ZN711_HUMAN - dbPTM
ZN711_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN711_HUMAN
UniProt AC Q9Y462
Protein Name Zinc finger protein 711
Gene Name ZNF711
Organism Homo sapiens (Human).
Sequence Length 761
Subcellular Localization Nucleus .
Protein Description Transcription regulator required for brain development. Probably acts as a transcription factor that binds to the promoter of target genes and recruits PHF8 histone demethylase, leading to activate expression of genes involved in neuron development, such as KDM5C..
Protein Sequence MDSGGGSLGLHTPDSRMAHTMIMQDFVAGMAGTAHIDGDHIVVSVPEAVLVSDVVTDDGITLDHGLAAEVVHGPDIITETDVVTEGVIVPEAVLEADVAIEEDLEEDDGDHILTSELITETVRVPEQVFVADLVTGPNGHLEHVVQDCVSGVDSPTMVSEEVLVTNSDTETVIQAAGGVPGSTVTIKTEDDDDDDVKSTSEDYLMISLDDVGEKLEHMGNTPLKIGSDGSQEDAKEDGFGSEVIKVYIFKAEAEDDVEIGGTEIVTESEYTSGHSVAGVLDQSRMQREKMVYMAVKDSSQEEDDIRDERRVSRRYEDCQASGNTLDSALESRSSTAAQYLQICDGINTNKVLKQKAKKRRRGETRQWQTAVIIGPDGQPLTVYPCHICTKKFKSRGFLKRHMKNHPDHLMRKKYQCTDCDFTTNKKVSFHNHLESHKLINKVDKTHEFTEYTRRYREASPLSSNKLILRDKEPKMHKCKYCDYETAEQGLLNRHLLAVHSKNFPHVCVECGKGFRHPSELKKHMRTHTGEKPYQCQYCIFRCADQSNLKTHIKSKHGNNLPYKCEHCPQAFGDERELQRHLDLFQGHKTHQCPHCDHKSTNSSDLKRHIISVHTKDFPHKCEVCDKGFHRPSELKKHSDIHKGRKIHQCRHCDFKTSDPFILSGHILSVHTKDQPLKCKRCKRGFRQQNELKKHMKTHTGRKIYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEFCKKGFRRPSEKNQHIMRHHKEALM
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
3Phosphorylation-----MDSGGGSLGL
-----CCCCCCCCCC		37.73-
7Phosphorylation-MDSGGGSLGLHTPD
-CCCCCCCCCCCCCC		23.65-
12PhosphorylationGGSLGLHTPDSRMAH
CCCCCCCCCCHHHHH		33.56-
33PhosphorylationFVAGMAGTAHIDGDH
HHHHCCCCEEECCCE		12.9128787133
154PhosphorylationDCVSGVDSPTMVSEE
HHHCCCCCCCEECCE		21.6226074081
156PhosphorylationVSGVDSPTMVSEEVL
HCCCCCCCEECCEEE		33.8726074081
187SumoylationPGSTVTIKTEDDDDD
CCCEEEEECCCCCCC		36.17-
187SumoylationPGSTVTIKTEDDDDD
CCCEEEEECCCCCCC		36.17-
188PhosphorylationGSTVTIKTEDDDDDD
CCEEEEECCCCCCCC		40.5727732954
198PhosphorylationDDDDDVKSTSEDYLM
CCCCCCCCCCCCEEE		36.6922496350
199PhosphorylationDDDDVKSTSEDYLMI
CCCCCCCCCCCEEEE		30.3422496350
200PhosphorylationDDDVKSTSEDYLMIS
CCCCCCCCCCEEEEE		35.2529978859
203PhosphorylationVKSTSEDYLMISLDD
CCCCCCCEEEEEHHH		8.3027732954
204 (in isoform 1)Ubiquitination-3.6721890473
210PhosphorylationYLMISLDDVGEKLEH
EEEEEHHHHHHHHHH		56.4617525332
221PhosphorylationKLEHMGNTPLKIGSD
HHHHCCCCCCEECCC		25.0330266825
224UbiquitinationHMGNTPLKIGSDGSQ
HCCCCCCEECCCCCH		46.3421890473
224SumoylationHMGNTPLKIGSDGSQ
HCCCCCCEECCCCCH		46.3428112733
224UbiquitinationHMGNTPLKIGSDGSQ
HCCCCCCEECCCCCH		46.3421890473
224 (in isoform 2)Ubiquitination-46.3421890473
227PhosphorylationNTPLKIGSDGSQEDA
CCCCEECCCCCHHHH		42.1223312004
230PhosphorylationLKIGSDGSQEDAKED
CEECCCCCHHHHHHC		35.0717525332
235SumoylationDGSQEDAKEDGFGSE
CCCHHHHHHCCCCCE		69.5228112733
235UbiquitinationDGSQEDAKEDGFGSE
CCCHHHHHHCCCCCE		69.52-
262PhosphorylationDDVEIGGTEIVTESE
CCEEECCEEEECCCC		19.8219053533
266PhosphorylationIGGTEIVTESEYTSG
ECCEEEECCCCCCCC		39.1825954137
269 (in isoform 1)Ubiquitination-46.7421890473
275PhosphorylationSEYTSGHSVAGVLDQ
CCCCCCCCHHHHHCH		19.7225954137
289UbiquitinationQSRMQREKMVYMAVK
HHHHHHHHEEEEEEC		35.5421890473
289 (in isoform 2)Ubiquitination-35.5421890473
289UbiquitinationQSRMQREKMVYMAVK
HHHHHHHHEEEEEEC		35.542189047
296SumoylationKMVYMAVKDSSQEED
HEEEEEECCCCCCCC		42.2128112733
298PhosphorylationVYMAVKDSSQEEDDI
EEEEECCCCCCCCHH		28.3629449344
299PhosphorylationYMAVKDSSQEEDDIR
EEEECCCCCCCCHHH		52.3129449344
426UbiquitinationCDFTTNKKVSFHNHL
CCCCCCCCCEECHHH		45.22-
428PhosphorylationFTTNKKVSFHNHLES
CCCCCCCEECHHHHH		29.6626074081
444UbiquitinationKLINKVDKTHEFTEY
HHCCCCCCHHHHHHH		55.56-
455PhosphorylationFTEYTRRYREASPLS
HHHHHHHHHHCCCCC		14.9830576142
459PhosphorylationTRRYREASPLSSNKL
HHHHHHCCCCCCCCE		22.9430266825
462PhosphorylationYREASPLSSNKLILR
HHHCCCCCCCCEEEC		34.9430266825
463PhosphorylationREASPLSSNKLILRD
HHCCCCCCCCEEECC		45.7428450419
465UbiquitinationASPLSSNKLILRDKE
CCCCCCCCEEECCCC		38.56-
500PhosphorylationRHLLAVHSKNFPHVC
HHHHHHHCCCCCCEE		23.7728985074
526PhosphorylationELKKHMRTHTGEKPY
HHHHHHHHCCCCCCC		19.0627251275
528PhosphorylationKKHMRTHTGEKPYQC
HHHHHHCCCCCCCCC		46.5627251275
533PhosphorylationTHTGEKPYQCQYCIF
HCCCCCCCCCEEEEE		32.7527251275
537PhosphorylationEKPYQCQYCIFRCAD
CCCCCCEEEEEEECC		8.6427251275
549UbiquitinationCADQSNLKTHIKSKH
ECCCCCCHHHHHCCC		42.16-
562PhosphorylationKHGNNLPYKCEHCPQ
CCCCCCCCCCCCCCH		31.2822461510
599PhosphorylationCPHCDHKSTNSSDLK
CCCCCCCCCCHHHHH		29.4230576142
600PhosphorylationPHCDHKSTNSSDLKR
CCCCCCCCCHHHHHH		43.8730576142
611PhosphorylationDLKRHIISVHTKDFP
HHHHHEEEEECCCCC		13.7720068231
614PhosphorylationRHIISVHTKDFPHKC
HHEEEEECCCCCCCC		30.1020068231
635UbiquitinationFHRPSELKKHSDIHK
CCCHHHHHHCCCCCC		44.37-
656PhosphorylationCRHCDFKTSDPFILS
ECCCCCCCCCCEEEC		38.0525137130
657PhosphorylationRHCDFKTSDPFILSG
CCCCCCCCCCEEECE		43.8325137130
671PhosphorylationGHILSVHTKDQPLKC
EEEEEEECCCCCCCC		33.8725137130
704PhosphorylationTHTGRKIYQCEYCEY
HCCCCEEEEEECEEC		15.33-
720UbiquitinationTTDASGFKRHVISIH
CCCCCCCCEEEEEEE		45.15-
725PhosphorylationGFKRHVISIHTKDYP
CCCEEEEEEECCCCC		13.7627732954
728PhosphorylationRHVISIHTKDYPHRC
EEEEEEECCCCCCCC		24.7630576142
739UbiquitinationPHRCEFCKKGFRRPS
CCCCHHHHCCCCCCC		62.34-
740UbiquitinationHRCEFCKKGFRRPSE
CCCHHHHCCCCCCCH		65.54-
746PhosphorylationKKGFRRPSEKNQHIM
HCCCCCCCHHHHHHH		60.4324719451
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 ZN711_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN711_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 ZN711_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHF8_HUMANPHF8physical
20346720
KCTD5_HUMANKCTD5physical
26188516
CUL3_HUMANCUL3physical
26188516
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300803Mental retardation, X-linked, ZNF711-related (MRXZ)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN711_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-230, AND MASSSPECTROMETRY.

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