FOXK1_MOUSE - dbPTM
FOXK1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXK1_MOUSE
UniProt AC P42128
Protein Name Forkhead box protein K1
Gene Name Foxk1
Organism Mus musculus (Mouse).
Sequence Length 719
Subcellular Localization Nucleus . Cytoplasm . Accumulates in the nucleus upon viral infection.
Protein Description Transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin gene. [PubMed: 8007964 Important regulatory factor of the myogenic progenitor cell population]
Protein Sequence MAEVGEDSGARALLALRSAPCSPVLCAAAAAAAFPATTSPPPPAQPPPGPPALPAEPGPGPVPSTVATATTTAPALVAAAAASVRQSPGPALARLEGREFEFLMRQPSVTIGRNSSQGSVDLSMGLSSFISRRHLQLSFQEPHFYLRCLGKNGVFVDGAFQRRGAPALQLPQQCTFRFPSTAIKIQFTSLYHKEEAPASPLRPLYPQISPLKIHIPEPDLRSLVSPIPSPTGTISVPNSCPASPRGAGSSSYRFVQNVTSDLQLAAEFAAKAASEQQADASGGDSPKDESKPPYSYAQLIVQAISSAQDRQLTLSGIYAHITKHYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPGKGSFWRIDPASEAKLVEQAFRKRRQRGVSCFRTPFGPLSSRSAPASPTHPGLMSPRSSGLQTPECLSREGSPIPHDPDLGSKLASVPEYRYSQSAPGSPVSAQPVIMAVPPRPSNLVAKPVAYMPASIVTSQQPSGHAIHVVQQAPTVTMVRVVTTSANSANGYILASQGSTGTSHDTAGTAVLDLGNEARGLEEKPTIAFATIPAASRVIQTVASQMAPGVPGHTVTILQPATPVTIGQHHLPVRAVTQNGKHAVPTNSLTGNAYALSSPLQLLAAQASSSTPVVITRVCEVGPEEPAAAVSVAANAAPTPAASTTTSASSSGEPEVKRSRVEEPGGTATTQPTAMAATGPQGPGTGE
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
2Acetylation------MAEVGEDSG
------CCCCCCCHH
21.85-
87PhosphorylationAAASVRQSPGPALAR
HHHHHHCCCCCHHHH
22.6626824392
108PhosphorylationEFLMRQPSVTIGRNS
EEEECCCCEEECCCC
24.4529514104
110PhosphorylationLMRQPSVTIGRNSSQ
EECCCCEEECCCCCC
23.2728059163
147MethylationQEPHFYLRCLGKNGV
CCCCEEEEEECCCCE
11.3924129315
177DimethylationLPQQCTFRFPSTAIK
CCCCCEEECCCCEEE
25.14-
177MethylationLPQQCTFRFPSTAIK
CCCCCEEECCCCEEE
25.14-
188PhosphorylationTAIKIQFTSLYHKEE
CEEEEEEEECCCCCC
11.0521183079
189PhosphorylationAIKIQFTSLYHKEEA
EEEEEEEECCCCCCC
28.3723984901
191UbiquitinationKIQFTSLYHKEEAPA
EEEEEECCCCCCCCC
15.6027667366
191PhosphorylationKIQFTSLYHKEEAPA
EEEEEECCCCCCCCC
15.6025266776
199PhosphorylationHKEEAPASPLRPLYP
CCCCCCCCCCCCCCC
24.3327087446
205PhosphorylationASPLRPLYPQISPLK
CCCCCCCCCCCCCCE
8.8625168779
209PhosphorylationRPLYPQISPLKIHIP
CCCCCCCCCCEEECC
20.9425521595
222PhosphorylationIPEPDLRSLVSPIPS
CCCCCHHHHCCCCCC
40.1823527152
225PhosphorylationPDLRSLVSPIPSPTG
CCHHHHCCCCCCCCC
23.5426824392
229PhosphorylationSLVSPIPSPTGTISV
HHCCCCCCCCCCEEC
35.4926824392
231PhosphorylationVSPIPSPTGTISVPN
CCCCCCCCCCEECCC
51.8222942356
233PhosphorylationPIPSPTGTISVPNSC
CCCCCCCCEECCCCC
16.7422942356
235PhosphorylationPSPTGTISVPNSCPA
CCCCCCEECCCCCCC
31.2122942356
239PhosphorylationGTISVPNSCPASPRG
CCEECCCCCCCCCCC
18.5321082442
243PhosphorylationVPNSCPASPRGAGSS
CCCCCCCCCCCCCCC
10.5623527152
249PhosphorylationASPRGAGSSSYRFVQ
CCCCCCCCCCEECCC
18.6423984901
250PhosphorylationSPRGAGSSSYRFVQN
CCCCCCCCCEECCCH
30.3923984901
251PhosphorylationPRGAGSSSYRFVQNV
CCCCCCCCEECCCHH
23.2523984901
252PhosphorylationRGAGSSSYRFVQNVT
CCCCCCCEECCCHHC
15.2623984901
274PhosphorylationEFAAKAASEQQADAS
HHHHHHHHHHHHHCC
40.5826160508
281PhosphorylationSEQQADASGGDSPKD
HHHHHHCCCCCCCCC
43.8025521595
285PhosphorylationADASGGDSPKDESKP
HHCCCCCCCCCCCCC
36.8025521595
290PhosphorylationGDSPKDESKPPYSYA
CCCCCCCCCCCCCHH
61.6726160508
294PhosphorylationKDESKPPYSYAQLIV
CCCCCCCCCHHHHHH
23.8821659605
295PhosphorylationDESKPPYSYAQLIVQ
CCCCCCCCHHHHHHH
21.5526160508
296PhosphorylationESKPPYSYAQLIVQA
CCCCCCCHHHHHHHH
7.7926160508
305PhosphorylationQLIVQAISSAQDRQL
HHHHHHHHCHHHHEE
23.7223984901
306PhosphorylationLIVQAISSAQDRQLT
HHHHHHHCHHHHEEE
24.6823984901
344PhosphorylationNSIRHNLSLNRYFIK
HHHHHCCEECCEEEE
28.9919854140
361UbiquitinationRSQEEPGKGSFWRID
CCCCCCCCCCCEECC
63.2027667366
361AcetylationRSQEEPGKGSFWRID
CCCCCCCCCCCEECC
63.2023806337
363PhosphorylationQEEPGKGSFWRIDPA
CCCCCCCCCEECCHH
25.7323684622
374UbiquitinationIDPASEAKLVEQAFR
CCHHHHHHHHHHHHH
49.3522790023
389PhosphorylationKRRQRGVSCFRTPFG
HHHHHCCCCCCCCCC
15.4629514104
393PhosphorylationRGVSCFRTPFGPLSS
HCCCCCCCCCCCCCC
11.6126643407
399PhosphorylationRTPFGPLSSRSAPAS
CCCCCCCCCCCCCCC
27.1725266776
400PhosphorylationTPFGPLSSRSAPASP
CCCCCCCCCCCCCCC
37.6325266776
402PhosphorylationFGPLSSRSAPASPTH
CCCCCCCCCCCCCCC
40.3227087446
406PhosphorylationSSRSAPASPTHPGLM
CCCCCCCCCCCCCCC
29.3127087446
408PhosphorylationRSAPASPTHPGLMSP
CCCCCCCCCCCCCCC
37.9025521595
414PhosphorylationPTHPGLMSPRSSGLQ
CCCCCCCCCCCCCCC
23.3927087446
417PhosphorylationPGLMSPRSSGLQTPE
CCCCCCCCCCCCCHH
31.9425619855
418PhosphorylationGLMSPRSSGLQTPEC
CCCCCCCCCCCCHHH
44.8121082442
422PhosphorylationPRSSGLQTPECLSRE
CCCCCCCCHHHHCCC
26.5425521595
427PhosphorylationLQTPECLSREGSPIP
CCCHHHHCCCCCCCC
39.6925521595
431PhosphorylationECLSREGSPIPHDPD
HHHCCCCCCCCCCCC
18.2027087446
441PhosphorylationPHDPDLGSKLASVPE
CCCCCHHHHHCCCCC
31.6225619855
445PhosphorylationDLGSKLASVPEYRYS
CHHHHHCCCCCCCCC
48.9526643407
449PhosphorylationKLASVPEYRYSQSAP
HHCCCCCCCCCCCCC
14.5826643407
451PhosphorylationASVPEYRYSQSAPGS
CCCCCCCCCCCCCCC
15.3426643407
452PhosphorylationSVPEYRYSQSAPGSP
CCCCCCCCCCCCCCC
14.5225266776
454PhosphorylationPEYRYSQSAPGSPVS
CCCCCCCCCCCCCCC
30.4125266776
458PhosphorylationYSQSAPGSPVSAQPV
CCCCCCCCCCCCCCE
22.5225266776
461PhosphorylationSAPGSPVSAQPVIMA
CCCCCCCCCCCEEEE
25.2725293948
618PhosphorylationNGKHAVPTNSLTGNA
CCCCCCCCCCCCCCE
30.7323984901
620PhosphorylationKHAVPTNSLTGNAYA
CCCCCCCCCCCCEEH
29.7723984901
622PhosphorylationAVPTNSLTGNAYALS
CCCCCCCCCCEEHHC
28.3623984901
626PhosphorylationNSLTGNAYALSSPLQ
CCCCCCEEHHCCHHH
16.4523984901
629PhosphorylationTGNAYALSSPLQLLA
CCCEEHHCCHHHHHH
23.0323984901
630PhosphorylationGNAYALSSPLQLLAA
CCEEHHCCHHHHHHH
30.4023984901
640PhosphorylationQLLAAQASSSTPVVI
HHHHHHCCCCCCEEE
16.8523984901
641PhosphorylationLLAAQASSSTPVVIT
HHHHHCCCCCCEEEE
41.0423984901
642PhosphorylationLAAQASSSTPVVITR
HHHHCCCCCCEEEEE
33.9523984901
643PhosphorylationAAQASSSTPVVITRV
HHHCCCCCCEEEEEE
23.2723984901
663O-linked_GlycosylationEEPAAAVSVAANAAP
CCCCHHHHHHHCCCC
11.0022517741

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
427SPhosphorylationKinaseMTORQ9JLN9
PSP
431SPhosphorylationKinaseMTORQ9JLN9
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOXK1_MOUSE !!

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 FOXK1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FOXK1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOXK1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASSSPECTROMETRY.
"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 SER-199; SER-402; SER-406;SER-414 AND THR-422, AND MASS SPECTROMETRY.

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