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P14859 (PO2F1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
POU domain, class 2, transcription factor 1
Alternative name(s):
NF-A1
Octamer-binding protein 1
Short name=Oct-1
Octamer-binding transcription factor 1
Short name=OTF-1
Gene names
Name:POU2F1
Synonyms:OCT1, OTF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length743 AA.
Sequence statusComplete.
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. Ref.7

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.8 Ref.9

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous. Isoform 2 is lymphocyte-specific.

Post-translational modification

Phosphorylated by PRKDC. Ref.7 Ref.10

Sequence similarities

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

Contains 1 homeobox DNA-binding domain.

Contains 1 POU-specific domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SP1P080477EBI-624770,EBI-298336

Alternative products

This entry describes 6 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 6 (identifier: P14859-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGGAASQDESSAAAAAAADSRM
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.
Isoform 5 (identifier: P14859-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGGAASQDESSAAAAAAADSRM
     112-174: 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 Ref.7

Amino acid modifications

Modified residue2701Phosphothreonine Ref.13
Modified residue2831Phosphoserine Ref.13
Modified residue3851Phosphoserine Ref.7
Modified residue4481Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 2020MNNPS…DGNTG → MKTRMKIFVMIHFHLMNS in isoform 3.
VSP_013421
Alternative sequence11M → MLDCSDYVLDSRM in isoform 2.
VSP_002320
Alternative sequence11M → MADGGAASQDESSAAAAAAA DSRM in isoform 5 and isoform 6.
VSP_043195
Alternative sequence112 – 17463Missing in isoform 5.
VSP_043196
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.22
VAR_035816

Experimental info

Mutagenesis3851S → A: Loss of inhibition of DNA binding. Ref.7
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) [UniParc].

Checksum: 084E222919B616AA
Show »

FASTA75577,870
Isoform 3 [UniParc].

Checksum: 28E72DF211628CE3
Show »

FASTA74176,696
Isoform 6 [UniParc].

Checksum: 54C541CD1D6BA426
Show »

FASTA76678,535
Isoform 4 [UniParc].

Checksum: 1C82E7818D70A368
Show »

FASTA65368,143
Isoform 5 [UniParc].

Checksum: 1E6037CDCF41F528
Show »

FASTA70372,082

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] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: B-cell lymphoma.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Thymus.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] [Europe PMC] [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.
[7]"Mitotic phosphorylation of the Oct-1 homeodomain and regulation of Oct-1 DNA binding activity."
Segil N., Roberts S.B., Heintz N.
Science 254:1814-1816(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-385, MUTAGENESIS OF SER-385, FUNCTION IN DNA-BINDING ACTIVITY.
[8]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR3C1; AR AND PGR.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCFC1.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[11]"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] [Europe PMC] [Abstract]
Cited for: REVIEW ON HERPES INFECTION.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270; SER-283 AND SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 284-359.
[19]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 284-354.
[20]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 378-437.
[21]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 284-439.
[22]"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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-88.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13403 mRNA. Translation: CAA31767.1.
AY113189 mRNA. Translation: AAM77920.1.
AK303201 mRNA. Translation: BAG64291.1.
AL136984 Genomic DNA. Translation: CAI15167.1.
AL136984 Genomic DNA. Translation: CAI15169.1.
AL136984 Genomic DNA. Translation: CAI15170.1.
AL136984 Genomic DNA. Translation: CAI15171.1.
AL359962 Genomic DNA. No translation available.
AL451050 Genomic DNA. No translation available.
CH471067 Genomic DNA. Translation: EAW90786.1.
CH471067 Genomic DNA. Translation: EAW90788.1.
BC001664 mRNA. Translation: AAH01664.1.
BC003571 mRNA. Translation: AAH03571.1.
BC007388 mRNA. Translation: AAH07388.1.
BC052274 mRNA. Translation: AAH52274.1.
CCDSCCDS55655.1. [P14859-5]
CCDS55656.1. [P14859-2]
PIRA47001.
RefSeqNP_001185712.1. NM_001198783.1. [P14859-2]
NP_001185715.1. NM_001198786.1. [P14859-5]
NP_002688.3. NM_002697.3. [P14859-6]
UniGeneHs.283402.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQTX-ray3.20A/B278-439[»]
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.
ProteinModelPortalP14859.
SMRP14859. Positions 282-438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111447. 51 interactions.
DIPDIP-226N.
IntActP14859. 3 interactions.
MINTMINT-149153.
STRING9606.ENSP00000271411.

PTM databases

PhosphoSiteP14859.

Polymorphism databases

DMDM28202257.

Proteomic databases

MaxQBP14859.
PaxDbP14859.
PRIDEP14859.

Protocols and materials databases

DNASU5451.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367862; ENSP00000356836; ENSG00000143190. [P14859-2]
ENST00000420254; ENSP00000414660; ENSG00000143190. [P14859-4]
ENST00000429375; ENSP00000401217; ENSG00000143190. [P14859-5]
ENST00000443275; ENSP00000415993; ENSG00000143190.
ENST00000541643; ENSP00000441285; ENSG00000143190. [P14859-1]
GeneID5451.
KEGGhsa:5451.
UCSCuc001gec.3. human. [P14859-1]
uc001ged.3. human. [P14859-3]
uc001gef.3. human. [P14859-2]
uc001geg.3. human. [P14859-4]
uc010plh.2. human. [P14859-5]

Organism-specific databases

CTD5451.
GeneCardsGC01P167190.
H-InvDBHIX0018279.
HGNCHGNC:9212. POU2F1.
HPACAB002608.
HPA045784.
MIM164175. gene.
neXtProtNX_P14859.
PharmGKBPA33536.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267922.
HOGENOMHOG000220842.
HOVERGENHBG057016.
InParanoidP14859.
KOK09364.
PhylomeDBP14859.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
SignaLinkP14859.

Gene expression databases

ArrayExpressP14859.
BgeeP14859.
CleanExHS_POU2F1.
GenevestigatorP14859.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
1.10.260.40. 1 hit.
InterProIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
IPR013847. POU.
IPR000327. POU_specific.
IPR000972. TF_octamer.
[Graphical view]
PfamPF00046. Homeobox. 1 hit.
PF00157. Pou. 1 hit.
[Graphical view]
PRINTSPR00029. OCTAMER.
PR00028. POUDOMAIN.
SMARTSM00389. HOX. 1 hit.
SM00352. POU. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 1 hit.
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

ChiTaRSPOU2F1. human.
EvolutionaryTraceP14859.
GeneWikiPOU2F1.
GenomeRNAi5451.
NextBio21097.
PROP14859.
SOURCESearch...

Entry information

Entry namePO2F1_HUMAN
AccessionPrimary (citable) accession number: P14859
Secondary accession number(s): B1AL91 expand/collapse secondary AC list , B1AL93, B4E029, J3KP77, Q5TBT7, Q6PK46, Q8NEU9, Q9BPV1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 2003
Last modified: July 9, 2014
This is version 176 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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