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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
29 | Phosphorylation | RESDDEVSSSESADS CCCCCCCCCCCCCCC | 26.54 | - | |
30 | Phosphorylation | ESDDEVSSSESADSG CCCCCCCCCCCCCCC | 43.21 | - | |
31 | Phosphorylation | SDDEVSSSESADSGD CCCCCCCCCCCCCCC | 28.23 | - | |
51 | Phosphorylation | TSSHFTPSSILKREK CCCCCCHHHHHHHHH | 27.27 | - | |
52 | Phosphorylation | SSHFTPSSILKREKR CCCCCHHHHHHHHHH | 32.89 | 24719451 | |
62 | Phosphorylation | KREKRLRTKNVHFSC HHHHHHHCCCCCEEE | 31.40 | 22210691 | |
74 | Phosphorylation | FSCVTVYYFTRRQGF EEEEEEEEEECCCCC | 8.30 | 22210691 | |
82 | Phosphorylation | FTRRQGFTSVPSQGG EECCCCCEECCCCCC | 35.32 | 24114839 | |
95 | Phosphorylation | GGSTLGMSSRHNSVR CCCCCCCCCCCCCCH | 23.56 | 24114839 | |
96 | Phosphorylation | GSTLGMSSRHNSVRQ CCCCCCCCCCCCCHH | 28.77 | 24114839 | |
104 | Phosphorylation | RHNSVRQYTLGEFAR CCCCCHHHCHHHHHH | 8.05 | - | |
179 | Phosphorylation | FFLQPLPTKKRRALL EECCCCCCHHHHHHH | 57.81 | 22964224 | |
192 | Acetylation | LLRASGVKKIDVEEK HHHHHCCCCCCHHHH | 47.76 | 11790901 | |
193 | Acetylation | LRASGVKKIDVEEKH HHHHCCCCCCHHHHH | 41.55 | 11790911 | |
199 | Acetylation | KKIDVEEKHELRAIR CCCCHHHHHHHHHHC | 28.95 | 11790921 | |
274 | Ubiquitination | HFLHTIMKLELEKNR HHHHHHHHHHHHHCH | 34.65 | - | |
561 | Phosphorylation | SEHPAENSLSLAEKS CCCCCCCCCCHHHHH | 15.73 | 19690332 | |
563 | Phosphorylation | HPAENSLSLAEKSIL CCCCCCCCHHHHHHC | 25.92 | 19690332 | |
577 | Phosphorylation | LHEECIKSPVVETVP CCHHHHCCCCEEECC | 11.74 | 29978859 | |
582 | Phosphorylation | IKSPVVETVPV---- HCCCCEEECCC---- | 20.64 | 29978859 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CSRN3_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of CSRN3_HUMAN !! |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |