dbPTM

HIPK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HIPK2_HUMAN
UniProt AC	Q9H2X6
Protein Name	Homeodomain-interacting protein kinase 2
Gene Name	HIPK2
Organism	Homo sapiens (Human).
Sequence Length	1198
Subcellular Localization	Nucleus, PML body. Cytoplasm. Concentrated in PML/POD/ND10 nuclear bodies. Small amounts are cytoplasmic.
Protein Description	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..
Protein Sequence	MAPVYEGMASHVQVFSPHTLQSSAFCSVKKLKIEPSSNWDMTGYGSHSKVYSQSKNIPLSQPATTTVSTSLPVPNPSLPYEQTIVFPGSTGHIVVTSASSTSVTGQVLGGPHNLMRRSTVSLLDTYQKCGLKRKSEEIENTSSVQIIEEHPPMIQNNASGATVATATTSTATSKNSGSNSEGDYQLVQHEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPVLQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDTDSPYPLWRLKTPDDHEAETGIKSKEARKYIFNCLDDMAQVNMTTDLEGSDMLVEKADRREFIDLLKKMLTIDADKRITPIETLNHPFVTMTHLLDFPHSTHVKSCFQNMEICKRRVNMYDTVNQSKTPFITHVAPSTSTNLTMTFNNQLTTVHNQAPSSTSATISLANPEVSILNYPSTLYQPSAASMAAVAQRSMPLQTGTAQICARPDPFQQALIVCPPGFQGLQASPSKHAGYSVRMENAVPIVTQAPGAQPLQIQPGLLAQQAWPSGTQQILLPPAWQQLTGVATHTSVQHATVIPETMAGTQQLADWRNTHAHGSHYNPIMQQPALLTGHVTLPAAQPLNVGVAHVMRQQPTSTTSSRKSKQHQSSVRNVSTCEVSSSQAISSPQRSKRVKENTPPRCAMVHSSPACSTSVTCGWGDVASSTTRERQRQTIVIPDTPSPTVSVITISSDTDEEEEQKHAPTSTVSKQRKNVISCVTVHDSPYSDSSSNTSPYSVQQRAGHNNANAFDTKGSLENHCTGNPRTIIVPPLKTQASEVLVECDSLVPVNTSHHSSSYKSKSSSNVTSTSGHSSGSSSGAITYRQQRPGPHFQQQQPLNLSQAQQHITTDRTGSHRRQQAYITPTMAQAPYSFPHNSPSHGTVHPHLAAAAAAAHLPTQPHLYTYTAPAALGSTGTVAHLVASQGSARHTVQHTAYPASIVHQVPVSMGPRVLPSPTIHPSQYPAQFAHQTYISASPASTVYTGYPLSPAKVNQYPYI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MAPVYEGMASHV ---CCCCCCCCHHCE	13.00	26552605
10	Phosphorylation	PVYEGMASHVQVFSP CCCCCCHHCEEEECC	18.46	26552605
16	Phosphorylation	ASHVQVFSPHTLQSS HHCEEEECCHHHCCC	19.54	26552605
19	Phosphorylation	VQVFSPHTLQSSAFC EEEECCHHHCCCCEE	29.85	26552605
22	Phosphorylation	FSPHTLQSSAFCSVK ECCHHHCCCCEEEEE	27.09	26552605
23	Phosphorylation	SPHTLQSSAFCSVKK CCHHHCCCCEEEEEE	16.65	26552605
27	Phosphorylation	LQSSAFCSVKKLKIE HCCCCEEEEEEEEEC	30.44	26552605
29	Acetylation	SSAFCSVKKLKIEPS CCCEEEEEEEEECCC	35.77	22503103
32	Sumoylation	FCSVKKLKIEPSSNW EEEEEEEEECCCCCC	54.63	-
32	Sumoylation	FCSVKKLKIEPSSNW EEEEEEEEECCCCCC	54.63	17018294
32	Ubiquitination	FCSVKKLKIEPSSNW EEEEEEEEECCCCCC	54.63	18536714
44	Phosphorylation	SNWDMTGYGSHSKVY CCCCCCCCCCCCCEE	13.29	-
46	Phosphorylation	WDMTGYGSHSKVYSQ CCCCCCCCCCCEEEC	18.99	-
118	Phosphorylation	PHNLMRRSTVSLLDT HHHHHCHHHHHHHHH	23.85	23403867
119	Phosphorylation	HNLMRRSTVSLLDTY HHHHCHHHHHHHHHH	16.59	23403867
121	Phosphorylation	LMRRSTVSLLDTYQK HHCHHHHHHHHHHHH	24.25	-
128	Acetylation	SLLDTYQKCGLKRKS HHHHHHHHHCCCCCC	21.61	22503103
135	Phosphorylation	KCGLKRKSEEIENTS HHCCCCCCHHCCCCC	44.49	-
141	Phosphorylation	KSEEIENTSSVQIIE CCHHCCCCCCCEEEC	15.02	-
162	Phosphorylation	QNNASGATVATATTS ECCCCCCEEEEEECC	17.75	22468782
168	Phosphorylation	ATVATATTSTATSKN CEEEEEECCCCCCCC	22.93	22468782
173	Phosphorylation	ATTSTATSKNSGSNS EECCCCCCCCCCCCC	27.63	22468782
221	Phosphorylation	VKCWKRGTNEIVAIK HHHHHCCCCCEEEEE	33.44	-
228	Ubiquitination	TNEIVAIKILKNHPS CCCEEEEEEHHCCHH	32.04	-
231	Ubiquitination	IVAIKILKNHPSYAR EEEEEEHHCCHHHHH	57.60	-
252	Phosphorylation	SILARLSTESADDYN EEEEECCCCCCCCCC	38.25	-
258	Phosphorylation	STESADDYNFVRAYE CCCCCCCCCEEHHHH	15.85	-
264	Phosphorylation	DYNFVRAYECFQHKN CCCEEHHHHHHHCCC	11.58	-
273	Phosphorylation	CFQHKNHTCLVFEML HHHCCCCEEEHHHHH	19.54	-
294	Phosphorylation	FLKQNKFSPLPLKYI HHHCCCCCCCCHHHH	27.43	20068231
307	Ubiquitination	YIRPVLQQVATALMK HHHHHHHHHHHHHHH	23.74	23503661
309	Ubiquitination	RPVLQQVATALMKLK HHHHHHHHHHHHHHH	5.26	23503661
314	Ubiquitination	QVATALMKLKSLGLI HHHHHHHHHHHHCCE	54.32	23503661
316	Ubiquitination	ATALMKLKSLGLIHA HHHHHHHHHHCCEEC	37.81	23503661
317	O-linked_Glycosylation	TALMKLKSLGLIHAD HHHHHHHHHCCEECC	37.80	30379171
322	Ubiquitination	LKSLGLIHADLKPEN HHHHCCEECCCCHHH	20.45	23503661
324	Ubiquitination	SLGLIHADLKPENIM HHCCEECCCCHHHEE	40.85	23503661
336	Phosphorylation	NIMLVDPSRQPYRVK HEEEECCCCCCEEEE	38.80	-
340	Phosphorylation	VDPSRQPYRVKVIDF ECCCCCCEEEEEEEC	21.50	-
343	Ubiquitination	SRQPYRVKVIDFGSA CCCCEEEEEEECCCH	25.19	-
355	Ubiquitination	GSASHVSKAVCSTYL CCHHHHHHHHHHHHH	43.69	-
359	Phosphorylation	HVSKAVCSTYLQSRY HHHHHHHHHHHHHCC	17.31	21945579
360	Phosphorylation	VSKAVCSTYLQSRYY HHHHHHHHHHHHCCC	24.11	21945579
361	Phosphorylation	SKAVCSTYLQSRYYR HHHHHHHHHHHCCCC	6.10	19664994
364	Phosphorylation	VCSTYLQSRYYRAPE HHHHHHHHCCCCCCH	21.47	21945579
366	Phosphorylation	STYLQSRYYRAPEII HHHHHHCCCCCCHHH	11.53	22817900
367	Phosphorylation	TYLQSRYYRAPEIIL HHHHHCCCCCCHHHH	10.13	22817900
423	Phosphorylation	TQGLPAEYLLSAGTK CCCCCHHHHHCCCCC	18.30	-
423	Ubiquitination	TQGLPAEYLLSAGTK CCCCCHHHHHCCCCC	18.30	21963094
430	Acetylation	YLLSAGTKTTRFFNR HHHCCCCCEEECCCC	47.16	-
430	Ubiquitination	YLLSAGTKTTRFFNR HHHCCCCCEEECCCC	47.16	21906983
430 (in isoform 1)	Ubiquitination	-	47.16	21906983
430 (in isoform 2)	Ubiquitination	-	47.16	21906983
430 (in isoform 3)	Ubiquitination	-	47.16	21906983
438	Ubiquitination	TTRFFNRDTDSPYPL EEECCCCCCCCCCCC	56.84	21963094
441	Phosphorylation	FFNRDTDSPYPLWRL CCCCCCCCCCCCEEE	28.55	27067055
443	Phosphorylation	NRDTDSPYPLWRLKT CCCCCCCCCCEEECC	18.21	-
449	Acetylation	PYPLWRLKTPDDHEA CCCCEEECCCCCCCC	49.81	22503103
482	Phosphorylation	DMAQVNMTTDLEGSD HHHHCCCCCCCCCCC	16.38	-
493	Ubiquitination	EGSDMLVEKADRREF CCCCCEECHHCHHHH	38.27	23503661
495	Ubiquitination	SDMLVEKADRREFID CCCEECHHCHHHHHH	11.31	23503661
506	Ubiquitination	EFIDLLKKMLTIDAD HHHHHHHHHHCCCCC	38.83	-
514	Ubiquitination	MLTIDADKRITPIET HHCCCCCCCCCCHHH	47.63	-
517	Phosphorylation	IDADKRITPIETLNH CCCCCCCCCHHHCCC	23.42	-
545	Ubiquitination	STHVKSCFQNMEICK CHHHHHHHHCHHHHH	8.31	21963094
552	Ubiquitination	FQNMEICKRRVNMYD HHCHHHHHHHCCHHH	49.23	21963094
558	Phosphorylation	CKRRVNMYDTVNQSK HHHHCCHHHHCCCCC	11.85	27642862
560	Ubiquitination	RRVNMYDTVNQSKTP HHCCHHHHCCCCCCC	12.13	21963094
565	Ubiquitination	YDTVNQSKTPFITHV HHHCCCCCCCCEEEE	50.91	18536714
566	Phosphorylation	DTVNQSKTPFITHVA HHCCCCCCCCEEEEC	28.78	-
609	Ubiquitination	TISLANPEVSILNYP EEEECCCCCEECCCC	49.02	21963094
634	Phosphorylation	MAAVAQRSMPLQTGT HHHHHHHCCCCCCCC	16.81	-
668	Phosphorylation	GFQGLQASPSKHAGY CCCCCCCCCCCCCCE	19.42	27251275
671	Ubiquitination	GLQASPSKHAGYSVR CCCCCCCCCCCEEEE	40.64	6714
687	Phosphorylation	ENAVPIVTQAPGAQP CCCEEEEECCCCCCC	21.52	-
731	Ubiquitination	TGVATHTSVQHATVI HCEECCCCCCEEEEC	16.51	21963094
796	Phosphorylation	HVMRQQPTSTTSSRK HHHCCCCCCCCCCHH	34.07	-
797	Phosphorylation	VMRQQPTSTTSSRKS HHCCCCCCCCCCHHH	36.05	22210691
799	Phosphorylation	RQQPTSTTSSRKSKQ CCCCCCCCCCHHHHH	25.19	22210691
800	Phosphorylation	QQPTSTTSSRKSKQH CCCCCCCCCHHHHHH	28.38	19369195
801	Phosphorylation	QPTSTTSSRKSKQHQ CCCCCCCCHHHHHHH	41.45	28509920
803	Acetylation	TSTTSSRKSKQHQSS CCCCCCHHHHHHHHH	65.04	22503103
803	Ubiquitination	TSTTSSRKSKQHQSS CCCCCCHHHHHHHHH	65.04	18536714
804	Phosphorylation	STTSSRKSKQHQSSV CCCCCHHHHHHHHHC	36.12	22210691
805	Acetylation	TTSSRKSKQHQSSVR CCCCHHHHHHHHHCC	55.63	22503103
805	Ubiquitination	TTSSRKSKQHQSSVR CCCCHHHHHHHHHCC	55.63	18536714
815	Phosphorylation	QSSVRNVSTCEVSSS HHHCCCCEECEECHH	30.78	27080861
816	Phosphorylation	SSVRNVSTCEVSSSQ HHCCCCEECEECHHH	14.38	27080861
821	Phosphorylation	VSTCEVSSSQAISSP CEECEECHHHHCCCC	31.48	24719451
826	Phosphorylation	VSSSQAISSPQRSKR ECHHHHCCCCCHHHC	38.69	25850435
827	Phosphorylation	SSSQAISSPQRSKRV CHHHHCCCCCHHHCH	20.95	19369195
838	Phosphorylation	SKRVKENTPPRCAMV HHCHHCCCCCCEEEE	35.44	24825855
847	Phosphorylation	PRCAMVHSSPACSTS CCEEEECCCCCCCCE	26.97	27080861
848	Phosphorylation	RCAMVHSSPACSTSV CEEEECCCCCCCCEE	11.14	27251275
852	O-linked_Glycosylation	VHSSPACSTSVTCGW ECCCCCCCCEEECCC	26.31	30379171
880	Phosphorylation	QTIVIPDTPSPTVSV CEEECCCCCCCEEEE	21.95	-
882	Phosphorylation	IVIPDTPSPTVSVIT EECCCCCCCEEEEEE	34.98	-
905	Phosphorylation	EEQKHAPTSTVSKQR HHHHCCCCCHHHHHH	37.50	22210691
907	Phosphorylation	QKHAPTSTVSKQRKN HHCCCCCHHHHHHCC	31.14	28555341
909	Phosphorylation	HAPTSTVSKQRKNVI CCCCCHHHHHHCCEE	24.14	22210691
910	Acetylation	APTSTVSKQRKNVIS CCCCHHHHHHCCEEE	50.19	22503103
917	Phosphorylation	KQRKNVISCVTVHDS HHHCCEEEEEEECCC	9.76	27080861
920	Phosphorylation	KNVISCVTVHDSPYS CCEEEEEEECCCCCC	19.22	27080861
924	Phosphorylation	SCVTVHDSPYSDSSS EEEEECCCCCCCCCC	15.74	27080861
926	Phosphorylation	VTVHDSPYSDSSSNT EEECCCCCCCCCCCC	29.12	27080861
927	Phosphorylation	TVHDSPYSDSSSNTS EECCCCCCCCCCCCC	34.11	27080861
929	Phosphorylation	HDSPYSDSSSNTSPY CCCCCCCCCCCCCCC	29.71	27080861
930	Phosphorylation	DSPYSDSSSNTSPYS CCCCCCCCCCCCCCC	32.38	27080861
931	Phosphorylation	SPYSDSSSNTSPYSV CCCCCCCCCCCCCCH	48.34	27080861
933	Phosphorylation	YSDSSSNTSPYSVQQ CCCCCCCCCCCCHHH	32.78	27080861
934	Phosphorylation	SDSSSNTSPYSVQQR CCCCCCCCCCCHHHH	26.54	27080861
953	Sumoylation	NANAFDTKGSLENHC CCCCCCCCCCHHHCC	48.63	-
953	Acetylation	NANAFDTKGSLENHC CCCCCCCCCCHHHCC	48.63	22503103
953	Sumoylation	NANAFDTKGSLENHC CCCCCCCCCCHHHCC	48.63	28112733
973	Acetylation	TIIVPPLKTQASEVL EEEECCCCCCCCEEE	44.35	22503103
973	Sumoylation	TIIVPPLKTQASEVL EEEECCCCCCCCEEE	44.35	28112733
992	Phosphorylation	SLVPVNTSHHSSSYK CEEECCCCCCCCCCC	17.63	-
1001	Acetylation	HSSSYKSKSSSNVTS CCCCCCCCCCCCCEE	50.64	22503103
1004	Phosphorylation	SYKSKSSSNVTSTSG CCCCCCCCCCEECCC	42.27	24905233
1009	O-linked_Glycosylation	SSSNVTSTSGHSSGS CCCCCEECCCCCCCC	29.39	30379171
1014	Phosphorylation	TSTSGHSSGSSSGAI EECCCCCCCCCCCCE	36.70	24905233
1018	Phosphorylation	GHSSGSSSGAITYRQ CCCCCCCCCCEEECC	33.66	24905233
1041	Phosphorylation	QQQPLNLSQAQQHIT CCCCCCHHHHHHHHC	23.54	-
1114	Phosphorylation	APAALGSTGTVAHLV CCHHCCCCCHHHHHH	34.76	-
1136	Phosphorylation	HTVQHTAYPASIVHQ CCCEECCCCCEEEEE	10.65	-
1147	O-linked_Glycosylation	IVHQVPVSMGPRVLP EEEEEECCCCCCCCC	16.38	30379171
1151	Methylation	VPVSMGPRVLPSPTI EECCCCCCCCCCCCC	36.55	115478551
1155	Phosphorylation	MGPRVLPSPTIHPSQ CCCCCCCCCCCCHHH	30.43	-
1188	Phosphorylation	VYTGYPLSPAKVNQY EECCCCCCCHHCCCC	20.50	24719451
1191	Sumoylation	GYPLSPAKVNQYPYI CCCCCCHHCCCCCCC	45.14	-
1191	Sumoylation	GYPLSPAKVNQYPYI CCCCCCHHCCCCCCC	45.14	-
1191	Ubiquitination	GYPLSPAKVNQYPYI CCCCCCHHCCCCCCC	45.14	17349959
1197	Phosphorylation	AKVNQYPYI------ HHCCCCCCC------	17.83	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
119	T	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
119	T	Phosphorylation	Kinase	AMPKA2	P54646	PSP
121	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
121	S	Phosphorylation	Kinase	AMPKA2	P54646	PSP
361	Y	Phosphorylation	Kinase	SRC	P12931	PSP
361	Y	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
364	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
367	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
668	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
827	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
838	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
848	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
880	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
882	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
924	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
934	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
1114	T	Phosphorylation	Kinase	AMPKA2	P54646	PSP
1114	T	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:16212962
-	K	Ubiquitination	E3 ubiquitin ligase	WSB1	Q9Y6I7	PMID:18093972
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:18536714
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO3	Q9UK99	PMID:18809579

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
32	K	Sumoylation	17018294
Sumoylation on Lys-32 is promoted by the E3 SUMO-protein ligase CBX4.
46	S	Phosphorylation	16601678
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.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HIPK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DAXX_HUMAN	DAXX	physical	14678985
SP100_HUMAN	SP100	physical	14647468
SKI_HUMAN	SKI	physical	12874272
SMAD1_HUMAN	SMAD1	physical	12874272
T53I1_HUMAN	TP53INP1	physical	12851404
P53_HUMAN	TP53	physical	11740489
CBP_HUMAN	CREBBP	physical	11740489
RANB9_HUMAN	RANBP9	physical	12220523
UBC9_MOUSE	Ube2i	physical	10535925
TRADD_HUMAN	TRADD	physical	11032752
FBXW7_HUMAN	FBXW7	physical	18765672
FBW1A_HUMAN	BTRC	physical	18765672
CUL1_HUMAN	CUL1	physical	18765672
MYB_HUMAN	MYB	physical	16055500
RUNX1_HUMAN	RUNX1	physical	16917507
EP300_HUMAN	EP300	physical	16917507
HIPK2_HUMAN	HIPK2	physical	16917507
NLK_HUMAN	NLK	physical	15082531
MYB_HUMAN	MYB	physical	15082531
MYBA_HUMAN	MYBL1	physical	16055500
MYBB_HUMAN	MYBL2	physical	16055500
WSB1_HUMAN	WSB1	physical	18093972
SIAH1_HUMAN	SIAH1	physical	19043406
SIAH2_HUMAN	SIAH2	physical	19043406
GROA_HUMAN	CXCL1	physical	15896780
P53_HUMAN	TP53	physical	15896780
H2B2E_HUMAN	HIST2H2BE	physical	22658722
HIPK2_HUMAN	HIPK2	physical	22658722
UBC9_HUMAN	UBE2I	physical	15958389
SENP2_HUMAN	SENP2	physical	15958389
SIAH1_HUMAN	SIAH1	physical	18536714
FBX3_HUMAN	FBXO3	physical	18809579
PML_HUMAN	PML	physical	21145359
CBX4_HUMAN	CBX4	physical	21145359
SUMO1_HUMAN	SUMO1	physical	21145359
PML_HUMAN	PML	physical	20188669
PML_HUMAN	PML	physical	21192925
PML_HUMAN	PML	physical	19015637
SIAH1_HUMAN	SIAH1	physical	19250734
PAX6_HUMAN	PAX6	physical	16407227
DCAF7_HUMAN	DCAF7	physical	20940704
DYR1A_HUMAN	DYRK1A	physical	20940704
DYR1B_HUMAN	DYRK1B	physical	20940704
MDM2_HUMAN	MDM2	physical	16212962
MDM2_HUMAN	MDM2	physical	17349959
P53_HUMAN	TP53	physical	17349959
HIPK2_HUMAN	HIPK2	physical	17349959
ZBTB4_HUMAN	ZBTB4	physical	19448668
MECP2_HUMAN	MECP2	physical	19820693
MBP_HUMAN	MBP	physical	11120354
AXIN1_HUMAN	AXIN1	physical	23826318
MDM2_HUMAN	MDM2	physical	23826318
MKNK1_HUMAN	MKNK1	physical	21988832
AATF_HUMAN	AATF	physical	25210797
P53_HUMAN	TP53	physical	25313037
XAF1_HUMAN	XAF1	physical	25313037
ABL1_HUMAN	ABL1	physical	25944899
PARP1_HUMAN	PARP1	physical	27787517
CHIP_HUMAN	STUB1	physical	27787517
DCAF7_HUMAN	DCAF7	physical	27307198
ACTBL_HUMAN	ACTBL2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HIPK2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361; SER-827 ANDTHR-838, AND MASS SPECTROMETRY.	19369195 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361, AND MASSSPECTROMETRY.	18083107 [Abstract]
Sumoylation
Reference	PubMed
"Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity byits substrate protein HIPK2."; Roscic A., Moeller A., Calzado M.A., Renner F., Wimmer V.C.,Gresko E., Luedi K.S., Schmitz M.L.; Mol. Cell 24:77-89(2006). Cited for: INTERACTION WITH CBX4, SUMOYLATION AT LYS-32, AND FUNCTION.	17018294 [Abstract]

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