ZN180_HUMAN - dbPTM
ZN180_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN180_HUMAN
UniProt AC Q9UJW8
Protein Name Zinc finger protein 180
Gene Name ZNF180
Organism Homo sapiens (Human).
Sequence Length 692
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MRACAGSTREAGSGAQDLSTLLCLEESMEEQDEKPPEPPKACAQDSFLPQEIIIKVEGEDTGSLTIPSQEGVNFKIVTVDFTREEQGTWNPAQRTLDRDVILENHRDLVSWDLATAVGKKDSTSKQRIFDEEPANGVKIERFTRDDPWLSSCEEVDDCKDQLEKQQEKQEILLQEVAFTQRKAVIHERVCKSDETGEKSGLNSSLFSSPVIPIRNHFHKHVSHAKKWHLNAAVNSHQKINENETLYENNECGKPPQSIHLIQFTRTQTKDKCYGFSDRIQSFCHGTPLHIHEKIHGGGKTFDFKECGQVLNPKISHNEQQRIPFEESQYKCSETSHSSSLTQNMRNNSEEKPFECNQCGKSFSWSSHLVAHQRTHTGEKPYECSECGKSFSRSSHLVSHQRTHTGEKPYRCNQCGKSFSQSYVLVVHQRTHTGEKPYECNQCGKSFRQSYKLIAHQRTHTGEKPYECNQCGKSFIQSYKLIAHQRIHTGEKPYECNQCGKSFSQSYKLVAHQRTHTGEKPFECNQCGKSFSWSSQLVAHQRTHTGEKPYECSECGKSFNRSSHLVMHQRIHTGEKPYECNQCGKSFSQSYVLVVHQRTHTGEKPYECSQCGKSFRQSSCLTQHQRTHTGEKPFECNQCGKTFSLSARLIVHQRTHTGEKPFTCIQCGKAFINSYKLIRHQATHTEEKLYECN
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
68PhosphorylationTGSLTIPSQEGVNFK
CCCEEEECCCCCCEE		36.6917525332
120UbiquitinationLATAVGKKDSTSKQR
HHHHHCCCCCCCCCC		51.48-
138SumoylationEEPANGVKIERFTRD
CCCCCCCEEEEECCC		40.00-
138SumoylationEEPANGVKIERFTRD
CCCCCCCEEEEECCC		40.0028112733
159SumoylationCEEVDDCKDQLEKQQ
CCCHHHHHHHHHHHH		56.3428112733
168SumoylationQLEKQQEKQEILLQE
HHHHHHHHHHHHHHH		49.22-
168SumoylationQLEKQQEKQEILLQE
HHHHHHHHHHHHHHH		49.2228112733
191SumoylationVIHERVCKSDETGEK
HHEEEEECCCCCCCC		59.0728112733
198UbiquitinationKSDETGEKSGLNSSL
CCCCCCCCCCCCHHH		51.69-
198SumoylationKSDETGEKSGLNSSL
CCCCCCCCCCCCHHH		51.6928112733
199PhosphorylationSDETGEKSGLNSSLF
CCCCCCCCCCCHHHC		44.18-
226SumoylationKHVSHAKKWHLNAAV
HHHHHHHHHHHHHHH		40.40-
226SumoylationKHVSHAKKWHLNAAV
HHHHHHHHHHHHHHH		40.4028112733
286PhosphorylationIQSFCHGTPLHIHEK
HHHHCCCCCEEECEE		10.0628555341
293UbiquitinationTPLHIHEKIHGGGKT
CCEEECEEECCCCCE		26.32-
299SumoylationEKIHGGGKTFDFKEC
EEECCCCCEECHHHH		49.66-
299SumoylationEKIHGGGKTFDFKEC
EEECCCCCEECHHHH		49.66-
299UbiquitinationEKIHGGGKTFDFKEC
EEECCCCCEECHHHH		49.66-
304SumoylationGGKTFDFKECGQVLN
CCCEECHHHHCCCCC		54.6728112733
304SumoylationGGKTFDFKECGQVLN
CCCEECHHHHCCCCC		54.67-
313UbiquitinationCGQVLNPKISHNEQQ
HCCCCCCCCCCCCCC		56.63-
313SumoylationCGQVLNPKISHNEQQ
HCCCCCCCCCCCCCC		56.6328112733
330SumoylationPFEESQYKCSETSHS
CCCHHHHHHCCCCCC		24.52-
330UbiquitinationPFEESQYKCSETSHS
CCCHHHHHHCCCCCC		24.52-
330SumoylationPFEESQYKCSETSHS
CCCHHHHHHCCCCCC		24.5228112733
334PhosphorylationSQYKCSETSHSSSLT
HHHHHCCCCCCCHHH		18.5519690332
335PhosphorylationQYKCSETSHSSSLTQ
HHHHCCCCCCCHHHH		19.8119690332
338PhosphorylationCSETSHSSSLTQNMR
HCCCCCCCHHHHHHC		24.7619690332
374PhosphorylationHLVAHQRTHTGEKPY
CCEEECCCCCCCCCE		19.74-
376PhosphorylationVAHQRTHTGEKPYEC
EEECCCCCCCCCEEC		46.56-
379UbiquitinationQRTHTGEKPYECSEC
CCCCCCCCCEECCCC		55.00-
391PhosphorylationSECGKSFSRSSHLVS
CCCCCCCCCCCCCCC		38.0417081983
402PhosphorylationHLVSHQRTHTGEKPY
CCCCCCCCCCCCCCE		19.74-
404PhosphorylationVSHQRTHTGEKPYRC
CCCCCCCCCCCCEEC		46.5624719451
407AcetylationQRTHTGEKPYRCNQC
CCCCCCCCCEECCCC		49.0130593607
430PhosphorylationVLVVHQRTHTGEKPY
EEEEEECCCCCCCCC		19.74-
432PhosphorylationVVHQRTHTGEKPYEC
EEEECCCCCCCCCCC		46.56-
435UbiquitinationQRTHTGEKPYECNQC
ECCCCCCCCCCCCCC		55.00-
435SumoylationQRTHTGEKPYECNQC
ECCCCCCCCCCCCCC		55.00-
435SumoylationQRTHTGEKPYECNQC
ECCCCCCCCCCCCCC		55.00-
451SumoylationKSFRQSYKLIAHQRT
HHHHHHHHHHEECCC		38.37-
451SumoylationKSFRQSYKLIAHQRT
HHHHHHHHHHEECCC		38.37-
458PhosphorylationKLIAHQRTHTGEKPY
HHHEECCCCCCCCCC		19.74-
460PhosphorylationIAHQRTHTGEKPYEC
HEECCCCCCCCCCCC		46.56-
463UbiquitinationQRTHTGEKPYECNQC
CCCCCCCCCCCCCCC		55.00-
463SumoylationQRTHTGEKPYECNQC
CCCCCCCCCCCCCCC		55.00-
463SumoylationQRTHTGEKPYECNQC
CCCCCCCCCCCCCCC		55.00-
479SumoylationKSFIQSYKLIAHQRI
HHHHHHHHHHEECEE		38.37-
479SumoylationKSFIQSYKLIAHQRI
HHHHHHHHHHEECEE		38.37-
488PhosphorylationIAHQRIHTGEKPYEC
HEECEECCCCCCCCC		44.6727282143
491UbiquitinationQRIHTGEKPYECNQC
CEECCCCCCCCCCCC		55.00-
514PhosphorylationKLVAHQRTHTGEKPF
CEEEECCCCCCCCCE		19.74-
516PhosphorylationVAHQRTHTGEKPFEC
EEECCCCCCCCCEEC		46.56-
519UbiquitinationQRTHTGEKPFECNQC
CCCCCCCCCEECCCC		57.25-
542PhosphorylationQLVAHQRTHTGEKPY
HHHEECCCCCCCCCC		19.74-
544PhosphorylationVAHQRTHTGEKPYEC
HEECCCCCCCCCCCC		46.56-
547UbiquitinationQRTHTGEKPYECSEC
CCCCCCCCCCCCCCC		55.00-
572PhosphorylationVMHQRIHTGEKPYEC
EEECEEECCCCCCCC		44.6727282143
575UbiquitinationQRIHTGEKPYECNQC
CEEECCCCCCCCCCC		55.00-
598PhosphorylationVLVVHQRTHTGEKPY
EEEEEECCCCCCCCE		19.74-
600PhosphorylationVVHQRTHTGEKPYEC
EEEECCCCCCCCEEH		46.56-
621PhosphorylationFRQSSCLTQHQRTHT
HHHHHCCCCCCCCCC		28.47-
626PhosphorylationCLTQHQRTHTGEKPF
CCCCCCCCCCCCCCE		19.74-
628PhosphorylationTQHQRTHTGEKPFEC
CCCCCCCCCCCCEEC		46.56-
631UbiquitinationQRTHTGEKPFECNQC
CCCCCCCCCEECCCC		57.25-
641PhosphorylationECNQCGKTFSLSARL
ECCCCCCEEEEEEEE		12.0726552605
643PhosphorylationNQCGKTFSLSARLIV
CCCCCEEEEEEEEEE		27.0119664995
645PhosphorylationCGKTFSLSARLIVHQ
CCCEEEEEEEEEEEE		15.3326552605
654PhosphorylationRLIVHQRTHTGEKPF
EEEEEECCCCCCCCE		19.74-
656PhosphorylationIVHQRTHTGEKPFTC
EEEECCCCCCCCEEE		46.56-
675SumoylationKAFINSYKLIRHQAT
CHHHHHHHHHHHCCC		36.94-
675SumoylationKAFINSYKLIRHQAT
CHHHHHHHHHHHCCC		36.94-
689PhosphorylationTHTEEKLYECN----
CCCHHHHHCCC----		29.5127642862
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 ZN180_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN180_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 ZN180_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDEL1_HUMANNDEL1physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
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 ZN180_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-68, AND MASSSPECTROMETRY.

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