ZN544_HUMAN - dbPTM
ZN544_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN544_HUMAN
UniProt AC Q6NX49
Protein Name Zinc finger protein 544
Gene Name ZNF544
Organism Homo sapiens (Human).
Sequence Length 715
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEARSMLVPPQASVCFEDVAMAFTQEEWEQLDLAQRTLYREVTLETWEHIVSLGLFLSKSDVISQLEQEEDLCRAEQEAPRDWKATLEENRLNSEKDRAREELSHHVEVYRSGPEEPPSLVLGKVQDQSNQLREHQENSLRFMVLTSERLFAQREHCELELGGGYSLPSTLSLLPTTLPTSTGFPKPNSQVKELKQNSAFINHEKNGADGKHCESHQCARAFCQSIYLSKLGNVETGKKNPYEYIVSGDSLNYGSSLCFHGRTFSVKKSDDCKDYGNLFSHSVSLNEQKPVHFGKSQYECDECRETCSESLCLVQTERSGPGETPFRCEERCAAFPMASSFSDCNIIQTTEKPSVCNQCGKSFSCCKLIHQRTHTGEKPFECTQCGKSFSQSYDLVIHQRTHTGEKPYECDLCGKSFTQRSKLITHQRIHTGEKPYQCIECRKSFRWNSNLIVHQRIHTGEKPYECTHCGKSFSQSYELVTHKRTHTGEKPFKCTQCGKSFSQKYDLVVHQRTHTGEKPYECNLCGKSFSQSSKLITHQRIHTGEKPYQCIECGKSFRWNSNLVIHQRIHTGEKPYDCTHCGKSFSQSYQLVAHKRTHTGEKPYECNECGKAFNRSTQLIRHLQIHTGEKPYKCNQCNKAFARSSYLVMHQRTHTGEKPFECSQCGKAFSGSSNLLSHHRIHSGEKPYECSDCGKSFRQQSQLVVHRRTHTGEKP
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
52O-linked_GlycosylationETWEHIVSLGLFLSK
HHHHHHHHHHHHCCH		19.0030379171
84UbiquitinationQEAPRDWKATLEENR
HHCCCCHHHHHHHHC		35.46-
86PhosphorylationAPRDWKATLEENRLN
CCCCHHHHHHHHCCC		30.86-
124UbiquitinationPPSLVLGKVQDQSNQ
CCCEEEEEECCCCHH		32.34-
195SumoylationNSQVKELKQNSAFIN
CHHHHHHHHHCCCCC		48.83-
195SumoylationNSQVKELKQNSAFIN
CHHHHHHHHHCCCCC		48.83-
230SumoylationCQSIYLSKLGNVETG
HHHHHHHHCCCCCCC		58.79-
230SumoylationCQSIYLSKLGNVETG
HHHHHHHHCCCCCCC		58.79-
236PhosphorylationSKLGNVETGKKNPYE
HHCCCCCCCCCCCCE		50.4425690035
273SumoylationVKKSDDCKDYGNLFS
EECCCCCCCCCCCCC		62.0628112733
284PhosphorylationNLFSHSVSLNEQKPV
CCCCEECCCCCCCCC		28.6128555341
289SumoylationSVSLNEQKPVHFGKS
ECCCCCCCCCCCCCC		42.71-
289UbiquitinationSVSLNEQKPVHFGKS
ECCCCCCCCCCCCCC		42.71-
289SumoylationSVSLNEQKPVHFGKS
ECCCCCCCCCCCCCC		42.7128112733
298PhosphorylationVHFGKSQYECDECRE
CCCCCCCEECHHHHH		26.1422817900
319PhosphorylationCLVQTERSGPGETPF
EEEEECCCCCCCCCC		43.0122817900
324PhosphorylationERSGPGETPFRCEER
CCCCCCCCCCCCHHH		33.3723312004
367SumoylationGKSFSCCKLIHQRTH
CCCHHHHHHHCCCCC		55.60-
367SumoylationGKSFSCCKLIHQRTH
CCCHHHHHHHCCCCC		55.60-
373PhosphorylationCKLIHQRTHTGEKPF
HHHHCCCCCCCCCCE		19.74-
375O-linked_GlycosylationLIHQRTHTGEKPFEC
HHCCCCCCCCCCEEE		46.5630379171
375PhosphorylationLIHQRTHTGEKPFEC
HHCCCCCCCCCCEEE		46.56-
378AcetylationQRTHTGEKPFECTQC
CCCCCCCCCEEEECC		57.257428801
401PhosphorylationDLVIHQRTHTGEKPY
CEEEEEECCCCCCCE		19.74-
403PhosphorylationVIHQRTHTGEKPYEC
EEEEECCCCCCCEEC		46.5621857030
406AcetylationQRTHTGEKPYECDLC
EECCCCCCCEECCCC		55.007428809
422SumoylationKSFTQRSKLITHQRI
CCCCHHHHCCCCCCC		46.20-
422SumoylationKSFTQRSKLITHQRI
CCCCHHHHCCCCCCC		46.20-
431PhosphorylationITHQRIHTGEKPYQC
CCCCCCCCCCCCEEE		44.6721712546
459PhosphorylationIVHQRIHTGEKPYEC
EEEEEEECCCCCEEC		44.6728111955
485PhosphorylationELVTHKRTHTGEKPF
EEEECCCCCCCCCCE		28.7023312004
487PhosphorylationVTHKRTHTGEKPFKC
EECCCCCCCCCCEEC		46.5629496963
504SumoylationCGKSFSQKYDLVVHQ
CCCCHHHCCCEEEEE		39.26-
504SumoylationCGKSFSQKYDLVVHQ
CCCCHHHCCCEEEEE		39.26-
513PhosphorylationDLVVHQRTHTGEKPY
CEEEEECCCCCCCCE		19.74-
515PhosphorylationVVHQRTHTGEKPYEC
EEEECCCCCCCCEEC		46.56-
534SumoylationKSFSQSSKLITHQRI
CCCCCCCCCEECCCC		49.51-
534SumoylationKSFSQSSKLITHQRI
CCCCCCCCCEECCCC		49.5128112733
543PhosphorylationITHQRIHTGEKPYQC
EECCCCCCCCCCEEE		44.6728111955
571PhosphorylationVIHQRIHTGEKPYDC
EEEEEEECCCCCCCC		44.6728111955
595SumoylationSYQLVAHKRTHTGEK
EEEEEEECCCCCCCC		49.61-
595SumoylationSYQLVAHKRTHTGEK
EEEEEEECCCCCCCC		49.61-
597PhosphorylationQLVAHKRTHTGEKPY
EEEEECCCCCCCCCC		28.7028348404
599PhosphorylationVAHKRTHTGEKPYEC
EEECCCCCCCCCCCC		46.5629496963
602UbiquitinationKRTHTGEKPYECNEC
CCCCCCCCCCCCCHH		55.00-
627PhosphorylationIRHLQIHTGEKPYKC
HHHEEECCCCCCCCC		48.9829496963
630SumoylationLQIHTGEKPYKCNQC
EEECCCCCCCCCCCC		55.80-
630SumoylationLQIHTGEKPYKCNQC
EEECCCCCCCCCCCC		55.80-
653PhosphorylationYLVMHQRTHTGEKPF
EEEEECCCCCCCCCE		19.74-
655PhosphorylationVMHQRTHTGEKPFEC
EEECCCCCCCCCEEC		46.56-
709PhosphorylationQLVVHRRTHTGEKP-
CEEEEECCCCCCCC-		24.60-
711PhosphorylationVVHRRTHTGEKP---
EEEECCCCCCCC---		46.56-
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 ZN544_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN544_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 ZN544_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSG10_HUMANTSGA10physical
25416956
NDEL1_HUMANNDEL1physical
25416956
MSS4_HUMANRABIFphysical
21516116
M3K20_HUMANZAKphysical
28514442
GNPAT_HUMANGNPATphysical
28514442
CENPB_HUMANCENPBphysical
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 ZN544_HUMAN

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Related Literatures of Post-Translational Modification

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