Reviewed, UniProtKB/Swiss-Prot Q9QZR5 (HIPK2_MOUSE)

Names and origin

Protein names

Recommended name:
    Homeodomain-interacting protein kinase 2
    EC=2.7.11.1
Alternative name(s):
    Nuclear body-associated kinase 1
    Sialophorin tail-associated nuclear serine/threonine-protein kinase

Gene names

Name:	Hipk2
Synonyms:	Nbak1, Stank

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1196 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein kinase acting as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Inhibits cell growth and promotes apoptosis. Involved in transcriptional activation of TP53 and TP73. Phosphorylation of TP53 may be mediated by a TP53-HIPK2-AXIN1 complex. In response to TGFB, cooperates with DAXX to activate JNK By similarity. Phosphorylates the antiapoptotic factor CTBP1 and promotes its proteasomal degradation. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with TRADD, TP53, TP73, TP63, CREBBP, DAXX, P53DINP1, SKI, SMAD1, SMAD2 and SMAD3, but not SMAD4 By similarity. Interacts with NKX1-2, NKX2-5, SPN/CD43, UBE2I, HMGA1, CTBP1, AXIN1, NLK, MYB, POU4F1, POU4F2, POU4F3, UBE2I, UBL1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1. Interacts with CBX4.
Subcellular location	Nucleus. Note: Concentrated in PML/POD/ND10 nuclear bodies. Isoform 2 seems to be both nuclear and cytoplasmic. Ref.1 Ref.2 Ref.4 Ref.7
Tissue specificity	Ubiquitous. Abundant in muscle, heart, small intestine, stomach, kidney and brain; and low in testis, skin and lung. Ref.2 Ref.4 Ref.9
Developmental stage	At E15-E17, mainly in the developing retina, telencephalon and myoblasts. At E12.5, detected in the developing trigeminal and dorsal root ganglia, and in the developing spinal cord (at protein level). Ref.9 Ref.14
Induction	During T-cell activation. Ref.2
Post-translational modification	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. Autophosphorylated. Phosphorylated on tyrosines. Ref.8 Ref.10 Ref.15
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. HIPK subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAC63011.1 differs from that shown. Reason: Frameshift at position 2.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis Inferred from genetic interaction. Source: MGI adult walking behavior Inferred from mutant phenotype. Source: MGI anterior/posterior pattern formation Inferred from genetic interaction. Source: MGI apoptosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of neuron apoptosis Inferred from mutant phenotype. Source: MGI negative regulation of transcription from RNA polymerase II promoter Ref.1 Inferred from direct assay. Source: UniProtKB positive regulation of DNA binding Ref.1 Inferred from direct assay. Source: UniProtKB positive regulation of JNK cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from genetic interaction. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: MGI positive regulation of transforming growth factor beta receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid phosphorylation Ref.1 Inferred from direct assay. Source: UniProtKB smoothened signaling pathway Inferred from genetic interaction. Source: MGI transcription Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype. Source: MGI voluntary musculoskeletal movement Inferred from mutant phenotype. Source: MGI
Cellular component	PML body Traceable author statement. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW transcription corepressor activity Ref.1 Inferred from direct assay. Source: UniProtKB virion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Myb	P06876	1	EBI-366905,EBI-366934
Nlk	O54949	1	EBI-366905,EBI-366894
WSB1	Q9Y6I7	2	EBI-366905,EBI-1171494	From a different organism.
Wsb1	O54927	2	EBI-366905,EBI-1769862

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9QZR5-1)

Also known as: Nbak1b; b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9QZR5-2)

Also known as: Nbak1a; a;

The sequence of this isoform differs from the canonical sequence as follows:
     594-620: Missing.

Isoform 3 (identifier: Q9QZR5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.
     369-1196: Missing.

Isoform 4 (identifier: Q9QZR5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.
     594-620: Missing.

Isoform 5 (identifier: Q9QZR5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-480: Missing.
     595-605: APTTSSATLSL → KSQLIGLSPES
     606-1196: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1196	1196	Homeodomain-interacting protein kinase 2		PRO_0000085997
Regions
	Domain	199 – 527	329	Protein kinase
	Nucleotide binding	205 – 213	9	ATP Probable
	Region	97 – 230	134	Transcriptional corepression
	Region	189 – 520	332	Interaction with DAXX By similarity
	Region	539 – 844	306	Interaction with SKI and SMAD1 By similarity
	Region	752 – 897	146	Interaction with POU4F1
	Region	774 – 876	103	Interaction with CTBP1
	Region	787 – 897	111	Interaction with HMGA1
	Region	839 – 934	96	Interaction with TP53 and TP73
	Region	873 – 980	108	Localization to nuclear speckles
	Region	873 – 907	35	Interaction with UBE2I
	Region	935 – 1050	116	Interaction with AXIN1
	Compositional bias	1089 – 1092	4	Poly-Ala
Sites
	Active site	324	1	Proton acceptor Probable
	Binding site	228	1	ATP Probable
Amino acid modifications
	Modified residue	361	1	Phosphotyrosine Ref.15
	Cross-link	32		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	1189		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Natural variations
	Alternative sequence	1 – 480	480	Missing in isoform 5.		VSP_013136
	Alternative sequence	1 – 7	7	Missing in isoform 3 and isoform 4.		VSP_013135
	Alternative sequence	369 – 1196	828	Missing in isoform 3.		VSP_013137
	Alternative sequence	594 – 620	27	Missing in isoform 2 and isoform 4.		VSP_004808
	Alternative sequence	595 – 605	11	APTTSSATLSL → KSQLIGLSPES in isoform 5.		VSP_013138
	Alternative sequence	606 – 1196	591	Missing in isoform 5.		VSP_013139
Experimental info
	Mutagenesis	228	1	K → R: No enzymatic activity, but still interacts with TP53 and NLK. Blocks the ability to induce cell growth arrest. Decreases corepressor activity. Ref.1 Ref.8 Ref.10 Ref.13
	Mutagenesis	1189	1	K → R: Inhibits localization to nuclear speckles. Ref.7
	Sequence conflict	460	1	I → T in AAC63011. Ref.1
	Sequence conflict	479	1	V → G in AAC63011. Ref.1
	Sequence conflict	705	1	Missing in AAG41237. Ref.3
	Sequence conflict	705	1	Missing in AAK07649. Ref.4
	Sequence conflict	719	1	A → T in AAC63011. Ref.1
	Sequence conflict	1120	1	A → R in AAC63011. Ref.1
	Sequence conflict	1132	1	T → A in AAK07650. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Nbak1b) (b) [UniParc]. Last modified April 27, 2001. Version 2. Checksum: 5C863BE377F3AAEF	FASTA	1,196	130,498
	10 20 30 40 50 60 MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKVEPSSNWD MTGYGSHSKV YSQSKNIPPS 70 80 90 100 110 120 QPASTTVSTS LPIPNPSLPY EQTIIFPGST GHIVVTSASS TSVTGQVLGG PHNLMRRSTV 130 140 150 160 170 180 SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH PPMIQNNASG ATVATATTST ATSKNSGSNS 190 200 210 220 230 240 EGDYQLVQHE VLCSMTNTYE VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG 250 260 270 280 290 300 QIEVSILARL STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY 310 320 330 340 350 360 IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA SHVSKAVCST 370 380 390 400 410 420 YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL YPGASEYDQI RYISQTQGLP 430 440 450 460 470 480 AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT PDDHEAETGI KSKEARKYIF NCLDDMAQVN 490 500 510 520 530 540 MTTDLEGSDM LVEKADRREF IDLLKKMLTI DADKRVTPIE TLNHPFVTMT HLLDFPHSAH 550 560 570 580 590 600 VKSCFQNMEI CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQAPTTSS 610 620 630 640 650 660 ATLSLANPEV SILNYQSALY QPSAASMAAV APRSMPLQTG TAQICARPDP FQQALIVCPP 670 680 690 700 710 720 GFQGLQASPS KHAGYSVRME NAVPIVTQAP GAQPLQIQPG LLAQQAWPGG AQQILLPPAW 730 740 750 760 770 780 QQLTGVATHT SVQHAAVIPE TMAGTQQLAD WRNTHAHGSH YNPIMQQPAL LTGHVTLPAA 790 800 810 820 830 840 QPLNVGVAHV MRQQPTSTTS SRKSKQHQSS VRNVSTCEVT SSQAISSPQR SKRVKENTPP 850 860 870 880 890 900 RCAMVHSSPA CSTSVTCGWG DVASSTTRER QRQTIVIPDT PSPTVSVITI SSDTDEEEEQ 910 920 930 940 950 960 KHAPTSTVSK QRKNVISCVT VHDSPYSDSS SNTSPYSVQQ RTGHNGTNTL DTKGGLENHC 970 980 990 1000 1010 1020 TGNPRTIIVP PLKTQASEVL VECDSLGPAI SASHHSSSFK SKSSSTVTST SGHSSGSSSG 1030 1040 1050 1060 1070 1080 AIAYRQQRPG PHFQQQQPLN LSQAQQHMAA DRTGSHRRQQ AYITPTMAQA PYTFPHNSPS 1090 1100 1110 1120 1130 1140 HGTVHPHLAA AAHLPTQPHL YTYTAPTALG STGTVAHLVA SQGSARHTVQ HTAYPASIVH 1150 1160 1170 1180 1190 QVPVSMGPRV LPSPTIHPSQ YPAQFAHQTY ISASPASTVY TGYPLSPAKV NQYPYI
	Isoform 2 (Nbak1a) (a). Checksum: F8C5ED0ADE4CFE4F	FASTA	1,169	127,676
	10 20 30 40 50 60 MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKVEPSSNWD MTGYGSHSKV YSQSKNIPPS 70 80 90 100 110 120 QPASTTVSTS LPIPNPSLPY EQTIIFPGST GHIVVTSASS TSVTGQVLGG PHNLMRRSTV 130 140 150 160 170 180 SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH PPMIQNNASG ATVATATTST ATSKNSGSNS 190 200 210 220 230 240 EGDYQLVQHE VLCSMTNTYE VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG 250 260 270 280 290 300 QIEVSILARL STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY 310 320 330 340 350 360 IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA SHVSKAVCST 370 380 390 400 410 420 YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL YPGASEYDQI RYISQTQGLP 430 440 450 460 470 480 AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT PDDHEAETGI KSKEARKYIF NCLDDMAQVN 490 500 510 520 530 540 MTTDLEGSDM LVEKADRREF IDLLKKMLTI DADKRVTPIE TLNHPFVTMT HLLDFPHSAH 550 560 570 580 590 600 VKSCFQNMEI CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQPSAASM 610 620 630 640 650 660 AAVAPRSMPL QTGTAQICAR PDPFQQALIV CPPGFQGLQA SPSKHAGYSV RMENAVPIVT 670 680 690 700 710 720 QAPGAQPLQI QPGLLAQQAW PGGAQQILLP PAWQQLTGVA THTSVQHAAV IPETMAGTQQ 730 740 750 760 770 780 LADWRNTHAH GSHYNPIMQQ PALLTGHVTL PAAQPLNVGV AHVMRQQPTS TTSSRKSKQH 790 800 810 820 830 840 QSSVRNVSTC EVTSSQAISS PQRSKRVKEN TPPRCAMVHS SPACSTSVTC GWGDVASSTT 850 860 870 880 890 900 RERQRQTIVI PDTPSPTVSV ITISSDTDEE EEQKHAPTST VSKQRKNVIS CVTVHDSPYS 910 920 930 940 950 960 DSSSNTSPYS VQQRTGHNGT NTLDTKGGLE NHCTGNPRTI IVPPLKTQAS EVLVECDSLG 970 980 990 1000 1010 1020 PAISASHHSS SFKSKSSSTV TSTSGHSSGS SSGAIAYRQQ RPGPHFQQQQ PLNLSQAQQH 1030 1040 1050 1060 1070 1080 MAADRTGSHR RQQAYITPTM AQAPYTFPHN SPSHGTVHPH LAAAAHLPTQ PHLYTYTAPT 1090 1100 1110 1120 1130 1140 ALGSTGTVAH LVASQGSARH TVQHTAYPAS IVHQVPVSMG PRVLPSPTIH PSQYPAQFAH 1150 1160 QTYISASPAS TVYTGYPLSP AKVNQYPYI
	Isoform 3. Checksum: F1F5B6095C8BCDA5	FASTA	361	39,990
	10 20 30 40 50 60 MASHVQVFSP HTLQSSAFCS VKKLKVEPSS NWDMTGYGSH SKVYSQSKNI PPSQPASTTV 70 80 90 100 110 120 STSLPIPNPS LPYEQTIIFP GSTGHIVVTS ASSTSVTGQV LGGPHNLMRR STVSLLDTYQ 130 140 150 160 170 180 KCGLKRKSEE IENTSSVQII EEHPPMIQNN ASGATVATAT TSTATSKNSG SNSEGDYQLV 190 200 210 220 230 240 QHEVLCSMTN TYEVLEFLGR GTFGQVVKCW KRGTNEIVAI KILKNHPSYA RQGQIEVSIL 250 260 270 280 290 300 ARLSTESADD YNFVRAYECF QHKNHTCLVF EMLEQNLYDF LKQNKFSPLP LKYIRPVLQQ 310 320 330 340 350 360 VATALMKLKS LGLIHADLKP ENIMLVDPSR QPYRVKVIDF GSASHVSKAV CSTYLQSRYY R
	Isoform 4. Checksum: 7478F6F1DAF75DE1	FASTA	1,162	126,928
	10 20 30 40 50 60 MASHVQVFSP HTLQSSAFCS VKKLKVEPSS NWDMTGYGSH SKVYSQSKNI PPSQPASTTV 70 80 90 100 110 120 STSLPIPNPS LPYEQTIIFP GSTGHIVVTS ASSTSVTGQV LGGPHNLMRR STVSLLDTYQ 130 140 150 160 170 180 KCGLKRKSEE IENTSSVQII EEHPPMIQNN ASGATVATAT TSTATSKNSG SNSEGDYQLV 190 200 210 220 230 240 QHEVLCSMTN TYEVLEFLGR GTFGQVVKCW KRGTNEIVAI KILKNHPSYA RQGQIEVSIL 250 260 270 280 290 300 ARLSTESADD YNFVRAYECF QHKNHTCLVF EMLEQNLYDF LKQNKFSPLP LKYIRPVLQQ 310 320 330 340 350 360 VATALMKLKS LGLIHADLKP ENIMLVDPSR QPYRVKVIDF GSASHVSKAV CSTYLQSRYY 370 380 390 400 410 420 RAPEIILGLP FCEAIDMWSL GCVIAELFLG WPLYPGASEY DQIRYISQTQ GLPAEYLLSA 430 440 450 460 470 480 GTKTTRFFNR DTDSPYPLWR LKTPDDHEAE TGIKSKEARK YIFNCLDDMA QVNMTTDLEG 490 500 510 520 530 540 SDMLVEKADR REFIDLLKKM LTIDADKRVT PIETLNHPFV TMTHLLDFPH SAHVKSCFQN 550 560 570 580 590 600 MEICKRRVNM YDTVNQSKTP FITHVAPSTS TNLTMTFNNQ LTTVHNQPSA ASMAAVAPRS 610 620 630 640 650 660 MPLQTGTAQI CARPDPFQQA LIVCPPGFQG LQASPSKHAG YSVRMENAVP IVTQAPGAQP 670 680 690 700 710 720 LQIQPGLLAQ QAWPGGAQQI LLPPAWQQLT GVATHTSVQH AAVIPETMAG TQQLADWRNT 730 740 750 760 770 780 HAHGSHYNPI MQQPALLTGH VTLPAAQPLN VGVAHVMRQQ PTSTTSSRKS KQHQSSVRNV 790 800 810 820 830 840 STCEVTSSQA ISSPQRSKRV KENTPPRCAM VHSSPACSTS VTCGWGDVAS STTRERQRQT 850 860 870 880 890 900 IVIPDTPSPT VSVITISSDT DEEEEQKHAP TSTVSKQRKN VISCVTVHDS PYSDSSSNTS 910 920 930 940 950 960 PYSVQQRTGH NGTNTLDTKG GLENHCTGNP RTIIVPPLKT QASEVLVECD SLGPAISASH 970 980 990 1000 1010 1020 HSSSFKSKSS STVTSTSGHS SGSSSGAIAY RQQRPGPHFQ QQQPLNLSQA QQHMAADRTG 1030 1040 1050 1060 1070 1080 SHRRQQAYIT PTMAQAPYTF PHNSPSHGTV HPHLAAAAHL PTQPHLYTYT APTALGSTGT 1090 1100 1110 1120 1130 1140 VAHLVASQGS ARHTVQHTAY PASIVHQVPV SMGPRVLPSP TIHPSQYPAQ FAHQTYISAS 1150 1160 PASTVYTGYP LSPAKVNQYP YI
	Isoform 5. Checksum: 7052092228D50AD5	FASTA	125	14,279
	10 20 30 40 50 60 MTTDLEGSDM LVEKADRREF IDLLKKMLTI DADKRVTPIE TLNHPFVTMT HLLDFPHSAH 70 80 90 100 110 120 VKSCFQNMEI CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQKSQLIG LSPES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homeodomain-interacting protein kinases, a novel family of co-repressors for homeodomain transcription factors." Kim Y.H., Choi C.Y., Lee S.-J., Conti M.A., Kim Y. J. Biol. Chem. 273:25875-25879(1998) [PubMed: 9748262] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH NKX1-2 AND NKX2-5, MUTAGENESIS OF LYS-228. Strain: BALB/c.
[2]	"Identification and cloning of a CD43-associated serine/threonine kinase." Wang W., Link V., Green J.M. Cell. Immunol. 205:34-39(2000) [PubMed: 11078605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SPN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION. Strain: BALB/c. Tissue: Heart.
[3]	"Isolation and characterization of cDNAs for the protein kinase HIPK2." Wang Y., Hofmann T.G., Runkel L., Haaf T., Schaller H., Debatin K.-M., Hug H. Biochim. Biophys. Acta 1518:168-172(2001) [PubMed: 11267674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[4]	"US11 of herpes simplex virus type 1 interacts with HIPK2 and antagonizes HIPK2-induced cell growth arrest." Giraud S., Diaz-Latoud C., Hacot S., Textoris J., Bourette R.P., Diaz J.-J. J. Virol. 78:2984-2993(2004) [PubMed: 14990717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Heart.
[5]	"Protein kinases associated with PML/CBP nuclear bodies and filamentous threads regulate transcription and inhibit cell growth." Sather S.L., Johnson N.L., Johnson G.L. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[6]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). Strain: C57BL/6J. Tissue: Testis.
[7]	"Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1." Kim Y.H., Choi C.Y., Kim Y. Proc. Natl. Acad. Sci. U.S.A. 96:12350-12355(1999) [PubMed: 10535925] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH UBE2I, SUMOYLATION, MUTAGENESIS OF LYS-1189.
[8]	"High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth." Pierantoni G.M., Fedele M., Pentimalli F., Benvenuto G., Pero R., Viglietto G., Santoro M., Chiariotti L., Fusco A. Oncogene 20:6132-6141(2001) [PubMed: 11593421] [Abstract] Cited for: INTERACTION WITH HMGA1, FUNCTION, PHOSPHORYLATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-228.
[9]	"The homeodomain-interacting protein kinase 2 gene is expressed late in embryogenesis and preferentially in retina, muscle, and neural tissues." Pierantoni G.M., Bulfone A., Pentimalli F., Fedele M., Iuliano R., Santoro M., Chiariotti L., Ballabio A., Fusco A. Biochem. Biophys. Res. Commun. 290:942-947(2002) [PubMed: 11798164] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[10]	"Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis." D'Orazi G., Cecchinelli B., Bruno T., Manni I., Higashimoto Y., Saito S., Gostissa M., Coen S., Marchetti A., Del Sal G., Piaggio G., Fanciulli M., Appella E., Soddu S. Nat. Cell Biol. 4:11-19(2002) [PubMed: 11780126] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-228.
[11]	"Homeodomain interacting protein kinase 2 promotes apoptosis by downregulating the transcriptional corepressor CtBP." Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H. Cell 115:177-186(2003) [PubMed: 14567915] [Abstract] Cited for: FUNCTION, INTERACTION WITH CTBP1.
[12]	"Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation." Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M., Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C. EMBO J. 23:4583-4594(2004) [PubMed: 15526030] [Abstract] Cited for: INTERACTION WITH AXIN1, IDENTIFICATION IN A COMPLEX WITH TP53 AND AXIN1.
[13]	"Wnt-1 signal induces phosphorylation and degradation of c-Myb protein via TAK1, HIPK2, and NLK." Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T., Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E., Kim Y., Matsumoto K., Ishii S. Genes Dev. 18:816-829(2004) [PubMed: 15082531] [Abstract] Cited for: FUNCTION IN WNT SIGNALING, INTERACTION WITH NLK AND MYB, MUTAGENESIS OF LYS-228.
[14]	"Interaction of Brn3a and HIPK2 mediates transcriptional repression of sensory neuron survival." Wiggins A.K., Wei G., Doxakis E., Wong C., Tang A.A., Zang K., Luo E.J., Neve R.L., Reichardt L.F., Huang E.J. J. Cell Biol. 167:257-267(2004) [PubMed: 15492043] [Abstract] Cited for: FUNCTION, INTERACTION WITH POU4F1; POU4F2 AND POU4F3, DEVELOPMENTAL STAGE.
[15]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF077659 mRNA. Translation: AAC63011.1. Frameshift. AF273680 mRNA. Translation: AAG02078.1. AF208292 mRNA. Translation: AAG41237.1. AF333791 mRNA. Translation: AAK07649.1. AF333792 mRNA. Translation: AAK07650.1. AF170301 mRNA. Translation: AAD52566.1. AF170302 mRNA. Translation: AAD52567.1. AK016742 mRNA. Translation: BAB30405.1. AK019821 mRNA. Translation: BAB31866.1.
IPI	IPI00134753. IPI00137890. IPI00228078. IPI00553731. IPI00553825.
PIR	T17088.
RefSeq	NP_001129537.1. NP_034563.2.
UniGene	Mm.23790 Mm.391962
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QZR5. 5 interactions.
STRING	Q9QZR5.
PTM databases
PhosphoSite	Q9QZR5.
Proteomic databases
PRIDE	Q9QZR5.
Genome annotation databases
Ensembl	ENSMUST00000038777; ENSMUSP00000045457; ENSMUSG00000061436; Mus musculus. [Genome view] ENSMUST00000101516; ENSMUSP00000099053; ENSMUSG00000061436; Mus musculus. [Genome view] ENSMUST00000114855; ENSMUSP00000110505; ENSMUSG00000061436; Mus musculus. [Genome view] ENSMUST00000114856; ENSMUSP00000110506; ENSMUSG00000061436; Mus musculus. [Genome view]
GeneID	15258.
KEGG	mmu:15258.
UCSC	uc009bkw.1. mouse. uc009bkx.1. mouse. uc009blb.1. mouse.
Organism-specific databases
CTD	15258.
MGI	MGI:1314872. Hipk2.
Phylogenomic databases
HOVERGEN	Q9QZR5.
Enzyme and pathway databases
BRENDA	2.7.11.1. 244.
Gene expression databases
ArrayExpress	Q9QZR5.
Bgee	Q9QZR5.
CleanEx	MM_HIPK2.
Genevestigator	Q9QZR5.
GermOnline	ENSMUSG00000061436. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	287877.
SOURCE	Search...

Entry information

Entry name

HIPK2_MOUSE

Accession

Primary (citable) accession number: Q9QZR5
Secondary accession number(s): O88905 , Q99P45, Q99P46, Q9D2E6, Q9D474, Q9EQL2, Q9QZR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	April 27, 2001
Last modified:	November 24, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)