ZN484_HUMAN - dbPTM
ZN484_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN484_HUMAN
UniProt AC Q5JVG2
Protein Name Zinc finger protein 484
Gene Name ZNF484
Organism Homo sapiens (Human).
Sequence Length 852
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MTKSLESVSFKDVTVDFSRDEWQQLDLAQKSLYREVMLENYFNLISVGCQVPKPEVIFSLEQEEPCMLDGEIPSQSRPDGDIGFGPLQQRMSEEVSFQSEININLFTRDDPYSILEELWKDDEHTRKCGENQNKPLSRVVFINKKTLANDSIFEYKDIGEIVHVNTHLVSSRKRPHNCNSCGKNLEPIITLYNRNNATENSDKTIGDGDIFTHLNSHTEVTACECNQCGKPLHHKQALIQQQKIHTRESLYLFSDYVNVFSPKSHAFAHESICAEEKQHECHECEAVFTQKSQLDGSQRVYAGICTEYEKDFSLKSNRQKTPYEGNYYKCSDYGRAFIQKSDLFRCQRIHSGEKPYEYSECEKNLPQNSNLNIHKKIHTGGKHFECTECGKAFTRKSTLSMHQKIHTGEKPYVCTECGKAFIRKSHFITHERIHTGEKPYECSDCGKSFIKKSQLHVHQRIHTGENPFICSECGKVFTHKTNLIIHQKIHTGERPYICTVCGKAFTDRSNLIKHQKIHTGEKPYKCSDCGKSFTWKSRLRIHQKCHTGERHYECSECGKAFIQKSTLSMHQRIHRGEKPYVCTECGKAFFHKSHFITHERIHTGEKPYECSICGKSFTKKSQLHVHQQIHTGEKPYRCAECGKAFTDRSNLFTHQKIHTGEKPYKCSDCGKAFTRKSGLHIHQQSHTGERHYECSECGKAFARKSTLIMHQRIHTGEKPYICNECGKSFIQKSHLNRHRRIHTGEKPYECSDCGKSFIKKSQLHEHHRIHTGEKPYICAECGKAFTIRSNLIKHQKIHTKQKPYKCSDLGKALNWKPQLSMPQKSDNGEVECSMPQLWCGDSEGDQGQLSSI
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
9PhosphorylationTKSLESVSFKDVTVD
CCCCCCCCCEEEEEE		35.5424719451
108UbiquitinationININLFTRDDPYSIL
EEEEEEECCCHHHHH		38.7127667366
109UbiquitinationNINLFTRDDPYSILE
EEEEEECCCHHHHHH		59.1729967540
112PhosphorylationLFTRDDPYSILEELW
EEECCCHHHHHHHHH		18.4823927012
113PhosphorylationFTRDDPYSILEELWK
EECCCHHHHHHHHHC		26.5323927012
123UbiquitinationEELWKDDEHTRKCGE
HHHHCCCHHHHCCCC		58.2427667366
125PhosphorylationLWKDDEHTRKCGENQ
HHCCCHHHHCCCCCC		29.7623927012
144UbiquitinationSRVVFINKKTLANDS
EEEEEEECCCCCCCC		42.1727667366
145UbiquitinationRVVFINKKTLANDSI
EEEEEECCCCCCCCC		44.2629967540
146UbiquitinationVVFINKKTLANDSIF
EEEEECCCCCCCCCE		32.4827667366
147UbiquitinationVFINKKTLANDSIFE
EEEECCCCCCCCCEE		6.0229967540
156SumoylationNDSIFEYKDIGEIVH
CCCCEECCCHHEEEE		35.3528112733
159UbiquitinationIFEYKDIGEIVHVNT
CEECCCHHEEEEEEH		28.8127667366
161UbiquitinationEYKDIGEIVHVNTHL
ECCCHHEEEEEEHHH		1.8827667366
170PhosphorylationHVNTHLVSSRKRPHN
EEEHHHHCCCCCCCC		30.6824719451
176UbiquitinationVSSRKRPHNCNSCGK
HCCCCCCCCCCCCCC		56.3527667366
190PhosphorylationKNLEPIITLYNRNNA
CCCCCEEEEEECCCC		24.7430576142
192PhosphorylationLEPIITLYNRNNATE
CCCEEEEEECCCCCC		11.9230576142
199UbiquitinationYNRNNATENSDKTIG
EECCCCCCCCCCCCC		52.9429967540
235UbiquitinationCGKPLHHKQALIQQQ
CCCCCCHHHHHHHHH		26.9029967540
237UbiquitinationKPLHHKQALIQQQKI
CCCCHHHHHHHHHCC		16.0729967540
255UbiquitinationESLYLFSDYVNVFSP
HHHHHHHCCEEECCC		44.0329967540
261PhosphorylationSDYVNVFSPKSHAFA
HCCEEECCCCCCHHH		27.4324719451
284UbiquitinationKQHECHECEAVFTQK
HHHCCCCCCEEEEEH		1.4929967540
291UbiquitinationCEAVFTQKSQLDGSQ
CCEEEEEHHHCCCCC		36.7929967540
293UbiquitinationAVFTQKSQLDGSQRV
EEEEEHHHCCCCCEE		51.0829967540
304UbiquitinationSQRVYAGICTEYEKD
CCEEEEEECCCEECC		1.6829967540
315SumoylationYEKDFSLKSNRQKTP
EECCCCCCCCCCCCC		44.48-
315SumoylationYEKDFSLKSNRQKTP
EECCCCCCCCCCCCC		44.48-
315MethylationYEKDFSLKSNRQKTP
EECCCCCCCCCCCCC		44.48110928985
318UbiquitinationDFSLKSNRQKTPYEG
CCCCCCCCCCCCCCC		46.6029967540
320UbiquitinationSLKSNRQKTPYEGNY
CCCCCCCCCCCCCCE		48.5129967540
320AcetylationSLKSNRQKTPYEGNY
CCCCCCCCCCCCCCE		48.5119809837
322UbiquitinationKSNRQKTPYEGNYYK
CCCCCCCCCCCCEEE		32.0129967540
323PhosphorylationSNRQKTPYEGNYYKC
CCCCCCCCCCCEEEC		41.52-
327PhosphorylationKTPYEGNYYKCSDYG
CCCCCCCEEECCHHH		18.37-
328PhosphorylationTPYEGNYYKCSDYGR
CCCCCCEEECCHHHC		14.98-
329UbiquitinationPYEGNYYKCSDYGRA
CCCCCEEECCHHHCE		19.5329967540
329AcetylationPYEGNYYKCSDYGRA
CCCCCEEECCHHHCE		19.5319809843
331UbiquitinationEGNYYKCSDYGRAFI
CCCEEECCHHHCEEE		29.7029967540
340UbiquitinationYGRAFIQKSDLFRCQ
HHCEEECHHHCCCCE		40.9129967540
342UbiquitinationRAFIQKSDLFRCQRI
CEEECHHHCCCCEEC		57.7929967540
354UbiquitinationQRIHSGEKPYEYSEC
EECCCCCCCCCHHHH		57.3229967540
356UbiquitinationIHSGEKPYEYSECEK
CCCCCCCCCHHHHHH		38.2729967540
379PhosphorylationNIHKKIHTGGKHFEC
CCCCEEECCCCCEEE		51.61-
407PhosphorylationSMHQKIHTGEKPYVC
CCCCCCCCCCCCEEE		50.97-
410SumoylationQKIHTGEKPYVCTEC
CCCCCCCCCEEECCC		42.89-
410SumoylationQKIHTGEKPYVCTEC
CCCCCCCCCEEECCC		42.89-
419UbiquitinationYVCTECGKAFIRKSH
EEECCCCCCHHHHHC		52.35-
435PhosphorylationITHERIHTGEKPYEC
EECCEEECCCCCEEC		44.6727282143
438UbiquitinationERIHTGEKPYECSDC
CEEECCCCCEECCCC		55.00-
448PhosphorylationECSDCGKSFIKKSQL
ECCCCCCCHHHHHHC		19.9324719451
453PhosphorylationGKSFIKKSQLHVHQR
CCCHHHHHHCEEECC		32.73-
478PhosphorylationSECGKVFTHKTNLII
CCCCCEEECCCCEEE		26.0029396449
481PhosphorylationGKVFTHKTNLIIHQK
CCEEECCCCEEEEEE		27.8729396449
516UbiquitinationSNLIKHQKIHTGEKP
HHHHCCCCCCCCCCC		35.85-
519PhosphorylationIKHQKIHTGEKPYKC
HCCCCCCCCCCCEEC		50.9729496963
537PhosphorylationGKSFTWKSRLRIHQK
CCCCEEEHHEEEECC		28.2722210691
603PhosphorylationITHERIHTGEKPYEC
ECCCEEECCCCCEEE		44.6728111955
616PhosphorylationECSICGKSFTKKSQL
EEEECCCCCCCCCCE		24.3524719451
618PhosphorylationSICGKSFTKKSQLHV
EECCCCCCCCCCEEE		44.6630631047
631PhosphorylationHVHQQIHTGEKPYRC
EEECCCCCCCCCEEE		48.9829496963
634SumoylationQQIHTGEKPYRCAEC
CCCCCCCCCEEECCC		49.01-
634UbiquitinationQQIHTGEKPYRCAEC
CCCCCCCCCEEECCC		49.01-
634SumoylationQQIHTGEKPYRCAEC
CCCCCCCCCEEECCC		49.01-
656UbiquitinationSNLFTHQKIHTGEKP
CCCCCCCCEECCCCC		28.93-
659PhosphorylationFTHQKIHTGEKPYKC
CCCCCEECCCCCEEC		50.9729496963
715PhosphorylationIMHQRIHTGEKPYIC
EEEEEECCCCCCEEE		44.6728111955
720PhosphorylationIHTGEKPYICNECGK
ECCCCCCEEECCCCC		29.22-
743PhosphorylationNRHRRIHTGEKPYEC
HCCCCCCCCCCCEEC		44.6727282143
746UbiquitinationRRIHTGEKPYECSDC
CCCCCCCCCEECCCC		55.00-
756PhosphorylationECSDCGKSFIKKSQL
ECCCCCHHHHHHHHC		19.9324719451
771PhosphorylationHEHHRIHTGEKPYIC
CCCCCCCCCCCCEEE		44.6728111955
774SumoylationHRIHTGEKPYICAEC
CCCCCCCCCEEECCC		44.45-
774SumoylationHRIHTGEKPYICAEC
CCCCCCCCCEEECCC		44.45-
786PhosphorylationAECGKAFTIRSNLIK
CCCCCEEEEHHHHHH		21.9724719451
816SumoylationLGKALNWKPQLSMPQ
HHHHCCCCCCCCCCC		23.0828112733
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 ZN484_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN484_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 ZN484_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN484_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN484_HUMAN

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Related Literatures of Post-Translational Modification

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