ZN224_HUMAN - dbPTM
ZN224_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN224_HUMAN
UniProt AC Q9NZL3
Protein Name Zinc finger protein 224
Gene Name ZNF224
Organism Homo sapiens (Human).
Sequence Length 707
Subcellular Localization Nucleus . Colocalizes with DEPDC1A at the nucleus.
Protein Description May be involved in transcriptional regulation as a transcriptional repressor. The DEPDC1A-ZNF224 complex may play a critical role in bladder carcinogenesis by repressing the transcription of the A20 gene, leading to transport of NF-KB protein into the nucleus, resulting in suppression of apoptosis of bladder cancer cells..
Protein Sequence MTTFKEAMTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLSVGHQAFHRDTFHFLREEKIWMMKTAIQREGNSGDKIQTEMETVSEAGTHQEWSFQQIWEKIASDLTRSQDLMINSSQFSKEGDFPCQTEAGLSVIHTRQKSSQGNGYKPSFSDVSHFDFHQQLHSGEKSHTCDECGKNFCYISALRIHQRVHMGEKCYKCDVCGKEFSQSSHLQTHQRVHTGEKPFKCVECGKGFSRRSALNVHHKLHTGEKPYNCEECGKAFIHDSQLQEHQRIHTGEKPFKCDICGKSFCGRSRLNRHSMVHTAEKPFRCDTCDKSFRQRSALNSHRMIHTGEKPYKCEECGKGFICRRDLYTHHMVHTGEKPYNCKECGKSFRWASCLLKHQRVHSGEKPFKCEECGKGFYTNSQCYSHQRSHSGEKPYKCVECGKGYKRRLDLDFHQRVHTGEKLYNCKECGKSFSRAPCLLKHERLHSGEKPFQCEECGKRFTQNSHLHSHQRVHTGEKPYKCEKCGKGYNSKFNLDMHQKVHTGERPYNCKECGKSFGWASCLLKHQRLHSGEKPFKCEECGKRFTQNSQLHSHQRVHTGEKPYKCDECGKGFSWSSTRLTHQRRHSRETPLKCEQHGKNIVQNSFSKVQEKVHSVEKPYKCEDCGKGYNRRLNLDMHQRVHMGEKTWKCRECDMCFSQASSLRLHQNVHVGEKP
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
5Sumoylation---MTTFKEAMTFKD
---CCCHHHHCCCCC		42.33-
5Sumoylation---MTTFKEAMTFKD
---CCCHHHHCCCCC		42.33-
18PhosphorylationKDVAVVFTEEELGLL
CCEEEEEEHHHHCHH		30.77-
31SumoylationLLDLAQRKLYRDVML
HHHHHHHHHHHHHHH		37.48-
31SumoylationLLDLAQRKLYRDVML
HHHHHHHHHHHHHHH		37.48-
121PhosphorylationSQDLMINSSQFSKEG
CCCEECCHHHHCCCC		18.0029116813
122PhosphorylationQDLMINSSQFSKEGD
CCEECCHHHHCCCCC		30.6529116813
125PhosphorylationMINSSQFSKEGDFPC
ECCHHHHCCCCCCCC		23.3529116813
187PhosphorylationECGKNFCYISALRIH
CCCCCEEEEEHHHHH		8.1822817900
204PhosphorylationVHMGEKCYKCDVCGK
CCCCCCEEECCCCCC		26.2222817900
227PhosphorylationQTHQRVHTGEKPFKC
CCCCCCCCCCCCEEE		44.1523898821
233SumoylationHTGEKPFKCVECGKG
CCCCCCEEEEECCCC		45.99-
233SumoylationHTGEKPFKCVECGKG
CCCCCCEEEEECCCC		45.99-
245PhosphorylationGKGFSRRSALNVHHK
CCCCCHHHCHHHHCC		35.6815302935
255PhosphorylationNVHHKLHTGEKPYNC
HHHCCCCCCCCCCCH		58.4324719451
258SumoylationHKLHTGEKPYNCEEC
CCCCCCCCCCCHHHH		54.89-
258SumoylationHKLHTGEKPYNCEEC
CCCCCCCCCCCHHHH		54.89-
273PhosphorylationGKAFIHDSQLQEHQR
HCEEECHHHHHHHCC		20.7328555341
283PhosphorylationQEHQRIHTGEKPFKC
HHHCCCCCCCCCCCC		44.6718669648
311PhosphorylationNRHSMVHTAEKPFRC
CCCCCCCCCCCCCCC		25.7124719451
339PhosphorylationNSHRMIHTGEKPYKC
HCCCCEECCCCCEEC		35.7929496963
342UbiquitinationRMIHTGEKPYKCEEC
CCEECCCCCEECCCC		55.80-
344PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
345UbiquitinationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.6329967540
345SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
345SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
367PhosphorylationYTHHMVHTGEKPYNC
CCCCEECCCCCCCCC		35.31-
395PhosphorylationLKHQRVHSGEKPFKC
HHCCCCCCCCCCCCC		45.8720068231
398UbiquitinationQRVHSGEKPFKCEEC
CCCCCCCCCCCCCCC		60.32-
401SumoylationHSGEKPFKCEECGKG
CCCCCCCCCCCCCCC		49.62-
401SumoylationHSGEKPFKCEECGKG
CCCCCCCCCCCCCCC		49.62-
454SumoylationQRVHTGEKLYNCKEC
HHCCCCCCEECCCHH		58.58-
454SumoylationQRVHTGEKLYNCKEC
HHCCCCCCEECCCHH		58.58-
459SumoylationGEKLYNCKECGKSFS
CCCEECCCHHCCCCC		53.02-
459SumoylationGEKLYNCKECGKSFS
CCCEECCCHHCCCCC		53.02-
466PhosphorylationKECGKSFSRAPCLLK
CHHCCCCCCCCCEEC		34.3217081983
473SumoylationSRAPCLLKHERLHSG
CCCCCEECCCHHCCC		30.3928112733
473SumoylationSRAPCLLKHERLHSG
CCCCCEECCCHHCCC		30.39-
479PhosphorylationLKHERLHSGEKPFQC
ECCCHHCCCCCCCCC		53.9229214152
507PhosphorylationHSHQRVHTGEKPYKC
CCCCCCCCCCCCEEC		44.1529496963
510SumoylationQRVHTGEKPYKCEKC
CCCCCCCCCEECCCC		55.80-
510UbiquitinationQRVHTGEKPYKCEKC
CCCCCCCCCEECCCC		55.80-
510SumoylationQRVHTGEKPYKCEKC
CCCCCCCCCEECCCC		55.80-
521PhosphorylationCEKCGKGYNSKFNLD
CCCCCCCCCCCCCCC		21.54-
524SumoylationCGKGYNSKFNLDMHQ
CCCCCCCCCCCCCCC		34.33-
524SumoylationCGKGYNSKFNLDMHQ
CCCCCCCCCCCCCCC		34.33-
535PhosphorylationDMHQKVHTGERPYNC
CCCCCCCCCCCCCCC		43.66-
557SumoylationGWASCLLKHQRLHSG
CHHHHHHHHHHHHCC		25.41-
557SumoylationGWASCLLKHQRLHSG
CHHHHHHHHHHHHCC		25.41-
563PhosphorylationLKHQRLHSGEKPFKC
HHHHHHHCCCCCCCH		53.9223401153
566SumoylationQRLHSGEKPFKCEEC
HHHHCCCCCCCHHHH		60.32-
566UbiquitinationQRLHSGEKPFKCEEC
HHHHCCCCCCCHHHH		60.3229967540
566SumoylationQRLHSGEKPFKCEEC
HHHHCCCCCCCHHHH		60.32-
566AcetylationQRLHSGEKPFKCEEC
HHHHCCCCCCCHHHH		60.32-
569SumoylationHSGEKPFKCEECGKR
HCCCCCCCHHHHHCE		49.62-
569SumoylationHSGEKPFKCEECGKR
HCCCCCCCHHHHHCE		49.62-
591PhosphorylationHSHQRVHTGEKPYKC
CCCCCCCCCCCCEEC		44.1529496963
594SumoylationQRVHTGEKPYKCDEC
CCCCCCCCCEECCCC		55.80-
594UbiquitinationQRVHTGEKPYKCDEC
CCCCCCCCCEECCCC		55.80-
594SumoylationQRVHTGEKPYKCDEC
CCCCCCCCCEECCCC		55.80-
608PhosphorylationCGKGFSWSSTRLTHQ
CCCCCCCCHHHHHHC		22.1928555341
625SumoylationHSRETPLKCEQHGKN
HCCCCCCCHHHHHHH		36.6128112733
625SumoylationHSRETPLKCEQHGKN
HCCCCCCCHHHHHHH		36.61-
637PhosphorylationGKNIVQNSFSKVQEK
HHHHHHHCHHHHHHH		17.5124719451
639PhosphorylationNIVQNSFSKVQEKVH
HHHHHCHHHHHHHHH		31.5729978859
640SumoylationIVQNSFSKVQEKVHS
HHHHCHHHHHHHHHC		46.02-
640SumoylationIVQNSFSKVQEKVHS
HHHHCHHHHHHHHHC		46.02-
640AcetylationIVQNSFSKVQEKVHS
HHHHCHHHHHHHHHC		46.0212430237
650AcetylationEKVHSVEKPYKCEDC
HHHHCCCCCEECCCC		52.0312430245
653SumoylationHSVEKPYKCEDCGKG
HCCCCCEECCCCCCC		39.41-
653SumoylationHSVEKPYKCEDCGKG
HCCCCCEECCCCCCC		39.41-
678SumoylationQRVHMGEKTWKCREC
HCCCCCCCCEECCCC		54.69-
678SumoylationQRVHMGEKTWKCREC
HCCCCCCCCEECCCC		54.69-
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 ZN224_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN224_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 ZN224_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM5_HUMANPRMT5physical
19741270
MTUS2_HUMANMTUS2physical
25416956
PTX3_HUMANPTX3physical
28514442
LRP1B_HUMANLRP1Bphysical
28514442
LRP4_HUMANLRP4physical
28514442
SORL_HUMANSORL1physical
28514442
ZN813_HUMANZNF813physical
28514442
LRP2_HUMANLRP2physical
28514442
NOTC3_HUMANNOTCH3physical
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 ZN224_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-245, AND MASSSPECTROMETRY.

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