HIPK3_HUMAN - dbPTM
HIPK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIPK3_HUMAN
UniProt AC Q9H422
Protein Name Homeodomain-interacting protein kinase 3
Gene Name HIPK3
Organism Homo sapiens (Human).
Sequence Length 1215
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Serine/threonine-protein kinase involved in transcription regulation, apoptosis and steroidogenic gene expression. Phosphorylates JUN and RUNX2. Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors. The phosphorylation of NR5A1 activates SF1 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. In osteoblasts, supports transcription activation: phosphorylates RUNX2 that synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE)..
Protein Sequence MASQVLVYPPYVYQTQSSAFCSVKKLKVEPSSCVFQERNYPRTYVNGRNFGNSHPPTKGSAFQTKIPFNRPRGHNFSLQTSAVVLKNTAGATKVIAAQAQQAHVQAPQIGAWRNRLHFLEGPQRCGLKRKSEELDNHSSAMQIVDELSILPAMLQTNMGNPVTVVTATTGSKQNCTTGEGDYQLVQHEVLCSMKNTYEVLDFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTENADEYNFVRAYECFQHRNHTCLVFEMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKSTRFFCKETDMSHSGWRLKTLEEHEAETGMKSKEARKYIFNSLDDVAHVNTVMDLEGSDLLAEKADRREFVSLLKKMLLIDADLRITPAETLNHPFVNMKHLLDFPHSNHVKSCFHIMDICKSHLNSCDTNNHNKTSLLRPVASSSTATLTANFTKIGTLRSQALTTSAHSVVHHGIPLQAGTAQFGCGDAFQQTLIICPPAIQGIPATHGKPTSYSIRVDNTVPLVTQAPAVQPLQIRPGVLSQTWSGRTQQMLVPAWQQVTPLAPATTTLTSESVAGSHRLGDWGKMISCSNHYNSVMPQPLLTNQITLSAPQPVSVGIAHVVWPQPATTKKNKQCQNRGILVKLMEWEPGREEINAFSWSNSLQNTNIPHSAFISPKIINGKDVEEVSCIETQDNQNSEGEARNCCETSIRQDSDSSVSDKQRQTIIIADSPSPAVSVITISSDTDEEETSQRHSLRECKGSLDCEACQSTLNIDRMCSLSSPDSTLSTSSSGQSSPSPCKRPNSMSDEEQESSCDTVDGSPTSDSSGHDSPFAESTFVEDTHENTELVSSADTETKPAVCSVVVPPVELENGLNADEHMANTDSICQPLIKGRSAPGRLNQPSAVGTRQQKLTSAFQQQHLNFSQVQHFGSGHQEWNGNFGHRRQQAYIPTSVTSNPFTLSHGSPNHTAVHAHLAGNTHLGGQPTLLPYPSSATLSSAAPVAHLLASPCTSRPMLQHPTYNISHPSGIVHQVPVGLNPRLLPSPTIHQTQYKPIFPPHSYIAASPAYTGFPLSPTKLSQYPYM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
8PhosphorylationMASQVLVYPPYVYQT
CCCEEEECCCCEEEC		8.37-
27SumoylationFCSVKKLKVEPSSCV
CCCEEECEECCHHCE		54.13-
27SumoylationFCSVKKLKVEPSSCV
CCCEEECEECCHHCE		54.1328112733
58UbiquitinationGNSHPPTKGSAFQTK
CCCCCCCCCCCEECC		57.55-
131PhosphorylationRCGLKRKSEELDNHS
CCCCCCCHHHHCCCC		40.0924043423
138PhosphorylationSEELDNHSSAMQIVD
HHHHCCCCHHHHHHH		26.5024043423
139PhosphorylationEELDNHSSAMQIVDE
HHHCCCCHHHHHHHH		21.8724043423
148PhosphorylationMQIVDELSILPAMLQ
HHHHHHHCHHHHHHH		21.7424043423
156PhosphorylationILPAMLQTNMGNPVT
HHHHHHHHCCCCCEE		24.1824043423
163PhosphorylationTNMGNPVTVVTATTG
HCCCCCEEEEEECCC		15.5424043423
166PhosphorylationGNPVTVVTATTGSKQ
CCCEEEEEECCCCCC		17.6024043423
168PhosphorylationPVTVVTATTGSKQNC
CEEEEEECCCCCCCC		23.4824043423
169PhosphorylationVTVVTATTGSKQNCT
EEEEEECCCCCCCCC		36.6724043423
171PhosphorylationVVTATTGSKQNCTTG
EEEECCCCCCCCCCC		29.0424043423
219PhosphorylationVKCWKRGTNEIVAIK
HHHHHCCCCCEEEEE		33.44-
226UbiquitinationTNEIVAIKILKNHPS
CCCEEEEEEHHCCHH		32.04-
229UbiquitinationIVAIKILKNHPSYAR
EEEEEEHHCCHHHHH		57.60-
292PhosphorylationFLKQNKFSPLPLKVI
HHHCCCCCCCCHHHH		27.4320068231
324UbiquitinationGLIHADLKPENIMLV
CCEECCCCHHHEEEE		51.32-
341UbiquitinationVRQPYRVKVIDFGSA
CCCCEEEEEEECCCC		25.19-
353UbiquitinationGSASHVSKTVCSTYL
CCCCCCCHHHHHHHH		43.84-
354PhosphorylationSASHVSKTVCSTYLQ
CCCCCCHHHHHHHHH		21.1623403867
357PhosphorylationHVSKTVCSTYLQSRY
CCCHHHHHHHHHHCC		18.7523927012
358PhosphorylationVSKTVCSTYLQSRYY
CCHHHHHHHHHHCCC		24.1123927012
359PhosphorylationSKTVCSTYLQSRYYR
CHHHHHHHHHHCCCC		6.1023927012
359 (in isoform 2)Phosphorylation-6.1024719451
362PhosphorylationVCSTYLQSRYYRAPE
HHHHHHHHCCCCCCH		21.4723927012
365PhosphorylationTYLQSRYYRAPEIIL
HHHHHCCCCCCHHHH		10.1322817900
428 (in isoform 1)Ubiquitination-43.8521906983
428UbiquitinationQLLNVGTKSTRFFCK
HEEECCCCCCEEEEE		43.8521906983
428 (in isoform 2)Ubiquitination-43.8521906983
435UbiquitinationKSTRFFCKETDMSHS
CCCEEEEECCCCCCC		59.50-
447UbiquitinationSHSGWRLKTLEEHEA
CCCCEEEEEHHHHHH		42.35-
459 (in isoform 1)Ubiquitination-60.7721906983
459UbiquitinationHEAETGMKSKEARKY
HHHHHCCCCHHHHHH		60.772190698
459 (in isoform 2)Ubiquitination-60.7721906983
461UbiquitinationAETGMKSKEARKYIF
HHHCCCCHHHHHHHH		50.29-
466PhosphorylationKSKEARKYIFNSLDD
CCHHHHHHHHHCHHH		12.75-
492UbiquitinationGSDLLAEKADRREFV
CCHHHHHHCCHHHHH		50.40-
500PhosphorylationADRREFVSLLKKMLL
CCHHHHHHHHHHHHH		33.0524719451
503UbiquitinationREFVSLLKKMLLIDA
HHHHHHHHHHHHHCC		41.24-
504UbiquitinationEFVSLLKKMLLIDAD
HHHHHHHHHHHHCCC		34.45-
515 (in isoform 2)Phosphorylation-15.2624719451
515PhosphorylationIDADLRITPAETLNH
HCCCCCCCCHHHHCC		15.2624719451
519 (in isoform 2)Phosphorylation-34.6624719451
519PhosphorylationLRITPAETLNHPFVN
CCCCCHHHHCCCCCC		34.6624719451
528MethylationNHPFVNMKHLLDFPH
CCCCCCHHHHHCCCC		26.37115970639
528UbiquitinationNHPFVNMKHLLDFPH
CCCCCCHHHHHCCCC		26.37-
563UbiquitinationCDTNNHNKTSLLRPV
CCCCCCCCCCCCEEE		31.75-
565PhosphorylationTNNHNKTSLLRPVAS
CCCCCCCCCCEEECC		27.3224719451
565 (in isoform 2)Phosphorylation-27.3224719451
645PhosphorylationHGKPTSYSIRVDNTV
CCCCCEEEEEECCCE		12.0424719451
772 (in isoform 2)Phosphorylation-2.8624719451
791PhosphorylationEINAFSWSNSLQNTN
HCCEEECCCCCCCCC		18.4926437602
793PhosphorylationNAFSWSNSLQNTNIP
CEEECCCCCCCCCCC		26.3029802988
802PhosphorylationQNTNIPHSAFISPKI
CCCCCCCCCEECCEE		21.3725690035
806PhosphorylationIPHSAFISPKIINGK
CCCCCEECCEEECCC		17.4325627689
813UbiquitinationSPKIINGKDVEEVSC
CCEEECCCCCEEEEE		54.86-
852UbiquitinationSDSSVSDKQRQTIII
CCCCCCHHHCCEEEE		39.61-
891UbiquitinationRHSLRECKGSLDCEA
HHHHHHCCCCCCHHH		46.94-
893PhosphorylationSLRECKGSLDCEACQ
HHHHCCCCCCHHHHH		13.4128348404
944PhosphorylationMSDEEQESSCDTVDG
CCHHHHHHCCCCCCC		35.6422468782
952PhosphorylationSCDTVDGSPTSDSSG
CCCCCCCCCCCCCCC		22.1222468782
1191PhosphorylationKPIFPPHSYIAASPA
CCCCCCCCEEECCCC		24.8222210691
1200PhosphorylationIAASPAYTGFPLSPT
EECCCCCCCCCCCCC		34.1622210691
1205PhosphorylationAYTGFPLSPTKLSQY
CCCCCCCCCCCHHHC		30.6626074081
1207PhosphorylationTGFPLSPTKLSQYPY
CCCCCCCCCHHHCCC		41.0426074081
1214PhosphorylationTKLSQYPYM------
CCHHHCCCC------		15.5522210691
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

Oops, there are no upstream regulatory protein records of HIPK3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HIPK3_HUMAN !!
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 HIPK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P73_HUMANTP73physical
10961991
P53_HUMANTP53physical
10961991
SUMO1_HUMANSUMO1physical
10961991
TNR6_HUMANFASphysical
11034606
FADD_HUMANFADDphysical
11034606
TRA2B_HUMANTRA2Bphysical
16000324
SRSF5_HUMANSRSF5physical
16000324
ROA1_HUMANHNRNPA1physical
16000324
ROA2_HUMANHNRNPA2B1physical
16000324
HNRH1_HUMANHNRNPH1physical
16000324
SRSF1_HUMANSRSF1physical
16000324
SIAH2_HUMANSIAH2physical
15231748
TGFI1_HUMANTGFB1I1physical
15231748
TOX4_HUMANTOX4physical
15231748
C1QA_HUMANC1QAphysical
15231748
COT2_HUMANNR2F2physical
15231748
ARRB2_HUMANARRB2physical
15231748
LIMK2_HUMANLIMK2physical
15231748
ZYX_HUMANZYXphysical
15231748
LIMS2_HUMANLIMS2physical
15231748
SIAH1_HUMANSIAH1physical
15231748
GORS1_HUMANGORASP1physical
15231748
HEYL_HUMANHEYLphysical
15231748
MTMR4_HUMANMTMR4physical
15231748
LIMD1_HUMANLIMD1physical
15231748
ZN107_HUMANZNF107physical
15231748
P53_HUMANTP53physical
23602568
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 HIPK3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-359, AND MASSSPECTROMETRY.
"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-359, AND MASSSPECTROMETRY.
"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-359, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-359, AND MASSSPECTROMETRY.

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