SPIB_HUMAN
ID SPIB_HUMAN Reviewed; 262 AA.
AC Q01892; A8K9C9; B4DUG6; Q15359;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transcription factor Spi-B;
GN Name=SPIB;
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] (ISOFORM 1), AND FUNCTION.
RX PubMed=1406622; DOI=10.1128/mcb.12.10.4297-4304.1992;
RA Ray D., Bosselut R., Ghysdael J., Mattei M.-G., Tavitian A.,
RA Moreau-Gachelin F.;
RT "Characterization of Spi-B, a transcription factor related to the putative
RT oncoprotein Spi-1/PU.1.";
RL Mol. Cell. Biol. 12:4297-4304(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8670269; DOI=10.1006/bbrc.1996.0881;
RA Ray-Gallet D., Tavitian A., Moreau-Gachelin F.;
RT "An alternatively spliced isoform of the Spi-B transcription factor.";
RL Biochem. Biophys. Res. Commun. 223:257-263(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PRO-104.
RC TISSUE=Rectum, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
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 [7]
RP FUNCTION, INTERACTION WITH IRF4; JUN; SPIB; SPI1 AND TBP, DOMAINS PEST;
RP TAD1 AND TAD2, AND MUTAGENESIS OF SER-144 AND LYS-242.
RX PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
RA Rao S., Matsumura A., Yoon J., Simon M.C.;
RT "SPI-B activates transcription via a unique proline, serine, and threonine
RT domain and exhibits DNA binding affinity differences from PU.1.";
RL J. Biol. Chem. 274:11115-11124(1999).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11841448; DOI=10.1046/j.1365-2141.2002.03271.x;
RA Nagy M., Chapuis B., Matthes T.;
RT "Expression of transcription factors Pu.1, Spi-B, Blimp-1, BSAP and oct-2
RT in normal human plasma cells and in multiple myeloma cells.";
RL Br. J. Haematol. 116:429-435(2002).
RN [9]
RP INTERACTION WITH CREBBP AND EP300.
RX PubMed=11864910;
RA Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T., Oikawa T.;
RT "Interaction between the hematopoietic Ets transcription factor Spi-B and
RT the coactivator CREB-binding protein associated with negative cross-talk
RT with c-Myb.";
RL Cell Growth Differ. 13:69-75(2002).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12393575; DOI=10.1182/blood-2002-02-0438;
RA Schotte R., Rissoan M.-C., Bendriss-Vermare N., Bridon J.-M., Duhen T.,
RA Weijer K., Briere F., Spits H.;
RT "The transcription factor Spi-B is expressed in plasmacytoid DC precursors
RT and inhibits T-, B-, and NK-cell development.";
RL Blood 101:1015-1023(2003).
RN [11]
RP FUNCTION.
RX PubMed=15583020; DOI=10.1084/jem.20041231;
RA Schotte R., Nagasawa M., Weijer K., Spits H., Blom B.;
RT "The ETS transcription factor Spi-B is required for human plasmacytoid
RT dendritic cell development.";
RL J. Exp. Med. 200:1503-1509(2004).
CC -!- FUNCTION: Sequence specific transcriptional activator which binds to
CC the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a
CC lymphoid-specific enhancer. Promotes development of plasmacytoid
CC dendritic cells (pDCs), also known as type 2 DC precursors (pre-DC2) or
CC natural interferon (IFN)-producing cells. These cells have the capacity
CC to produce large amounts of interferon and block viral replication. May
CC be required for B-cell receptor (BCR) signaling, which is necessary for
CC normal B-cell development and antigenic stimulation.
CC {ECO:0000269|PubMed:10196196, ECO:0000269|PubMed:12393575,
CC ECO:0000269|PubMed:1406622, ECO:0000269|PubMed:15583020}.
CC -!- SUBUNIT: Can form homotypic interactions. Interacts with IRF4. May also
CC interact with CREBBP, EP300, SPI1/PU.1 related, JUN and TBP.
CC {ECO:0000269|PubMed:10196196, ECO:0000269|PubMed:11864910}.
CC -!- INTERACTION:
CC Q01892; P42858: HTT; NbExp=18; IntAct=EBI-2800992, EBI-466029;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:12393575}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:12393575}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q01892-1; Sequence=Displayed;
CC Name=2; Synonyms=DeltaSpi-B;
CC IsoId=Q01892-2; Sequence=VSP_001479, VSP_001480;
CC Name=3;
CC IsoId=Q01892-3; Sequence=VSP_045124, VSP_045125;
CC -!- TISSUE SPECIFICITY: Expressed in plasmacytoid dendritic cells (pDCs)
CC and B-cells, not expressed in T-cells or granulocytes. May also be
CC enriched in stem cell populations of the liver.
CC {ECO:0000269|PubMed:11841448, ECO:0000269|PubMed:12393575}.
CC -!- DOMAIN: The protein contains a weakly acidic N-terminal transactivation
CC domain (TAD) followed by a second TAD rich in proline, serine and
CC threonine. Each of these domains may be required for transcriptional
CC activation of a subset of target genes. {ECO:0000269|PubMed:10196196}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; X66079; CAA46878.1; -; mRNA.
DR EMBL; X96998; CAA65726.1; -; mRNA.
DR EMBL; AK292644; BAF85333.1; -; mRNA.
DR EMBL; AK300639; BAG62328.1; -; mRNA.
DR EMBL; AC020909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW71858.1; -; Genomic_DNA.
DR EMBL; BC007921; AAH07921.1; -; mRNA.
DR CCDS; CCDS33080.1; -. [Q01892-1]
DR CCDS; CCDS58674.1; -. [Q01892-3]
DR CCDS; CCDS59412.1; -. [Q01892-2]
DR PIR; JC4839; JC4839.
DR PIR; S25655; S25655.
DR RefSeq; NP_001230927.1; NM_001243998.1. [Q01892-3]
DR RefSeq; NP_001230928.1; NM_001243999.1. [Q01892-2]
DR RefSeq; NP_001230929.1; NM_001244000.1.
DR RefSeq; NP_003112.2; NM_003121.4. [Q01892-1]
DR AlphaFoldDB; Q01892; -.
DR SMR; Q01892; -.
DR BioGRID; 112567; 16.
DR IntAct; Q01892; 7.
DR STRING; 9606.ENSP00000471921; -.
DR iPTMnet; Q01892; -.
DR BioMuta; SPIB; -.
DR DMDM; 548971; -.
DR MassIVE; Q01892; -.
DR MaxQB; Q01892; -.
DR PaxDb; Q01892; -.
DR PeptideAtlas; Q01892; -.
DR PRIDE; Q01892; -.
DR ProteomicsDB; 5187; -.
DR ProteomicsDB; 58013; -. [Q01892-1]
DR Antibodypedia; 71687; 194 antibodies from 29 providers.
DR DNASU; 6689; -.
DR Ensembl; ENST00000270632.7; ENSP00000270632.7; ENSG00000269404.7. [Q01892-2]
DR Ensembl; ENST00000439922.6; ENSP00000391877.2; ENSG00000269404.7. [Q01892-3]
DR Ensembl; ENST00000595883.6; ENSP00000471921.1; ENSG00000269404.7. [Q01892-1]
DR GeneID; 6689; -.
DR KEGG; hsa:6689; -.
DR MANE-Select; ENST00000595883.6; ENSP00000471921.1; NM_003121.5; NP_003112.2.
DR UCSC; uc002psd.4; human. [Q01892-1]
DR CTD; 6689; -.
DR DisGeNET; 6689; -.
DR GeneCards; SPIB; -.
DR HGNC; HGNC:11242; SPIB.
DR HPA; ENSG00000269404; Group enriched (intestine, lymphoid tissue).
DR MalaCards; SPIB; -.
DR MIM; 606802; gene.
DR neXtProt; NX_Q01892; -.
DR OpenTargets; ENSG00000269404; -.
DR Orphanet; 186; Primary biliary cholangitis.
DR PharmGKB; PA36072; -.
DR VEuPathDB; HostDB:ENSG00000269404; -.
DR eggNOG; KOG3805; Eukaryota.
DR GeneTree; ENSGT00940000162754; -.
DR HOGENOM; CLU_066451_2_0_1; -.
DR InParanoid; Q01892; -.
DR OMA; CKHPSYP; -.
DR PhylomeDB; Q01892; -.
DR TreeFam; TF352494; -.
DR PathwayCommons; Q01892; -.
DR SignaLink; Q01892; -.
DR SIGNOR; Q01892; -.
DR BioGRID-ORCS; 6689; 15 hits in 1091 CRISPR screens.
DR ChiTaRS; SPIB; human.
DR GeneWiki; SPIB; -.
DR GenomeRNAi; 6689; -.
DR Pharos; Q01892; Tbio.
DR PRO; PR:Q01892; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q01892; protein.
DR Bgee; ENSG00000269404; Expressed in lymph node and 131 other tissues.
DR ExpressionAtlas; Q01892; baseline and differential.
DR Genevisible; Q01892; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..262
FT /note="Transcription factor Spi-B"
FT /id="PRO_0000204136"
FT DNA_BIND 169..252
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 1..31
FT /note="TAD1 (Acidic)"
FT REGION 41..61
FT /note="TAD2"
FT REGION 140..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045124"
FT VAR_SEQ 92..113
FT /note="APSLEAPGPGLPAYPTENFASQ -> MASSMTWTAASIPATLIQRGLL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045125"
FT VAR_SEQ 163..177
FT /note="AGTRKKLRLYQFLLG -> GLARSCACTSSCWGY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8670269"
FT /id="VSP_001479"
FT VAR_SEQ 178..262
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8670269"
FT /id="VSP_001480"
FT VARIANT 104
FT /note="A -> P (in dbSNP:rs11546996)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061150"
FT MUTAGEN 144
FT /note="S->A: Reduces interaction with IRF4 and
FT transcriptional activation."
FT /evidence="ECO:0000269|PubMed:10196196"
FT MUTAGEN 242
FT /note="K->G: Abrogates DNA-binding."
FT /evidence="ECO:0000269|PubMed:10196196"
SQ 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
