Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Forkhead box protein K2  

UniProtKB / Swiss-Prot ID :  FOXK2_HUMAN

Gene Name (Synonyms) : 
FOXK2, ILF, ILF1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (Probable). 

Protein Function :  Recognizes the core sequence 5'-TAAACA-3'. Binds to NFAT-like motifs (purine-rich) in the IL2 promoter. Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements. 

Protein Sequence MAAAAAALSGAGTPPAGGGAGGGGAGGGGSPPGGWAVARLEGREFEYLMKKRSVTIGRNSSQGSVDVSMG...
Predicted Secondary Structure CCCCCCHHCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEEECCEEEEEEEEEEEEEEECCCCCCEEEEEC...
Protein Variant -
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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
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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
2N-acetylalanine.---MAAAAA
---CCCCCC
13.05UniProtKB
Link-
13PhosphothreonineSGAGTPPAG
CCCCCCCCC
26.09HPRD
Link-
13PhosphothreonineSGAGTPPAG
CCCCCCCCC
26.09Phosphositeplus
Link-
13Phosphothreonine.SGAGTPPAG
CCCCCCCCC
26.09UniProtKB
Link-
30PhosphoserineGGGGSPPGG
CCCCCCCCC
31.06HPRD
Link-
30PhosphoserineGGGGSPPGG
CCCCCCCCC
31.06Phosphositeplus
Link-
30Phosphoserine.GGGGSPPGG
CCCCCCCCC
31.06UniProtKB
Link-
61PhosphoserineGRNSSQGSV
EECCCCCCE
41.95HPRD
Link-
61PhosphoserineGRNSSQGSV
EECCCCCCE
41.95PhosphoELM
Link-
61PhosphoserineGRNSSQGSV
EECCCCCCE
41.95Phosphositeplus
Link-
61Phosphoserine.GRNSSQGSV
EECCCCCCE
41.95UniProtKB
Link-
170PhosphoserineEASESPVKA
CCCCCCCCC
32.28HPRD
Link-
170PhosphoserineEASESPVKA
CCCCCCCCC
32.28Phosphositeplus
Link-
180PhosphoserineQPHISPLTI
CCCCCCCCC
15.72HPRD
Link-
183PhosphothreonineISPLTINIP
CCCCCCCCC
18.50HPRD
Link-
201PhosphothreonineLPSPTGTIS
CCCCCCCCC
51.82HPRD
Link-
205PhosphoserineTGTISAANS
CCCCCCCCC
22.59HPRD
Link-
209PhosphoserineSAANSCPSS
CCCCCCCCC
23.76HPRD
Link-
222PhosphotyrosineGSSGYKVGR
CCCCCCCCC
12.40HPRD
Link-
239PhosphoserineMADNSQPEN
CCCCCCCCC
47.89HPRD
Link-
239PhosphoserineMADNSQPEN
CCCCCCCCC
47.89PhosphoELM
Link-
239PhosphoserineMADNSQPEN
CCCCCCCCC
47.89Phosphositeplus
Link-
239Phosphoserine.MADNSQPEN
CCCCCCCCC
47.89UniProtKB
Link-
369PhosphoserineLSSRSAPAS
CCCCCCCCC
40.32Phosphositeplus
Link-
373PhosphoserineSAPASPNHA
CCCCCCCCC
25.77HPRD
Link-
373PhosphoserineSAPASPNHA
CCCCCCCCC
25.77PhosphoELM
Link-
373PhosphoserineSAPASPNHA
CCCCCCCCC
25.77Phosphositeplus
Link-
384PhosphoserineLSAHSSGAQ
CCCCCCCCC
30.13Phosphositeplus
Link-
389PhosphothreonineSGAQTPESL
CCCCCCCCC
28.61HPRD
Link-
389PhosphothreonineSGAQTPESL
CCCCCCCCC
28.61PhosphoELM
Link-
389PhosphothreonineSGAQTPESL
CCCCCCCCC
28.61Phosphositeplus
Link-
394PhosphoserinePESLSREGS
CCCCCCCCC
37.25HPRD
Link-
394PhosphoserinePESLSREGS
CCCCCCCCC
37.25PhosphoELM
Link-
394PhosphoserinePESLSREGS
CCCCCCCCC
37.25Phosphositeplus
Link-
398PhosphoserineSREGSPAPL
CCCCCCCCC
17.09HPRD
Link-
398PhosphoserineSREGSPAPL
CCCCCCCCC
17.09PhosphoELM
Link-
398PhosphoserineSREGSPAPL
CCCCCCCCC
17.09Phosphositeplus
Link-
398PhosphoserineSREGSPAPL
CCCCCCCCC
17.09SysPTM
Link-
398Phosphoserine.SREGSPAPL
CCCCCCCCC
17.09UniProtKB
Link-
424PhosphoserineRFAQSAPGS
CCCCCCCCC
32.76HPRD
Link-
424PhosphoserineRFAQSAPGS
CCCCCCCCC
32.76Phosphositeplus
Link-
428PhosphoserineSAPGSPLSS
CCCCCCCCC
22.93HPRD
Link-
428PhosphoserineSAPGSPLSS
CCCCCCCCC
22.93PhosphoELM
Link-
428PhosphoserineSAPGSPLSS
CCCCCCCCC
22.93Phosphositeplus
Link-
428Phosphoserine.SAPGSPLSS
CCCCCCCCC
22.93UniProtKB
Link-
634PhosphothreonineKRIKTEDGE
EEECCCCCC
36.62Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IL2_HUMANphysical interactionMINT-14832MINT9065434
IL2_HUMANin vitroHPRD:00982HPRD9065434
IL2_HUMANENSP00000335677STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-13; SER-30; SER-398 AND SER-428, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-13; SER-30; SER-398 AND SER-428, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-239, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures