Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Forkhead box protein K1

Gene

Foxk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin gene. Has a role in myogenic differentiation and in remodeling processes of adult muscles that occur in response to physiological stimuli.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi291 – 38696Fork-headPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • sequence-specific DNA binding Source: UniProtKB
  • sequence-specific DNA binding RNA polymerase II transcription factor activity Source: NTNU_SB

GO - Biological processi

  • anatomical structure morphogenesis Source: GO_Central
  • cell differentiation Source: GO_Central
  • muscle organ development Source: UniProtKB-KW
  • negative regulation of cell cycle Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Repressor

Keywords - Biological processi

Differentiation, Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein K1
Alternative name(s):
Myocyte nuclear factor
Short name:
MNF
Gene namesi
Name:Foxk1
Synonyms:Mnf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1347488. Foxk1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 719718Forkhead box protein K1PRO_0000091857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei225 – 2251PhosphoserineBy similarity
Modified residuei229 – 2291PhosphoserineBy similarity
Modified residuei239 – 2391PhosphoserineBy similarity
Modified residuei243 – 2431PhosphoserineBy similarity
Modified residuei422 – 4221Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP42128.
PaxDbiP42128.
PRIDEiP42128.

PTM databases

PhosphoSiteiP42128.

Expressioni

Tissue specificityi

Expressed in tissues and cells in which the myoglobin gene is transcriptionally active including cardiac and skeletal myocytes, brain and kidney. In the adult brain, expressed in the piriform cortex and the indusium griseum. In the hippocampus, expression is localized to the dentate gyrus and CA3 area. In the cerebellum, expression is confined to the Purkinje cell layer.3 Publications

Gene expression databases

BgeeiP42128.
CleanExiMM_FOXK1.
GenevestigatoriP42128.

Interactioni

Subunit structurei

Interacts with SIN3B to form a complex which represses transcription.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Sin3bQ62141-211EBI-878270,EBI-591466

Protein-protein interaction databases

IntActiP42128. 2 interactions.
MINTiMINT-4095257.

Structurei

Secondary structure

1
719
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi292 – 2943Combined sources
Helixi298 – 3047Combined sources
Beta strandi307 – 3126Combined sources
Helixi314 – 32411Combined sources
Beta strandi326 – 3305Combined sources
Helixi335 – 34511Combined sources
Beta strandi347 – 35610Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi365 – 3673Combined sources
Helixi372 – 3809Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A3SNMR-A289-389[»]
2D2WNMR-A289-389[»]
ProteinModelPortaliP42128.
SMRiP42128. Positions 289-389.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42128.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 16153FHAPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 8273Ala-richAdd
BLAST
Compositional biasi35 – 6329Pro-richAdd
BLAST

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.
InParanoidiP42128.
KOiK09404.
OMAiCEVGPKE.
OrthoDBiEOG7CRTS2.
PhylomeDBiP42128.
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]

Sequencei

Sequence statusi: Complete.

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

P42128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVGEDSGA RALLALRSAP CSPVLCAAAA AAAFPATTSP PPPAQPPPGP
60 70 80 90 100
PALPAEPGPG PVPSTVATAT TTAPALVAAA AASVRQSPGP ALARLEGREF
110 120 130 140 150
EFLMRQPSVT IGRNSSQGSV DLSMGLSSFI SRRHLQLSFQ EPHFYLRCLG
160 170 180 190 200
KNGVFVDGAF QRRGAPALQL PQQCTFRFPS TAIKIQFTSL YHKEEAPASP
210 220 230 240 250
LRPLYPQISP LKIHIPEPDL RSLVSPIPSP TGTISVPNSC PASPRGAGSS
260 270 280 290 300
SYRFVQNVTS DLQLAAEFAA KAASEQQADA SGGDSPKDES KPPYSYAQLI
310 320 330 340 350
VQAISSAQDR QLTLSGIYAH ITKHYPYYRT ADKGWQNSIR HNLSLNRYFI
360 370 380 390 400
KVPRSQEEPG KGSFWRIDPA SEAKLVEQAF RKRRQRGVSC FRTPFGPLSS
410 420 430 440 450
RSAPASPTHP GLMSPRSSGL QTPECLSREG SPIPHDPDLG SKLASVPEYR
460 470 480 490 500
YSQSAPGSPV SAQPVIMAVP PRPSNLVAKP VAYMPASIVT SQQPSGHAIH
510 520 530 540 550
VVQQAPTVTM VRVVTTSANS ANGYILASQG STGTSHDTAG TAVLDLGNEA
560 570 580 590 600
RGLEEKPTIA FATIPAASRV IQTVASQMAP GVPGHTVTIL QPATPVTIGQ
610 620 630 640 650
HHLPVRAVTQ NGKHAVPTNS LTGNAYALSS PLQLLAAQAS SSTPVVITRV
660 670 680 690 700
CEVGPEEPAA AVSVAANAAP TPAASTTTSA SSSGEPEVKR SRVEEPGGTA
710
TTQPTAMAAT GPQGPGTGE
Length:719
Mass (Da):74,920
Last modified:November 28, 2006 - v2
Checksum:i0A0D3049B7846328
GO

Sequence cautioni

The sequence AAA37529.1 differs from that shown. Reason: Frameshift at positions 61, 88, 582, 603, 615 and 711. Curated
The sequence AAB69641.1 differs from that shown. Reason: Frameshift at positions 61 and 88. Curated
The sequence BAE25880.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431Missing in AAA37529 (PubMed:8007964).Curated
Sequence conflicti43 – 431Missing in AAB69641 (PubMed:9271401).Curated
Sequence conflicti402 – 4032SA → RS in AAA37529 (PubMed:8007964).Curated
Sequence conflicti407 – 4115PTHPG → HTSHA in AAB69641 (PubMed:9271401).Curated
Sequence conflicti551 – 5511R → A in AAA37529 (PubMed:8007964).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26507 mRNA. Translation: AAA37529.1. Frameshift.
AK144418 mRNA. Translation: BAE25880.1. Different initiation.
AK147375 mRNA. Translation: BAE27871.1.
U95016 mRNA. Translation: AAB69641.1. Frameshift.
CCDSiCCDS19826.1.
PIRiA56051.
RefSeqiNP_951031.2. NM_199068.2.
UniGeneiMm.24214.

Genome annotation databases

EnsembliENSMUST00000072837; ENSMUSP00000072616; ENSMUSG00000056493.
GeneIDi17425.
KEGGimmu:17425.
UCSCiuc009aio.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26507 mRNA. Translation: AAA37529.1. Frameshift.
AK144418 mRNA. Translation: BAE25880.1. Different initiation.
AK147375 mRNA. Translation: BAE27871.1.
U95016 mRNA. Translation: AAB69641.1. Frameshift.
CCDSiCCDS19826.1.
PIRiA56051.
RefSeqiNP_951031.2. NM_199068.2.
UniGeneiMm.24214.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A3SNMR-A289-389[»]
2D2WNMR-A289-389[»]
ProteinModelPortaliP42128.
SMRiP42128. Positions 289-389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP42128. 2 interactions.
MINTiMINT-4095257.

PTM databases

PhosphoSiteiP42128.

Proteomic databases

MaxQBiP42128.
PaxDbiP42128.
PRIDEiP42128.

Protocols and materials databases

DNASUi17425.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072837; ENSMUSP00000072616; ENSMUSG00000056493.
GeneIDi17425.
KEGGimmu:17425.
UCSCiuc009aio.1. mouse.

Organism-specific databases

CTDi221937.
MGIiMGI:1347488. Foxk1.

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00780000121840.
HOGENOMiHOG000072588.
HOVERGENiHBG051649.
InParanoidiP42128.
KOiK09404.
OMAiCEVGPKE.
OrthoDBiEOG7CRTS2.
PhylomeDBiP42128.
TreeFamiTF325718.

Miscellaneous databases

ChiTaRSiFoxk1. mouse.
EvolutionaryTraceiP42128.
NextBioi292048.
PROiP42128.
SOURCEiSearch...

Gene expression databases

BgeeiP42128.
CleanExiMM_FOXK1.
GenevestigatoriP42128.

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. "Myocyte nuclear factor, a novel winged-helix transcription factor under both developmental and neural regulation in striated myocytes."
    Bassel-Duby R., Hernandez M.D., Yang Q., Rochelle J.M., Seldin M.F., Williams R.S.
    Mol. Cell. Biol. 14:4596-4605(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    Tissue: Pancreatic acinar cell.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Diencephalon.
  3. "Transient expression of a winged-helix protein, MNF-beta, during myogenesis."
    Yang Q., Bassel-Duby R., Williams R.S.
    Mol. Cell. Biol. 17:5236-5243(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-411, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  4. "The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta) forms a co-repressor complex with mammalian Sin3B."
    Yang Q., Kong Y., Rothermel B., Garry D.J., Bassel-Duby R., Williams R.S.
    Biochem. J. 345:335-343(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIN3B.
    Tissue: Heart.
  5. "Identification of forkhead transcription factors in cortical and dopaminergic areas of the adult murine brain."
    Wijchers P.J.E.C., Hoekman M.F.M., Burbach J.P.H., Smidt M.P.
    Brain Res. 1068:23-33(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiFOXK1_MOUSE
AccessioniPrimary (citable) accession number: P42128
Secondary accession number(s): O35939, Q3UHI6, Q3UN67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 28, 2006
Last modified: April 29, 2015
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.