NKX31_HUMAN
ID NKX31_HUMAN Reviewed; 234 AA.
AC Q99801; O15465; Q9H2P4; Q9H2P5; Q9H2P6; Q9H2P7; Q9HBG0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Homeobox protein Nkx-3.1 {ECO:0000303|PubMed:9226374};
DE AltName: Full=Homeobox protein NK-3 homolog A {ECO:0000303|PubMed:11137288};
GN Name=NKX3-1 {ECO:0000312|HGNC:HGNC:7838};
GN Synonyms=NKX3.1 {ECO:0000303|PubMed:9226374},
GN NKX3A {ECO:0000303|PubMed:11137288};
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), TISSUE SPECIFICITY, AND INDUCTION
RP BY ANDROGENS.
RC TISSUE=Prostate;
RX PubMed=9226374; DOI=10.1006/geno.1997.4715;
RA He W.-W., Sciavolino P.J., Wing J., Augustus M., Hudson P., Meissner P.S.,
RA Curtis R.T., Shell B.K., Bostwick D.G., Tindall D.J., Gelmann E.P.,
RA Abate-Shen C., Carter K.C.;
RT "A novel human prostate-specific, androgen-regulated homeobox gene (NKX3.1)
RT that maps to 8p21, a region frequently deleted in prostate cancer.";
RL Genomics 43:69-77(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION
RP BY ANDROGENS.
RX PubMed=9537602;
RX DOI=10.1002/(sici)1097-0045(19980401)35:1<71::aid-pros10>3.0.co;2-h;
RA Prescott J.L., Blok L., Tindall D.J.;
RT "Isolation and androgen regulation of the human homeobox cDNA, NKX3.1.";
RL Prostate 35:71-80(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), SUBCELLULAR
RP LOCATION, AND INDUCTION BY ESTROGENS.
RC TISSUE=Prostate;
RX PubMed=11137288; DOI=10.1016/s0378-1119(00)00453-4;
RA Korkmaz K.S., Korkmaz C.G., Ragnhildstveit E., Kizildag S., Pretlow T.G.,
RA Saatcioglu F.;
RT "Full-length cDNA sequence and genomic organization of human NKX3A
RT -- alternative mRNA forms and regulation by both androgens and estrogens.";
RL Gene 260:25-36(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [5]
RP INTERACTION WITH SPDEF.
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 [6]
RP INTERACTION WITH WDR77.
RX PubMed=12972618; DOI=10.1128/mcb.23.19.7019-7029.2003;
RA Hosohata K., Li P., Hosohata Y., Qin J., Roeder R.G., Wang Z.;
RT "Purification and identification of a novel complex which is involved in
RT androgen receptor-dependent transcription.";
RL Mol. Cell. Biol. 23:7019-7029(2003).
RN [7]
RP INTERACTION WITH TOPORS, AND UBIQUITINATION BY TOPORS.
RX PubMed=18077445; DOI=10.1074/jbc.m708630200;
RA Guan B., Pungaliya P., Li X., Uquillas C., Mutton L.N., Rubin E.H.,
RA Bieberich C.J.;
RT "Ubiquitination by TOPORS regulates the prostate tumor suppressor NKX3.1.";
RL J. Biol. Chem. 283:4834-4840(2008).
RN [8]
RP FUNCTION AS TUMOR SUPPRESSOR.
RX PubMed=19462257; DOI=10.1007/s11033-009-9549-8;
RA Zhang P., Liu W., Zhang J., Guan H., Chen W., Cui X., Liu Q., Jiang A.;
RT "Gene expression profiles in the PC-3 human prostate cancer cells induced
RT by NKX3.1.";
RL Mol. Biol. Rep. 37:1505-1512(2010).
RN [9]
RP STRUCTURE BY NMR OF 132-189.
RG Northeast structural genomics consortium (NESG);
RT "Solution NMR structure of homeobox domain of homeobox protein NKX-3.1 from
RT Homo sapiens, Northeast structural genomics consortium target HR6470A.";
RL Submitted (APR-2011) to the PDB data bank.
RN [10]
RP VARIANT CYS-52.
RX PubMed=9377551;
RA Voeller H.J., Augustus M., Madike V., Bova G.S., Carter K.C., Gelmann E.P.;
RT "Coding region of NKX3.1, a prostate-specific homeobox gene on 8p21, is not
RT mutated in human prostate cancers.";
RL Cancer Res. 57:4455-4459(1997).
RN [11]
RP ERRATUM OF PUBMED:9377551.
RA Voeller H.J., Augustus M., Madike V., Bova G.S., Carter K.C., Gelmann E.P.;
RL Cancer Res. 57:5613-5613(1997).
CC -!- FUNCTION: Transcription factor, which binds preferentially the
CC consensus sequence 5'-TAAGT[AG]-3' and can behave as a transcriptional
CC repressor. Plays an important role in normal prostate development,
CC regulating proliferation of glandular epithelium and in the formation
CC of ducts in prostate. Acts as a tumor suppressor controlling prostate
CC carcinogenesis, as shown by the ability to inhibit proliferation and
CC invasion activities of PC-3 prostate cancer cells.
CC {ECO:0000269|PubMed:19462257}.
CC -!- SUBUNIT: Interacts with serum response factor (SRF) (By similarity).
CC Interacts with SPDEF (PubMed:11809674). Interacts with WDR77
CC (PubMed:12972618). Interacts with TOPORS which polyubiquitinates NKX3-1
CC and induces its proteasomal degradation (PubMed:18077445). Interacts
CC with FEM1B (By similarity). {ECO:0000250|UniProtKB:P97436,
CC ECO:0000269|PubMed:11809674, ECO:0000269|PubMed:12972618,
CC ECO:0000269|PubMed:18077445}.
CC -!- INTERACTION:
CC Q99801; Q6Q8B3: CD200R1L; NbExp=3; IntAct=EBI-1385894, EBI-18552964;
CC Q99801; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-1385894, EBI-372094;
CC Q99801; P78317: RNF4; NbExp=3; IntAct=EBI-1385894, EBI-2340927;
CC Q99801; Q96BI1: SLC22A18; NbExp=3; IntAct=EBI-1385894, EBI-11721845;
CC Q99801; P11387: TOP1; NbExp=6; IntAct=EBI-1385894, EBI-876302;
CC Q99801; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1385894, EBI-740727;
CC Q99801-1; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-16208773, EBI-744366;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:11137288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q99801-1; Sequence=Displayed;
CC Name=2; Synonyms=V2;
CC IsoId=Q99801-2; Sequence=VSP_002230;
CC Name=3; Synonyms=V4;
CC IsoId=Q99801-3; Sequence=VSP_002231;
CC Name=4; Synonyms=V3;
CC IsoId=Q99801-4; Sequence=VSP_002232;
CC Name=5; Synonyms=V1;
CC IsoId=Q99801-5; Sequence=VSP_002233;
CC -!- TISSUE SPECIFICITY: Highly expressed in the prostate and, at a lower
CC level, in the testis. {ECO:0000269|PubMed:9226374,
CC ECO:0000269|PubMed:9537602}.
CC -!- INDUCTION: By androgens and, in the LNCaP cell line, by estrogens.
CC Androgenic control may be lost in prostate cancer cells during tumor
CC progression from an androgen-dependent to an androgen-independent
CC phase. {ECO:0000269|PubMed:11137288, ECO:0000269|PubMed:9226374,
CC ECO:0000269|PubMed:9537602}.
CC -!- PTM: Ubiquitinated by TOPORS; monoubiquitinated at several residues and
CC also polyubiquitinated on single residues.
CC {ECO:0000269|PubMed:18077445}.
CC -!- SIMILARITY: Belongs to the NK-3 homeobox family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NKX31ID41541ch8p21.html";
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DR EMBL; U91540; AAB68662.1; -; mRNA.
DR EMBL; U80669; AAB38747.1; -; mRNA.
DR EMBL; AF247704; AAG09781.1; -; mRNA.
DR EMBL; AF249669; AAG39735.1; -; mRNA.
DR EMBL; AF249670; AAG39736.1; -; mRNA.
DR EMBL; AF249671; AAG39737.1; -; mRNA.
DR EMBL; AF249672; AAG39738.1; -; mRNA.
DR EMBL; BC074863; AAH74863.1; -; mRNA.
DR EMBL; BC074864; AAH74864.1; -; mRNA.
DR CCDS; CCDS59095.1; -. [Q99801-3]
DR CCDS; CCDS6042.1; -. [Q99801-1]
DR RefSeq; NP_001243268.1; NM_001256339.1. [Q99801-3]
DR RefSeq; NP_006158.2; NM_006167.3. [Q99801-1]
DR PDB; 2L9R; NMR; -; A=132-189.
DR PDBsum; 2L9R; -.
DR AlphaFoldDB; Q99801; -.
DR SMR; Q99801; -.
DR BioGRID; 110888; 44.
DR CORUM; Q99801; -.
DR DIP; DIP-39687N; -.
DR IntAct; Q99801; 15.
DR STRING; 9606.ENSP00000370253; -.
DR iPTMnet; Q99801; -.
DR PhosphoSitePlus; Q99801; -.
DR BioMuta; NKX3-1; -.
DR DMDM; 17377578; -.
DR jPOST; Q99801; -.
DR MassIVE; Q99801; -.
DR MaxQB; Q99801; -.
DR PaxDb; Q99801; -.
DR PeptideAtlas; Q99801; -.
DR PRIDE; Q99801; -.
DR ProteomicsDB; 78479; -. [Q99801-1]
DR ProteomicsDB; 78480; -. [Q99801-2]
DR ProteomicsDB; 78481; -. [Q99801-3]
DR ProteomicsDB; 78482; -. [Q99801-4]
DR ProteomicsDB; 78483; -. [Q99801-5]
DR Antibodypedia; 9788; 776 antibodies from 40 providers.
DR DNASU; 4824; -.
DR Ensembl; ENST00000380871.5; ENSP00000370253.4; ENSG00000167034.10. [Q99801-1]
DR Ensembl; ENST00000523261.1; ENSP00000429729.1; ENSG00000167034.10. [Q99801-3]
DR GeneID; 4824; -.
DR KEGG; hsa:4824; -.
DR MANE-Select; ENST00000380871.5; ENSP00000370253.4; NM_006167.4; NP_006158.2.
DR UCSC; uc011kzx.3; human. [Q99801-1]
DR CTD; 4824; -.
DR DisGeNET; 4824; -.
DR GeneCards; NKX3-1; -.
DR HGNC; HGNC:7838; NKX3-1.
DR HPA; ENSG00000167034; Tissue enriched (prostate).
DR MIM; 602041; gene.
DR neXtProt; NX_Q99801; -.
DR OpenTargets; ENSG00000167034; -.
DR PharmGKB; PA31645; -.
DR VEuPathDB; HostDB:ENSG00000167034; -.
DR eggNOG; KOG0842; Eukaryota.
DR GeneTree; ENSGT00940000160930; -.
DR HOGENOM; CLU_049543_2_0_1; -.
DR InParanoid; Q99801; -.
DR OMA; LYCLGSW; -.
DR OrthoDB; 1398668at2759; -.
DR PhylomeDB; Q99801; -.
DR TreeFam; TF315720; -.
DR PathwayCommons; Q99801; -.
DR SignaLink; Q99801; -.
DR SIGNOR; Q99801; -.
DR BioGRID-ORCS; 4824; 15 hits in 1097 CRISPR screens.
DR ChiTaRS; NKX3-1; human.
DR GeneWiki; NKX3-1; -.
DR GenomeRNAi; 4824; -.
DR Pharos; Q99801; Tbio.
DR PRO; PR:Q99801; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q99801; protein.
DR Bgee; ENSG00000167034; Expressed in palpebral conjunctiva and 141 other tissues.
DR Genevisible; Q99801; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0097162; F:MADS box domain binding; IEA:Ensembl.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:GO_Central.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0060442; P:branching involved in prostate gland morphogenesis; ISS:UniProtKB.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:UniProtKB.
DR GO; GO:0035907; P:dorsal aorta development; IEA:Ensembl.
DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0001656; P:metanephros development; IEA:Ensembl.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IGI:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
DR GO; GO:2000836; P:positive regulation of androgen secretion; IDA:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:BHF-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0033574; P:response to testosterone; ISS:UniProtKB.
DR GO; GO:0007431; P:salivary gland development; ISS:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR DisProt; DP00683; -.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..234
FT /note="Homeobox protein Nkx-3.1"
FT /id="PRO_0000048945"
FT DNA_BIND 124..183
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 8..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11137288"
FT /id="VSP_002230"
FT VAR_SEQ 13..87
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11137288"
FT /id="VSP_002231"
FT VAR_SEQ 15..83
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11137288"
FT /id="VSP_002232"
FT VAR_SEQ 40..83
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11137288"
FT /id="VSP_002233"
FT VARIANT 52
FT /note="R -> C (in dbSNP:rs2228013)"
FT /evidence="ECO:0000269|PubMed:9377551"
FT /id="VAR_011612"
FT CONFLICT 8
FT /note="R -> W (in Ref. 3; AAG39737)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="E -> D (in Ref. 2; AAB38747)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="Q -> R (in Ref. 3; AAG39738)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="S -> F (in Ref. 2; AAB38747)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="Y -> H (in Ref. 2; AAB38747)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="W -> G (in Ref. 1; AAB68662)"
FT /evidence="ECO:0000305"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:2L9R"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:2L9R"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:2L9R"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:2L9R"
SQ SEQUENCE 234 AA; 26350 MW; C99A0943E15B2A55 CRC64;
MLRVPEPRPG EAKAEGAAPP TPSKPLTSFL IQDILRDGAQ RQGGRTSSQR QRDPEPEPEP
EPEGGRSRAG AQNDQLSTGP RAAPEEAETL AETEPERHLG SYLLDSENTS GALPRLPQTP
KQPQKRSRAA FSHTQVIELE RKFSHQKYLS APERAHLAKN LKLTETQVKI WFQNRRYKTK
RKQLSSELGD LEKHSSLPAL KEEAFSRASL VSVYNSYPYY PYLYCVGSWS PAFW
