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Protein

Forkhead box protein K2

Gene

FOXK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi310 – 3101Magnesium; via carbonyl oxygen
Metal bindingi311 – 3111Magnesium; via carbonyl oxygen
Metal bindingi313 – 3131Magnesium; via carbonyl oxygen
Metal bindingi316 – 3161Magnesium; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi258 – 35396Fork-headPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  4. sequence-specific DNA binding Source: UniProtKB
  5. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  2. regulation of transcription, DNA-templated Source: UniProtKB
  3. regulation of transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein K2
Alternative name(s):
Cellular transcription factor ILF-1
FOXK1
Interleukin enhancer-binding factor 1
Gene namesi
Name:FOXK2
Synonyms:ILF, ILF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6036. FOXK2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. nucleoplasm Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi258 – 2581K → A: Decreases DNA-binding to 40%. 1 Publication
Mutagenesisi300 – 3001K → A: Decreases DNA-binding to 20%. 1 Publication
Mutagenesisi305 – 3051S → A: Decreases DNA-binding to 70%. 1 Publication
Mutagenesisi307 – 3071R → A: Abolishes DNA-binding. 1 Publication
Mutagenesisi328 – 3281K → A: Decreases DNA-binding to 25%. 1 Publication

Organism-specific databases

PharmGKBiPA29851.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 660659Forkhead box protein K2PRO_0000091858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei30 – 301Phosphoserine1 Publication
Modified residuei239 – 2391Phosphoserine1 Publication
Modified residuei398 – 3981Phosphoserine4 Publications
Modified residuei424 – 4241Phosphoserine1 Publication
Modified residuei428 – 4281Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ01167.
PaxDbiQ01167.
PRIDEiQ01167.

PTM databases

PhosphoSiteiQ01167.

Expressioni

Tissue specificityi

Expressed in both lymphoid and non-lymphoid cells.1 Publication

Gene expression databases

BgeeiQ01167.
CleanExiHS_FOXK2.
ExpressionAtlasiQ01167. baseline and differential.
GenevestigatoriQ01167.

Organism-specific databases

HPAiHPA027523.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
IRF2P143162EBI-2509991,EBI-2866589

Protein-protein interaction databases

BioGridi109820. 10 interactions.
IntActiQ01167. 9 interactions.
MINTiMINT-1522265.
STRINGi9606.ENSP00000335677.

Structurei

Secondary structure

1
660
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi263 – 27210Combined sources
Beta strandi277 – 2793Combined sources
Helixi281 – 29111Combined sources
Beta strandi295 – 2984Combined sources
Helixi300 – 31213Combined sources
Beta strandi316 – 3194Combined sources
Beta strandi324 – 3296Combined sources
Beta strandi331 – 3344Combined sources
Helixi336 – 34611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXSNMR-A256-353[»]
2C6YX-ray2.40A/B256-353[»]
ProteinModelPortaliQ01167.
SMRiQ01167. Positions 256-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01167.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 12875FHAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni300 – 31819DNA-binding; major grooveAdd
BLAST
Regioni328 – 3325DNA-binding; minor groove
Regioni348 – 3536DNA-binding; minor groove

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 9384Gly-richAdd
BLAST

Domaini

The C-terminal part of the DNA-binding domain may contribute to DNA recognition specificity.1 Publication

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation
Contains 1 fork-head DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00780000121840.
HOGENOMiHOG000072588.
HOVERGENiHBG051649.
InParanoidiQ01167.
KOiK09404.
OMAiMADNSQS.
OrthoDBiEOG7CRTS2.
PhylomeDBiQ01167.
TreeFamiTF325718.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS_1.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
PF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
SM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q01167-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAAAAALSG AGTPPAGGGA GGGGAGGGGS PPGGWAVARL EGREFEYLMK
60 70 80 90 100
KRSVTIGRNS SQGSVDVSMG HSSFISRRHL EIFTPPGGGG HGGAAPELPP
110 120 130 140 150
AQPRPDAGGD FYLRCLGKNG VFVDGVFQRR GAPPLQLPRV CTFRFPSTNI
160 170 180 190 200
KITFTALSSE KREKQEASES PVKAVQPHIS PLTINIPDTM AHLISPLPSP
210 220 230 240 250
TGTISAANSC PSSPRGAGSS GYKVGRVMPS DLNLMADNSQ PENEKEASGG
260 270 280 290 300
DSPKDDSKPP YSYAQLIVQA ITMAPDKQLT LNGIYTHITK NYPYYRTADK
310 320 330 340 350
GWQNSIRHNL SLNRYFIKVP RSQEEPGKGS FWRIDPASES KLIEQAFRKR
360 370 380 390 400
RPRGVPCFRT PLGPLSSRSA PASPNHAGVL SAHSSGAQTP ESLSREGSPA
410 420 430 440 450
PLEPEPGAAQ PKLAVIQEAR FAQSAPGSPL SSQPVLITVQ RQLPQAIKPV
460 470 480 490 500
TYTVATPVTT STSQPPVVQT VHVVHQIPAV SVTSVAGLAP ANTYTVSGQA
510 520 530 540 550
VVTPAAVLAP PKAEAQENGD HREVKVKVEP IPAIGHATLG TASRIIQTAQ
560 570 580 590 600
TTPVQTVTIV QQAPLGQHQL PIKTVTQNGT HVASVPTAVH GQVNNAAASP
610 620 630 640 650
LHMLATHASA SASLPTKRHN GDQPEQPELK RIKTEDGEGI VIALSVDTPP
660
AAVREKGVQN
Length:660
Mass (Da):69,062
Last modified:November 27, 2006 - v3
Checksum:iE11C0B24370F1260
GO
Isoform 2 (identifier: Q01167-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     596-660: AAASPLHMLA...AAVREKGVQN → GPLGLRRPPCASSDWSCLS

Show »
Length:614
Mass (Da):64,256
Checksum:iF5BE52BA84587655
GO
Isoform 3 (identifier: Q01167-3) [UniParc]FASTAAdd to basket

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

Show »
Length:328
Mass (Da):34,325
Checksum:i4FCFB7F9FA67C9CA
GO

Sequence cautioni

The sequence AAB02820.1 differs from that shown.The N-terminal sequence differs due to frameshifts and sequencing errors.Curated
The sequence AAB02821.1 differs from that shown.The N-terminal sequence differs due to frameshifts and sequencing errors.Curated
The sequence AAB02822.1 differs from that shown.The N-terminal sequence differs due to frameshifts and sequencing errors.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 120118AAAAA…LGKNG → Q in CAA43200 (PubMed:1909027).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei304 – 32825NSIRH…EEPGK → RGESFAHVGNTRIRIGLPAH KAPQR in isoform 3. CuratedVSP_001560Add
BLAST
Alternative sequencei329 – 660332Missing in isoform 3. CuratedVSP_001561Add
BLAST
Alternative sequencei596 – 66065AAASP…KGVQN → GPLGLRRPPCASSDWSCLS in isoform 2. 1 PublicationVSP_001559Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11813.1. [Q01167-1]
PIRiA41285.
RefSeqiNP_004505.2. NM_004514.3. [Q01167-1]
UniGeneiHs.591140.

Genome annotation databases

EnsembliENST00000335255; ENSP00000335677; ENSG00000141568. [Q01167-1]
ENST00000473637; ENSP00000436108; ENSG00000141568. [Q01167-2]
GeneIDi3607.
KEGGihsa:3607.
UCSCiuc002kfm.1. human. [Q01167-2]
uc002kfn.3. human. [Q01167-1]
uc010diu.3. human. [Q01167-3]

Polymorphism databases

DMDMi118572648.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11813.1. [Q01167-1]
PIRiA41285.
RefSeqiNP_004505.2. NM_004514.3. [Q01167-1]
UniGeneiHs.591140.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXSNMR-A256-353[»]
2C6YX-ray2.40A/B256-353[»]
ProteinModelPortaliQ01167.
SMRiQ01167. Positions 256-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109820. 10 interactions.
IntActiQ01167. 9 interactions.
MINTiMINT-1522265.
STRINGi9606.ENSP00000335677.

PTM databases

PhosphoSiteiQ01167.

Polymorphism databases

DMDMi118572648.

Proteomic databases

MaxQBiQ01167.
PaxDbiQ01167.
PRIDEiQ01167.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335255; ENSP00000335677; ENSG00000141568. [Q01167-1]
ENST00000473637; ENSP00000436108; ENSG00000141568. [Q01167-2]
GeneIDi3607.
KEGGihsa:3607.
UCSCiuc002kfm.1. human. [Q01167-2]
uc002kfn.3. human. [Q01167-1]
uc010diu.3. human. [Q01167-3]

Organism-specific databases

CTDi3607.
GeneCardsiGC17P080477.
H-InvDBHIX0014279.
HGNCiHGNC:6036. FOXK2.
HPAiHPA027523.
MIMi147685. gene.
neXtProtiNX_Q01167.
PharmGKBiPA29851.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00780000121840.
HOGENOMiHOG000072588.
HOVERGENiHBG051649.
InParanoidiQ01167.
KOiK09404.
OMAiMADNSQS.
OrthoDBiEOG7CRTS2.
PhylomeDBiQ01167.
TreeFamiTF325718.

Miscellaneous databases

ChiTaRSiFOXK2. human.
EvolutionaryTraceiQ01167.
GeneWikiiFOXK2.
GenomeRNAii3607.
NextBioi14097.
PROiQ01167.
SOURCEiSearch...

Gene expression databases

BgeeiQ01167.
CleanExiHS_FOXK2.
ExpressionAtlasiQ01167. baseline and differential.
GenevestigatoriQ01167.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS_1.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
PF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
SM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1990) [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(1991) [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 (APR-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.
    , 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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. 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(2008) [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(2008) [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(2009) [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], CLEAVAGE OF INITIATOR METHIONINE [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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 256-353 (ISOFORM 1), DNA-BINDING.
  14. "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(2005) [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.

Entry informationi

Entry nameiFOXK2_HUMAN
AccessioniPrimary (citable) accession number: Q01167
Secondary accession number(s): A6NEP5
, Q13622, Q13623, Q13624
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1993
Last sequence update: November 27, 2006
Last modified: March 31, 2015
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.