CSRN3_HUMAN - dbPTM
CSRN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSRN3_HUMAN
UniProt AC Q8WYN3
Protein Name Cysteine/serine-rich nuclear protein 3
Gene Name CSRNP3
Organism Homo sapiens (Human).
Sequence Length 585
Subcellular Localization Nucleus.
Protein Description Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity. Plays a role in apoptosis (By similarity)..
Protein Sequence MSGILKRKFEEVDGSSPCSSVRESDDEVSSSESADSGDSVNPSTSSHFTPSSILKREKRLRTKNVHFSCVTVYYFTRRQGFTSVPSQGGSTLGMSSRHNSVRQYTLGEFAREQERLHREMLREHLREEKLNSLKLKMTKNGTVESEEASTLTLDDISDDDIDLDNTEVDEYFFLQPLPTKKRRALLRASGVKKIDVEEKHELRAIRLSREDCGCDCRVFCDPDTCTCSLAGIKCQVDRMSFPCGCTKEGCSNTAGRIEFNPIRVRTHFLHTIMKLELEKNREQQIPTLNGCHSEISAHSSSMGPVAHSVEYSIADSFEIETEPQAAVLHLQSAEELDCQGEEEEEEEDGSSFCSGVTDSSTQSLAPSESDEEEEEEEEEEEEEDDDDDKGDGFVEGLGTHAEVVPLPSVLCYSDGTAVHESHAKNASFYANSSTLYYQIDSHIPGTPNQISENYSERDTVKNGTLSLVPYTMTPEQFVDYARQAEEAYGASHYPAANPSVIVCCSSSENDSGVPCNSLYPEHRSNHPQVEFHSYLKGPSQEGFVSALNGDSHISEHPAENSLSLAEKSILHEECIKSPVVETVPV
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
29PhosphorylationRESDDEVSSSESADS
CCCCCCCCCCCCCCC
26.54-
30PhosphorylationESDDEVSSSESADSG
CCCCCCCCCCCCCCC
43.21-
31PhosphorylationSDDEVSSSESADSGD
CCCCCCCCCCCCCCC
28.23-
51PhosphorylationTSSHFTPSSILKREK
CCCCCCHHHHHHHHH
27.27-
52PhosphorylationSSHFTPSSILKREKR
CCCCCHHHHHHHHHH
32.8924719451
62PhosphorylationKREKRLRTKNVHFSC
HHHHHHHCCCCCEEE
31.4022210691
74PhosphorylationFSCVTVYYFTRRQGF
EEEEEEEEEECCCCC
8.3022210691
82PhosphorylationFTRRQGFTSVPSQGG
EECCCCCEECCCCCC
35.3224114839
95PhosphorylationGGSTLGMSSRHNSVR
CCCCCCCCCCCCCCH
23.5624114839
96PhosphorylationGSTLGMSSRHNSVRQ
CCCCCCCCCCCCCHH
28.7724114839
104PhosphorylationRHNSVRQYTLGEFAR
CCCCCHHHCHHHHHH
8.05-
179PhosphorylationFFLQPLPTKKRRALL
EECCCCCCHHHHHHH
57.8122964224
192AcetylationLLRASGVKKIDVEEK
HHHHHCCCCCCHHHH
47.7611790901
193AcetylationLRASGVKKIDVEEKH
HHHHCCCCCCHHHHH
41.5511790911
199AcetylationKKIDVEEKHELRAIR
CCCCHHHHHHHHHHC
28.9511790921
274UbiquitinationHFLHTIMKLELEKNR
HHHHHHHHHHHHHCH
34.65-
561PhosphorylationSEHPAENSLSLAEKS
CCCCCCCCCCHHHHH
15.7319690332
563PhosphorylationHPAENSLSLAEKSIL
CCCCCCCCHHHHHHC
25.9219690332
577PhosphorylationLHEECIKSPVVETVP
CCHHHHCCCCEEECC
11.7429978859
582PhosphorylationIKSPVVETVPV----
HCCCCEEECCC----
20.6429978859

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 CSRN3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSRN3_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 CSRN3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CSRN3_HUMAN !!

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 CSRN3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561 AND SER-563, ANDMASS SPECTROMETRY.

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