCCCCCCCC
24.9023984901
167PhosphorylationVLSQQITSPISGING
HHHHHCCCCCCCCCC
23.1222817900
170PhosphorylationQQITSPISGINGDIR
HHCCCCCCCCCCCHH
36.6823984901
180UbiquitinationNGDIRAKKIANITDV
CCCHHHHHHHCHHHH
46.1722790023
188S-palmitoylationIANITDVCESMKEQL
HHCHHHHHHHHHHHH
3.4028526873
234UbiquitinationHLLLGATKRSMVFKD
HHHHCCHHHHHHHHC
41.7722790023
300UbiquitinationIFFDPDAKGLSDPGK
EEECCCCCCCCCHHH
68.7022790023
313PhosphorylationGKIKRLRSQVQVSLE
HHHHHHHHHEEEEHH
39.02-
429PhosphorylationRPRGQAATPETPQPS
CCCCCCCCCCCCCCC
25.3625521595
432PhosphorylationGQAATPETPQPSPPS
CCCCCCCCCCCCCCC
28.5525521595
436PhosphorylationTPETPQPSPPSGSGS
CCCCCCCCCCCCCCC
44.1725521595
439PhosphorylationTPQPSPPSGSGSESY
CCCCCCCCCCCCCCE
49.3119060867
441PhosphorylationQPSPPSGSGSESYKL
CCCCCCCCCCCCEEE
43.4119060867
443PhosphorylationSPPSGSGSESYKLLP
CCCCCCCCCCEEECC
25.6825521595
445PhosphorylationPSGSGSESYKLLPGA
CCCCCCCCEEECCCC
29.3023984901
446PhosphorylationSGSGSESYKLLPGAI
CCCCCCCEEECCCCE
11.1223984901
458AcetylationGAITTIVKPPSAIPQ
CCEEEEECCCCCCCC
47.57-

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
143SPhosphorylationKinasePKACAP17612
PSP
143SPhosphorylationKinasePRKACAP05132
GPS
313SPhosphorylationKinaseAMPK-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
313SPhosphorylation

-
458KAcetylation

-

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 HNF4A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF7L2_MOUSETcf7l2physical
19805521
NR0B1_MOUSENr0b1physical
19651776

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNF4A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429 AND THR-432, ANDMASS SPECTROMETRY.

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