OBF1_HUMAN
ID OBF1_HUMAN Reviewed; 256 AA.
AC Q16633; B2R8Z9; Q14983;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=POU domain class 2-associating factor 1 {ECO:0000305};
DE AltName: Full=B-cell-specific coactivator OBF-1;
DE AltName: Full=BOB-1 {ECO:0000303|PubMed:7779176};
DE AltName: Full=OCA-B;
DE AltName: Full=OCT-binding factor 1;
GN Name=POU2AF1 {ECO:0000312|HGNC:HGNC:9211};
GN Synonyms=BOB1 {ECO:0000303|PubMed:7779176},
GN OBF1 {ECO:0000303|PubMed:7859290};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH POU2F1 AND POU2F2.
RC TISSUE=Spleen;
RX PubMed=7859290; DOI=10.1016/0092-8674(95)90500-6;
RA Strubin M., Newell J.W., Matthias P.;
RT "OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin
RT promoter activity through association with octamer-binding proteins.";
RL Cell 80:497-506(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood lymphocyte;
RX PubMed=7779176; DOI=10.1038/373360a0;
RA Gstaiger M., Knoepfel L., Georgiev O., Schaffner W., Hovens C.M.;
RT "A B-cell coactivator of octamer-binding transcription factors.";
RL Nature 373:360-362(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION WITH BCL6.
RC TISSUE=Lymphoma;
RX PubMed=8574789;
RA Galiegue-Zouitina S., Quief S., Hildebrand M.-P., Denis C., Lecocq G.,
RA Collyn-D'Hooghe M., Bastard C., Yuille M., Dyer M.J., Kerckaert J.-P.;
RT "Fusion of the LAZ3/BCL6 and BOB1/OBF1 genes by t(3; 11) (q27; q23)
RT chromosomal translocation.";
RL C. R. Acad. Sci. III, Sci. Vie 318:1125-1131(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-27 AND 235-256, AND
RP FUNCTION.
RX PubMed=7623806; DOI=10.1128/mcb.15.8.4115;
RA Luo Y., Roeder R.G.;
RT "Cloning, functional characterization, and mechanism of action of the B-
RT cell-specific transcriptional coactivator OCA-B.";
RL Mol. Cell. Biol. 15:4115-4124(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH SIAH1, AND DEGRADATION.
RX PubMed=11483517; DOI=10.1093/emboj/20.15.4143;
RA Tiedt R., Bartholdy B.A., Matthias G., Newell J.W., Matthias P.;
RT "The RING finger protein Siah-1 regulates the level of the transcriptional
RT coactivator OBF-1.";
RL EMBO J. 20:4143-4152(2001).
RN [9]
RP INTERACTION WITH SIAH1 AND SIAH2, AND DEGRADATION.
RX PubMed=11483518; DOI=10.1093/emboj/20.15.4153;
RA Boehm J., He Y., Greiner A., Staudt L., Wirth T.;
RT "Regulation of BOB.1/OBF.1 stability by SIAH.";
RL EMBO J. 20:4153-4162(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-44 IN COMPLEX WITH OCT1 AND DNA.
RX PubMed=10541551; DOI=10.1101/gad.13.20.2650;
RA Chasman D., Cepek K., Sharp P.A., Pabo C.O.;
RT "Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer
RT DNA complex: specific recognition of a protein-DNA interface.";
RL Genes Dev. 13:2650-2657(1999).
CC -!- FUNCTION: Transcriptional coactivator that specifically associates with
CC either POU2F1/OCT1 or POU2F2/OCT2 (PubMed:7859290). It boosts the
CC POU2F1/OCT1 mediated promoter activity and to a lesser extent, that of
CC POU2F2/OCT2 (PubMed:7779176). It has no intrinsic DNA-binding activity.
CC It recognizes the POU domains of POU2F1/OCT1 and POU2F2/OCT2
CC (PubMed:7779176). It is essential for the response of B-cells to
CC antigens and required for the formation of germinal centers
CC (PubMed:7623806, PubMed:7859290). Regulates IL6 expression in B cells
CC as POU2F2/OCT2 coactivator (By similarity).
CC {ECO:0000250|UniProtKB:Q64693, ECO:0000269|PubMed:7623806,
CC ECO:0000269|PubMed:7779176, ECO:0000269|PubMed:7859290}.
CC -!- SUBUNIT: Interacts with POU2F1/OCT1 and POU2F2/OCT2; the interaction
CC increases POU2F1 and POU2F2 transactivation activity.
CC {ECO:0000269|PubMed:7859290}.
CC -!- INTERACTION:
CC Q16633; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-943588, EBI-744556;
CC Q16633; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-943588, EBI-742953;
CC Q16633; A8MTA8-2: FAM166B; NbExp=3; IntAct=EBI-943588, EBI-12160437;
CC Q16633; O60548: FOXD2; NbExp=3; IntAct=EBI-943588, EBI-17282008;
CC Q16633; Q13227: GPS2; NbExp=3; IntAct=EBI-943588, EBI-713355;
CC Q16633; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-943588, EBI-10329202;
CC Q16633; O14964: HGS; NbExp=5; IntAct=EBI-943588, EBI-740220;
CC Q16633; P31273: HOXC8; NbExp=3; IntAct=EBI-943588, EBI-1752118;
CC Q16633; P31274: HOXC9; NbExp=3; IntAct=EBI-943588, EBI-1779423;
CC Q16633; P16144-2: ITGB4; NbExp=3; IntAct=EBI-943588, EBI-11051601;
CC Q16633; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-943588, EBI-6426443;
CC Q16633; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-943588, EBI-10210845;
CC Q16633; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-943588, EBI-11953846;
CC Q16633; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-943588, EBI-11992140;
CC Q16633; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-943588, EBI-12020132;
CC Q16633; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-943588, EBI-1048945;
CC Q16633; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-943588, EBI-10241353;
CC Q16633; O14770-4: MEIS2; NbExp=3; IntAct=EBI-943588, EBI-8025850;
CC Q16633; Q9BU61: NDUFAF3; NbExp=3; IntAct=EBI-943588, EBI-2114801;
CC Q16633; P32242: OTX1; NbExp=3; IntAct=EBI-943588, EBI-740446;
CC Q16633; Q99697-2: PITX2; NbExp=3; IntAct=EBI-943588, EBI-12138495;
CC Q16633; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-943588, EBI-1389308;
CC Q16633; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-943588, EBI-744023;
CC Q16633; Q9BX46-2: RBM24; NbExp=3; IntAct=EBI-943588, EBI-12224445;
CC Q16633; Q01974: ROR2; NbExp=3; IntAct=EBI-943588, EBI-6422642;
CC Q16633; P57086: SCAND1; NbExp=3; IntAct=EBI-943588, EBI-745846;
CC Q16633; Q8IUQ4: SIAH1; NbExp=2; IntAct=EBI-943588, EBI-747107;
CC Q16633; O95947: TBX6; NbExp=3; IntAct=EBI-943588, EBI-2824328;
CC Q16633; Q96A09: TENT5B; NbExp=3; IntAct=EBI-943588, EBI-752030;
CC Q16633; Q92734: TFG; NbExp=3; IntAct=EBI-943588, EBI-357061;
CC Q16633; O43711: TLX3; NbExp=3; IntAct=EBI-943588, EBI-3939165;
CC Q16633; O75604: USP2; NbExp=3; IntAct=EBI-943588, EBI-743272;
CC Q16633; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-943588, EBI-11957216;
CC Q16633; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-943588, EBI-2559305;
CC Q16633; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-943588, EBI-744257;
CC Q16633; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-943588, EBI-745520;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: B-cell specific (PubMed:7779176, PubMed:7859290).
CC Detected in mainly in spleen, but also in thymus, periphral blood
CC leukocyte and small intestine (PubMed:7779176, PubMed:7859290).
CC {ECO:0000269|PubMed:7779176, ECO:0000269|PubMed:7859290}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000305|PubMed:11483517}.
CC -!- DISEASE: Note=A chromosomal aberration involving POU2AF1/OBF1 may be a
CC cause of a form of B-cell leukemia. Translocation t(3;11)(q27;q23) with
CC BCL6. {ECO:0000269|PubMed:8574789}.
CC -!- SIMILARITY: Belongs to the POU2AF1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/OBFID94.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z47550; CAA87630.1; -; mRNA.
DR EMBL; X83504; CAA58494.1; -; mRNA.
DR EMBL; Z49194; CAA89053.1; -; mRNA.
DR EMBL; AK313573; BAG36346.1; -; mRNA.
DR EMBL; CH471065; EAW67137.1; -; Genomic_DNA.
DR EMBL; BC032549; AAH32549.1; -; mRNA.
DR CCDS; CCDS31675.1; -.
DR PIR; A55652; A55652.
DR RefSeq; NP_006226.2; NM_006235.2.
DR PDB; 1CQT; X-ray; 3.20 A; I/J=1-44.
DR PDBsum; 1CQT; -.
DR AlphaFoldDB; Q16633; -.
DR SMR; Q16633; -.
DR BioGRID; 111446; 84.
DR CORUM; Q16633; -.
DR ELM; Q16633; -.
DR IntAct; Q16633; 50.
DR STRING; 9606.ENSP00000376786; -.
DR GlyGen; Q16633; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16633; -.
DR PhosphoSitePlus; Q16633; -.
DR BioMuta; POU2AF1; -.
DR DMDM; 2833276; -.
DR MassIVE; Q16633; -.
DR MaxQB; Q16633; -.
DR PaxDb; Q16633; -.
DR PeptideAtlas; Q16633; -.
DR PRIDE; Q16633; -.
DR ProteomicsDB; 60982; -.
DR Antibodypedia; 4401; 663 antibodies from 41 providers.
DR DNASU; 5450; -.
DR Ensembl; ENST00000393067.8; ENSP00000376786.3; ENSG00000110777.12.
DR GeneID; 5450; -.
DR KEGG; hsa:5450; -.
DR MANE-Select; ENST00000393067.8; ENSP00000376786.3; NM_006235.3; NP_006226.2.
DR UCSC; uc001plg.5; human.
DR CTD; 5450; -.
DR DisGeNET; 5450; -.
DR GeneCards; POU2AF1; -.
DR HGNC; HGNC:9211; POU2AF1.
DR HPA; ENSG00000110777; Group enriched (intestine, lymphoid tissue, stomach).
DR MalaCards; POU2AF1; -.
DR MIM; 601206; gene.
DR neXtProt; NX_Q16633; -.
DR OpenTargets; ENSG00000110777; -.
DR Orphanet; 186; Primary biliary cholangitis.
DR PharmGKB; PA33535; -.
DR VEuPathDB; HostDB:ENSG00000110777; -.
DR eggNOG; ENOG502R5JD; Eukaryota.
DR GeneTree; ENSGT00390000017499; -.
DR HOGENOM; CLU_095920_0_0_1; -.
DR InParanoid; Q16633; -.
DR OMA; GQPCIDM; -.
DR OrthoDB; 1172888at2759; -.
DR PhylomeDB; Q16633; -.
DR TreeFam; TF332565; -.
DR PathwayCommons; Q16633; -.
DR SignaLink; Q16633; -.
DR SIGNOR; Q16633; -.
DR BioGRID-ORCS; 5450; 25 hits in 1079 CRISPR screens.
DR ChiTaRS; POU2AF1; human.
DR EvolutionaryTrace; Q16633; -.
DR GeneWiki; POU2AF1; -.
DR GenomeRNAi; 5450; -.
DR Pharos; Q16633; Tbio.
DR PRO; PR:Q16633; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q16633; protein.
DR Bgee; ENSG00000110777; Expressed in epithelium of nasopharynx and 150 other tissues.
DR ExpressionAtlas; Q16633; baseline and differential.
DR Genevisible; Q16633; HS.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:CAFA.
DR GO; GO:0003712; F:transcription coregulator activity; TAS:ProtInc.
DR GO; GO:0098586; P:cellular response to virus; ISS:UniProtKB.
DR GO; GO:0002314; P:germinal center B cell differentiation; ISS:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:CAFA.
DR IDEAL; IID00175; -.
DR InterPro; IPR015389; PD-C2-AF1.
DR Pfam; PF09310; PD-C2-AF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosomal rearrangement; Direct protein sequencing;
KW Nucleus; Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..256
FT /note="POU domain class 2-associating factor 1"
FT /id="PRO_0000058018"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 141
FT /note="T -> A (in dbSNP:rs1042750)"
FT /id="VAR_005521"
FT VARIANT 194
FT /note="Q -> R (in dbSNP:rs1042751)"
FT /id="VAR_005522"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:1CQT"
SQ 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
