ZHX1_HUMAN - dbPTM
ZHX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZHX1_HUMAN
UniProt AC Q9UKY1
Protein Name Zinc fingers and homeoboxes protein 1
Gene Name ZHX1
Organism Homo sapiens (Human).
Sequence Length 873
Subcellular Localization Nucleus . Colocalized in the nucleus with DNMT3B.
Protein Description Acts as a transcriptional repressor. Increases DNMT3B-mediated repressive transcriptional activity when DNMT3B is tethered to DNA. May link molecule between DNMT3B and other co-repressor proteins..
Protein Sequence MASRRKSTTPCMVLASEQDPDLELISDLDEGPPVLTPVENTRAESISSDEEVHESVDSDNQQNKKVEGGYECKYCTFQTPDLNMFTFHVDSEHPNVVLNSSYVCVECNFLTKRYDALSEHNLKYHPGEENFKLTMVKRNNQTIFEQTINDLTFDGSFVKEENAEQAESTEVSSSGISISKTPIMKMMKNKVENKRIAVHHNSVEDVPEEKENEIKPDREEIVENPSSSASESNTSTSIVNRIHPSTASTVVTPAAVLPGLAQVITAVSAQQNSNLIPKVLIPVNSIPTYNAALDNNPLLLNTYNKFPYPTMSEITVLSAQAKYTEEQIKIWFSAQRLKHGVSWTPEEVEEARRKQFNGTVHTVPQTITVIPTHISTGSNGLPSILQTCQIVGQPGLVLTQVAGTNTLPVTAPIALTVAGVPSQNNIQKSQVPAAQPTAETKPATAAVPTSQSVKHETALVNPDSFGIRAKKTKEQLAELKVSYLKNQFPHDSEIIRLMKITGLTKGEIKKWFSDTRYNQRNSKSNQCLHLNNDSSTTIIIDSSDETTESPTVGTAQPKQSWNPFPDFTPQKFKEKTAEQLRVLQASFLNSSVLTDEELNRLRAQTKLTRREIDAWFTEKKKSKALKEEKMEIDESNAGSSKEEAGETSPADESGAPKSGSTGKICKKTPEQLHMLKSAFVRTQWPSPEEYDKLAKESGLARTDIVSWFGDTRYAWKNGNLKWYYYYQSANSSSMNGLSSLRKRGRGRPKGRGRGRPRGRPRGSKRINNWDRGPSLIKFKTGTAILKDYYLKHKFLNEQDLDELVNKSHMGYEQVREWFAERQRRSELGIELFEENEEEDEVIDDQEEDEEETDDSDTWEPPRHVKRKLSKSDD
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
3Phosphorylation-----MASRRKSTTP
-----CCCCCCCCCC		31.1826074081
7Phosphorylation-MASRRKSTTPCMVL
-CCCCCCCCCCCEEE		35.3826074081
8PhosphorylationMASRRKSTTPCMVLA
CCCCCCCCCCCEEEE		37.4826074081
9PhosphorylationASRRKSTTPCMVLAS
CCCCCCCCCCEEEEC		22.9118669648
16PhosphorylationTPCMVLASEQDPDLE
CCCEEEECCCCCCCC		31.4626074081
26PhosphorylationDPDLELISDLDEGPP
CCCCCCCCCCCCCCC		44.7518669648
36PhosphorylationDEGPPVLTPVENTRA
CCCCCCCCCCCCCCC		26.0622817900
45PhosphorylationVENTRAESISSDEEV
CCCCCCCCCCCCHHH		27.1322167270
47PhosphorylationNTRAESISSDEEVHE
CCCCCCCCCCHHHHH		40.8022167270
48PhosphorylationTRAESISSDEEVHES
CCCCCCCCCHHHHHH		47.5822167270
55PhosphorylationSDEEVHESVDSDNQQ
CCHHHHHHCCCCCCC		19.1523663014
58PhosphorylationEVHESVDSDNQQNKK
HHHHHCCCCCCCCCE		35.9822167270
147PhosphorylationNQTIFEQTINDLTFD
CEEEEEEECCCCCCC		17.9828102081
152PhosphorylationEQTINDLTFDGSFVK
EEECCCCCCCCCEEC		23.6529523821
156PhosphorylationNDLTFDGSFVKEENA
CCCCCCCCEECHHHH		28.8025159151
159SumoylationTFDGSFVKEENAEQA
CCCCCEECHHHHHHH		58.2528112733
173PhosphorylationAESTEVSSSGISISK
HCCCCCCCCCCCCCC		37.4522210691
174PhosphorylationESTEVSSSGISISKT
CCCCCCCCCCCCCCC		32.4122210691
177PhosphorylationEVSSSGISISKTPIM
CCCCCCCCCCCCHHH		25.0822210691
202PhosphorylationRIAVHHNSVEDVPEE
EEEEECCCHHCCCHH		23.6429255136
210SumoylationVEDVPEEKENEIKPD
HHCCCHHHCCCCCCC		65.27-
226O-linked_GlycosylationEEIVENPSSSASESN
HHHHCCCCCCCCCCC		48.8120068230
232O-linked_GlycosylationPSSSASESNTSTSIV
CCCCCCCCCCCCCHH		42.8020068230
252PhosphorylationSTASTVVTPAAVLPG
CCCCCCCCHHHHCHH		11.6825627689
289PhosphorylationPVNSIPTYNAALDNN
ECCCCCCCCHHHCCC		9.4622817900
303PhosphorylationNPLLLNTYNKFPYPT
CCEEEECCCCCCCCC		18.4522817900
333PhosphorylationEQIKIWFSAQRLKHG
HHHHHHHHHHHHHCC		14.4328555341
429PhosphorylationSQNNIQKSQVPAAQP
CCCCCCHHCCCCCCC		21.7530576142
437O-linked_GlycosylationQVPAAQPTAETKPAT
CCCCCCCCCCCCCCC		25.6620068230
441SumoylationAQPTAETKPATAAVP
CCCCCCCCCCCCCCC		24.94-
441AcetylationAQPTAETKPATAAVP
CCCCCCCCCCCCCCC		24.9426051181
441SumoylationAQPTAETKPATAAVP
CCCCCCCCCCCCCCC		24.9428112733
444PhosphorylationTAETKPATAAVPTSQ
CCCCCCCCCCCCCCC		24.5530576142
450O-linked_GlycosylationATAAVPTSQSVKHET
CCCCCCCCCCCCCCE		17.8730059200
450O-linked_GlycosylationATAAVPTSQSVKHET
CCCCCCCCCCCCCCE		17.8720068230
452PhosphorylationAAVPTSQSVKHETAL
CCCCCCCCCCCCEEC		32.6630576142
452O-linked_GlycosylationAAVPTSQSVKHETAL
CCCCCCCCCCCCEEC		32.6620068230
454SumoylationVPTSQSVKHETALVN
CCCCCCCCCCEECCC		40.7628112733
454SumoylationVPTSQSVKHETALVN
CCCCCCCCCCEECCC		40.76-
485SumoylationELKVSYLKNQFPHDS
HHHHHHHHHCCCCHH		40.23-
485SumoylationELKVSYLKNQFPHDS
HHHHHHHHHCCCCHH		40.2328112733
513PhosphorylationGEIKKWFSDTRYNQR
HHHHHHHCCCCCCCC		36.6427174698
515PhosphorylationIKKWFSDTRYNQRNS
HHHHHCCCCCCCCCC		33.5827174698
517PhosphorylationKWFSDTRYNQRNSKS
HHHCCCCCCCCCCCC		20.1027174698
542PhosphorylationSTTIIIDSSDETTES
CCEEEEECCCCCCCC		29.3125627689
543PhosphorylationTTIIIDSSDETTESP
CEEEEECCCCCCCCC		35.4025627689
546PhosphorylationIIDSSDETTESPTVG
EEECCCCCCCCCCCC		40.6327251275
547PhosphorylationIDSSDETTESPTVGT
EECCCCCCCCCCCCC		32.2027251275
549PhosphorylationSSDETTESPTVGTAQ
CCCCCCCCCCCCCCC		24.6328348404
551PhosphorylationDETTESPTVGTAQPK
CCCCCCCCCCCCCCC		40.6328348404
568PhosphorylationWNPFPDFTPQKFKEK
CCCCCCCCCHHHHHH		31.9925159151
576PhosphorylationPQKFKEKTAEQLRVL
CHHHHHHHHHHHHHH		36.2022985185
590PhosphorylationLQASFLNSSVLTDEE
HHHHHHCCCCCCHHH		24.7824732914
591PhosphorylationQASFLNSSVLTDEEL
HHHHHCCCCCCHHHH		21.7724732914
594PhosphorylationFLNSSVLTDEELNRL
HHCCCCCCHHHHHHH		38.9324732914
629SumoylationSKALKEEKMEIDESN
HHHHHHHHHHCCCCC		42.8128112733
635PhosphorylationEKMEIDESNAGSSKE
HHHHCCCCCCCCCHH		28.3825159151
639PhosphorylationIDESNAGSSKEEAGE
CCCCCCCCCHHHCCC		35.5125159151
640PhosphorylationDESNAGSSKEEAGET
CCCCCCCCHHHCCCC		43.0723401153
647PhosphorylationSKEEAGETSPADESG
CHHHCCCCCCCCCCC		38.8129255136
648PhosphorylationKEEAGETSPADESGA
HHHCCCCCCCCCCCC		17.4929255136
653PhosphorylationETSPADESGAPKSGS
CCCCCCCCCCCCCCC		40.5823927012
660PhosphorylationSGAPKSGSTGKICKK
CCCCCCCCCCCCCCC		40.87-
668PhosphorylationTGKICKKTPEQLHML
CCCCCCCCHHHHHHH		19.9725159151
682PhosphorylationLKSAFVRTQWPSPEE
HHHHHHHCCCCCHHH		29.6817525332
686PhosphorylationFVRTQWPSPEEYDKL
HHHCCCCCHHHHHHH		41.8221815630
690PhosphorylationQWPSPEEYDKLAKES
CCCCHHHHHHHHHHH		19.4023312004
738PhosphorylationSSSMNGLSSLRKRGR
CCCCCHHHHHHHCCC		28.8230301811
739PhosphorylationSSMNGLSSLRKRGRG
CCCCHHHHHHHCCCC		36.9225954137
774PhosphorylationNNWDRGPSLIKFKTG
CCCCCCCCEEEECCC		45.6228112733
779UbiquitinationGPSLIKFKTGTAILK
CCCEEEECCCCHHHH		40.83-
780PhosphorylationPSLIKFKTGTAILKD
CCEEEECCCCHHHHH		42.78-
782PhosphorylationLIKFKTGTAILKDYY
EEEECCCCHHHHHHH		18.76-
789PhosphorylationTAILKDYYLKHKFLN
CHHHHHHHHHHCCCC		21.2924719451
793UbiquitinationKDYYLKHKFLNEQDL
HHHHHHHCCCCHHHH		50.38-
869PhosphorylationRHVKRKLSKSDD---
HHHHHHHHCCCC---		32.9024719451
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
568TPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZHX1_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 ZHX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZHX3_HUMANZHX3physical
12659632
ZHX1_HUMANZHX1physical
12237128
ZMY11_HUMANZMYND11physical
12659632
ATX1_HUMANATXN1physical
12659632
EFNA2_HUMANEFNA2physical
12659632
ELL_HUMANELLphysical
12659632
ZHX1_HUMANZHX1physical
12659632
ZYX_HUMANZYXphysical
12659632
ZHX1_HUMANZHX1physical
12062805
ZHX1_RATZhx1physical
12062805
NFYA_HUMANNFYAphysical
10441475
NFYA_HUMANNFYAphysical
10571058
PR40A_HUMANPRPF40Aphysical
15383276
PIAS4_HUMANPIAS4physical
15383276
ZMY11_HUMANZMYND11physical
21988832
UBC9_HUMANUBE2Iphysical
23686912
ZHX2_HUMANZHX2physical
26496610
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 ZHX1_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 SER-47; SER-48 AND SER-648,AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-639 ANDSER-648, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-47 AND SER-48,AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND SER-648, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-682, 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-289 AND TYR-303, ANDMASS SPECTROMETRY.

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