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Transcription factor Spi-B

 SPIB_HUMAN              Reviewed;         262 AA.
Q01892; A8K9C9; B4DUG6; Q15359;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
23-MAY-2018, entry version 166.
RecName: Full=Transcription factor Spi-B;
Name=SPIB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=1406622; DOI=10.1128/MCB.12.10.4297;
Ray D., Bosselut R., Ghysdael J., Mattei M.-G., Tavitian A.,
Moreau-Gachelin F.;
"Characterization of Spi-B, a transcription factor related to the
putative oncoprotein Spi-1/PU.1.";
Mol. Cell. Biol. 12:4297-4304(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8670269; DOI=10.1006/bbrc.1996.0881;
Ray-Gallet D., Tavitian A., Moreau-Gachelin F.;
"An alternatively spliced isoform of the Spi-B transcription factor.";
Biochem. Biophys. Res. Commun. 223:257-263(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
PRO-104.
TISSUE=Rectum, and Thymus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell;
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).
[7]
FUNCTION, INTERACTION WITH IRF4; JUN; SPIB; SPI1 AND TBP, DOMAINS
PEST; TAD1 AND TAD2, AND MUTAGENESIS OF SER-144 AND LYS-242.
PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
Rao S., Matsumura A., Yoon J., Simon M.C.;
"SPI-B activates transcription via a unique proline, serine, and
threonine domain and exhibits DNA binding affinity differences from
PU.1.";
J. Biol. Chem. 274:11115-11124(1999).
[8]
TISSUE SPECIFICITY.
PubMed=11841448; DOI=10.1046/j.1365-2141.2002.03271.x;
Nagy M., Chapuis B., Matthes T.;
"Expression of transcription factors Pu.1, Spi-B, Blimp-1, BSAP and
oct-2 in normal human plasma cells and in multiple myeloma cells.";
Br. J. Haematol. 116:429-435(2002).
[9]
INTERACTION WITH CREBBP AND EP300.
PubMed=11864910;
Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T.,
Oikawa T.;
"Interaction between the hematopoietic Ets transcription factor Spi-B
and the coactivator CREB-binding protein associated with negative
cross-talk with c-Myb.";
Cell Growth Differ. 13:69-75(2002).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12393575; DOI=10.1182/blood-2002-02-0438;
Schotte R., Rissoan M.-C., Bendriss-Vermare N., Bridon J.-M.,
Duhen T., Weijer K., Briere F., Spits H.;
"The transcription factor Spi-B is expressed in plasmacytoid DC
precursors and inhibits T-, B-, and NK-cell development.";
Blood 101:1015-1023(2003).
[11]
FUNCTION.
PubMed=15583020; DOI=10.1084/jem.20041231;
Schotte R., Nagasawa M., Weijer K., Spits H., Blom B.;
"The ETS transcription factor Spi-B is required for human plasmacytoid
dendritic cell development.";
J. Exp. Med. 200:1503-1509(2004).
-!- FUNCTION: Sequence specific transcriptional activator which binds
to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can
act as a lymphoid-specific enhancer. Promotes development of
plasmacytoid dendritic cells (pDCs), also known as type 2 DC
precursors (pre-DC2) or natural interferon (IFN)-producing cells.
These cells have the capacity to produce large amounts of
interferon and block viral replication. May be required for B-cell
receptor (BCR) signaling, which is necessary for normal B-cell
development and antigenic stimulation.
{ECO:0000269|PubMed:10196196, ECO:0000269|PubMed:12393575,
ECO:0000269|PubMed:1406622, ECO:0000269|PubMed:15583020}.
-!- SUBUNIT: Can form homotypic interactions. Interacts with IRF4. May
also interact with CREBBP, EP300, SPI1/PU.1 related, JUN and TBP.
{ECO:0000269|PubMed:10196196, ECO:0000269|PubMed:11864910}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus
{ECO:0000269|PubMed:12393575}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:12393575}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q01892-1; Sequence=Displayed;
Name=2; Synonyms=DeltaSpi-B;
IsoId=Q01892-2; Sequence=VSP_001479, VSP_001480;
Name=3;
IsoId=Q01892-3; Sequence=VSP_045124, VSP_045125;
-!- TISSUE SPECIFICITY: Expressed in plasmacytoid dendritic cells
(pDCs) and B-cells, not expressed in T-cells or granulocytes. May
also be enriched in stem cell populations of the liver.
{ECO:0000269|PubMed:11841448, ECO:0000269|PubMed:12393575}.
-!- DOMAIN: The protein contains a weakly acidic N-terminal
transactivation domain (TAD) followed by a second TAD rich in
proline, serine and threonine. Each of these domains may be
required for transcriptional activation of a subset of target
genes. {ECO:0000269|PubMed:10196196}.
-!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X66079; CAA46878.1; -; mRNA.
EMBL; X96998; CAA65726.1; -; mRNA.
EMBL; AK292644; BAF85333.1; -; mRNA.
EMBL; AK300639; BAG62328.1; -; mRNA.
EMBL; AC020909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW71858.1; -; Genomic_DNA.
EMBL; BC007921; AAH07921.1; -; mRNA.
CCDS; CCDS33080.1; -. [Q01892-1]
CCDS; CCDS58674.1; -. [Q01892-3]
CCDS; CCDS59412.1; -. [Q01892-2]
PIR; JC4839; JC4839.
PIR; S25655; S25655.
RefSeq; NP_001230927.1; NM_001243998.1. [Q01892-3]
RefSeq; NP_001230928.1; NM_001243999.1. [Q01892-2]
RefSeq; NP_001230929.1; NM_001244000.1.
RefSeq; NP_003112.2; NM_003121.4. [Q01892-1]
UniGene; Hs.437905; -.
ProteinModelPortal; Q01892; -.
SMR; Q01892; -.
BioGrid; 112567; 16.
IntAct; Q01892; 3.
STRING; 9606.ENSP00000471921; -.
iPTMnet; Q01892; -.
BioMuta; SPIB; -.
DMDM; 548971; -.
MaxQB; Q01892; -.
PaxDb; Q01892; -.
PeptideAtlas; Q01892; -.
PRIDE; Q01892; -.
DNASU; 6689; -.
Ensembl; ENST00000270632; ENSP00000270632; ENSG00000269404. [Q01892-2]
Ensembl; ENST00000439922; ENSP00000391877; ENSG00000269404. [Q01892-3]
Ensembl; ENST00000595883; ENSP00000471921; ENSG00000269404. [Q01892-1]
GeneID; 6689; -.
KEGG; hsa:6689; -.
UCSC; uc002psd.4; human. [Q01892-1]
CTD; 6689; -.
DisGeNET; 6689; -.
EuPathDB; HostDB:ENSG00000269404.6; -.
GeneCards; SPIB; -.
HGNC; HGNC:11242; SPIB.
HPA; HPA018523; -.
MalaCards; SPIB; -.
MIM; 606802; gene.
neXtProt; NX_Q01892; -.
OpenTargets; ENSG00000269404; -.
Orphanet; 186; Primary biliary cirrhosis.
PharmGKB; PA36072; -.
eggNOG; KOG3805; Eukaryota.
eggNOG; ENOG410XSXU; LUCA.
GeneTree; ENSGT00390000015212; -.
HOGENOM; HOG000095520; -.
HOVERGEN; HBG002474; -.
InParanoid; Q01892; -.
KO; K09439; -.
OrthoDB; EOG091G0DTY; -.
PhylomeDB; Q01892; -.
TreeFam; TF352494; -.
SignaLink; Q01892; -.
SIGNOR; Q01892; -.
GeneWiki; SPIB; -.
GenomeRNAi; 6689; -.
PRO; PR:Q01892; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000269404; -.
CleanEx; HS_SPIB; -.
ExpressionAtlas; Q01892; baseline and differential.
Genevisible; Q01892; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000418; Ets_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00178; Ets; 1.
PRINTS; PR00454; ETSDOMAIN.
SMART; SM00413; ETS; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00345; ETS_DOMAIN_1; 1.
PROSITE; PS00346; ETS_DOMAIN_2; 1.
PROSITE; PS50061; ETS_DOMAIN_3; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Cytoplasm;
DNA-binding; Nucleus; Polymorphism; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 262 Transcription factor Spi-B.
/FTId=PRO_0000204136.
DNA_BIND 169 252 ETS. {ECO:0000255|PROSITE-
ProRule:PRU00237}.
REGION 1 31 TAD1 (Acidic).
REGION 41 61 TAD2.
VAR_SEQ 1 91 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045124.
VAR_SEQ 92 113 APSLEAPGPGLPAYPTENFASQ -> MASSMTWTAASIPAT
LIQRGLL (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045125.
VAR_SEQ 163 177 AGTRKKLRLYQFLLG -> GLARSCACTSSCWGY (in
isoform 2). {ECO:0000303|PubMed:8670269}.
/FTId=VSP_001479.
VAR_SEQ 178 262 Missing (in isoform 2).
{ECO:0000303|PubMed:8670269}.
/FTId=VSP_001480.
VARIANT 104 104 A -> P (in dbSNP:rs11546996).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_061150.
MUTAGEN 144 144 S->A: Reduces interaction with IRF4 and
transcriptional activation.
{ECO:0000269|PubMed:10196196}.
MUTAGEN 242 242 K->G: Abrogates DNA-binding.
{ECO:0000269|PubMed:10196196}.
SEQUENCE 262 AA; 28819 MW; A6C21DA1BBF61B6F CRC64;
MLALEAAQLD GPHFSCLYPD GVFYDLDSCK HSSYPDSEGA PDSLWDWTVA PPVPATPYEA
FDPAAAAFSH PQAAQLCYEP PTYSPAGNLE LAPSLEAPGP GLPAYPTENF ASQTLVPPAY
APYPSPVLSE EEDLPLDSPA LEVSDSESDE ALVAGPEGKG SEAGTRKKLR LYQFLLGLLT
RGDMRECVWW VEPGAGVFQF SSKHKELLAR RWGQQKGNRK RMTYQKLARA LRNYAKTGEI
RKVKRKLTYQ FDSALLPAVR RA


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