HIPK1_HUMAN - dbPTM
HIPK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIPK1_HUMAN
UniProt AC Q86Z02
Protein Name Homeodomain-interacting protein kinase 1
Gene Name HIPK1
Organism Homo sapiens (Human).
Sequence Length 1210
Subcellular Localization Nucleus. Cytoplasm. Predominantly nuclear. Translocates from nucleus to cytoplasm in response to stress stimuli via SENP1-mediated desumoylation.
Protein Description Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti-oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation..
Protein Sequence MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQANSSHQVANFNIPAYDQGLLLPAPAVEHIVVTAADSSGSAATSTFQSSQTLTHRSNVSLLEPYQKCGLKRKSEEVDSNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDPNLGYPLWRLKTPEEHELETGIKSKEARKYIFNCLDDMAQVNMSTDLEGTDMLAEKADRREYIDLLKKMLTIDADKRITPLKTLNHQFVTMTHLLDFPHSNHVKSCFQNMEICKRRVHMYDTVSQIKSPFTTHVAPNTSTNLTMSFSNQLNTVHNQASVLASSSTAAAATLSLANSDVSLLNYQSALYPSSAAPVPGVAQQGVSLQPGTTQICTQTDPFQQTFIVCPPAFQTGLQATTKHSGFPVRMDNAVPIVPQAPAAQPLQIQSGVLTQGSCTPLMVATLHPQVATITPQYAVPFTLSCAAGRPALVEQTAAVLQAWPGGTQQILLPSTWQQLPGVALHNSVQPTAMIPEAMGSGQQLADWRNAHSHGNQYSTIMQQPSLLTNHVTLATAQPLNVGVAHVVRQQQSSSLPSKKNKQSAPVSSKSSLDVLPSQVYSLVGSSPLRTTSSYNSLVPVQDQHQPIIIPDTPSPPVSVITIRSDTDEEEDNKYKPSSSGLKPRSNVISYVTVNDSPDSDSSLSSPYSTDTLSALRGNSGSVLEGPGRVVADGTGTRTIIVPPLKTQLGDCTVATQASGLLSNKTKPVASVSGQSSGCCITPTGYRAQRGGTSAAQPLNLSQNQQSSAAPTSQERSSNPAPRRQQAFVAPLSQAPYTFQHGSPLHSTGHPHLAPAPAHLPSQAHLYTYAAPTSAAALGSTSSIAHLFSPQGSSRHAAAYTTHPSTLVHQVPVSVGPSLLTSASVAPAQYQHQFATQSYIGSSRGSTIYTGYPLSPTKISQYSYL
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
9PhosphorylationASQLQVFSPPSVSSS
CCCCEECCCCCCCHH		36.7228348404
22AcetylationSSAFCSAKKLKIEPS
HHHHCCCCCCEECCC		42.2025953088
25SumoylationFCSAKKLKIEPSGWD
HCCCCCCEECCCCCC		54.63-
25SumoylationFCSAKKLKIEPSGWD
HCCCCCCEECCCCCC		54.6328112733
27 (in isoform 4)Ubiquitination-31.6521890473
29PhosphorylationKKLKIEPSGWDVSGQ
CCCEECCCCCCCCCC		39.46-
34PhosphorylationEPSGWDVSGQSSNDK
CCCCCCCCCCCCCCC		28.74-
37PhosphorylationGWDVSGQSSNDKYYT
CCCCCCCCCCCCEEE		34.3325159151
38PhosphorylationWDVSGQSSNDKYYTH
CCCCCCCCCCCEEEE		40.9525159151
46 (in isoform 4)Ubiquitination-21.3821890473
47UbiquitinationDKYYTHSKTLPATQG
CCEEEEECCEECCCC		46.61-
47 (in isoform 3)Ubiquitination-46.6121890473
58 (in isoform 4)Ubiquitination-32.0121890473
66 (in isoform 3)Ubiquitination-38.8621890473
78 (in isoform 3)Ubiquitination-12.4921890473
102 (in isoform 4)Ubiquitination-21.8821890473
120SumoylationSLLEPYQKCGLKRKS
HHCHHHHHCCCCCCC		25.15-
120SumoylationSLLEPYQKCGLKRKS
HHCHHHHHCCCCCCC		25.1528112733
120UbiquitinationSLLEPYQKCGLKRKS
HHCHHHHHCCCCCCC		25.15-
122 (in isoform 3)Ubiquitination-41.0721890473
124SumoylationPYQKCGLKRKSEEVD
HHHHCCCCCCCEEEC		42.9628112733
124UbiquitinationPYQKCGLKRKSEEVD
HHHHCCCCCCCEEEC		42.96-
127PhosphorylationKCGLKRKSEEVDSNG
HCCCCCCCEEECCCC		42.92-
151O-linked_GlycosylationPLMLQNRTVVGAAAT
CCEECCCEEEEEEEE		27.3928314751
213UbiquitinationKCWKRSTKEIVAIKI
HHHHCCCCEEEEEEE		46.84-
219UbiquitinationTKEIVAIKILKNHPS
CCEEEEEEEHHHCHH		32.04-
222UbiquitinationIVAIKILKNHPSYAR
EEEEEEHHHCHHHHH		57.60-
236PhosphorylationRQGQIEVSILSRLSS
HCCCEEEHHHHHCCC		12.6724719451
239PhosphorylationQIEVSILSRLSSENA
CEEEHHHHHCCCCCC		29.5224719451
285PhosphorylationFLKQNKFSPLPLKYI
HHHCCCCCCCCHHHH		27.4320068231
307 (in isoform 2)Ubiquitination-37.81-
317UbiquitinationGLIHADLKPENIMLV
CCEECCCCHHHEEEE		51.32-
334UbiquitinationVRQPYRVKVIDFGSA
CCCCEEEEEEECCCH		25.19-
346UbiquitinationGSASHVSKAVCSTYL
CCHHHHHHHHHHHHH		43.69-
350PhosphorylationHVSKAVCSTYLQSRY
HHHHHHHHHHHHHCC		17.3121945579
351PhosphorylationVSKAVCSTYLQSRYY
HHHHHHHHHHHHCCC		24.1121945579
352PhosphorylationSKAVCSTYLQSRYYR
HHHHHHHHHHHCCCC		6.1019664994
355PhosphorylationVCSTYLQSRYYRAPE
HHHHHHHHCCCCCCH		21.4721945579
357PhosphorylationSTYLQSRYYRAPEII
HHHHHHCCCCCCHHH		11.5322817900
358PhosphorylationTYLQSRYYRAPEIIL
HHHHHCCCCCCHHHH		10.1322817900
414PhosphorylationTQGLPAEYLLSAGTK
CCCCCHHHHHCCCCC		18.30-
421UbiquitinationYLLSAGTKTTRFFNR
HHHCCCCCCEECCCC		47.1621906983
421 (in isoform 2)Ubiquitination-47.1621890473
440UbiquitinationGYPLWRLKTPEEHEL
CCCEEECCCCCHHHC		54.1621906983
440 (in isoform 2)Ubiquitination-54.1621890473
449PhosphorylationPEEHELETGIKSKEA
CCHHHCHHCCCCHHH		57.7528634298
452UbiquitinationHELETGIKSKEARKY
HHCHHCCCCHHHHHH		57.7421906983
452 (in isoform 2)Ubiquitination-57.7421890473
461 (in isoform 4)Ubiquitination-4.8521890473
481 (in isoform 3)Ubiquitination-3.7121890473
491PhosphorylationEKADRREYIDLLKKM
HHCCHHHHHHHHHHH		9.6420068231
492 (in isoform 1)Ubiquitination-2.2921890473
496UbiquitinationREYIDLLKKMLTIDA
HHHHHHHHHHHCCCC		43.35-
496 (in isoform 2)Ubiquitination-43.3521890473
497UbiquitinationEYIDLLKKMLTIDAD
HHHHHHHHHHCCCCC		38.83-
505UbiquitinationMLTIDADKRITPLKT
HHCCCCCCCCCCCCC		47.63-
511 (in isoform 1)Ubiquitination-52.7721890473
523 (in isoform 1)Ubiquitination-3.4521890473
534 (in isoform 4)Ubiquitination-21.0521890473
543UbiquitinationFQNMEICKRRVHMYD
HHCHHHHHHHHHHHC		49.23-
549PhosphorylationCKRRVHMYDTVSQIK
HHHHHHHHCHHHHCC		8.1227642862
554 (in isoform 3)Ubiquitination-42.6721890473
593PhosphorylationASVLASSSTAAAATL
HHHHHCCHHHHHHHH		21.4119664994
838PhosphorylationHVVRQQQSSSLPSKK
HHHHHHHCCCCCCCC		19.9822210691
840PhosphorylationVRQQQSSSLPSKKNK
HHHHHCCCCCCCCCC		49.9328290473
843PhosphorylationQQSSSLPSKKNKQSA
HHCCCCCCCCCCCCC		62.6524719451
853PhosphorylationNKQSAPVSSKSSLDV
CCCCCCCCCCHHHHC		30.8720068231
854PhosphorylationKQSAPVSSKSSLDVL
CCCCCCCCCHHHHCC		36.4720068231
855UbiquitinationQSAPVSSKSSLDVLP
CCCCCCCCHHHHCCH		36.2421906983
855 (in isoform 2)Ubiquitination-36.2421890473
863PhosphorylationSSLDVLPSQVYSLVG
HHHHCCHHHHHHHHC		28.2827732954
866PhosphorylationDVLPSQVYSLVGSSP
HCCHHHHHHHHCCCC		6.6628450419
867PhosphorylationVLPSQVYSLVGSSPL
CCHHHHHHHHCCCCC		20.0928450419
871PhosphorylationQVYSLVGSSPLRTTS
HHHHHHCCCCCCCCC		22.6925849741
872PhosphorylationVYSLVGSSPLRTTSS
HHHHHCCCCCCCCCC		23.2528102081
876PhosphorylationVGSSPLRTTSSYNSL
HCCCCCCCCCCCCCC		38.4222817900
879PhosphorylationSPLRTTSSYNSLVPV
CCCCCCCCCCCCCCC		26.6622817900
920PhosphorylationDEEEDNKYKPSSSGL
CHHCCCCCCCCCCCC		34.0923403867
921UbiquitinationEEEDNKYKPSSSGLK
HHCCCCCCCCCCCCC		39.78-
923PhosphorylationEDNKYKPSSSGLKPR
CCCCCCCCCCCCCCC		32.7428555341
926 (in isoform 1)Ubiquitination-39.4021890473
928UbiquitinationKPSSSGLKPRSNVIS
CCCCCCCCCCCCEEE		41.742190698
928 (in isoform 2)Ubiquitination-41.7421890473
959PhosphorylationPYSTDTLSALRGNSG
CCCHHHHHHHCCCCC		27.6124719451
965PhosphorylationLSALRGNSGSVLEGP
HHHHCCCCCCCCCCC		34.9629255136
967PhosphorylationALRGNSGSVLEGPGR
HHCCCCCCCCCCCCE		24.2919664994
984PhosphorylationADGTGTRTIIVPPLK
ECCCCCEEEEECCCC		18.2020068231
991SumoylationTIIVPPLKTQLGDCT
EEEECCCCCCCCCCC		39.7428112733
991UbiquitinationTIIVPPLKTQLGDCT
EEEECCCCCCCCCCC		39.74-
992PhosphorylationIIVPPLKTQLGDCTV
EEECCCCCCCCCCCH		36.3920068231
998PhosphorylationKTQLGDCTVATQASG
CCCCCCCCHHHHHHC		20.2220068231
999 (in isoform 1)Ubiquitination-7.3521890473
1001PhosphorylationLGDCTVATQASGLLS
CCCCCHHHHHHCCCC		21.9720068231
1004PhosphorylationCTVATQASGLLSNKT
CCHHHHHHCCCCCCC		21.8420068231
1008PhosphorylationTQASGLLSNKTKPVA
HHHHCCCCCCCCCCE		41.1220068231
1021PhosphorylationVASVSGQSSGCCITP
CEEECCCCCCEEECC		32.0228450419
1022PhosphorylationASVSGQSSGCCITPT
EEECCCCCCEEECCC		28.1428450419
1027PhosphorylationQSSGCCITPTGYRAQ
CCCCEEECCCCCCCC		10.8225849741
1029PhosphorylationSGCCITPTGYRAQRG
CCEEECCCCCCCCCC		37.8928450419
1031PhosphorylationCCITPTGYRAQRGGT
EEECCCCCCCCCCCC		12.7827732954
1035MethylationPTGYRAQRGGTSAAQ
CCCCCCCCCCCCCCC		44.52115478543
1063PhosphorylationPTSQERSSNPAPRRQ
CCCHHHCCCCCCCHH		53.7224275569
1191PhosphorylationYIGSSRGSTIYTGYP
HCCCCCCCEEECCCC		15.5526074081
1192PhosphorylationIGSSRGSTIYTGYPL
CCCCCCCEEECCCCC		22.3426074081
1194PhosphorylationSSRGSTIYTGYPLSP
CCCCCEEECCCCCCC		8.3226074081
1195PhosphorylationSRGSTIYTGYPLSPT
CCCCEEECCCCCCCC		26.7928450419
1197PhosphorylationGSTIYTGYPLSPTKI
CCEEECCCCCCCCCC		8.0028450419
1200PhosphorylationIYTGYPLSPTKISQY
EECCCCCCCCCCCCC		26.4715701637
1202PhosphorylationTGYPLSPTKISQYSY
CCCCCCCCCCCCCCC		37.3228450419
1203SumoylationGYPLSPTKISQYSYL
CCCCCCCCCCCCCCC		43.6815701637
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
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:22173032
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HIPK1_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 HIPK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
12702766
DAXX_HUMANDAXXphysical
12529400
RASF5_HUMANRASSF5physical
22173032
HAX1_HUMANHAX1physical
23602568
A2MG_HUMANA2Mphysical
23602568
NEBU_HUMANNEBphysical
23602568
DDX54_HUMANDDX54physical
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 HIPK1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-352 AND SER-872, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-352, 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-352, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"Tumor necrosis factor alpha-induced desumoylation and cytoplasmictranslocation of homeodomain-interacting protein kinase 1 are criticalfor apoptosis signal-regulating kinase 1-JNK/p38 activation.";
Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.;
J. Biol. Chem. 280:15061-15070(2005).
Cited for: FUNCTION, INTERACTION WITH DAB2IP AND MAP3K5, SUBCELLULAR LOCATION,SUMOYLATION AT LYS-25 AND LYS-1203, DESUMOYLATION MEDIATED BY TNF, ANDMUTAGENESIS OF LYS-25; ASP-315; LYS-317; LYS-440; LYS-556 ANDLYS-1203.

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