ZN219_HUMAN - dbPTM
ZN219_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN219_HUMAN
UniProt AC Q9P2Y4
Protein Name Zinc finger protein 219
Gene Name ZNF219
Organism Homo sapiens (Human).
Sequence Length 722
Subcellular Localization Nucleus .
Protein Description Transcriptional regulator. [PubMed: 14621294]
Protein Sequence MEGSRPRAPSGHLAPSPPAFDGELDLQRYSNGPAVSAGSLGMGAVSWSESRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQATPATEGLARPQAPSSSAFRCPYCKGKFRTSAERERHLHILHRPWKCGLCSFGSSQEEELLHHSLTAHGAPERPLAATSAAPPPQPQPQPPPQPEPRSVPQPEPEPEPEREATPTPAPAAPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFLKNHMKVHASKLGPLRAPGPASGPARAPQPPDLGLLAYEPLGPALLLAPAPTPAERREPPSLLGYLSLRAGEGRPNGEGAEPGPGRSFGGFRPLSSALPARARRHRAEEPEEEEEVVEAEEETWARGRSLGSLASLHPRPGEGPGHSASAAGAQARSTATQEENGLLVGGTRPEGGRGATGKDCPFCGKSFRSAHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSGAGPGPPPEPPPPSQRGSAPQSGAKPSPQPATWVEGASSPRPPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPELMALHLQVHHSRRARGRRPPQADASPPYARVPSGETPPSPSQEGEEGSGLSRPGEAGLGGQER
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
10PhosphorylationGSRPRAPSGHLAPSP
CCCCCCCCCCCCCCC		37.5530266825
16PhosphorylationPSGHLAPSPPAFDGE
CCCCCCCCCCCCCCC		37.6023401153
36O-linked_GlycosylationYSNGPAVSAGSLGMG
HCCCCCCCCCCCCCC		29.0830620550
106PhosphorylationLLRSHLRTHQPERPR
HHHHHHHHCCCCCCC		31.0927251275
114PhosphorylationHQPERPRSPAARLLL
CCCCCCCCHHHHHHH		22.9029116813
139PhosphorylationARLGRARSSGGMQAT
HHHHCHHCCCCCCCC		32.14-
140PhosphorylationRLGRARSSGGMQATP
HHHCHHCCCCCCCCC		33.54-
175PhosphorylationCKGKFRTSAERERHL
CCCCCCCHHHHHHHH		24.7117081983
242PhosphorylationPPQPEPRSVPQPEPE
CCCCCCCCCCCCCCC		49.1928464451
257PhosphorylationPEPEREATPTPAPAA
CCCCCCCCCCCCCCC		23.9623401153
259PhosphorylationPEREATPTPAPAAPE
CCCCCCCCCCCCCCC		27.9426657352
354PhosphorylationPDLGLLAYEPLGPAL
CCCCEEEECCCCCEE		20.3222210691
368PhosphorylationLLLAPAPTPAERREP
EEECCCCCHHHHCCC		36.9222210691
381PhosphorylationEPPSLLGYLSLRAGE
CCCCHHHHHHEECCC		7.9623186163
383PhosphorylationPSLLGYLSLRAGEGR
CCHHHHHHEECCCCC		13.8123186163
473PhosphorylationAAGAQARSTATQEEN
HHHHHHHCCCCCHHC		25.9623312004
474PhosphorylationAGAQARSTATQEENG
HHHHHHCCCCCHHCC		28.3323312004
476PhosphorylationAQARSTATQEENGLL
HHHHCCCCCHHCCEE		36.2823312004
487PhosphorylationNGLLVGGTRPEGGRG
CCEEECCCCCCCCCC		36.8023312004
509PhosphorylationFCGKSFRSAHHLKVH
CCCCCHHHCCEEEEE		29.9122496350
521PhosphorylationKVHLRVHTGERPYKC
EEEEEEECCCCCCCC		37.5727251275
536PhosphorylationPHCDYAGTQSGSLKY
CCCCCCCCCCCHHHH		16.0527251275
538PhosphorylationCDYAGTQSGSLKYHL
CCCCCCCCCHHHHHH		30.1327251275
540PhosphorylationYAGTQSGSLKYHLQR
CCCCCCCHHHHHHHH		27.2527251275
581PhosphorylationPQSGAKPSPQPATWV
CCCCCCCCCCCCCCC		35.1523312004
586PhosphorylationKPSPQPATWVEGASS
CCCCCCCCCCCCCCC		36.4025332170
592PhosphorylationATWVEGASSPRPPSS
CCCCCCCCCCCCCCC		52.2928348404
593PhosphorylationTWVEGASSPRPPSSG
CCCCCCCCCCCCCCC		25.1324719451
598PhosphorylationASSPRPPSSGAGPGS
CCCCCCCCCCCCCCC		44.0525332170
599PhosphorylationSSPRPPSSGAGPGSR
CCCCCCCCCCCCCCC		38.1423312004
605PhosphorylationSSGAGPGSRRKPASP
CCCCCCCCCCCCCCC		31.8523312004
611PhosphorylationGSRRKPASPGRTLRN
CCCCCCCCCCCCCCC		36.0928111955
615PhosphorylationKPASPGRTLRNGRGG
CCCCCCCCCCCCCCC		35.6628111955
630PhosphorylationEAEPLDLSLRAGPGG
CCCCCCEEEECCCCC		18.5724719451
655PhosphorylationCLFCPFATGAPELMA
HHCCCCCCCCHHHHH		33.9724043423
684PhosphorylationRPPQADASPPYARVP
CCCCCCCCCCCCCCC		27.2730266825
687PhosphorylationQADASPPYARVPSGE
CCCCCCCCCCCCCCC		15.4926074081
692PhosphorylationPPYARVPSGETPPSP
CCCCCCCCCCCCCCC		46.5429255136
695PhosphorylationARVPSGETPPSPSQE
CCCCCCCCCCCCCCC		43.9830266825
698PhosphorylationPSGETPPSPSQEGEE
CCCCCCCCCCCCCCC		38.0919664994
700PhosphorylationGETPPSPSQEGEEGS
CCCCCCCCCCCCCCC		45.2430266825
707PhosphorylationSQEGEEGSGLSRPGE
CCCCCCCCCCCCCCC		39.5829255136
710PhosphorylationGEEGSGLSRPGEAGL
CCCCCCCCCCCCCCC		39.7029255136
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 ZN219_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN219_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 ZN219_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TTC32_HUMANTTC32physical
25416956
NPAT_HUMANNPATphysical
26186194
RBBP4_HUMANRBBP4physical
26186194
RBBP7_HUMANRBBP7physical
26186194
HDAC1_HUMANHDAC1physical
26186194
HDAC2_HUMANHDAC2physical
26186194
P66B_HUMANGATAD2Bphysical
26186194
P66A_HUMANGATAD2Aphysical
26186194
ZN521_HUMANZNF521physical
26186194
ZN423_HUMANZNF423physical
26186194
CYTSA_HUMANSPECC1Lphysical
26186194
MBD2_HUMANMBD2physical
26186194
MBD3_HUMANMBD3physical
26186194
CHD3_HUMANCHD3physical
26186194
CHD4_HUMANCHD4physical
26186194
CHD5_HUMANCHD5physical
26186194
MTA2_HUMANMTA2physical
26186194
MTA1_HUMANMTA1physical
26186194
MTA3_HUMANMTA3physical
26186194
2AAB_HUMANPPP2R1Bphysical
26186194
2AAA_HUMANPPP2R1Aphysical
26186194
P3H2_HUMANP3H2physical
26186194
CDKA1_HUMANCDK2AP1physical
26186194
TRI27_HUMANTRIM27physical
26186194
SOGA1_HUMANSOGA1physical
26186194
STRN3_HUMANSTRN3physical
26186194
ZBTB2_HUMANZBTB2physical
26186194
STRN4_HUMANSTRN4physical
26186194
BEND7_HUMANBEND7physical
26186194
HDAC1_HUMANHDAC1physical
28514442
RBBP7_HUMANRBBP7physical
28514442
MTA3_HUMANMTA3physical
28514442
CHD5_HUMANCHD5physical
28514442
P66B_HUMANGATAD2Bphysical
28514442
MBD2_HUMANMBD2physical
28514442
MBD3_HUMANMBD3physical
28514442
P3H2_HUMANP3H2physical
28514442
MTA1_HUMANMTA1physical
28514442
CHD4_HUMANCHD4physical
28514442
P66A_HUMANGATAD2Aphysical
28514442
ZN423_HUMANZNF423physical
28514442
CHD3_HUMANCHD3physical
28514442
ZN521_HUMANZNF521physical
28514442
MTA2_HUMANMTA2physical
28514442
NPAT_HUMANNPATphysical
28514442
CDKA1_HUMANCDK2AP1physical
28514442
ZBTB2_HUMANZBTB2physical
28514442
RBBP4_HUMANRBBP4physical
28514442
SOGA1_HUMANSOGA1physical
28514442
HDAC2_HUMANHDAC2physical
28514442
BEND7_HUMANBEND7physical
28514442
TRI27_HUMANTRIM27physical
28514442
CYTSA_HUMANSPECC1Lphysical
28514442
2AAB_HUMANPPP2R1Bphysical
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 ZN219_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASSSPECTROMETRY.

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