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Q16633

- OBF1_HUMAN

UniProt

Q16633 - OBF1_HUMAN

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Protein

POU domain class 2-associating factor 1

Gene
POU2AF1, OBF1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. DNA binding Source: Ensembl
  2. protein binding Source: IntAct
  3. transcription coactivator activity Source: ProtInc
  4. transcription cofactor activity Source: ProtInc

GO - Biological processi

  1. humoral immune response Source: ProtInc
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:POU2AF1
Synonyms:OBF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9211. POU2AF1.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti186. Primary biliary cirrhosis.
PharmGKBiPA33535.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256POU domain class 2-associating factor 1PRO_0000058018Add
BLAST

Post-translational modificationi

Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation Inferred.2 Publications

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ16633.
PRIDEiQ16633.

PTM databases

PhosphoSiteiQ16633.

Expressioni

Tissue specificityi

B-cell specific.

Gene expression databases

ArrayExpressiQ16633.
BgeeiQ16633.
CleanExiHS_POU2AF1.
GenevestigatoriQ16633.

Organism-specific databases

HPAiCAB011193.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SIAH1Q8IUQ42EBI-943588,EBI-747107

Protein-protein interaction databases

BioGridi111446. 11 interactions.
IntActiQ16633. 3 interactions.
MINTiMINT-206323.
STRINGi9606.ENSP00000228217.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 347

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQTX-ray3.20I/J1-44[»]
DisProtiDP00172.
ProteinModelPortaliQ16633.

Miscellaneous databases

EvolutionaryTraceiQ16633.

Family & Domainsi

Sequence similaritiesi

Belongs to the POU2AF1 family.

Phylogenomic databases

eggNOGiNOG80789.
HOGENOMiHOG000059584.
HOVERGENiHBG007859.
InParanoidiQ16633.
OMAiCLDMEGS.
OrthoDBiEOG7JDQZ9.
PhylomeDBiQ16633.
TreeFamiTF332565.

Family and domain databases

InterProiIPR015389. PD-C2-AF1.
[Graphical view]
PfamiPF09310. PD-C2-AF1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16633-1 [UniParc]FASTAAdd to Basket

« Hide

MLWQKPTAPE QAPAPARPYQ GVRVKEPVKE LLRRKRGHAS SGAAPAPTAV    50
VLPHQPLATY TTVGPSCLDM EGSVSAVTEE AALCAGWLSQ PTPATLQPLA 100
PWTPYTEYVP HEAVSCPYSA DMYVQPVCPS YTVVGPSSVL TYASPPLITN 150
VTTRSSATPA VGPPLEGPEH QAPLTYFPWP QPLSTLPTST LQYQPPAPAL 200
PGPQFVQLPI SIPEPVLQDM EDPRRAASSL TIDKLLLEEE DSDAYALNHT 250
LSVEGF 256
Length:256
Mass (Da):27,436
Last modified:November 1, 1996 - v1
Checksum:i2C46F1796774D614
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411T → A.
Corresponds to variant rs1042750 [ dbSNP | Ensembl ].
VAR_005521
Natural varianti194 – 1941Q → R.
Corresponds to variant rs1042751 [ dbSNP | Ensembl ].
VAR_005522

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31675.1.
PIRiA55652.
RefSeqiNP_006226.2. NM_006235.2.
UniGeneiHs.654525.

Genome annotation databases

EnsembliENST00000393067; ENSP00000376786; ENSG00000110777.
GeneIDi5450.
KEGGihsa:5450.
UCSCiuc001plg.4. human.

Polymorphism databases

DMDMi2833276.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31675.1.
PIRi A55652.
RefSeqi NP_006226.2. NM_006235.2.
UniGenei Hs.654525.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CQT X-ray 3.20 I/J 1-44 [» ]
DisProti DP00172.
ProteinModelPortali Q16633.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111446. 11 interactions.
IntActi Q16633. 3 interactions.
MINTi MINT-206323.
STRINGi 9606.ENSP00000228217.

PTM databases

PhosphoSitei Q16633.

Polymorphism databases

DMDMi 2833276.

Proteomic databases

MaxQBi Q16633.
PRIDEi Q16633.

Protocols and materials databases

DNASUi 5450.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000393067 ; ENSP00000376786 ; ENSG00000110777 .
GeneIDi 5450.
KEGGi hsa:5450.
UCSCi uc001plg.4. human.

Organism-specific databases

CTDi 5450.
GeneCardsi GC11M111222.
HGNCi HGNC:9211. POU2AF1.
HPAi CAB011193.
MIMi 601206. gene.
neXtProti NX_Q16633.
Orphaneti 186. Primary biliary cirrhosis.
PharmGKBi PA33535.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80789.
HOGENOMi HOG000059584.
HOVERGENi HBG007859.
InParanoidi Q16633.
OMAi CLDMEGS.
OrthoDBi EOG7JDQZ9.
PhylomeDBi Q16633.
TreeFami TF332565.

Miscellaneous databases

EvolutionaryTracei Q16633.
GeneWikii POU2AF1.
GenomeRNAii 5450.
NextBioi 21093.
PROi Q16633.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16633.
Bgeei Q16633.
CleanExi HS_POU2AF1.
Genevestigatori Q16633.

Family and domain databases

InterProi IPR015389. PD-C2-AF1.
[Graphical view ]
Pfami PF09310. PD-C2-AF1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiOBF1_HUMAN
AccessioniPrimary (citable) accession number: Q16633
Secondary accession number(s): B2R8Z9, Q14983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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