Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Staphylococcal nuclease domain-containing protein 1  

UniProtKB / Swiss-Prot ID :  SND1_HUMAN

Gene Name (Synonyms) : 
SND1, TDRD11  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Melanosome. Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. 

Protein Function :  Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). 

Protein Sequence MASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDA...
Predicted Secondary Structure CCCCCCCCCCCCCCCCHHHHHHHHHHHHHCCEEEEECCCCCCCCCCCEEEHHHCCHHHHHHHHHCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASSAQ
---CCCCCC
16.52UniProtKB
Link-
3Phosphoserine--MASSAQS
--CCCCCCC
25.55HPRD
Link-
3Phosphoserine--MASSAQS
--CCCCCCC
25.55Phosphositeplus
Link-
3Phosphoserine--MASSAQS
--CCCCCCC
25.55SysPTM
Link-
4Phosphoserine.-MASSAQSG
-CCCCCCCC
22.31UniProtKB
Link-
10PhosphoserineQSGGSSGGP
CCCCCCCCC
29.36HPRD
Link-
10Phosphoserine.QSGGSSGGP
CCCCCCCCC
29.36UniProtKB
Link-
29PhosphoserineKMVLSGCAI
HHHHHCCEE
22.03Phosphositeplus
Link-
71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QPDAKDTPD
CCCCCCCCC
70.30Phosphositeplus
Link-
103PhosphothreonineIENKTPQGR
EECCCCCCC
32.21HPRD
Link-
103PhosphothreonineIENKTPQGR
EECCCCCCC
32.21Phosphositeplus
Link-
109PhosphotyrosineQGREYGMIY
CCCCEEEEE
15.61HPRD
Link-
109PhosphotyrosineQGREYGMIY
CCCCEEEEE
15.61PhosphoELM
Link-
109PhosphotyrosineQGREYGMIY
CCCCEEEEE
15.61Phosphositeplus
Link-
109Phosphotyrosine.QGREYGMIY
CCCCEEEEE
15.61UniProtKB
Link-
177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IRDLKYTIE
EEEHHEECC
44.64Phosphositeplus
Link-
193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SHHQKPVNA
HHHCCHHHH
46.72Phosphositeplus
Link-
193N6-acetyllysineSHHQKPVNA
HHHCCHHHH
46.72HPRD
Link-
193N6-acetyllysineSHHQKPVNA
HHHCCHHHH
46.72Phosphositeplus
Link-
193N6-acetyllysine.SHHQKPVNA
HHHCCHHHH
46.72UniProtKB
Link-
238PhosphoserineEADGSETPE
CCCCCCCCC
38.55HPRD
Link-
238PhosphoserineEADGSETPE
CCCCCCCCC
38.55SysPTM
Link-
240PhosphothreonineDGSETPEPF
CCCCCCCCC
34.35HPRD
Link-
240PhosphothreonineDGSETPEPF
CCCCCCCCC
34.35PhosphoELM
Link-
240PhosphothreonineDGSETPEPF
CCCCCCCCC
34.35SysPTM
Link-
249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AAEAKFFTE
HHHHHHHHH
32.30Phosphositeplus
Link-
329PhosphotyrosineIWRDYVAPT
HHHHHCCCC
7.02Phosphositeplus
Link-
339Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NLDQKDKQF
CCCHHHHHH
67.56Phosphositeplus
Link-
366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SGDYKTIHL
CCCEEEEEE
45.82Phosphositeplus
Link-
418PhosphothreonineKVNVTVDYI
EEEEEEEEE
11.49HPRD
Link-
418PhosphothreonineKVNVTVDYI
EEEEEEEEE
11.49Phosphositeplus
Link-
421PhosphotyrosineVTVDYIRPA
EEEEEEECC
8.42Phosphositeplus
Link-
426PhosphoserineIRPASPATE
EECCCCHHH
20.11HPRD
Link-
426PhosphoserineIRPASPATE
EECCCCHHH
20.11PhosphoELM
Link-
426PhosphoserineIRPASPATE
EECCCCHHH
20.11Phosphositeplus
Link-
429PhosphothreonineASPATETVP
CCCHHHCCC
35.26HPRD
Link-
429PhosphothreonineASPATETVP
CCCHHHCCC
35.26PhosphoELM
Link-
429PhosphothreonineASPATETVP
CCCHHHCCC
35.26SysPTM
Link-
429Phosphothreonine.ASPATETVP
CCCHHHCCC
35.26UniProtKB
Link-
440S-nitrosocysteineSERTCATVT
CCCCEEEEE
3.61dbSNO
Link-
513Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GDTQKAKQF
CCHHHHHHH
60.69Phosphositeplus
Link-
515Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TQKAKQFLP
HHHHHHHHH
48.93Phosphositeplus
Link-
641Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SSYYKSLLS
HHHHHHHHH
26.79Phosphositeplus
Link-
641N6-acetyllysineSSYYKSLLS
HHHHHHHHH
26.79HPRD
Link-
641N6-acetyllysineSSYYKSLLS
HHHHHHHHH
26.79Phosphositeplus
Link-
641N6-acetyllysine.SSYYKSLLS
HHHHHHHHH
26.79UniProtKB
Link-
661PhosphotyrosineVWAHYEEQP
HHHCCCCCC
17.26Phosphositeplus
Link-
739Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FCIAKFVDG
EEEEECCCC
26.47Phosphositeplus
Link
752N6-acetyllysineARVEKVESP
EEEEEEECC
48.74HPRD
Link
752N6-acetyllysineARVEKVESP
EEEEEEECC
48.74Phosphositeplus
Link
752N6-acetyllysine.ARVEKVESP
EEEEEEECC
48.74UniProtKB
Link
781PhosphoserineLGTLSPAFS
CEECCHHHH
17.64HPRD
Link
781PhosphoserineLGTLSPAFS
CEECCHHHH
17.64PhosphoELM
Link
781PhosphoserineLGTLSPAFS
CEECCHHHH
17.64Phosphositeplus
Link
781PhosphoserineLGTLSPAFS
CEECCHHHH
17.64SysPTM
Link
781Phosphoserine.LGTLSPAFS
CEECCHHHH
17.64UniProtKB
Link
848Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FADSKGDVG
ECCCCCHHH
60.73Phosphositeplus
Link-
857Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LGLVKEGLV
HHHHHHCEE
51.62Phosphositeplus
Link-
873Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KQFQKVITE
HHHHHHHHH
36.57Phosphositeplus
Link-
886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QESAKSARL
HHHCCCCEE
54.66Phosphositeplus
Link-
908PhosphotyrosineDEFGYSR
HHCCCCC
13.44HPRD
Link-
908PhosphotyrosineDEFGYSR
HHCCCCC
13.44PhosphoELM
Link-
908PhosphotyrosineDEFGYSR
HHCCCCC
13.44Phosphositeplus
Link-
908Phosphotyrosine.DEFGYSR
HHCCCCC
13.44UniProtKB
Link-
909PhosphoserineEFGYSR
HCCCCC
31.71Phosphositeplus
Link-
909Phosphoserine.EFGYSR
HCCCCC
31.71UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SUH_HUMANin vitro
in vivo
HPRD:03714HPRD7651391
PIM1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03714HPRD9809063
T2EA_HUMANin vitro
in vivo
HPRD:03714HPRD7651391
T2EB_HUMANin vitro
in vivo
HPRD:03714HPRD7651391
MYB_HUMANin vitro
yeast 2-hybrid
HPRD:03714HPRD9809063
8756344
MYBB_HUMANin vitroHPRD:03714HPRD11259168
STAT6_HUMANin vitro
in vivo
HPRD:03714HPRD12234934
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4 AND SER-10, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-193; LYS-641 AND LYS-752,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-109, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4 AND SER-10, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-109, AND MASSSPECTROMETRY.
"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-909, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-109 AND TYR-908, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429 AND SER-781, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures