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P09086 (PO2F2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
POU domain, class 2, transcription factor 2
Alternative name(s):
Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2
Octamer-binding protein 2
Short name=Oct-2
Octamer-binding transcription factor 2
Short name=OTF-2
Gene names
Name:POU2F2
Synonyms:OCT2, OTF2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that specifically binds to the octamer motif (5'-ATTTGCAT-3'). Regulates transcription in a number of tissues in addition to activating immunoglobulin gene expression. Modulates transcription transactivation by NR3C1, AR and PGR. Isoform 5 activates the U2 small nuclear RNA (snRNA) promoter. Ref.2 Ref.6 Ref.8 Ref.9

Subunit structure

Interacts with NR3C1, AR and PGR. Ref.11

Subcellular location

Cytoplasm By similarity. Nucleus.

Tissue specificity

Isoform 3 is B-cell specific. Isoform 5 is expressed in B-cells and the immunoglobulin-expressing T-cell line Molt-4, but not in the T-cell line BW 5147. Ref.2 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.

Sequence caution

The sequence CAA32039.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainHomeobox
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhumoral immune response

Traceable author statement. Source: ProtInc

transcription from RNA polymerase II promoter

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: MGI

   Molecular functionsequence-specific DNA binding

Inferred from direct assay. Source: MGI

sequence-specific DNA binding transcription factor activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09086-1)

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: P09086-2)

The sequence of this isoform differs from the canonical sequence as follows:
     468-479: Missing.
Isoform 3 (identifier: P09086-3)

The sequence of this isoform differs from the canonical sequence as follows:
     168-183: Missing.
Isoform 4 (identifier: P09086-4)

The sequence of this isoform differs from the canonical sequence as follows:
     168-183: Missing.
     400-416: VTTLSSAVGTLHPSRTA → AQTPALKAATRLSACQA
     417-479: Missing.
Isoform 5 (identifier: P09086-5)

Also known as: Oct-2B;

The sequence of this isoform differs from the canonical sequence as follows:
     468-479: PGLWWNPAPYQP → STMVGLSSGL...GGPEAGSKAE
Note: Incomplete sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 479478POU domain, class 2, transcription factor 2
PRO_0000100714

Regions

Domain195 – 26975POU-specific
Domain389 – 41022Leucine-zipper
DNA binding297 – 35660Homeobox
Compositional bias417 – 4248Gly-rich

Amino acid modifications

Modified residue2501Phosphoserine Ref.12

Natural variations

Alternative sequence168 – 18316Missing in isoform 3 and isoform 4.
VSP_002324
Alternative sequence400 – 41617VTTLS…PSRTA → AQTPALKAATRLSACQA in isoform 4.
VSP_007848
Alternative sequence417 – 47963Missing in isoform 4.
VSP_007849
Alternative sequence468 – 47912Missing in isoform 2.
VSP_002325
Alternative sequence468 – 47912PGLWW…APYQP → STMVGLSSGLSPALMSNNPL ATIQALASGGTLPLTSLDGS GNLVLGAAGAAPGSPSLVTS PLFLNHTGLPLLSAPPGVGL VSAAAAAVAASISSKSPGLS SSSSSSSSSSSSTCSDVAAQ TPGGPGGPEAGSKAE in isoform 5.
VSP_032187

Experimental info

Mutagenesis340 – 3423VIR → FNP: Suppresses DNA-binding ability.

Secondary structure

.......... 479
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 8DA661DC07644D43

FASTA47951,209
        10         20         30         40         50         60 
MVHSSMGAPE IRMSKPLEAE KQGLDSPSEH TDTERNGPDT NHQNPQNKTS PFSVSPTGPS 

        70         80         90        100        110        120 
TKIKAEDPSG DSAPAAPLPP QPAQPHLPQA QLMLTGSQLA GDIQQLLQLQ QLVLVPGHHL 

       130        140        150        160        170        180 
QPPAQFLLPQ AQQSQPGLLP TPNLFQLPQQ TQGALLTSQP RAGLPTQAVT RPTLPDPHLS 

       190        200        210        220        230        240 
HPQPPKCLEP PSHPEEPSDL EELEQFARTF KQRRIKLGFT QGDVGLAMGK LYGNDFSQTT 

       250        260        270        280        290        300 
ISRFEALNLS FKNMCKLKPL LEKWLNDAET MSVDSSLPSP NQLSSPSLGF DGLPGRRRKK 

       310        320        330        340        350        360 
RTSIETNVRF ALEKSFLANQ KPTSEEILLI AEQLHMEKEV IRVWFCNRRQ KEKRINPCSA 

       370        380        390        400        410        420 
APMLPSPGKP ASYSPHMVTP QGGAGTLPLS QASSSLSTTV TTLSSAVGTL HPSRTAGGGG 

       430        440        450        460        470 
GGGGAAPPLN SIPSVTPPPP ATTNSTNPSP QGSHSAIGLS GLNPSTGPGL WWNPAPYQP 

« Hide

Isoform 2 [UniParc].

Checksum: 444B5AB65B950050
Show »

FASTA46749,801
Isoform 3 [UniParc].

Checksum: 5DCCA37A76A65AB9
Show »

FASTA46349,461
Isoform 4 [UniParc].

Checksum: 074B384660350FCE
Show »

FASTA40043,528
Isoform 5 (Oct-2B) [UniParc].

Checksum: F5E4E2B0D206FC15
Show »

FASTA60262,172

References

« Hide 'large scale' references
[1]"The B-cell-specific Oct-2 protein contains POU box- and homeo box-type domains."
Clerc R.G., Corcoran L.M., Lebowitz J.H., Baltimore D., Sharp P.A.
Genes Dev. 2:1570-1581(1988) [PubMed: 3265124] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 450-479 (ISOFORM 1).
[2]"A human lymphoid-specific transcription factor that activates immunoglobulin genes is a homoeobox protein."
Scheidereit C., Cromlish J.A., Gerster T., Kawakami K., Balmaceda C.-G., Currie R.A., Roder R.G.
Nature 336:551-557(1988) [PubMed: 2904654] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY.
Tissue: B-cell lymphoma.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[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 4).
Tissue: Lymph.
[5]"A cloned octamer transcription factor stimulates transcription from lymphoid-specific promoters in non-B cells."
Mueller M.M., Ruppert S., Schaffner W., Matthias P.
Nature 336:544-551(1988) [PubMed: 2904653] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-479 (ISOFORM 1).
Tissue: B-cell.
[6]"Transcription factor Oct-2A contains functionally redundant activating domains and works selectively from a promoter but not from a remote enhancer position in non-lymphoid (HeLa) cells."
Muller-Immergluck M.M., Schaffner W., Matthias P.
EMBO J. 9:1625-1634(1990) [PubMed: 2328728] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-161, FUNCTION.
[7]"Short introns interrupting the Oct-2 POU domain may prevent recombination between POU family genes without interfering with potential POU domain 'shuffling' in evolution."
Matsuo K., Clay O., Kuenzler P., Georgiev O., Urbanek P., Schaffner W.
Biol. Chem. Hoppe-Seyler 375:675-683(1994) [PubMed: 7888080] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-377.
[8]"A human protein specific for the immunoglobulin octamer DNA motif contains a functional homeobox domain."
Ko H.-S., Fast P., McBride W., Staudt L.M.
Cell 55:135-144(1988) [PubMed: 2901913] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 240-387, FUNCTION.
[9]"Promoter-selective activation domains in Oct-1 and Oct-2 direct differential activation of an snRNA and mRNA promoter."
Tanaka M., Lai J.-S., Herr W.
Cell 68:755-767(1992) [PubMed: 1739980] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 468-479 (ISOFORM 5), FUNCTION.
[10]"Identification of a novel lymphoid specific octamer binding protein (OTF-2B) by proteolytic clipping bandshift assay (PCBA)."
Schreiber E., Matthias P., Mueller M.M., Schaffner W.
EMBO J. 7:4221-4229(1988) [PubMed: 3072196] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 5), TISSUE SPECIFICITY.
[11]"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.
[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 SER-250, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"Solution structure of a POU-specific homeodomain: 3D-NMR studies of human B-cell transcription factor Oct-2."
Sivaraja M., Botfield M.C., Mueller M., Jancso A., Weiss M.A.
Biochemistry 33:9845-9855(1994) [PubMed: 7914745] [Abstract]
Cited for: STRUCTURE BY NMR OF 297-359.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36653 mRNA. Translation: AAA36389.1.
X53468 mRNA. Translation: CAA37562.1.
X53469 mRNA. Translation: CAA37565.1.
M36542 mRNA. Translation: AAA36732.1.
X13810 mRNA. Translation: CAA32040.1.
BT007438 mRNA. Translation: AAP36106.1.
BC006101 mRNA. Translation: AAH06101.1.
M36718 mRNA. Translation: AAA59978.1.
X13809 mRNA. Translation: CAA32039.1. Different initiation.
X81030 Genomic DNA. Translation: CAA56933.1.
IPIIPI00002666.
IPI00012533.
IPI00221055.
IPI00335926.
IPI00888702.
PIRA31753.
A42098.
RefSeqNP_001193954.1. NM_001207025.2.
NP_001193955.1. NM_001207026.1.
NP_001234923.1. NM_001247994.1.
NP_002689.1. NM_002698.4.
UniGeneHs.654420.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDPNMR-A297-359[»]
ProteinModelPortalP09086.
SMRP09086. Positions 199-359.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-51N.
STRINGP09086.

PTM databases

PhosphoSiteP09086.

Polymorphism databases

DMDM123402.

Proteomic databases

PRIDEP09086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292077; ENSP00000292077; ENSG00000028277.
GeneID5452.
KEGGhsa:5452.
UCSCuc002osn.1. human.
uc002osp.1. human.
uc002osq.1. human.

Organism-specific databases

CTD5452.
GeneCardsGC19M042592.
HGNCHGNC:9213. POU2F2.
HPACAB002513.
MIM164176. gene.
neXtProtNX_P09086.
PharmGKBPA33537.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19715.
HOVERGENHBG052783.
InParanoidP09086.
OrthoDBEOG4BCDNJ.
PhylomeDBP09086.

Enzyme and pathway databases

Pathway_Interaction_DBbcr_5pathway. BCR signaling pathway.

Gene expression databases

ArrayExpressP09086.
BgeeP09086.
CleanExHS_POU2F2.
GenevestigatorP09086.
GermOnlineENSG00000028277. Homo sapiens.

Family and domain databases

InterProIPR001356. Homeobox.
IPR017970. Homeobox_CS.
IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR010982. Lambda_DNA-bd.
IPR013847. POU.
IPR000327. POU_specific.
IPR000972. TF_octamer.
[Graphical view]
Gene3DG3DSA:1.10.260.40. G3DSA:1.10.260.40. 1 hit.
G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
KOK09364.
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. Homeodomain_like. 1 hit.
SSF47413. Lambda_like_DNA. 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

NextBio21101.
SOURCESearch...

Entry information

Entry namePO2F2_HUMAN
AccessionPrimary (citable) accession number: P09086
Secondary accession number(s): Q16648, Q7M4M8, Q9BRS4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 147 of the entry and version 3 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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

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