ZHX2_HUMAN - dbPTM
ZHX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZHX2_HUMAN
UniProt AC Q9Y6X8
Protein Name Zinc fingers and homeoboxes protein 2
Gene Name ZHX2
Organism Homo sapiens (Human).
Sequence Length 837
Subcellular Localization Nucleus .
Protein Description Acts as a transcriptional repressor. Represses the promoter activity of the CDC25C gene stimulated by NFYA..
Protein Sequence MASKRKSTTPCMVRTSQVVEQDVPEEVDRAKEKGIGTPQPDVAKDSWAAELENSSKENEVIEVKSMGESQSKKLQGGYECKYCPYSTQNLNEFTEHVDMQHPNVILNPLYVCAECNFTTKKYDSLSDHNSKFHPGEANFKLKLIKRNNQTVLEQSIETTNHVVSITTSGPGTGDSDSGISVSKTPIMKPGKPKADAKKVPKKPEEITPENHVEGTARLVTDTAEILSRLGGVELLQDTLGHVMPSVQLPPNINLVPKVPVPLNTTKYNSALDTNATMINSFNKFPYPTQAELSWLTAASKHPEEHIRIWFATQRLKHGISWSPEEVEEARKKMFNGTIQSVPPTITVLPAQLAPTKVTQPILQTALPCQILGQTSLVLTQVTSGSTTVSCSPITLAVAGVTNHGQKRPLVTPQAAPEPKRPHIAQVPEPPPKVANPPLTPASDRKKTKEQIAHLKASFLQSQFPDDAEVYRLIEVTGLARSEIKKWFSDHRYRCQRGIVHITSESLAKDQLAIAASRHGRTYHAYPDFAPQKFKEKTQGQVKILEDSFLKSSFPTQAELDRLRVETKLSRREIDSWFSERRKLRDSMEQAVLDSMGSGKKGQDVGAPNGALSRLDQLSGAQLTSSLPSPSPAIAKSQEQVHLLRSTFARTQWPTPQEYDQLAAKTGLVRTEIVRWFKENRCLLKTGTVKWMEQYQHQPMADDHGYDAVARKATKPMAESPKNGGDVVPQYYKDPKKLCEEDLEKLVTRVKVGSEPAKDCLPAKPSEATSDRSEGSSRDGQGSDENEESSVVDYVEVTVGEEDAISDRSDSWSQAAAEGVSELAESDSDCVPAEAGQA
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
7Phosphorylation-MASKRKSTTPCMVR
-CCCCCCCCCCCEEE		41.36-
8PhosphorylationMASKRKSTTPCMVRT
CCCCCCCCCCCEEEH		37.4822468782
9PhosphorylationASKRKSTTPCMVRTS
CCCCCCCCCCEEEHH		22.91-
15PhosphorylationTTPCMVRTSQVVEQD
CCCCEEEHHHHCCCC		16.4622468782
16PhosphorylationTPCMVRTSQVVEQDV
CCCEEEHHHHCCCCC		15.4819060867
37PhosphorylationAKEKGIGTPQPDVAK
HHHCCCCCCCCCHHH		19.4830266825
64SumoylationENEVIEVKSMGESQS
CCCEEEEEECCCCCC		23.1828112733
180PhosphorylationGDSDSGISVSKTPIM
CCCCCCCCCCCCCCC		24.7024719451
207PhosphorylationPKKPEEITPENHVEG
CCCCCCCCCCCCCCC		28.0329396449
215PhosphorylationPENHVEGTARLVTDT
CCCCCCCCHHHHHHH		8.6329396449
220PhosphorylationEGTARLVTDTAEILS
CCCHHHHHHHHHHHH		32.02-
222PhosphorylationTARLVTDTAEILSRL
CHHHHHHHHHHHHHC		19.47-
227PhosphorylationTDTAEILSRLGGVEL
HHHHHHHHHCCCHHH		30.9924719451
264O-linked_GlycosylationKVPVPLNTTKYNSAL
CCCCCCCCCCCCCCC		32.1423301498
267PhosphorylationVPLNTTKYNSALDTN
CCCCCCCCCCCCCCC		16.56-
269PhosphorylationLNTTKYNSALDTNAT
CCCCCCCCCCCCCCC		27.41-
280PhosphorylationTNATMINSFNKFPYP
CCCCEECCCCCCCCC		21.1920068231
286PhosphorylationNSFNKFPYPTQAELS
CCCCCCCCCCHHHHH		23.2624719451
293PhosphorylationYPTQAELSWLTAASK
CCCHHHHHHHHHHHH		16.1424719451
299PhosphorylationLSWLTAASKHPEEHI
HHHHHHHHHCHHHHH		29.0924719451
344PhosphorylationTIQSVPPTITVLPAQ
CCCCCCCEEEEEECC		24.1818491316
355PhosphorylationLPAQLAPTKVTQPIL
EECCCCCCCCCHHHH		32.3218491316
401O-linked_GlycosylationTLAVAGVTNHGQKRP
EEEEEECCCCCCCCC		22.1523301498
411PhosphorylationGQKRPLVTPQAAPEP
CCCCCCCCCCCCCCC		19.8422817900
439PhosphorylationKVANPPLTPASDRKK
CCCCCCCCCHHHCCC		23.6821815630
442PhosphorylationNPPLTPASDRKKTKE
CCCCCCHHHCCCHHH		38.8728555341
455UbiquitinationKEQIAHLKASFLQSQ
HHHHHHHHHHHHHHC		31.9229967540
455SumoylationKEQIAHLKASFLQSQ
HHHHHHHHHHHHHHC		31.9228112733
470PhosphorylationFPDDAEVYRLIEVTG
CCCCHHHHHHHHHHC		7.39-
516O-linked_GlycosylationDQLAIAASRHGRTYH
HHHHHHHHHCCCEEE		18.7823301498
547PhosphorylationQVKILEDSFLKSSFP
CEEECCCHHHHCCCC		24.0924719451
566PhosphorylationLDRLRVETKLSRREI
HHHHHHHHHHCHHHH		34.13-
569PhosphorylationLRVETKLSRREIDSW
HHHHHHHCHHHHHHH		30.74-
575PhosphorylationLSRREIDSWFSERRK
HCHHHHHHHHHHHHH		35.3628509920
578PhosphorylationREIDSWFSERRKLRD
HHHHHHHHHHHHHHH		24.7621815630
586PhosphorylationERRKLRDSMEQAVLD
HHHHHHHHHHHHHHH		20.13-
594PhosphorylationMEQAVLDSMGSGKKG
HHHHHHHHCCCCCCC		22.3828555341
597PhosphorylationAVLDSMGSGKKGQDV
HHHHHCCCCCCCCCC		38.5128555341
618PhosphorylationLSRLDQLSGAQLTSS
HHHHHHCCCCCCCCC		26.8422210691
623PhosphorylationQLSGAQLTSSLPSPS
HCCCCCCCCCCCCCC		12.2829978859
624PhosphorylationLSGAQLTSSLPSPSP
CCCCCCCCCCCCCCH		38.1729978859
625PhosphorylationSGAQLTSSLPSPSPA
CCCCCCCCCCCCCHH		38.7829978859
628PhosphorylationQLTSSLPSPSPAIAK
CCCCCCCCCCHHHHC		43.2129255136
630PhosphorylationTSSLPSPSPAIAKSQ
CCCCCCCCHHHHCCH		31.1629255136
654PhosphorylationFARTQWPTPQEYDQL
HCCCCCCCHHHHHHH		34.34-
658PhosphorylationQWPTPQEYDQLAAKT
CCCCHHHHHHHHHHH		12.07-
705PhosphorylationPMADDHGYDAVARKA
CCCCCCCHHHHHHHC		9.4127642862
713PhosphorylationDAVARKATKPMAESP
HHHHHHCCCCCCCCC		38.4228857561
719PhosphorylationATKPMAESPKNGGDV
CCCCCCCCCCCCCCC		31.4729514088
765PhosphorylationDCLPAKPSEATSDRS
HCCCCCCCCCCCCCC		38.8723312004
768PhosphorylationPAKPSEATSDRSEGS
CCCCCCCCCCCCCCC		27.4023312004
769PhosphorylationAKPSEATSDRSEGSS
CCCCCCCCCCCCCCC		37.7723312004
772PhosphorylationSEATSDRSEGSSRDG
CCCCCCCCCCCCCCC		51.8326714015
775PhosphorylationTSDRSEGSSRDGQGS
CCCCCCCCCCCCCCC		20.3927251275
776PhosphorylationSDRSEGSSRDGQGSD
CCCCCCCCCCCCCCC		45.2927251275
820PhosphorylationQAAAEGVSELAESDS
HHHHHHHHHHHHCCC		37.4430108239
825PhosphorylationGVSELAESDSDCVPA
HHHHHHHCCCCCCCC		36.4930108239
827PhosphorylationSELAESDSDCVPAEA
HHHHHCCCCCCCCCC		42.0430108239
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 ZHX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZHX2_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 ZHX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZHX3_HUMANZHX3physical
14659886
RRAS_HUMANRRASphysical
19805522
RASH_HUMANHRASphysical
11205744
RASH_HUMANHRASphysical
15824104
A4_HUMANAPPphysical
21832049
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 ZHX2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-37, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory