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Homeodomain-interacting protein kinase 2 (EC 2.7.11.1) (Mx-interacting protein kinase) (PKM)

 HIPK2_MESAU             Reviewed;        1168 AA.
Q9WUM7;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 2.
22-NOV-2017, entry version 98.
RecName: Full=Homeodomain-interacting protein kinase 2;
EC=2.7.11.1;
AltName: Full=Mx-interacting protein kinase;
AltName: Full=PKM;
Name=Hipk2;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AUTOPHOSPHORYLATION,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-228.
PubMed=10702310; DOI=10.1074/jbc.275.10.7373;
Trost M., Kochs G., Haller O.;
"Characterization of a novel serine/threonine kinase associated with
nuclear bodies.";
J. Biol. Chem. 275:7373-7377(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH
UBL1, MUTAGENESIS OF LYS-228, AND FUNCTION.
PubMed=12565818; DOI=10.1016/S0014-4827(02)00025-3;
Engelhardt O.G., Boutell C., Orr A., Ullrich E., Haller O.,
Everett R.D.;
"The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through
both its kinase domain and a SUMO-1 interaction motif and alters the
posttranslational modification of PML.";
Exp. Cell Res. 283:36-50(2003).
[3]
INTERACTION WITH TP73; TP53 AND TP63, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=11925430; DOI=10.1074/jbc.M200153200;
Kim E.-J., Park J.-S., Um S.-J.;
"Identification and characterization of HIPK2 interacting with p73 and
modulating functions of the p53 family in vivo.";
J. Biol. Chem. 277:32020-32028(2002).
-!- FUNCTION: Serine/threonine-protein kinase involved in
transcription regulation, p53/TP53-mediated cellular apoptosis and
regulation of the cell cycle. Acts as a corepressor of several
transcription factors, including SMAD1 and POU4F1/Brn3a and
probably NK homeodomain transcription factors. Phosphorylates
PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300,
CTNNB1, HMGA1 and ZBTB4. Inhibits cell growth and promotes
apoptosis through the activation of p53/TP53 both at the
transcription level and at the protein level (by phosphorylation
and indirect acetylation). The phosphorylation of p53/TP53 may be
mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the
response to hypoxia by acting as a transcriptional co-suppressor
of HIF1A. Mediates transcriptional activation of TP73. In response
to TGFB, cooperates with DAXX to activate JNK. Negative regulator
through phosphorylation and subsequent proteasomal degradation of
CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin
signaling pathway acts as an intermediate kinase between
MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB.
Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-
protein ligase activity. Activates CREB1 and ATF1 transcription
factors by phosphorylation in response to genotoxic stress. In
response to DNA damage, stabilizes PML by phosphorylation. PML,
HIPK2 and FBXO3 may act synergically to activate p53/TP53-
dependent transactivation. Promotes angiogenesis, and is involved
in erythroid differentiation, especially during fetal liver
erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates
EP300 transcription regulation activity. Triggers ZBTB4 protein
degradation in response to DNA damage. Modulates HMGA1 DNA-binding
affinity. In response to high glucose, triggers phosphorylation-
mediated subnuclear localization shifting of PDX1. Involved in the
regulation of eye size, lens formation and retinal lamination
during late embryogenesis (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11925430, ECO:0000269|PubMed:12565818}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10702310}.
-!- SUBUNIT: Interacts with CREB1, SIAH1, WSB1, CBX4, TRADD, p53/TP53,
TP73, TP63, CREBBP, DAXX, P53DINP1, SKI, SMAD1, SMAD2 and SMAD3,
but not SMAD4. Interacts with ATF1, PML, RUNX1, EP300, NKX1-2,
NKX2-5, SPN/CD43, UBE2I, HMGA1, CTBP1, AXIN1, NLK, MYB, POU4F1,
POU4F2, POU4F3, UBE2I, UBL1 and ZBTB4. Probably part of a complex
consisting of p53/TP53, HIPK2 and AXIN1. Interacts with SP100;
positively regulates TP53-dependent transcription (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus, PML body
{ECO:0000269|PubMed:10702310, ECO:0000269|PubMed:11925430,
ECO:0000269|PubMed:12565818}. Cytoplasm {ECO:0000250}.
-!- PTM: Autophosphorylation at Tyr-361 in the activation loop
activates the kinase and promotes nuclear localization.
{ECO:0000250}.
-!- PTM: Sumoylated. When conjugated it is directed to nuclear
speckles. Desumoylated by SENP1. Sumoylation on Lys-32 is promoted
by the E3 SUMO-protein ligase CBX4 (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by FBXO3, WSB1 and SIAH1, leading to rapid
proteasome-dependent degradation. The degradation mediated by
FBXO3, but not ubiquitination, is prevented in the presence of
PML. The degradation mediated by WSB1 and SIAH1 is reversibly
reduced upon DNA damage (By similarity). {ECO:0000250}.
-!- PTM: Cleaved at Asp-895 and Asp-956 by CASP6 in a p53/TP53-
dependent manner. The cleaved form lacks the autoinhibitory C-
terminal domain (AID), resulting in a hyperactive kinase, which
potentiates p53/TP53 Ser-46 phosphorylation and subsequent
activation of the cell death machinery.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. HIPK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF144573; AAD31319.2; -; mRNA.
RefSeq; NP_001268561.1; NM_001281632.1.
ProteinModelPortal; Q9WUM7; -.
SMR; Q9WUM7; -.
GeneID; 101842840; -.
CTD; 28996; -.
HOVERGEN; HBG051908; -.
OrthoDB; EOG091G0UMX; -.
Proteomes; UP000189706; Genome assembly.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Apoptosis; ATP-binding; Complete proteome; Cytoplasm; DNA damage;
Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Tumor suppressor;
Ubl conjugation.
CHAIN 1 1168 Homeodomain-interacting protein kinase 2.
/FTId=PRO_0000085996.
DOMAIN 199 527 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 205 213 ATP. {ECO:0000305}.
REGION 97 230 Transcriptional corepression.
{ECO:0000250}.
REGION 189 520 Interaction with DAXX. {ECO:0000250}.
REGION 539 816 Interaction with SKI and SMAD1.
{ECO:0000250}.
REGION 724 869 Interaction with POU4F1. {ECO:0000250}.
REGION 746 848 Interaction with CTBP1. {ECO:0000250}.
REGION 759 869 Interaction with HMGA1. {ECO:0000250}.
REGION 812 907 Interaction with TP53 and TP73.
{ECO:0000269|PubMed:11925430}.
REGION 845 952 Localization to nuclear speckles.
{ECO:0000250}.
REGION 845 952 Required for localization to nuclear
speckles. {ECO:0000250}.
REGION 845 879 Interaction with UBE2I. {ECO:0000250}.
REGION 854 876 Interaction with UBL1.
{ECO:0000269|PubMed:12565818}.
REGION 856 880 SUMO interaction motifs (SIM); required
for nuclear localization and kinase
activity. {ECO:0000250}.
REGION 907 1022 Interaction with AXIN1. {ECO:0000250}.
REGION 956 1168 Autoinhibitory domain (AID).
{ECO:0000250}.
MOTIF 774 777 Nuclear localization signal 1 (NLS1).
{ECO:0000250}.
MOTIF 804 807 Nuclear localization signal 2 (NLS2).
{ECO:0000250}.
COMPBIAS 1061 1064 Poly-Ala.
ACT_SITE 324 324 Proton acceptor. {ECO:0000305}.
BINDING 228 228 ATP. {ECO:0000305}.
SITE 895 896 Cleavage; by CASP6. {ECO:0000250}.
SITE 956 957 Cleavage; by CASP6. {ECO:0000250}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 252 252 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 273 273 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 361 361 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 482 482 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 517 517 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 566 566 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 641 641 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 660 660 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 799 799 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 906 906 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 963 963 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 1014 1014 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 1125 1125 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
MOD_RES 1158 1158 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZR5}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q9H2X6}.
CROSSLNK 925 925 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H2X6}.
CROSSLNK 945 945 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H2X6}.
CROSSLNK 1161 1161 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
MUTAGEN 228 228 K->W: Abolishes enzymatic activity.
Diffuse nuclear staining.
{ECO:0000269|PubMed:10702310,
ECO:0000269|PubMed:12565818}.
SEQUENCE 1168 AA; 127641 MW; BA1DF9C43B117F09 CRC64;
MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKVEPSSNWD MTGYGSHSKL CSQSKNIPPS
QPASTTVSTS LPIPNPSLPY EQTIIFPGST GHIVVTSASS TSVTGQVLGG PHNLMRRSTV
SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH PPMIQNNASG ATVATATTST ATSKNSGSNS
EGDYQLVQHE VLCSMTNTYE VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG
QIEVSILARL STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY
IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA SHVSKAVCST
YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL YPGASEYDQI RYISQTQGLP
AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT PDDHEAETGI KSKEARKYIF NCLDDMAQVS
MTTDLEGSDM LVEKADRREF IDLLKKMLTI DADKRITPIE TLNHPFVTMT HLLDFPHSTH
VKSCFQNMEI CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQPSAASM
AAVAQRSMPL QTGTAQICAR PDPFQQALIV CPPGFQGLQA SPSKHAGYSV RMENAVPIVT
QAPGAQPLQI QPGLLAQAWP GGAQQILLPP AWQQLTGVAT HTSVQHAAVI PETMAGTQQL
ADWRNTHAHG SHYNPIMQQP TLLTGHVTLP AAQPLNVGVA HVMRQQPTST TSSRKSKQHQ
PSMRNVSTCE VTSSQSTSSP QRSKRVKENT PPRCAMVHSS PACSTSVTCG WGDVASSTTR
ERQRQTIVIP DTPSPTVSVI TISSDTDEEE EQKHAPTSTV SKQRKNVISC VTVHDSPYSD
SSSNTSPYSV QQRTGHNGTN TLDTKGALEN HCTGNPRTII VPPLKTQASE VLVECDSLGP
AVSTGHHSSS FKCKSSSTVT STSGHSSGSS SGAIAYRQQR PGPHFQQQQP LNLSQAQPHM
ATDRTGSHRR QQAYITPTMA QAPYTFPHNS PSHGTVHPHL AAAAHLPTQP HLYTYTAPTA
LGSTGTVAHL VASQGSARHT VQHTAYPASI VHQVPVSMGP RVLPSPTIHP SQYPAQFAHQ
TYISASPAST VYTGYPLSPA KVNQYPYI


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