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Q16633 (OBF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
POU domain class 2-associating factor 1
Alternative name(s):
B-cell-specific coactivator OBF-1
BOB-1
OCA-B
OCT-binding factor 1
Gene names
Name:POU2AF1
Synonyms:OBF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subcellular location

Nucleus.

Tissue specificity

B-cell specific.

Post-translational modification

Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation Probable. Ref.8 Ref.9

Involvement in disease

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.

Sequence similarities

Belongs to the POU2AF1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SIAH1Q8IUQ42EBI-943588,EBI-747107

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256POU domain class 2-associating factor 1
PRO_0000058018

Natural variations

Natural variant1411T → A.
Corresponds to variant rs1042750 [ dbSNP | Ensembl ].
VAR_005521
Natural variant1941Q → R.
Corresponds to variant rs1042751 [ dbSNP | Ensembl ].
VAR_005522

Secondary structure

... 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16633 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2C46F1796774D614

FASTA25627,436
        10         20         30         40         50         60 
MLWQKPTAPE QAPAPARPYQ GVRVKEPVKE LLRRKRGHAS SGAAPAPTAV VLPHQPLATY 

        70         80         90        100        110        120 
TTVGPSCLDM EGSVSAVTEE AALCAGWLSQ PTPATLQPLA PWTPYTEYVP HEAVSCPYSA 

       130        140        150        160        170        180 
DMYVQPVCPS YTVVGPSSVL TYASPPLITN VTTRSSATPA VGPPLEGPEH QAPLTYFPWP 

       190        200        210        220        230        240 
QPLSTLPTST LQYQPPAPAL PGPQFVQLPI SIPEPVLQDM EDPRRAASSL TIDKLLLEEE 

       250 
DSDAYALNHT LSVEGF 

« Hide

References

« Hide 'large scale' references
[1]"OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin promoter activity through association with octamer-binding proteins."
Strubin M., Newell J.W., Matthias P.
Cell 80:497-506(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[2]"A B-cell coactivator of octamer-binding transcription factors."
Gstaiger M., Knoepfel L., Georgiev O., Schaffner W., Hovens C.M.
Nature 373:360-362(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood lymphocyte.
[3]"Fusion of the LAZ3/BCL6 and BOB1/OBF1 genes by t(3; 11) (q27; q23) chromosomal translocation."
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.
C. R. Acad. Sci. III, Sci. Vie 318:1125-1131(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoma.
[4]"Cloning, functional characterization, and mechanism of action of the B-cell-specific transcriptional coactivator OCA-B."
Luo Y., Roeder R.G.
Mol. Cell. Biol. 15:4115-4124(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-27 AND 235-256.
[5]"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].
Tissue: Small intestine.
[6]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].
[7]"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].
Tissue: Lymph.
[8]"The RING finger protein Siah-1 regulates the level of the transcriptional coactivator OBF-1."
Tiedt R., Bartholdy B.A., Matthias G., Newell J.W., Matthias P.
EMBO J. 20:4143-4152(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[9]"Regulation of BOB.1/OBF.1 stability by SIAH."
Boehm J., He Y., Greiner A., Staudt L., Wirth T.
EMBO J. 20:4153-4162(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH1 AND SIAH2, DEGRADATION.
[10]"Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface."
Chasman D., Cepek K., Sharp P.A., Pabo C.O.
Genes Dev. 13:2650-2657(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-44 IN COMPLEX WITH OCT1 AND DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z47550 mRNA. Translation: CAA87630.1.
X83504 mRNA. Translation: CAA58494.1.
Z49194 mRNA. Translation: CAA89053.1.
AK313573 mRNA. Translation: BAG36346.1.
CH471065 Genomic DNA. Translation: EAW67137.1.
BC032549 mRNA. Translation: AAH32549.1.
PIRA55652.
RefSeqNP_006226.2. NM_006235.2.
UniGeneHs.654525.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQTX-ray3.20I/J1-44[»]
DisProtDP00172.
ProteinModelPortalQ16633.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111446. 11 interactions.
IntActQ16633. 3 interactions.
MINTMINT-206323.
STRING9606.ENSP00000228217.

PTM databases

PhosphoSiteQ16633.

Polymorphism databases

DMDM2833276.

Proteomic databases

PRIDEQ16633.

Protocols and materials databases

DNASU5450.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393067; ENSP00000376786; ENSG00000110777.
GeneID5450.
KEGGhsa:5450.
UCSCuc001plg.4. human.

Organism-specific databases

CTD5450.
GeneCardsGC11M111222.
HGNCHGNC:9211. POU2AF1.
HPACAB011193.
MIM601206. gene.
neXtProtNX_Q16633.
Orphanet186. Primary biliary cirrhosis.
PharmGKBPA33535.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80789.
HOGENOMHOG000059584.
HOVERGENHBG007859.
InParanoidQ16633.
OMACLDMEGS.
OrthoDBEOG7JDQZ9.
PhylomeDBQ16633.
TreeFamTF332565.

Gene expression databases

ArrayExpressQ16633.
BgeeQ16633.
CleanExHS_POU2AF1.
GenevestigatorQ16633.

Family and domain databases

InterProIPR015389. PD-C2-AF1.
[Graphical view]
PfamPF09310. PD-C2-AF1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16633.
GeneWikiPOU2AF1.
GenomeRNAi5450.
NextBio21093.
PROQ16633.
SOURCESearch...

Entry information

Entry nameOBF1_HUMAN
AccessionPrimary (citable) accession number: Q16633
Secondary accession number(s): B2R8Z9, Q14983
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 124 of the entry and version 1 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 11

Human chromosome 11: entries, gene names and cross-references to MIM