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Protein Page:
ZNF469 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ZNF469 May be involved in transcriptional regulation. Defects in ZNF469 are the cause of brittle cornea syndrome type 1 (BCS1). A disorder characterized by extreme corneal thinning resulting in corneal rupture after minor trauma, blue sclerae, keratoconus or keratoglobus, hyperelasticity of the skin, and hypermobility of the joints. It shares some features with, but is much less severe than, the ocular form of Ehlers-Danlos syndrome (EDS6). Belongs to the krueppel C2H2-type zinc-finger protein family. Note: This description may include information from UniProtKB.
Protein type: C2H2-type zinc finger protein
Cellular Component: nucleus
Molecular Function: DNA binding; metal ion binding
Biological Process: regulation of transcription, DNA-dependent; transcription, DNA-dependent
Reference #:  Q96JG9 (UniProtKB)
Alt. Names/Synonyms: BCS; KIAA1858; Zinc finger protein 469; ZN469; ZNF469
Gene Symbols: ZNF469
Molecular weight: 410,202 Da
Basal Isoelectric point: 7.88  Predict pI for various phosphorylation states
Select Structure to View Below

ZNF469

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S1522-p PGKGSGCsVALMSHL
0 2 S1530-p VALMSHLsEDELEIQ
0 1 T1553-p QLQRSKDtRGAPREL
0 1 S1709-p GPQLDAGsLAKCSPD
0 1 - gap
0 3 T2263-p RATGLSStPTGDEAQ
0 2 T2369-p ATKMPRVtCPSTGLG
0 6 S2619-p GRRLREEsILPVSAD
0 6 S2629-p PVSADVIsDGRGSRP
0 4 S3593-p KRAPLVFsGKRRAPG
0 1 K3673-m3 KFPVHPRkAVGSLAP
0 1 S3703 PKAKPGPSSQGSGSP
0 1 G3706 KPGPSSQGSGSPRPG
0 1 T3735 QLQSETATTPAKPSF
0 1 T3736 LQSETATTPAKPSFP
0 1 A3738 SETATTPAKPSFPSR
0 1 S3741 ATTPAKPSFPSRSPA
0 1 S3744 PAKPSFPSRSPAPER
0 1 S3746 KPSFPSRSPAPERLP
0 1 P3747 PSFPSRSPAPERLPA
0 1 A3748 SFPSRSPAPERLPAR
  mouse

 
- gap
C1460 GSECSNLCEDELEIK
T1483 QLQGEGSTVGTSGEP
S1618 VALLHAGSLAKDSPK
S1850-p DGRLGSPsQPEKIKG
I2134 EAAPLTSIAPKDGLD
- gap
- gap
S2507 GGTTHVTSDLPTACG
P3433 KRALHLFPGKHKSPG
K3512 KPPAPPRKPGGMGIP
T3543-p SKGKLRGtPQsSGGL
S3546-p KLRGtPQsSGGLQPG
S3575-p QLQSEMAstPtEPsC
T3576-p LQSEMAstPtEPsCP
T3578-p SEMAstPtEPsCPsW
S3581-p AstPtEPsCPsWAss
S3584-p PtEPsCPsWAsstPD
S3587-p PsCPsWAsstPDQPP
S3588-p sCPsWAsstPDQPPP
T3589-p CPsWAsstPDQPPPR
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