ID   HIPK4_MACFA             Reviewed;         616 AA.
AC   Q8WP28;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Homeodomain-interacting protein kinase 4;
DE            EC=2.7.11.1;
GN   Name=HIPK4; ORFNames=QtsA-20664;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
CC   -!- FUNCTION: Protein kinase that phosphorylates TP53, and thus induces
CC       TP53 repression of BIRC5 promoter (By similarity). May act as a
CC       corepressor of transcription factors (Potential). {ECO:0000250,
CC       ECO:0000305}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {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; AB074449; BAB72080.1; -; mRNA.
DR   RefSeq; NP_001306374.1; NM_001319445.1.
DR   AlphaFoldDB; Q8WP28; -.
DR   SMR; Q8WP28; -.
DR   STRING; 9541.XP_005589328.1; -.
DR   GeneID; 102139471; -.
DR   CTD; 147746; -.
DR   eggNOG; KOG0667; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..616
FT                   /note="Homeodomain-interacting protein kinase 4"
FT                   /id="PRO_0000232402"
FT   DOMAIN          11..347
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          485..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         17..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3V016"
SQ   SEQUENCE   616 AA;  69568 MW;  B439F531D1895BF5 CRC64;
     MATTQSETDC YDIIEVLGKG TFGEVAKGWR RSTGEMVAIK ILKNDAYRNR IIKNELKLLH
     CMRGLDPEEA HVIRFLEFFH DALKFYLVFE LLEQNLFEFQ KENNFAPLPA RHIRTVTLQV
     LRALARLKEL AIIHADLKPE NIMLVDQTRC PFRVKVIDFG SASIFSEVRY VKEPYIQSRF
     YRAPEILLGL PFCEKVDVWS LGCVMAELHL GWPLYPGNNE YDQVRYICET QGLPKPHLLH
     AARKAHHFFK RNPHPDAANP WQLKSSADYL AETKVRPLER RKYMLKSLDQ IETVNGGSVA
     SRLTFPDREA LAEHADLKSM VELIKRMLTW ESHERISPSA ALRHPFVSMQ QLRNAHETTH
     YYQLSLRSYR LSLQVEGKPP APVVAAEDGT PYYRLAEEKE AAGMGSVASS SPFFREEKAP
     GMQRAIDQLD DLSLQEAGHG LWGETCTDVV SDMMAPLKAA ITGRHMPDSG PEPILAFYSS
     RLAGRHKARK PPAGSKSDSN LSNLIRLSQV SPEDDRPCRG SSWEEGEHLG ASAEPPAILQ
     RDGDGPNIDN MTMEAERPDP ELFDPSSCPG EWLSEPDWTL EGVRGPRAQG LPPRRSHQHG
     PPRGATSFLQ HVTGHH