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Homeobox protein Nkx-3.1 (Homeobox protein NK-3 homolog A)

 NKX31_HUMAN             Reviewed;         234 AA.
Q99801; O15465; Q9H2P4; Q9H2P5; Q9H2P6; Q9H2P7; Q9HBG0;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 2.
12-SEP-2018, entry version 170.
RecName: Full=Homeobox protein Nkx-3.1;
AltName: Full=Homeobox protein NK-3 homolog A;
Name=NKX3-1; Synonyms=NKX3.1, NKX3A;
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), TISSUE SPECIFICITY, AND
INDUCTION BY ANDROGENS.
TISSUE=Prostate;
PubMed=9226374; DOI=10.1006/geno.1997.4715;
He W.-W., Sciavolino P.J., Wing J., Augustus M., Hudson P.,
Meissner P.S., Curtis R.T., Shell B.K., Bostwick D.G., Tindall D.J.,
Gelmann E.P., Abate-Shen C., Carter K.C.;
"A novel human prostate-specific, androgen-regulated homeobox gene
(NKX3.1) that maps to 8p21, a region frequently deleted in prostate
cancer.";
Genomics 43:69-77(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INDUCTION BY ANDROGENS.
PubMed=9537602;
DOI=10.1002/(SICI)1097-0045(19980401)35:1<71::AID-PROS10>3.0.CO;2-H;
Prescott J.L., Blok L., Tindall D.J.;
"Isolation and androgen regulation of the human homeobox cDNA,
NKX3.1.";
Prostate 35:71-80(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), SUBCELLULAR
LOCATION, AND INDUCTION BY ESTROGENS.
TISSUE=Prostate;
PubMed=11137288; DOI=10.1016/S0378-1119(00)00453-4;
Korkmaz K.S., Korkmaz C.G., Ragnhildstveit E., Kizildag S.,
Pretlow T.G., Saatcioglu F.;
"Full-length cDNA sequence and genomic organization of human NKX3A
-- alternative mRNA forms and regulation by both androgens and
estrogens.";
Gene 260:25-36(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[5]
INTERACTION WITH SPDEF.
PubMed=11809674;
Chen H., Nandi A.K., Li X., Bieberich C.J.;
"NKX-3.1 interacts with prostate-derived Ets factor and regulates the
activity of the PSA promoter.";
Cancer Res. 62:338-340(2002).
[6]
INTERACTION WITH WDR77.
PubMed=12972618; DOI=10.1128/MCB.23.19.7019-7029.2003;
Hosohata K., Li P., Hosohata Y., Qin J., Roeder R.G., Wang Z.;
"Purification and identification of a novel complex which is involved
in androgen receptor-dependent transcription.";
Mol. Cell. Biol. 23:7019-7029(2003).
[7]
INTERACTION WITH TOPORS, AND UBIQUITINATION BY TOPORS.
PubMed=18077445; DOI=10.1074/jbc.M708630200;
Guan B., Pungaliya P., Li X., Uquillas C., Mutton L.N., Rubin E.H.,
Bieberich C.J.;
"Ubiquitination by TOPORS regulates the prostate tumor suppressor
NKX3.1.";
J. Biol. Chem. 283:4834-4840(2008).
[8]
FUNCTION AS TUMOR SUPPRESSOR.
PubMed=19462257; DOI=10.1007/s11033-009-9549-8;
Zhang P., Liu W., Zhang J., Guan H., Chen W., Cui X., Liu Q.,
Jiang A.;
"Gene expression profiles in the PC-3 human prostate cancer cells
induced by NKX3.1.";
Mol. Biol. Rep. 37:1505-1512(2010).
[9]
STRUCTURE BY NMR OF 132-189.
Northeast structural genomics consortium (NESG);
"Solution NMR structure of homeobox domain of homeobox protein NKX-3.1
from Homo sapiens, Northeast structural genomics consortium target
HR6470A.";
Submitted (APR-2011) to the PDB data bank.
[10]
VARIANT CYS-52.
PubMed=9377551;
Voeller H.J., Augustus M., Madike V., Bova G.S., Carter K.C.,
Gelmann E.P.;
"Coding region of NKX3.1, a prostate-specific homeobox gene on 8p21,
is not mutated in human prostate cancers.";
Cancer Res. 57:4455-4459(1997).
[11]
ERRATUM.
Voeller H.J., Augustus M., Madike V., Bova G.S., Carter K.C.,
Gelmann E.P.;
Cancer Res. 57:5613-5613(1997).
-!- FUNCTION: Transcription factor, which binds preferentially the
consensus sequence 5'-TAAGT[AG]-3' and can behave as a
transcriptional repressor. Plays an important role in normal
prostate development, regulating proliferation of glandular
epithelium and in the formation of ducts in prostate. Acts as a
tumor suppressor controlling prostate carcinogenesis, as shown by
the ability to inhibit proliferation and invasion activities of
PC-3 prostate cancer cells. {ECO:0000269|PubMed:19462257}.
-!- SUBUNIT: Interacts with serum response factor (SRF) (By
similarity). Interacts with SPDEF. Interacts with WDR77. Interacts
with TOPORS which polyubiquitinates NKX3-1 and induces its
proteasomal degradation. {ECO:0000250,
ECO:0000269|PubMed:11809674, ECO:0000269|PubMed:12972618,
ECO:0000269|PubMed:18077445}.
-!- INTERACTION:
Q96KQ7:EHMT2; NbExp=3; IntAct=EBI-16208773, EBI-744366;
P11387:TOP1; NbExp=6; IntAct=EBI-1385894, EBI-876302;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00108, ECO:0000269|PubMed:11137288}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q99801-1; Sequence=Displayed;
Name=2; Synonyms=V2;
IsoId=Q99801-2; Sequence=VSP_002230;
Name=3; Synonyms=V4;
IsoId=Q99801-3; Sequence=VSP_002231;
Name=4; Synonyms=V3;
IsoId=Q99801-4; Sequence=VSP_002232;
Name=5; Synonyms=V1;
IsoId=Q99801-5; Sequence=VSP_002233;
-!- TISSUE SPECIFICITY: Highly expressed in the prostate and, at a
lower level, in the testis. {ECO:0000269|PubMed:9226374,
ECO:0000269|PubMed:9537602}.
-!- INDUCTION: By androgens and, in the LNCaP cell line, by estrogens.
Androgenic control may be lost in prostate cancer cells during
tumor progression from an androgen-dependent to an androgen-
independent phase. {ECO:0000269|PubMed:11137288,
ECO:0000269|PubMed:9226374, ECO:0000269|PubMed:9537602}.
-!- PTM: Ubiquitinated by TOPORS; monoubiquitinated at several
residues and also polyubiquitinated on single residues.
{ECO:0000269|PubMed:18077445}.
-!- SIMILARITY: Belongs to the NK-3 homeobox family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NKX31ID41541ch8p21.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U91540; AAB68662.1; -; mRNA.
EMBL; U80669; AAB38747.1; -; mRNA.
EMBL; AF247704; AAG09781.1; -; mRNA.
EMBL; AF249669; AAG39735.1; -; mRNA.
EMBL; AF249670; AAG39736.1; -; mRNA.
EMBL; AF249671; AAG39737.1; -; mRNA.
EMBL; AF249672; AAG39738.1; -; mRNA.
EMBL; BC074863; AAH74863.1; -; mRNA.
EMBL; BC074864; AAH74864.1; -; mRNA.
CCDS; CCDS59095.1; -. [Q99801-3]
CCDS; CCDS6042.1; -. [Q99801-1]
RefSeq; NP_001243268.1; NM_001256339.1. [Q99801-3]
RefSeq; NP_006158.2; NM_006167.3. [Q99801-1]
UniGene; Hs.55999; -.
PDB; 2L9R; NMR; -; A=132-189.
PDBsum; 2L9R; -.
DisProt; DP00683; -.
ProteinModelPortal; Q99801; -.
SMR; Q99801; -.
BioGrid; 110888; 35.
CORUM; Q99801; -.
DIP; DIP-39687N; -.
IntAct; Q99801; 14.
STRING; 9606.ENSP00000370253; -.
iPTMnet; Q99801; -.
PhosphoSitePlus; Q99801; -.
BioMuta; NKX3-1; -.
DMDM; 17377578; -.
MaxQB; Q99801; -.
PaxDb; Q99801; -.
PeptideAtlas; Q99801; -.
PRIDE; Q99801; -.
ProteomicsDB; 78479; -.
ProteomicsDB; 78480; -. [Q99801-2]
ProteomicsDB; 78481; -. [Q99801-3]
ProteomicsDB; 78482; -. [Q99801-4]
ProteomicsDB; 78483; -. [Q99801-5]
DNASU; 4824; -.
Ensembl; ENST00000380871; ENSP00000370253; ENSG00000167034. [Q99801-1]
Ensembl; ENST00000523261; ENSP00000429729; ENSG00000167034. [Q99801-3]
GeneID; 4824; -.
KEGG; hsa:4824; -.
UCSC; uc011kzx.3; human. [Q99801-1]
CTD; 4824; -.
DisGeNET; 4824; -.
EuPathDB; HostDB:ENSG00000167034.9; -.
GeneCards; NKX3-1; -.
HGNC; HGNC:7838; NKX3-1.
HPA; HPA078571; -.
MIM; 602041; gene.
neXtProt; NX_Q99801; -.
OpenTargets; ENSG00000167034; -.
PharmGKB; PA31645; -.
eggNOG; KOG0842; Eukaryota.
eggNOG; ENOG410XR21; LUCA.
GeneTree; ENSGT00910000144003; -.
HOGENOM; HOG000231923; -.
HOVERGEN; HBG006689; -.
InParanoid; Q99801; -.
KO; K09348; -.
OMA; QTAKQPQ; -.
OrthoDB; EOG091G0RNV; -.
PhylomeDB; Q99801; -.
TreeFam; TF315720; -.
SignaLink; Q99801; -.
SIGNOR; Q99801; -.
ChiTaRS; NKX3-1; human.
GeneWiki; NKX3-1; -.
GenomeRNAi; 4824; -.
PRO; PR:Q99801; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000167034; Expressed in 164 organ(s), highest expression level in palpebral conjunctiva.
CleanEx; HS_NKX3-1; -.
Genevisible; Q99801; HS.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004882; F:androgen receptor activity; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0030284; F:estrogen receptor activity; IDA:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0097162; F:MADS box domain binding; IEA:Ensembl.
GO; GO:0030295; F:protein kinase activator activity; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0060442; P:branching involved in prostate gland morphogenesis; ISS:UniProtKB.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IEP:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
GO; GO:0035907; P:dorsal aorta development; IEA:Ensembl.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0001656; P:metanephros development; IEA:Ensembl.
GO; GO:0071850; P:mitotic cell cycle arrest; IDA:UniProtKB.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; ISS:UniProtKB.
GO; GO:0071899; P:negative regulation of estrogen receptor binding; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
GO; GO:2000836; P:positive regulation of androgen secretion; IDA:UniProtKB.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0033574; P:response to testosterone; ISS:UniProtKB.
GO; GO:0007431; P:salivary gland development; ISS:UniProtKB.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00086; homeodomain; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017970; Homeobox_CS.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR020479; Homeobox_metazoa.
Pfam; PF00046; Homeobox; 1.
PRINTS; PR00024; HOMEOBOX.
SMART; SM00389; HOX; 1.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS00027; HOMEOBOX_1; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA-binding;
Homeobox; Nucleus; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation.
CHAIN 1 234 Homeobox protein Nkx-3.1.
/FTId=PRO_0000048945.
DNA_BIND 124 183 Homeobox. {ECO:0000255|PROSITE-
ProRule:PRU00108}.
VAR_SEQ 8 56 Missing (in isoform 2).
{ECO:0000303|PubMed:11137288}.
/FTId=VSP_002230.
VAR_SEQ 13 87 Missing (in isoform 3).
{ECO:0000303|PubMed:11137288}.
/FTId=VSP_002231.
VAR_SEQ 15 83 Missing (in isoform 4).
{ECO:0000303|PubMed:11137288}.
/FTId=VSP_002232.
VAR_SEQ 40 83 Missing (in isoform 5).
{ECO:0000303|PubMed:11137288}.
/FTId=VSP_002233.
VARIANT 52 52 R -> C (in dbSNP:rs2228013).
{ECO:0000269|PubMed:9377551}.
/FTId=VAR_011612.
CONFLICT 8 8 R -> W (in Ref. 3; AAG39737).
{ECO:0000305}.
CONFLICT 85 85 E -> D (in Ref. 2; AAB38747).
{ECO:0000305}.
CONFLICT 135 135 Q -> R (in Ref. 3; AAG39738).
{ECO:0000305}.
CONFLICT 196 196 S -> F (in Ref. 2; AAB38747).
{ECO:0000305}.
CONFLICT 224 224 Y -> H (in Ref. 2; AAB38747).
{ECO:0000305}.
CONFLICT 234 234 W -> G (in Ref. 1; AAB68662).
{ECO:0000305}.
HELIX 133 145 {ECO:0000244|PDB:2L9R}.
HELIX 151 160 {ECO:0000244|PDB:2L9R}.
HELIX 165 178 {ECO:0000244|PDB:2L9R}.
STRAND 182 185 {ECO:0000244|PDB:2L9R}.
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


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