HIPK4_RAT
ID HIPK4_RAT Reviewed; 616 AA.
AC Q4V793;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Homeodomain-interacting protein kinase 4;
DE EC=2.7.11.1;
GN Name=Hipk4;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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; BC098070; AAH98070.1; -; mRNA.
DR RefSeq; NP_001019947.1; NM_001024776.1.
DR AlphaFoldDB; Q4V793; -.
DR SMR; Q4V793; -.
DR STRING; 10116.ENSRNOP00000028266; -.
DR iPTMnet; Q4V793; -.
DR PhosphoSitePlus; Q4V793; -.
DR PaxDb; Q4V793; -.
DR Ensembl; ENSRNOT00000028266; ENSRNOP00000028266; ENSRNOG00000020835.
DR GeneID; 308449; -.
DR KEGG; rno:308449; -.
DR UCSC; RGD:1307541; rat.
DR CTD; 147746; -.
DR RGD; 1307541; Hipk4.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000161512; -.
DR HOGENOM; CLU_000288_5_14_1; -.
DR InParanoid; Q4V793; -.
DR OMA; DWTLEGI; -.
DR OrthoDB; 59821at2759; -.
DR PhylomeDB; Q4V793; -.
DR TreeFam; TF105417; -.
DR PRO; PR:Q4V793; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020835; Expressed in testis and 17 other tissues.
DR Genevisible; Q4V793; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; 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; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0016572; P:histone phosphorylation; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; 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 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_0000232403"
FT DOMAIN 11..347
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 487..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Basic and acidic 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 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V016"
SQ SEQUENCE 616 AA; 69298 MW; 12E14628743474AA CRC64;
MATIQSETDC YDIIEVLGKG TFGEVAKGWR RSTGEMVAIK ILKNDAYRSR IIKNELKLLR
CVRGLDPDEA HVIRFLEFFH DALKFYLVFE LLEQNLFEFQ KENNFAPLPA RHIRTVTLQV
LRALARLKEL AIIHADLKPE NIMLVDQTRC PFRVKVIDFG SASIFSEVRY VKEPYIQSRF
YRAPEILLGL PFCEKVDVWS LGCVMAELHL GWPLYPGNNE YDQVRYICET QGLPKPHLLH
AARKAHHFFK RNPHPDATNP WQLKSSADYL AETKVRPLER RKYMLKSLDQ IETVNGGGAV
NRLSFPDREA LAEHADLKSM VELIKRMLTW ESHERISPSA ALRHPFVSMQ QLRSAHEATR
YYQLSLRGCR LSLQVDGKPP PPVIANAEDG PPYYRLAEEE ETAGLGGVTG SGSFFREDKA
PGMQRAIDQL DDLSLQEARR GLWSDTRADM VSDMLAPLKV ATTSHRVPDS GPEPILAFYG
SRLTGRHKAR KAPAGSKSDS NFSNLIRLSQ ASPEDAGSCR GSGWEEGEGH TTSTEPSAIP
QREGDGPSIK DRPMDAERSG PELFDPSGCP GEWLNEPEWT LEGIRGSRAQ GLPARHPHPH
GPPRTTSFLQ HVGGHH
