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POU domain class 2-associating factor 1 (B-cell-specific coactivator OBF-1) (BOB-1) (OCA-B) (OCT-binding factor 1)

 OBF1_HUMAN              Reviewed;         256 AA.
Q16633; B2R8Z9; Q14983;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
27-SEP-2017, entry version 153.
RecName: Full=POU domain class 2-associating factor 1;
AltName: Full=B-cell-specific coactivator OBF-1;
AltName: Full=BOB-1;
AltName: Full=OCA-B;
AltName: Full=OCT-binding factor 1;
Name=POU2AF1; Synonyms=OBF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=7859290; DOI=10.1016/0092-8674(95)90500-6;
Strubin M., Newell J.W., Matthias P.;
"OBF-1, a novel B cell-specific coactivator that stimulates
immunoglobulin promoter activity through association with octamer-
binding proteins.";
Cell 80:497-506(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Peripheral blood lymphocyte;
PubMed=7779176; DOI=10.1038/373360a0;
Gstaiger M., Knoepfel L., Georgiev O., Schaffner W., Hovens C.M.;
"A B-cell coactivator of octamer-binding transcription factors.";
Nature 373:360-362(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION WITH BCL6.
TISSUE=Lymphoma;
PubMed=8574789;
Galiegue-Zouitina S., Quief S., Hildebrand M.-P., Denis C., Lecocq G.,
Collyn-D'Hooghe M., Bastard C., Yuille M., Dyer M.J., Kerckaert J.-P.;
"Fusion of the LAZ3/BCL6 and BOB1/OBF1 genes by t(3; 11) (q27; q23)
chromosomal translocation.";
C. R. Acad. Sci. III, Sci. Vie 318:1125-1131(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-27 AND 235-256.
PubMed=7623806; DOI=10.1128/MCB.15.8.4115;
Luo Y., Roeder R.G.;
"Cloning, functional characterization, and mechanism of action of the
B-cell-specific transcriptional coactivator OCA-B.";
Mol. Cell. Biol. 15:4115-4124(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH SIAH1, AND DEGRADATION.
PubMed=11483517; DOI=10.1093/emboj/20.15.4143;
Tiedt R., Bartholdy B.A., Matthias G., Newell J.W., Matthias P.;
"The RING finger protein Siah-1 regulates the level of the
transcriptional coactivator OBF-1.";
EMBO J. 20:4143-4152(2001).
[9]
INTERACTION WITH SIAH1 AND SIAH2, AND DEGRADATION.
PubMed=11483518; DOI=10.1093/emboj/20.15.4153;
Boehm J., He Y., Greiner A., Staudt L., Wirth T.;
"Regulation of BOB.1/OBF.1 stability by SIAH.";
EMBO J. 20:4153-4162(2001).
[10]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-44 IN COMPLEX WITH OCT1 AND
DNA.
PubMed=10541551; DOI=10.1101/gad.13.20.2650;
Chasman D., Cepek K., Sharp P.A., Pabo C.O.;
"Crystal structure of an OCA-B peptide bound to an Oct-1 POU
domain/octamer DNA complex: specific recognition of a protein-DNA
interface.";
Genes Dev. 13:2650-2657(1999).
-!- FUNCTION: Transcriptional coactivator that specifically associates
with either OCT1 or OCT2. It boosts the OCT1 mediated promoter
activity and to a lesser extent, that of OCT2. It has no intrinsic
DNA-binding activity. It recognizes the POU domains of OCT1 and
OCT2. It is essential for the response of B-cells to antigens and
required for the formation of germinal centers.
-!- INTERACTION:
Q3SYF9:KRTAP19-7; NbExp=4; IntAct=EBI-943588, EBI-10241353;
P32242:OTX1; NbExp=4; IntAct=EBI-943588, EBI-740446;
Q9BX46-2:RBM24; NbExp=4; IntAct=EBI-943588, EBI-12224445;
Q8IUQ4:SIAH1; NbExp=2; IntAct=EBI-943588, EBI-747107;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: B-cell specific.
-!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
subsequent proteasomal degradation. {ECO:0000305}.
-!- DISEASE: Note=A chromosomal aberration involving POU2AF1/OBF1 may
be a cause of a form of B-cell leukemia. Translocation
t(3;11)(q27;q23) with BCL6. {ECO:0000269|PubMed:8574789}.
-!- SIMILARITY: Belongs to the POU2AF1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/OBFID94.html";
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EMBL; Z47550; CAA87630.1; -; mRNA.
EMBL; X83504; CAA58494.1; -; mRNA.
EMBL; Z49194; CAA89053.1; -; mRNA.
EMBL; AK313573; BAG36346.1; -; mRNA.
EMBL; CH471065; EAW67137.1; -; Genomic_DNA.
EMBL; BC032549; AAH32549.1; -; mRNA.
CCDS; CCDS31675.1; -.
PIR; A55652; A55652.
RefSeq; NP_006226.2; NM_006235.2.
UniGene; Hs.654525; -.
PDB; 1CQT; X-ray; 3.20 A; I/J=1-44.
PDBsum; 1CQT; -.
DisProt; DP00172; -.
ProteinModelPortal; Q16633; -.
SMR; Q16633; -.
BioGrid; 111446; 12.
CORUM; Q16633; -.
ELM; Q16633; -.
IntAct; Q16633; 42.
MINT; MINT-206323; -.
STRING; 9606.ENSP00000376786; -.
iPTMnet; Q16633; -.
PhosphoSitePlus; Q16633; -.
BioMuta; POU2AF1; -.
DMDM; 2833276; -.
MaxQB; Q16633; -.
PaxDb; Q16633; -.
PeptideAtlas; Q16633; -.
PRIDE; Q16633; -.
DNASU; 5450; -.
Ensembl; ENST00000393067; ENSP00000376786; ENSG00000110777.
GeneID; 5450; -.
KEGG; hsa:5450; -.
UCSC; uc001plg.5; human.
CTD; 5450; -.
DisGeNET; 5450; -.
EuPathDB; HostDB:ENSG00000110777.11; -.
GeneCards; POU2AF1; -.
HGNC; HGNC:9211; POU2AF1.
HPA; CAB011193; -.
MalaCards; POU2AF1; -.
MIM; 601206; gene.
neXtProt; NX_Q16633; -.
OpenTargets; ENSG00000110777; -.
Orphanet; 186; Primary biliary cirrhosis.
PharmGKB; PA33535; -.
eggNOG; ENOG410IJXZ; Eukaryota.
eggNOG; ENOG41123CN; LUCA.
GeneTree; ENSGT00390000017499; -.
HOGENOM; HOG000059584; -.
HOVERGEN; HBG007859; -.
InParanoid; Q16633; -.
OMA; CLDMEGS; -.
OrthoDB; EOG091G0EUL; -.
PhylomeDB; Q16633; -.
TreeFam; TF332565; -.
SIGNOR; Q16633; -.
ChiTaRS; POU2AF1; human.
EvolutionaryTrace; Q16633; -.
GeneWiki; POU2AF1; -.
GenomeRNAi; 5450; -.
PRO; PR:Q16633; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110777; -.
CleanEx; HS_POU2AF1; -.
ExpressionAtlas; Q16633; baseline and differential.
Genevisible; Q16633; HS.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:CAFA.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:CAFA.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IMP:CAFA.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:CAFA.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IC:CAFA.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
InterPro; IPR015389; PD-C2-AF1.
Pfam; PF09310; PD-C2-AF1; 1.
1: Evidence at protein level;
3D-structure; Chromosomal rearrangement; Complete proteome;
Direct protein sequencing; Nucleus; Polymorphism; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 256 POU domain class 2-associating factor 1.
/FTId=PRO_0000058018.
VARIANT 141 141 T -> A (in dbSNP:rs1042750).
/FTId=VAR_005521.
VARIANT 194 194 Q -> R (in dbSNP:rs1042751).
/FTId=VAR_005522.
HELIX 28 34 {ECO:0000244|PDB:1CQT}.
SEQUENCE 256 AA; 27436 MW; 2C46F1796774D614 CRC64;
MLWQKPTAPE QAPAPARPYQ GVRVKEPVKE LLRRKRGHAS SGAAPAPTAV VLPHQPLATY
TTVGPSCLDM EGSVSAVTEE AALCAGWLSQ PTPATLQPLA PWTPYTEYVP HEAVSCPYSA
DMYVQPVCPS YTVVGPSSVL TYASPPLITN VTTRSSATPA VGPPLEGPEH QAPLTYFPWP
QPLSTLPTST LQYQPPAPAL PGPQFVQLPI SIPEPVLQDM EDPRRAASSL TIDKLLLEEE
DSDAYALNHT LSVEGF


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