GenomeNet

Database: UniProt
Entry: O95238
LinkDB: O95238
Original site: O95238 
ID   SPDEF_HUMAN             Reviewed;         335 AA.
AC   O95238; B4DWH8; F5H778;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   07-OCT-2020, entry version 181.
DE   RecName: Full=SAM pointed domain-containing Ets transcription factor;
DE   AltName: Full=Prostate epithelium-specific Ets transcription factor;
DE            Short=Prostate-specific Ets;
DE   AltName: Full=Prostate-derived Ets factor;
GN   Name=SPDEF; Synonyms=PDEF, PSE;
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).
RC   TISSUE=Prostatic carcinoma;
RX   PubMed=10675039; DOI=10.1016/s0378-1119(99)00484-9;
RA   Yamada N., Tamai Y., Miyamoto H., Nozaki M.;
RT   "Cloning and expression of the mouse Pse gene encoding a novel Ets family
RT   member.";
RL   Gene 241:267-274(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH AR.
RC   TISSUE=Prostate;
RX   PubMed=10625666; DOI=10.1074/jbc.275.2.1216;
RA   Oettgen P., Finger E., Sun Z., Akbarali Y., Thamrongsak U., Boltax J.,
RA   Grall F., Dube A., Weiss A., Brown L., Quinn G., Kas K., Endress G.,
RA   Kunsch C., Libermann T.A.;
RT   "PDEF, a novel prostate epithelium-specific ets transcription factor,
RT   interacts with the androgen receptor and activates prostate-specific
RT   antigen gene expression.";
RL   J. Biol. Chem. 275:1216-1225(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary gland;
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=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
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   [6]
RP   INTERACTION WITH NKX3-1.
RX   PubMed=11809674;
RA   Chen H., Nandi A.K., Li X., Bieberich C.J.;
RT   "NKX-3.1 interacts with prostate-derived Ets factor and regulates the
RT   activity of the PSA promoter.";
RL   Cancer Res. 62:338-340(2002).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 247-335 IN COMPLEX WITH DNA.
RX   PubMed=15882048; DOI=10.1021/bi047352t;
RA   Wang Y., Feng L., Said M., Balderman S., Fayazi Z., Liu Y., Ghosh D.,
RA   Gulick A.M.;
RT   "Analysis of the 2.0 A crystal structure of the protein-DNA complex of the
RT   human PDEF Ets domain bound to the prostate specific antigen regulatory
RT   site.";
RL   Biochemistry 44:7095-7106(2005).
RN   [8]
RP   STRUCTURE BY NMR OF 131-213.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SAM_pnt-domain of ETS transcription factor PDEF
RT   (prostate Ets).";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: May function as an androgen-independent transactivator of the
CC       prostate-specific antigen (PSA) promoter. Binds to 5'-GGAT-3' DNA
CC       sequences. May play a role in the regulation of the prostate gland
CC       and/or prostate cancer development. Acts as a transcriptional activator
CC       for SERPINB5 promoter. {ECO:0000269|PubMed:10625666}.
CC   -!- SUBUNIT: Interacts with the DNA-binding domain of the androgen
CC       receptor. Interacts with NKX3-1. {ECO:0000269|PubMed:10625666,
CC       ECO:0000269|PubMed:11809674, ECO:0000269|PubMed:15882048}.
CC   -!- INTERACTION:
CC       O95238; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-12811275, EBI-11752486;
CC       O95238; P20674: COX5A; NbExp=3; IntAct=EBI-12811275, EBI-715032;
CC       O95238; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-12811275, EBI-744099;
CC       O95238; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-12811275, EBI-7225287;
CC       O95238; P25786: PSMA1; NbExp=3; IntAct=EBI-12811275, EBI-359352;
CC       O95238; Q7Z614-3: SNX20; NbExp=3; IntAct=EBI-12811275, EBI-12336127;
CC       O95238; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-12811275, EBI-9090990;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O95238-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95238-2; Sequence=VSP_044722;
CC   -!- TISSUE SPECIFICITY: Expressed in a very restricted set of primarily
CC       hormone-regulated epithelial tissues with particularly high expression
CC       in the prostate gland. Significantly lower expression is seen in other
CC       hormone regulated tissues such as mammary gland, salivary gland, and
CC       ovary. Expressed in prostate carcinoma cells.
CC       {ECO:0000269|PubMed:10625666}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
DR   EMBL; AB031549; BAA89543.1; -; mRNA.
DR   EMBL; AF071538; AAC95296.1; -; mRNA.
DR   EMBL; AK301543; BAG63040.1; -; mRNA.
DR   EMBL; BX255971; CAI23605.1; -; Genomic_DNA.
DR   EMBL; AL157372; CAI23605.1; JOINED; Genomic_DNA.
DR   EMBL; BX255972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX255973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021299; AAH21299.1; -; mRNA.
DR   CCDS; CCDS4794.1; -. [O95238-1]
DR   CCDS; CCDS59013.1; -. [O95238-2]
DR   RefSeq; NP_001239223.1; NM_001252294.1. [O95238-2]
DR   RefSeq; NP_036523.1; NM_012391.2. [O95238-1]
DR   PDB; 1YO5; X-ray; 2.00 A; C=247-335.
DR   PDB; 2DKX; NMR; -; A=131-213.
DR   PDBsum; 1YO5; -.
DR   PDBsum; 2DKX; -.
DR   SMR; O95238; -.
DR   BioGRID; 117335; 24.
DR   IntAct; O95238; 17.
DR   STRING; 9606.ENSP00000363149; -.
DR   iPTMnet; O95238; -.
DR   PhosphoSitePlus; O95238; -.
DR   BioMuta; SPDEF; -.
DR   EPD; O95238; -.
DR   MassIVE; O95238; -.
DR   MaxQB; O95238; -.
DR   PaxDb; O95238; -.
DR   PeptideAtlas; O95238; -.
DR   PRIDE; O95238; -.
DR   ProteomicsDB; 27406; -.
DR   ProteomicsDB; 50737; -. [O95238-1]
DR   Antibodypedia; 15077; 217 antibodies.
DR   DNASU; 25803; -.
DR   Ensembl; ENST00000374037; ENSP00000363149; ENSG00000124664. [O95238-1]
DR   Ensembl; ENST00000544425; ENSP00000442715; ENSG00000124664. [O95238-2]
DR   GeneID; 25803; -.
DR   KEGG; hsa:25803; -.
DR   UCSC; uc003ojq.3; human. [O95238-1]
DR   CTD; 25803; -.
DR   DisGeNET; 25803; -.
DR   EuPathDB; HostDB:ENSG00000124664.10; -.
DR   GeneCards; SPDEF; -.
DR   HGNC; HGNC:17257; SPDEF.
DR   HPA; ENSG00000124664; Tissue enhanced (prostate, salivary gland).
DR   MIM; 608144; gene.
DR   neXtProt; NX_O95238; -.
DR   OpenTargets; ENSG00000124664; -.
DR   PharmGKB; PA134993886; -.
DR   eggNOG; KOG3805; Eukaryota.
DR   GeneTree; ENSGT00940000157549; -.
DR   HOGENOM; CLU_877059_0_0_1; -.
DR   InParanoid; O95238; -.
DR   KO; K09442; -.
DR   OMA; CFDMLLT; -.
DR   OrthoDB; 908495at2759; -.
DR   PhylomeDB; O95238; -.
DR   TreeFam; TF318679; -.
DR   PathwayCommons; O95238; -.
DR   SIGNOR; O95238; -.
DR   BioGRID-ORCS; 25803; 25 hits in 893 CRISPR screens.
DR   ChiTaRS; SPDEF; human.
DR   EvolutionaryTrace; O95238; -.
DR   GeneWiki; SPDEF; -.
DR   GenomeRNAi; 25803; -.
DR   Pharos; O95238; Tbio.
DR   PRO; PR:O95238; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O95238; protein.
DR   Bgee; ENSG00000124664; Expressed in prostate gland and 138 other tissues.
DR   Genevisible; O95238; HS.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA: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:0060576; P:intestinal epithelial cell development; IEA:Ensembl.
DR   GO; GO:0060480; P:lung goblet cell differentiation; IEA:Ensembl.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0010454; P:negative regulation of cell fate commitment; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:BHF-UCL.
DR   GO; GO:0010455; P:positive regulation of cell fate commitment; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus;
KW   Polymorphism; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..335
FT                   /note="SAM pointed domain-containing Ets transcription
FT                   factor"
FT                   /id="PRO_0000223958"
FT   DOMAIN          129..213
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        249..332
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   VAR_SEQ         212..227
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044722"
FT   VARIANT         57
FT                   /note="A -> T (in dbSNP:rs2233639)"
FT                   /id="VAR_048955"
FT   CONFLICT        49
FT                   /note="A -> G (in Ref. 3; BAG63040)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="K -> N (in Ref. 3; BAG63040)"
FT                   /evidence="ECO:0000305"
FT   HELIX           132..139
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   TURN            140..142
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   HELIX           147..149
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   HELIX           155..165
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   HELIX           172..175
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   HELIX           180..185
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   HELIX           188..194
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   STRAND          196..198
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   HELIX           200..213
FT                   /evidence="ECO:0000244|PDB:2DKX"
FT   HELIX           251..260
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   HELIX           262..265
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   TURN            266..268
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   STRAND          269..273
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   TURN            274..277
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   STRAND          278..282
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   HELIX           284..295
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   HELIX           302..311
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   TURN            312..316
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   STRAND          317..319
FT                   /evidence="ECO:0000244|PDB:1YO5"
FT   STRAND          328..332
FT                   /evidence="ECO:0000244|PDB:1YO5"
SQ   SEQUENCE   335 AA;  37518 MW;  D3117E1AEEBA95EC CRC64;
     MGSASPGLSS VSPSHLLLPP DTVSRTGLEK AAAGAVGLER RDWSPSPPAT PEQGLSAFYL
     SYFDMLYPED SSWAAKAPGA SSREEPPEEP EQCPVIDSQA PAGSLDLVPG GLTLEEHSLE
     QVQSMVVGEV LKDIETACKL LNITADPMDW SPSNVQKWLL WTEHQYRLPP MGKAFQELAG
     KELCAMSEEQ FRQRSPLGGD VLHAHLDIWK SAAWMKERTS PGAIHYCAST SEESWTDSEV
     DSSCSGQPIH LWQFLKELLL KPHSYGRFIR WLNKEKGIFK IEDSAQVARL WGIRKNRPAM
     NYDKLSRSIR QYYKKGIIRK PDISQRLVYQ FVHPI
//
DBGET integrated database retrieval system