ZN423_HUMAN - dbPTM
ZN423_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN423_HUMAN
UniProt AC Q2M1K9
Protein Name Zinc finger protein 423
Gene Name ZNF423
Organism Homo sapiens (Human).
Sequence Length 1284
Subcellular Localization Nucleus .
Protein Description Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved in terminal olfactory receptor neurons differentiation; this interaction preventing EBF1 to bind DNA and activate olfactory-specific genes. Involved in olfactory neurogenesis by participating in a developmental switch that regulates the transition from differentiation to maturation in olfactory receptor neurons. Controls proliferation and differentiation of neural precursors in cerebellar vermis formation..
Protein Sequence MHKKRVEEGEASDFSLAWDSSVTAAGGLEGEPECDQKTSRALEDRNSVTSQEERNEDDEDMEDESIYTCDHCQQDFESLADLTDHRAHRCPGDGDDDPQLSWVASSPSSKDVASPTQMIGDGCDLGLGEEEGGTGLPYPCQFCDKSFIRLSYLKRHEQIHSDKLPFKCTYCSRLFKHKRSRDRHIKLHTGDKKYHCHECEAAFSRSDHLKIHLKTHSSSKPFKCTVCKRGFSSTSSLQSHMQAHKKNKEHLAKSEKEAKKDDFMCDYCEDTFSQTEELEKHVLTRHPQLSEKADLQCIHCPEVFVDENTLLAHIHQAHANQKHKCPMCPEQFSSVEGVYCHLDSHRQPDSSNHSVSPDPVLGSVASMSSATPDSSASVERGSTPDSTLKPLRGQKKMRDDGQGWTKVVYSCPYCSKRDFNSLAVLEIHLKTIHADKPQQSHTCQICLDSMPTLYNLNEHVRKLHKNHAYPVMQFGNISAFHCNYCPEMFADINSLQEHIRVSHCGPNANPSDGNNAFFCNQCSMGFLTESSLTEHIQQAHCSVGSAKLESPVVQPTQSFMEVYSCPYCTNSPIFGSILKLTKHIKENHKNIPLAHSKKSKAEQSPVSSDVEVSSPKRQRLSASANSISNGEYPCNQCDLKFSNFESFQTHLKLHLELLLRKQACPQCKEDFDSQESLLQHLTVHYMTTSTHYVCESCDKQFSSVDDLQKHLLDMHTFVLYHCTLCQEVFDSKVSIQVHLAVKHSNEKKMYRCTACNWDFRKEADLQVHVKHSHLGNPAKAHKCIFCGETFSTEVELQCHITTHSKKYNCKFCSKAFHAIILLEKHLREKHCVFDAATENGTANGVPPMATKKAEPADLQGMLLKNPEAPNSHEASEDDVDASEPMYGCDICGAAYTMEVLLQNHRLRDHNIRPGEDDGSRKKAEFIKGSHKCNVCSRTFFSENGLREHLQTHRGPAKHYMCPICGERFPSLLTLTEHKVTHSKSLDTGTCRICKMPLQSEEEFIEHCQMHPDLRNSLTGFRCVVCMQTVTSTLELKIHGTFHMQKLAGSSAASSPNGQGLQKLYKCALCLKEFRSKQDLVKLDVNGLPYGLCAGCMARSANGQVGGLAPPEPADRPCAGLRCPECSVKFESAEDLESHMQVDHRDLTPETSGPRKGTQTSPVPRKKTYQCIKCQMTFENEREIQIHVANHMIEEGINHECKLCNQMFDSPAKLLCHLIEHSFEGMGGTFKCPVCFTVFVQANKLQQHIFAVHGQEDKIYDCSQCPQKFFFQTELQNHTMSQHAQ
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
47PhosphorylationRALEDRNSVTSQEER
HHHHHHHCCCCHHHH		27.8921406692
49PhosphorylationLEDRNSVTSQEERNE
HHHHHCCCCHHHHCC		25.2321406692
50PhosphorylationEDRNSVTSQEERNED
HHHHCCCCHHHHCCC		33.1821406692
105PhosphorylationPQLSWVASSPSSKDV
CCCCCEECCCCCCCC		32.9127251275
106PhosphorylationQLSWVASSPSSKDVA
CCCCEECCCCCCCCC		21.0427251275
146PhosphorylationPCQFCDKSFIRLSYL
CCCCCCCHHHHHHHH		16.8024719451
151PhosphorylationDKSFIRLSYLKRHEQ
CCHHHHHHHHHHHHH		20.6924719451
169PhosphorylationDKLPFKCTYCSRLFK
CCCCCCCHHHHHHHH		28.3125690035
170PhosphorylationKLPFKCTYCSRLFKH
CCCCCCHHHHHHHHC		9.6324719451
172PhosphorylationPFKCTYCSRLFKHKR
CCCCHHHHHHHHCCC		22.9227135362
271PhosphorylationMCDYCEDTFSQTEEL
CHHHCCCCCCCHHHH		11.6827732954
273PhosphorylationDYCEDTFSQTEELEK
HHCCCCCCCHHHHHH		37.9827732954
275PhosphorylationCEDTFSQTEELEKHV
CCCCCCCHHHHHHHH		30.1727732954
350PhosphorylationDSHRQPDSSNHSVSP
CCCCCCCCCCCCCCC		39.4627732954
351PhosphorylationSHRQPDSSNHSVSPD
CCCCCCCCCCCCCCC		46.0427732954
354PhosphorylationQPDSSNHSVSPDPVL
CCCCCCCCCCCCCCH		28.6527732954
356PhosphorylationDSSNHSVSPDPVLGS
CCCCCCCCCCCCHHH		26.9727732954
363PhosphorylationSPDPVLGSVASMSSA
CCCCCHHHHHHCCCC		15.4527732954
382PhosphorylationSASVERGSTPDSTLK
CCCCCCCCCCCCCCC		42.8830266825
383PhosphorylationASVERGSTPDSTLKP
CCCCCCCCCCCCCCC		33.6626657352
386PhosphorylationERGSTPDSTLKPLRG
CCCCCCCCCCCCCCC		36.5230266825
387PhosphorylationRGSTPDSTLKPLRGQ
CCCCCCCCCCCCCCC		46.2930266825
550PhosphorylationVGSAKLESPVVQPTQ
CCCCCCCCCCCCCCC		33.1724173317
576PhosphorylationTNSPIFGSILKLTKH
CCCCCHHHHHHHHHH		17.6324719451
599PhosphorylationPLAHSKKSKAEQSPV
CCCCCCCCCCCCCCC		40.6129888752
604PhosphorylationKKSKAEQSPVSSDVE
CCCCCCCCCCCCCCC		20.8319664994
607PhosphorylationKAEQSPVSSDVEVSS
CCCCCCCCCCCCCCC		24.9721406692
608PhosphorylationAEQSPVSSDVEVSSP
CCCCCCCCCCCCCCC		46.0020363803
613PhosphorylationVSSDVEVSSPKRQRL
CCCCCCCCCCCHHHH		27.6721406692
614PhosphorylationSSDVEVSSPKRQRLS
CCCCCCCCCCHHHHC		39.3519664994
750PhosphorylationHSNEKKMYRCTACNW
CCCCCEEEEEEECCC		16.0626657352
753PhosphorylationEKKMYRCTACNWDFR
CCEEEEEEECCCCCC		25.8326657352
770UbiquitinationADLQVHVKHSHLGNP
CCEEEEEECCCCCCH		25.22-
970PhosphorylationICGERFPSLLTLTEH
CCCCCCCCEEEEEEC		33.04-
1018PhosphorylationPDLRNSLTGFRCVVC
HHHHHHCCCCEEEEE		33.8124719451
1049PhosphorylationHMQKLAGSSAASSPN
EHHHHHCCCCCCCCC		15.9327732954
1050PhosphorylationMQKLAGSSAASSPNG
HHHHHCCCCCCCCCC		27.2627732954
1053PhosphorylationLAGSSAASSPNGQGL
HHCCCCCCCCCCHHH		46.1521406692
1054PhosphorylationAGSSAASSPNGQGLQ
HCCCCCCCCCCHHHH		20.0519664995
1147PhosphorylationQVDHRDLTPETSGPR
CCCCCCCCCCCCCCC		24.3022617229
1157PhosphorylationTSGPRKGTQTSPVPR
CCCCCCCCCCCCCCC		31.5430576142
1159PhosphorylationGPRKGTQTSPVPRKK
CCCCCCCCCCCCCCC		34.5321406692
1160PhosphorylationPRKGTQTSPVPRKKT
CCCCCCCCCCCCCCC		17.6821406692
1236PhosphorylationFKCPVCFTVFVQANK
CCCCEEEEEEEECCC		14.12-
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 ZN423_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN423_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 ZN423_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PARP1_HUMANPARP1physical
14623329
SMAD4_HUMANSMAD4physical
10660046
SMAD1_HUMANSMAD1physical
10660046
COE1_HUMANEBF1physical
9151733
COE2_HUMANEBF2physical
9151733
COE3_HUMANEBF3physical
9151733
PARP1_HUMANPARP1physical
22863007
SMAD1_HUMANSMAD1physical
14630787
SMAD4_HUMANSMAD4physical
14630787
BRCA1_HUMANBRCA1physical
25184681
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614844Nephronophthisis 14 (NPHP14)
614844Joubert syndrome 19 (JBTS19)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN423_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-604 ANDSER-608, AND MASS SPECTROMETRY.

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