Reviewed, UniProtKB/Swiss-Prot P42128 (FOXK1_MOUSE)

Names and origin

Protein names

Recommended name:
    Forkhead box protein K1
Alternative name(s):
    Myocyte nuclear factor
      Short name=MNF

Gene names

Name:	Foxk1
Synonyms:	Mnf

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.1 Ref.3
Subunit structure	Interacts with SIN3B to form a complex which represses transcription. Ref.4
Subcellular location	Nucleus.
Tissue specificity	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. Ref.1 Ref.3 Ref.5
Sequence similarities	Contains 1 FHA domain. Contains 1 fork-head DNA-binding domain.
Sequence caution	The sequence AAA37529.1 differs from that shown. Reason: Frameshift at positions 61, 88, 582, 603, 615 and 711. The sequence AAB69641.1 differs from that shown. Reason: Frameshift at positions 61 and 88.

Ontologies

Keywords
Biological process	Differentiation Myogenesis Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator Developmental protein Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW muscle organ development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Traceable author statement. Source: UniProtKB negative regulation of cell growth Inferred from direct assay. Source: UniProtKB negative regulation of transcription, DNA-dependent Ref.3 Inferred from direct assay. Source: UniProtKB positive regulation of transcription, DNA-dependent Ref.1 Inferred from direct assay. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Ref.3 Inferred from direct assay. Source: MGI transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.1 Inferred by curator. Source: UniProtKB
Molecular function	DNA binding Ref.3 Inferred from direct assay. Source: UniProtKB protein binding Ref.4 Inferred from physical interaction. Source: IntAct sequence-specific DNA binding Ref.1 Ref.3 Inferred from direct assay. Source: UniProtKB transcription activator activity Ref.1 Inferred from direct assay. Source: UniProtKB transcription factor activity Inferred from electronic annotation. Source: InterPro transcription repressor activity Ref.3 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sin3b	Q62141-2	2	EBI-878285,EBI-591466
Sin3b	Q62141-2	2	EBI-878281,EBI-591466

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 719

718

Forkhead box protein K1

PRO_0000091857

Regions

Domain

109 – 161

53

FHA

DNA binding

291 – 386

96

Fork-head

Compositional bias

10 – 82

73

Ala-rich

Compositional bias

35 – 63

29

Pro-rich

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

87

1

Phosphoserine By similarity

Modified residue

199

1

Phosphoserine Ref.6 Ref.7

Modified residue

209

1

Phosphoserine By similarity

Modified residue

222

1

Phosphoserine By similarity

Modified residue

225

1

Phosphoserine By similarity

Modified residue

229

1

Phosphoserine By similarity

Modified residue

231

1

Phosphothreonine By similarity

Modified residue

233

1

Phosphothreonine By similarity

Modified residue

239

1

Phosphoserine By similarity

Modified residue

243

1

Phosphoserine By similarity

Modified residue

402

1

Phosphoserine Ref.6

Modified residue

406

1

Phosphoserine Ref.6

Modified residue

408

1

Phosphothreonine By similarity

Modified residue

414

1

Phosphoserine Ref.6

Modified residue

422

1

Phosphothreonine Ref.6

Modified residue

427

1

Phosphoserine By similarity

Modified residue

431

1

Phosphoserine By similarity

Modified residue

441

1

Phosphoserine By similarity

Experimental info

Sequence conflict

43

1

Missing in AAA37529. Ref.1

Sequence conflict

43

1

Missing in AAB69641. Ref.3

Sequence conflict

402 – 403

2

SA → RS in AAA37529. Ref.1

Sequence conflict

407 – 411

5

PTHPG → HTSHA in AAB69641. Ref.3

Sequence conflict

551

1

R → A in AAA37529. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

719

Helix Strand Turn

Details...

Beta strand

292 – 294

3

Helix

298 – 304

7

Beta strand

307 – 312

6

Helix

314 – 324

11

Beta strand

326 – 330

5

Helix

335 – 345

11

Beta strand

347 – 356

10

Beta strand

360 – 362

3

Beta strand

365 – 367

3

Helix

372 – 380

9

Sequences

	Sequence		Length	Mass (Da)
	P42128-1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 0A0D3049B7846328	FASTA	719	74,920
	10 20 30 40 50 60 MAEVGEDSGA RALLALRSAP CSPVLCAAAA AAAFPATTSP PPPAQPPPGP PALPAEPGPG 70 80 90 100 110 120 PVPSTVATAT TTAPALVAAA AASVRQSPGP ALARLEGREF EFLMRQPSVT IGRNSSQGSV 130 140 150 160 170 180 DLSMGLSSFI SRRHLQLSFQ EPHFYLRCLG KNGVFVDGAF QRRGAPALQL PQQCTFRFPS 190 200 210 220 230 240 TAIKIQFTSL YHKEEAPASP LRPLYPQISP LKIHIPEPDL RSLVSPIPSP TGTISVPNSC 250 260 270 280 290 300 PASPRGAGSS SYRFVQNVTS DLQLAAEFAA KAASEQQADA SGGDSPKDES KPPYSYAQLI 310 320 330 340 350 360 VQAISSAQDR QLTLSGIYAH ITKHYPYYRT ADKGWQNSIR HNLSLNRYFI KVPRSQEEPG 370 380 390 400 410 420 KGSFWRIDPA SEAKLVEQAF RKRRQRGVSC FRTPFGPLSS RSAPASPTHP GLMSPRSSGL 430 440 450 460 470 480 QTPECLSREG SPIPHDPDLG SKLASVPEYR YSQSAPGSPV SAQPVIMAVP PRPSNLVAKP 490 500 510 520 530 540 VAYMPASIVT SQQPSGHAIH VVQQAPTVTM VRVVTTSANS ANGYILASQG STGTSHDTAG 550 560 570 580 590 600 TAVLDLGNEA RGLEEKPTIA FATIPAASRV IQTVASQMAP GVPGHTVTIL QPATPVTIGQ 610 620 630 640 650 660 HHLPVRAVTQ NGKHAVPTNS LTGNAYALSS PLQLLAAQAS SSTPVVITRV CEVGPEEPAA 670 680 690 700 710 AVSVAANAAP TPAASTTTSA SSSGEPEVKR SRVEEPGGTA TTQPTAMAAT GPQGPGTGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8007964] [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: 16141072] [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: 9271401] [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: 10620510] [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: 16376864] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"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) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-402; SER-406; SER-414 AND THR-422, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass 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) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L26507 mRNA. Translation: AAA37529.1. Frameshift.
AK144418 mRNA. Translation: BAE25880.1. Different initiation.
AK147375 mRNA. Translation: BAE27871.1.
U95016 mRNA. Translation: AAB69641.1. Frameshift.

IPI

IPI00656285.

PIR

A56051.

RefSeq

NP_951031.2.

UniGene

Mm.24214

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A3S	NMR	-	A	289-387	[»]
2D2W	NMR	-	A	289-387	[»]

SMR

P42128. Positions 101-166.

ModBase

Search...

Protein-protein interaction databases

IntAct

P42128. 4 interactions.

STRING

P42128.

Proteomic databases

PRIDE

P42128.

Genome annotation databases

Ensembl

ENSMUST00000072837; ENSMUSP00000072616; ENSMUSG00000056493; Mus musculus. [Genome view]

GeneID

17425.

KEGG

mmu:17425.

UCSC

uc009aio.1. mouse.

Organism-specific databases

CTD

17425.

MGI

MGI:1347488. Foxk1.

Phylogenomic databases

eggNOG

roNOG06378.

HOGENOM

HBG402857.

HOVERGEN

P42128.

InParanoid

P42128.

OMA

VTSQQPS.

OrthoDB

EOG95QKZF.

Gene expression databases

ArrayExpress

P42128.

Bgee

P42128.

CleanEx

MM_FOXK1.

Genevestigator

P42128.

GermOnline

ENSMUSG00000056493. Mus musculus.

Family and domain databases

InterPro

IPR000253. FHA.
IPR008984. SMAD_FHA_domain.
IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
[Graphical view]

Gene3D

G3DSA:2.60.200.20. FHA. 1 hit.

PANTHER

PTHR11829. Fork_box_protein. 1 hit.

Pfam

PF00498. FHA. 1 hit.
PF00250. Fork_head. 1 hit.
[Graphical view]

PRINTS

PR00053. FORKHEAD.

SMART

SM00339. FH. 1 hit.
SM00240. FHA. 1 hit.
[Graphical view]

PROSITE

PS50006. FHA_DOMAIN. 1 hit.
PS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

292048.

SOURCE

Search...

Entry information

Entry name

FOXK1_MOUSE

Accession

Primary (citable) accession number: P42128
Secondary accession number(s): O35939, Q3UHI6, Q3UN67

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 28, 2006
Last modified:	January 19, 2010
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)