Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q01167 (FOXK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Forkhead box protein K2
Alternative name(s):
Cellular transcription factor ILF-1
FOXK1
Interleukin enhancer-binding factor 1
Gene names
Name:FOXK2
Synonyms:ILF, ILF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2

Cofactor

Binds 1 magnesium ion per subunit. Ref.13

Subcellular location

Nucleus Probable.

Tissue specificity

Expressed in both lymphoid and non-lymphoid cells. Ref.2

Domain

The C-terminal part of the DNA-binding domain may contribute to DNA recognition specificity. Ref.13

Sequence similarities

Contains 1 FHA domain.

Contains 1 fork-head DNA-binding domain.

Sequence caution

The sequence AAB02820.1 differs from that shown. Reason: The N-terminal sequence differs due to frameshifts and sequencing errors.

The sequence AAB02821.1 differs from that shown. Reason: The N-terminal sequence differs due to frameshifts and sequencing errors.

The sequence AAB02822.1 differs from that shown. Reason: The N-terminal sequence differs due to frameshifts and sequencing errors.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IRF2P143162EBI-2509991,EBI-2866589

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01167-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q01167-2)

The sequence of this isoform differs from the canonical sequence as follows:
     596-660: AAASPLHMLA...AAVREKGVQN → GPLGLRRPPCASSDWSCLS
Isoform 3 (identifier: Q01167-3)

The sequence of this isoform differs from the canonical sequence as follows:
     304-328: NSIRHNLSLNRYFIKVPRSQEEPGK → RGESFAHVGNTRIRIGLPAHKAPQR
     329-660: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 660659Forkhead box protein K2
PRO_0000091858

Regions

Domain54 – 12875FHA
DNA binding258 – 35396Fork-head Ref.12 Ref.13
Region300 – 31819DNA-binding; major groove
Region328 – 3325DNA-binding; minor groove
Region348 – 3536DNA-binding; minor groove
Compositional bias10 – 9384Gly-rich

Sites

Metal binding3101Magnesium; via carbonyl oxygen
Metal binding3111Magnesium; via carbonyl oxygen
Metal binding3131Magnesium; via carbonyl oxygen
Metal binding3161Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.10
Modified residue301Phosphoserine Ref.10
Modified residue2391Phosphoserine Ref.5
Modified residue3981Phosphoserine Ref.9 Ref.10 Ref.11
Modified residue4241Phosphoserine Ref.10
Modified residue4281Phosphoserine Ref.6 Ref.9 Ref.10

Natural variations

Alternative sequence304 – 32825NSIRH…EEPGK → RGESFAHVGNTRIRIGLPAH KAPQR in isoform 3.
VSP_001560
Alternative sequence329 – 660332Missing in isoform 3.
VSP_001561
Alternative sequence596 – 66065AAASP…KGVQN → GPLGLRRPPCASSDWSCLS in isoform 2.
VSP_001559

Experimental info

Mutagenesis2581K → A: Decreases DNA-binding to 40%. Ref.13
Mutagenesis3001K → A: Decreases DNA-binding to 20%. Ref.13
Mutagenesis3051S → A: Decreases DNA-binding to 70%. Ref.13
Mutagenesis3071R → A: Abolishes DNA-binding. Ref.13
Mutagenesis3281K → A: Decreases DNA-binding to 25%. Ref.13
Sequence conflict3 – 120118AAAAA…LGKNG → Q in CAA43200. Ref.1

Secondary structure

................... 660
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 3.
Checksum: E11C0B24370F1260

FASTA66069,062
        10         20         30         40         50         60 
MAAAAAALSG AGTPPAGGGA GGGGAGGGGS PPGGWAVARL EGREFEYLMK KRSVTIGRNS 

        70         80         90        100        110        120 
SQGSVDVSMG HSSFISRRHL EIFTPPGGGG HGGAAPELPP AQPRPDAGGD FYLRCLGKNG 

       130        140        150        160        170        180 
VFVDGVFQRR GAPPLQLPRV CTFRFPSTNI KITFTALSSE KREKQEASES PVKAVQPHIS 

       190        200        210        220        230        240 
PLTINIPDTM AHLISPLPSP TGTISAANSC PSSPRGAGSS GYKVGRVMPS DLNLMADNSQ 

       250        260        270        280        290        300 
PENEKEASGG DSPKDDSKPP YSYAQLIVQA ITMAPDKQLT LNGIYTHITK NYPYYRTADK 

       310        320        330        340        350        360 
GWQNSIRHNL SLNRYFIKVP RSQEEPGKGS FWRIDPASES KLIEQAFRKR RPRGVPCFRT 

       370        380        390        400        410        420 
PLGPLSSRSA PASPNHAGVL SAHSSGAQTP ESLSREGSPA PLEPEPGAAQ PKLAVIQEAR 

       430        440        450        460        470        480 
FAQSAPGSPL SSQPVLITVQ RQLPQAIKPV TYTVATPVTT STSQPPVVQT VHVVHQIPAV 

       490        500        510        520        530        540 
SVTSVAGLAP ANTYTVSGQA VVTPAAVLAP PKAEAQENGD HREVKVKVEP IPAIGHATLG 

       550        560        570        580        590        600 
TASRIIQTAQ TTPVQTVTIV QQAPLGQHQL PIKTVTQNGT HVASVPTAVH GQVNNAAASP 

       610        620        630        640        650        660 
LHMLATHASA SASLPTKRHN GDQPEQPELK RIKTEDGEGI VIALSVDTPP AAVREKGVQN 

« Hide

Isoform 2 [UniParc].

Checksum: F5BE52BA84587655
Show »

FASTA61464,256
Isoform 3 [UniParc].

Checksum: 4FCFB7F9FA67C9CA
Show »

FASTA32834,325

References

« Hide 'large scale' references
[1]"Cloning of a cellular factor, interleukin binding factor, that binds to NFAT-like motifs in the human immunodeficiency virus long terminal repeat."
Li C., Lai C., Sigman D.S., Gaynor R.B.
Proc. Natl. Acad. Sci. U.S.A. 88:7739-7743(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
Tissue: Cervix carcinoma.
[2]"Characterization and chromosomal mapping of the gene encoding the cellular DNA binding protein ILF."
Li C., Lusis A.J., Sparkes R., Nirula A., Gaynor R.B.
Genomics 13:665-671(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma and Lymphoid tissue.
[3]Nirula A., Moore D.J., Li C., Gaynor R.B.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION (ISOFORMS 1; 2 AND 3).
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"ATM and ATR substrate analysis reveals extensive protein networks responsive 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[6]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-398; SER-424 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a)."
Liu P.-P., Chen Y.-C., Li C., Hsieh Y.-H., Chen S.-W., Chen S.-H., Jeng W.-Y., Chuang W.-J.
Proteins 49:543-553(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 256-353 (ISOFORM 1), DNA-BINDING.
[13]"Crystal structure of the human FOXK1a-DNA complex and its implications on the diverse binding specificity of winged helix/forkhead proteins."
Tsai K.-L., Huang C.-Y., Chang C.-H., Sun Y.-J., Chuang W.-J., Hsiao C.-D.
J. Biol. Chem. 281:17400-17409(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 256-353 (ISOFORM 1) IN COMPLEX WITH MAGNESIUM AND DUPLEX DNA, DNA-BINDING, COFACTOR, DOMAIN, MUTAGENESIS OF LYS-258; LYS-300; SER-305; ARG-307 AND LYS-328.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60787 mRNA. Translation: CAA43200.1.
U58196 mRNA. Translation: AAB02820.1. Sequence problems.
U58197 mRNA. Translation: AAB02821.1. Sequence problems.
U58198 mRNA. Translation: AAB02822.1. Sequence problems.
AC124287 Genomic DNA. No translation available.
CCDSCCDS11813.1. [Q01167-1]
PIRA41285.
RefSeqNP_004505.2. NM_004514.3. [Q01167-1]
UniGeneHs.591140.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXSNMR-A256-353[»]
2C6YX-ray2.40A/B256-353[»]
ProteinModelPortalQ01167.
SMRQ01167. Positions 256-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109820. 7 interactions.
IntActQ01167. 9 interactions.
MINTMINT-1522265.
STRING9606.ENSP00000335677.

PTM databases

PhosphoSiteQ01167.

Polymorphism databases

DMDM118572648.

Proteomic databases

MaxQBQ01167.
PaxDbQ01167.
PRIDEQ01167.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335255; ENSP00000335677; ENSG00000141568. [Q01167-1]
ENST00000473637; ENSP00000436108; ENSG00000141568. [Q01167-2]
GeneID3607.
KEGGhsa:3607.
UCSCuc002kfm.1. human. [Q01167-2]
uc002kfn.3. human. [Q01167-1]
uc010diu.3. human. [Q01167-3]

Organism-specific databases

CTD3607.
GeneCardsGC17P080477.
H-InvDBHIX0014279.
HGNCHGNC:6036. FOXK2.
HPAHPA027523.
MIM147685. gene.
neXtProtNX_Q01167.
PharmGKBPA29851.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5025.
HOGENOMHOG000072588.
HOVERGENHBG051649.
InParanoidQ01167.
KOK09404.
OMAHGQVNNA.
OrthoDBEOG7CRTS2.
PhylomeDBQ01167.
TreeFamTF325718.

Gene expression databases

ArrayExpressQ01167.
BgeeQ01167.
CleanExHS_FOXK2.
GenevestigatorQ01167.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.60.200.20. 1 hit.
InterProIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00498. FHA. 1 hit.
PF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSPR00053. FORKHEAD.
SMARTSM00339. FH. 1 hit.
SM00240. FHA. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
PS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFOXK2. human.
EvolutionaryTraceQ01167.
GeneWikiFOXK2.
GenomeRNAi3607.
NextBio14097.
PROQ01167.
SOURCESearch...

Entry information

Entry nameFOXK2_HUMAN
AccessionPrimary (citable) accession number: Q01167
Secondary accession number(s): A6NEP5 expand/collapse secondary AC list , Q13622, Q13623, Q13624
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM