Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P14859 (PO2F1_HUMAN)

Last modified November 3, 2009. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    POU domain, class 2, transcription factor 1
Alternative name(s):
    Octamer-binding transcription factor 1
      Short name=Oct-1
      Short name=OTF-1
      Short name=NF-A1
Gene names
Name: POU2F1
Synonyms: OCT1, OTF1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length743 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR By similarity. In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes.

Subunit structure

Interacts with NR3C1, AR, PGR and HCFC1. Associates with the herpes simplex virus VP16-induced complex; binding to HCFC1 activates the viral transcriptional activator VP16 for association with POU2F1, to form a multiprotein-DNA complex responsible for activating transcription of the viral immediate early genes. Ref.5 Ref.6

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous. Isoform 2 is lymphocyte-specific.

Post-translational modification

Phosphorylated by PRKDC. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the POU transcription factor family. Class-2 subfamily.

Contains 1 homeobox DNA-binding domain.

Contains 1 POU-specific domain.

Ontologies

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14859-1)

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: P14859-2)

Also known as: Oct-1L; lymphocyte-specific;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLDCSDYVLDSRM
Isoform 3 (identifier: P14859-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MNNPSETSKPSMESGDGNTG → MKTRMKIFVMIHFHLMNS
Note: No experimental confirmation available.
Isoform 4 (identifier: P14859-4)

The sequence of this isoform differs from the canonical sequence as follows:
     641-653: ALASGGSLPITSL → GLLHGLENFLTKN
     654-743: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 743743POU domain, class 2, transcription factor 1
PRO_0000100707

Regions

Domain280 – 35475POU-specific
DNA binding379 – 43860Homeobox

Amino acid modifications

Modified residue2701Phosphothreonine Ref.12
Modified residue2831Phosphoserine Ref.12
Modified residue3351Phosphoserine Ref.11
Modified residue3851Phosphoserine Ref.11
Modified residue4481Phosphoserine Ref.9 Ref.10 Ref.12

Natural variations

Alternative sequence1 – 2020MNNPS…DGNTG → MKTRMKIFVMIHFHLMNS in isoform 3.
VSP_013421
Alternative sequence11M → MLDCSDYVLDSRM in isoform 2.
VSP_002320
Alternative sequence641 – 65313ALASG…PITSL → GLLHGLENFLTKN in isoform 4.
VSP_013422
Alternative sequence654 – 74390Missing in isoform 4.
VSP_013423
Natural variant881S → F in a breast cancer sample; somatic mutation. Ref.17
VAR_035816

Experimental info

Sequence conflict2251L → Q in CAA31767. Ref.1
Sequence conflict5461T → I in AAM77920. Ref.2

Secondary structure

............... 743
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 2003. Version 2.
Checksum: FAB27FFC79CF2276

FASTA74376,472
        10         20         30         40         50         60 
MNNPSETSKP SMESGDGNTG TQTNGLDFQK QPVPVGGAIS TAQAQAFLGH LHQVQLAGTS 

        70         80         90        100        110        120 
LQAAAQSLNV QSKSNEESGD SQQPSQPSQQ PSVQAAIPQT QLMLAGGQIT GLTLTPAQQQ 

       130        140        150        160        170        180 
LLLQQAQAQA QLLAAAVQQH SASQQHSAAG ATISASAATP MTQIPLSQPI QIAQDLQQLQ 

       190        200        210        220        230        240 
QLQQQNLNLQ QFVLVHPTTN LQPAQFIISQ TPQGQQGLLQ AQNLLTQLPQ QSQANLLQSQ 

       250        260        270        280        290        300 
PSITLTSQPA TPTRTIAATP IQTLPQSQST PKRIDTPSLE EPSDLEELEQ FAKTFKQRRI 

       310        320        330        340        350        360 
KLGFTQGDVG LAMGKLYGND FSQTTISRFE ALNLSFKNMC KLKPLLEKWL NDAENLSSDS 

       370        380        390        400        410        420 
SLSSPSALNS PGIEGLSRRR KKRTSIETNI RVALEKSFLE NQKPTSEEIT MIADQLNMEK 

       430        440        450        460        470        480 
EVIRVWFCNR RQKEKRINPP SSGGTSSSPI KAIFPSPTSL VATTPSLVTS SAATTLTVSP 

       490        500        510        520        530        540 
VLPLTSAAVT NLSVTGTSDT TSNNTATVIS TAPPASSAVT SPSLSPSPSA SASTSEASSA 

       550        560        570        580        590        600 
SETSTTQTTS TPLSSPLGTS QVMVTASGLQ TAAAAALQGA AQLPANASLA AMAAAAGLNP 

       610        620        630        640        650        660 
SLMAPSQFAA GGALLSLNPG TLSGALSPAL MSNSTLATIQ ALASGGSLPI TSLDATGNLV 

       670        680        690        700        710        720 
FANAGGAPNI VTAPLFLNPQ NLSLLTSNPV SLVSAAAASA GNSAPVASLH ATSTSAESIQ 

       730        740 
NSLFTVASAS GAASTTTTAS KAQ 

« Hide

Isoform 2 (Oct-1L) (lymphocyte-specific).

Checksum: 084E222919B616AA
Show »

FASTA75577,870
Isoform 3.

Checksum: 28E72DF211628CE3
Show »

FASTA74176,696
Isoform 4.

Checksum: 1C82E7818D70A368
Show »

FASTA65368,143

References

« Hide 'large scale' references
[1]"The ubiquitous octamer-binding protein Oct-1 contains a POU domain with a homeo box subdomain."
Sturm R.A., Das G., Herr W.
Genes Dev. 2:1582-1599(1988) [PubMed: 2905684] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Teratocarcinoma.
[2]"Human Oct-1L isoform has tissue-specific expression pattern similar to Oct-2."
Luchina N.N., Krivega I.V., Pankratova E.V.
Immunol. Lett. 85:237-241(2003) [PubMed: 12663137] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: B-cell lymphoma.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], NUCLEOTIDE SEQUENCE OF 93-653.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-653 (ISOFORM 4).
Tissue: Lung, Lymph and Skin.
[5]"Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter."
Prefontaine G.G., Walther R., Giffin W., Lemieux M.E., Pope L., Hache R.J.G.
J. Biol. Chem. 274:26713-26719(1999) [PubMed: 10480874] [Abstract]
Cited for: INTERACTION WITH NR3C1; AR AND PGR.
[6]"Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP."
Mahajan S.S., Wilson A.C.
Mol. Cell. Biol. 20:919-928(2000) [PubMed: 10629049] [Abstract]
Cited for: INTERACTION WITH HCFC1.
[7]"Down-regulation of histone H2B by DNA-dependent protein kinase in response to DNA damage through modulation of octamer transcription factor 1."
Schild-Poulter C., Shih A., Yarymowich N.C., Hache R.J.G.
Cancer Res. 63:7197-7205(2003) [PubMed: 14612514] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"The herpes simplex virus VP16-induced complex: the makings of a regulatory switch."
Wysocka J., Herr W.
Trends Biochem. Sci. 28:294-304(2003) [PubMed: 12826401] [Abstract]
Cited for: REVIEW ON HERPES INFECTION.
[9]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, MASS SPECTROMETRY.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-385, MASS SPECTROMETRY.
[12]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270; SER-283 AND SER-448, MASS SPECTROMETRY.
[13]"Solution structure of the POU-specific DNA-binding domain of Oct-1."
Dekker N., Cox M., Boelens R., Verrijzer C.P., van der Vliet P.C., Kaptein R.
Nature 362:852-855(1993) [PubMed: 8479524] [Abstract]
Cited for: STRUCTURE BY NMR OF 284-359.
[14]"The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain."
Assa-Munt N., Mortishire-Smith R.J., Aurora R., Herr W., Wright P.E.
Cell 73:193-205(1993) [PubMed: 8462099] [Abstract]
Cited for: STRUCTURE BY NMR OF 284-354.
[15]"Solution structure of the Oct-1 POU homeodomain determined by NMR and restrained molecular dynamics."
Cox M., van Tilborg P.J.A., de Laat W., Boelens R., van Leeuwen H.C., van der Vliet P.C., Kaptein R.
J. Biomol. NMR 6:23-32(1995) [PubMed: 7663141] [Abstract]
Cited for: STRUCTURE BY NMR OF 378-437.
[16]"Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules."
Klemm J.D., Rould M.A., Aurora R., Herr W., Pabo C.O.
Cell 77:21-32(1994) [PubMed: 8156594] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 284-439.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-88.
+Additional computationally mapped references.

Cross-references

Sequence databases

X13403 mRNA. Translation: CAA31767.1.
AY113189 mRNA. Translation: AAM77920.1.
BC001664 mRNA. Translation: AAH01664.1.
BC003571 mRNA. Translation: AAH03571.1.
BC007388 mRNA. Translation: AAH07388.1.
BC052274 mRNA. Translation: AAH52274.1.
AL136984 Genomic DNA. Translation: CAI15167.1.
AL136984 Genomic DNA. Translation: CAI15170.1.
AL136984 Genomic DNA. Translation: CAI15171.1.
IPIIPI00027828.
IPI00219171.
IPI00555623.
IPI00555806.
PIRA47001.
RefSeqNP_002688.2.
UniGeneHs.493649

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CQTX-ray3.20A/B280-438[»]
1E3OX-ray1.90C280-438[»]
1GT0X-ray2.60C280-438[»]
1HF0X-ray2.70A/B280-438[»]
1O4XNMR-A280-442[»]
1OCTX-ray3.00C284-439[»]
1POGNMR-A378-437[»]
1POUNMR-A284-354[»]
DisProtDP00231.
ModBaseSearch...

Protein-protein interaction databases

IntActP14859. 2 interactions.
STRINGP14859.

PTM databases

PhosphoSiteP14859.

Proteomic databases

PRIDEP14859.

Genome annotation databases

EnsemblENST00000271411; ENSP00000271411; ENSG00000143190; Homo sapiens. [Genome view]
ENST00000367862; ENSP00000356836; ENSG00000143190; Homo sapiens. [Genome view]
ENST00000367865; ENSP00000356839; ENSG00000143190; Homo sapiens. [Genome view]
ENST00000367866; ENSP00000356840; ENSG00000143190; Homo sapiens. [Genome view]
ENST00000420254; ENSP00000414660; ENSG00000143190; Homo sapiens. [Genome view]
ENST00000429375; ENSP00000401217; ENSG00000143190; Homo sapiens. [Genome view]
ENST00000442313; ENSP00000404571; ENSG00000143190; Homo sapiens. [Genome view]
ENST00000443275; ENSP00000415993; ENSG00000143190; Homo sapiens. [Genome view]
ENST00000452019; ENSP00000391523; ENSG00000143190; Homo sapiens. [Genome view]
GeneID5451.
KEGGhsa:5451.
UCSCuc001gec.1. human.
uc001ged.1. human.
uc001geg.2. human.

Organism-specific databases

CTD5451.
GeneCardsGC01P165456.
H-InvDBHIX0018279.
HGNCHGNC:9212. POU2F1.
HPACAB002608.
MIM164175. gene.
PharmGKBPA33536.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP14859.
OMATTDTTSN.

Enzyme and pathway databases

Pathway_Interaction_DBnfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
tcrcalciumpathway. Calcium signaling in the CD4+ TCR pathway.
hnf3apathway. FOXA1 transcription factor network.
ar_tf_pathway. Regulation of Androgen receptor activity.
ReactomeREACT_1788. Transcription.

Gene expression databases

ArrayExpressP14859.
BgeeP14859.
CleanExHS_POU2F1.
GenevestigatorP14859.
GermOnlineENSG00000143190. Homo sapiens.

Family and domain databases

InterProIPR001356. Homeobox.
IPR017970. Homeobox_CS.
IPR012287. Homeodomain-rel.
IPR013847. POU.
IPR000327. POU_specific.
IPR000972. TF_octamer_bd.
[Graphical view]
Gene3DG3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
PfamPF00046. Homeobox. 1 hit.
PF00157. Pou. 1 hit.
[Graphical view]
PRINTSPR00029. OCTAMER.
PR00028. POUDOMAIN.
ProDomPD000010. Homeobox. 1 hit.
PD000583. POU. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00389. HOX. 1 hit.
SM00352. POU. 1 hit.
[Graphical view]
PROSITEPS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
PS00035. POU_1. 1 hit.
PS00465. POU_2. 1 hit.
PS51179. POU_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21097.
SOURCESearch...

Entry information

Entry namePO2F1_HUMAN
AccessionPrimary (citable) accession number: P14859
Secondary accession number(s): B1AL91 expand/collapse secondary AC list , Q5TBT7, Q6PK46, Q8NEU9, Q9BPV1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 2003
Last modified: November 3, 2009
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents