HIPK3_RAT
ID HIPK3_RAT Reviewed; 1191 AA.
AC O88850;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Homeodomain-interacting protein kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=Androgen receptor-interacting nuclear protein kinase;
DE Short=ANPK;
GN Name=Hipk3; Synonyms=Fist;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-226;
RP SER-357 AND TYR-359, AUTOPHOSPHORYLATION, INTERACTION WITH AR, AND
RP FUNCTION.
RC TISSUE=Testis;
RX PubMed=9725910; DOI=10.1091/mbc.9.9.2527;
RA Moilanen A.-M., Karvonen U., Poukka H., Jaenne O.A., Palvimo J.J.;
RT "Activation of androgen receptor function by a novel nuclear protein
RT kinase.";
RL Mol. Biol. Cell 9:2527-2543(1998).
CC -!- FUNCTION: Seems to negatively regulate apoptosis by promoting FADD
CC phosphorylation. Enhances androgen receptor-mediated transcription. May
CC act as a transcriptional corepressor for NK homeodomain transcription
CC factors. {ECO:0000269|PubMed:9725910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with Nkx1-2. Interacts with FAS and DAXX. Probably
CC part of a complex consisting of HIPK3, FAS and FADD. Interacts with
CC UBL1/SUMO-1 (By similarity). Interacts with and stabilizes ligand-bound
CC androgen receptor (AR). {ECO:0000250, ECO:0000269|PubMed:9725910}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9725910}.
CC -!- PTM: Autophosphorylated. Autophosphorylation is not required for
CC catalytic activity.
CC -!- PTM: May be sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. HIPK subfamily. {ECO:0000305}.
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DR EMBL; AF036959; AAC35249.1; -; mRNA.
DR PIR; T14154; T14154.
DR RefSeq; NP_113975.1; NM_031787.1.
DR AlphaFoldDB; O88850; -.
DR SMR; O88850; -.
DR DIP; DIP-5932N; -.
DR STRING; 10116.ENSRNOP00000015775; -.
DR iPTMnet; O88850; -.
DR PhosphoSitePlus; O88850; -.
DR PaxDb; O88850; -.
DR PRIDE; O88850; -.
DR GeneID; 83617; -.
DR KEGG; rno:83617; -.
DR UCSC; RGD:619884; rat.
DR CTD; 10114; -.
DR RGD; 619884; Hipk3.
DR eggNOG; KOG0667; Eukaryota.
DR InParanoid; O88850; -.
DR OrthoDB; 59821at2759; -.
DR PRO; PR:O88850; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0009299; P:mRNA transcription; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Isopeptide bond; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..1191
FT /note="Homeodomain-interacting protein kinase 3"
FT /id="PRO_0000086000"
FT DOMAIN 197..525
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 766..920
FT /note="Interaction with AR"
FT /evidence="ECO:0000269|PubMed:9725910"
FT REGION 774..867
FT /note="Interaction with FAS"
FT /evidence="ECO:0000250"
FT REGION 801..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..856
FT /note="Interaction with UBL1"
FT /evidence="ECO:0000250"
FT REGION 888..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 322
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 203..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 359
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERH7"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H422"
FT MUTAGEN 226
FT /note="K->R: No enzymatic activity."
FT /evidence="ECO:0000269|PubMed:9725910"
FT MUTAGEN 357
FT /note="S->A: Reduces enzymatic activity but no effect on
FT autophosphorylation; when associated with A-359."
FT /evidence="ECO:0000269|PubMed:9725910"
FT MUTAGEN 359
FT /note="Y->A: Reduces enzymatic activity; but no effect on
FT autophosphorylation; when associated with A-357."
FT /evidence="ECO:0000269|PubMed:9725910"
SQ SEQUENCE 1191 AA; 129744 MW; 0C2D05ED947A53ED CRC64;
MASQVLVYPP YVYQTQSSAF CSVKKLKVEP SGCVFQERAC PQIHVNGRHF GNPLPSTKGS
AFQTKIPFSK PRGHSFSLQA GAIVVKDTAG ATKVIAAQAQ QAGVEAPRAV VWRNRLHFLG
GPQRCGLKRK SEELDNHSGA MQIVDELSIL PAMLQTNMGN PVTVVTATTG SKQNCTSGEG
DYQLVQHEVL CSVKNTYEVL DFLGRGTFGQ VVKCWKRGTN EIVAIKILKN HPSYARQGQI
EVSILARLST ENADEYNFVR AYECFQHRNH TCLVFEMLEQ NLYDFLKQNK FSPLPLKVIR
PVLQQVATAL KKLKSLGLIH ADLKPENIML VDPVRQPYRV KVIDFGSASH VSKTVCSTYL
QSRYYRAPEI ILGLPFCEAI DMWSLGCVIA ELFLGWPLYP GALEYDQIRY ISQTQGLPGE
QLLNVGTKST RFFCRETDMS HSGWRLKTLE EHEAETGMKS KEARKYIFNS LDDIVHVNTV
MDLEGSDLLA EKADRREFVS LLKKMLLIDA DLRITPIETL NHPFVSMKHL LDFPHSSHVK
SCFHIMDICK SPSSCETNNH SKMSLLRPVA SNGTAALAAN FTKVGTLRSQ ALTTSAHSVV
HHGIPLQAGT AQFGCGDAFH QTLIICPPAI QGIPAAHGKP TSYSIRVDNT VPLVTQAPAV
QPLQIRPGVL SQTWSGRTQQ MLIPAWQQVT PMAPAAATLT SEGMAGSQRL GDWGKMIPHS
NHYNSVMPPP LLTNQITLSA PQPISVGIAH VVWPQPATTK KNKLCQNRSN SLQNTNVPHS
AFISPKIISG KEVEEVSCVE TQDNHTSEGE ARTCHEASVR QDSSVSDKQR QTIIIADSPS
PAVSVITISS DTDDEETSPR PSLRECKGSL DCEACQSTLN IDRMCSLSSP DSTLSTSSSG
QSSPSPCKRP NSMSDDEQES GCETVDGSPT SDSSGHDSPF AESSFVEDTP QNPELGTCAG
TEAKPALSTA VEPPVGTERG LNVDAHMANT DSTCQPLTKG QPAPGKLNQP SASAARQQKP
TSAFQQQHLN LSQVQHFGTG HQEWNGNFGH RRQQAYIPTS VTSNPFTLSH GSPNHTAVHA
HLAGSAHLGG QPTLLPYPPS TALSSAAPVA HLLASPCTSR PMLQHPTYNI SHPSGIVHQV
PVGINPRLLP SPTIHQTQYK PIFPPHSYIA ASPAYTGFPL SPTKLSQYPY M
