Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  SAFB-like transcription modulator  

UniProtKB / Swiss-Prot ID :  SLTM_HUMAN

Gene Name (Synonyms) : 
SLTM, MET  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). Note=Detected in punctate structures (By similarity). 

Protein Function :  When overexpressed, acts as a general inhibitor of transcription that eventually leads to apoptosis (By similarity). 

Protein Sequence MAAATGAVAASAASGQAEGKKITDLRVIDLKSELKRRNLDITGVKTVLISRLKQAIEEEGGDPDNIELTV...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
235V -> L (in dbSNP:rs7175939). VAR_037088
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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
Protein Variant
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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.---MAAATG
---
19.67UniProtKB
Link-
11PhosphoserineAVAASAASG
18.03HPRD
Link-
14PhosphoserineASAASGQAE
31.02HPRD
Link-
14PhosphoserineASAASGQAE
31.02Phosphositeplus
Link-
69PhosphothreonineNIELTVSTD
10.30HPRD
Link-
74PhosphothreonineVSTDTPNKK
28.93HPRD
Link-
74PhosphothreonineVSTDTPNKK
28.93Phosphositeplus
Link-
74Phosphothreonine.VSTDTPNKK
28.93UniProtKB
Link-
80PhosphothreonineNKKPTKGKG
62.40Phosphositeplus
Link-
93PhosphoserineADELSGDAS
32.36HPRD
Link-
93PhosphoserineADELSGDAS
32.36Phosphositeplus
Link-
93Phosphoserine.ADELSGDAS
32.36UniProtKB
Link-
97PhosphoserineSGDASVEDD
30.68HPRD
Link-
97PhosphoserineSGDASVEDD
30.68Phosphositeplus
Link-
97Phosphoserine.SGDASVEDD
30.68UniProtKB
Link-
144PhosphoserineKELLSAEEN
46.38HPRD
Link-
144PhosphoserineKELLSAEEN
46.38Phosphositeplus
Link-
170PhosphoserineEDIESQEIE
33.19Phosphositeplus
Link-
244PhosphoserineDDNISVTIQ
21.33HPRD
Link-
244Phosphoserine.DDNISVTIQ
21.33UniProtKB
Link-
254PhosphothreonineEDAITLDFD
23.23HPRD
Link-
272PhosphothreonineNVKITDSEA
27.96HPRD
Link-
289PhosphoserineAIAQSPEKE
26.46HPRD
Link-
289PhosphoserineAIAQSPEKE
26.46Phosphositeplus
Link-
289PhosphoserineAIAQSPEKE
26.46SysPTM
Link-
289PhosphoserineAIAQSPEKE
26.46SysPTM
Link-
289Phosphoserine.AIAQSPEKE
26.46UniProtKB
Link-
294PhosphoserinePEKESKDYE
41.73HPRD
Link-
297PhosphotyrosineESKDYEMNA
22.33HPRD
Link-
343PhosphoserineKKGPSSTGA
49.56Phosphositeplus
Link-
344PhosphoserineKGPSSTGAS
33.71Phosphositeplus
Link-
401N6-acetyllysineAADLKNLFG
52.75HPRD
Link-
401N6-acetyllysineAADLKNLFG
52.75Phosphositeplus
Link-
401N6-acetyllysine.AADLKNLFG
52.75UniProtKB
Link-
406N6-acetyllysineNLFGKYGKV
43.42HPRD
Link-
406N6-acetyllysineNLFGKYGKV
43.42Phosphositeplus
Link-
406N6-acetyllysine.NLFGKYGKV
43.42UniProtKB
Link-
417PhosphothreonineAKVVTNARS
26.58HPRD
Link-
421PhosphoserineTNARSPGAK
25.85HPRD
Link-
421PhosphoserineTNARSPGAK
25.85Phosphositeplus
Link-
421Phosphoserine.TNARSPGAK
25.85UniProtKB
Link-
433PhosphoserineIVTMSSSTE
16.27HPRD
Link-
436PhosphothreonineMSSSTEVSR
42.21HPRD
Link-
436PhosphothreonineMSSSTEVSR
42.21Phosphositeplus
Link-
477PhosphoserineNDEKSSSRS
31.34Phosphositeplus
Link-
482PhosphoserineSSRSSGDKK
50.31Phosphositeplus
Link-
515PhosphoserineEKKESKDTK
44.72HPRD
Link-
515PhosphoserineEKKESKDTK
44.72Phosphositeplus
Link-
533PhosphoserineDNGASGQTS
32.60HPRD
Link-
539PhosphoserineQTSESIKKS
39.20Phosphositeplus
Link-
543PhosphoserineSIKKSEEKK
46.08HPRD
Link-
543PhosphoserineSIKKSEEKK
46.08Phosphositeplus
Link-
550PhosphoserineKKRISSKSP
35.43HPRD
Link-
550PhosphoserineKKRISSKSP
35.43Phosphositeplus
Link-
550Phosphoserine.KKRISSKSP
35.43UniProtKB
Link-
551PhosphoserineKRISSKSPG
34.48HPRD
Link-
551PhosphoserineKRISSKSPG
34.48Phosphositeplus
Link-
551Phosphoserine.KRISSKSPG
34.48UniProtKB
Link-
553PhosphoserineISSKSPGHM
37.75HPRD
Link-
553PhosphoserineISSKSPGHM
37.75Phosphositeplus
Link-
553Phosphoserine.ISSKSPGHM
37.75UniProtKB
Link-
583PhosphoserineIHGRSKEKE
50.16HPRD
Link-
583PhosphoserineIHGRSKEKE
50.16Phosphositeplus
Link-
590PhosphoserineKERASLDKK
43.24HPRD
Link-
590PhosphoserineKERASLDKK
43.24Phosphositeplus
Link-
590Phosphoserine.KERASLDKK
43.24UniProtKB
Link-
748PhosphoserineNKKLSLDTD
32.83HPRD
Link-
748PhosphoserineNKKLSLDTD
32.83Phosphositeplus
Link-
748Phosphoserine.NKKLSLDTD
32.83UniProtKB
Link-
751PhosphothreonineLSLDTDARF
36.53HPRD
Link-
751PhosphothreonineLSLDTDARF
36.53Phosphositeplus
Link-
782PhosphoserineRFPESSAVQ
24.68HPRD
Link-
800PhosphoserineFVGQSEGKK
42.25HPRD
Link-
800PhosphoserineFVGQSEGKK
42.25Phosphositeplus
Link-
815PhosphoserineREDPSFERY
52.65HPRD
Link-
909PhosphoserineGREVSGHSV
26.49HPRD
Link-
909PhosphoserineGREVSGHSV
26.49Phosphositeplus
Link-
944PhosphoserineRGGGSQHYP
19.63Phosphositeplus
Link-
995PhosphothreonineAGMITQHSS
16.01HPRD
Link-
995PhosphothreonineAGMITQHSS
16.01Phosphositeplus
Link-
998PhosphoserineITQHSSNAS
18.57HPRD
Link-
1002PhosphoserineSSNASPINR
30.48HPRD
Link-
1002PhosphoserineSSNASPINR
30.48Phosphositeplus
Link-
1002Phosphoserine.SSNASPINR
30.48UniProtKB
Link-
1014PhosphoserineISGNSMPRG
33.42HPRD
Link-
1014PhosphoserineISGNSMPRG
33.42Phosphositeplus
Link-
1014Phosphoserine.ISGNSMPRG
33.42UniProtKB
Link-
1019PhosphoserineMPRGSGSGF
30.94HPRD
Link-
1019PhosphoserineMPRGSGSGF
30.94Phosphositeplus
Link-
1021PhosphoserineRGSGSGFKP
42.63HPRD
Link-
1021PhosphoserineRGSGSGFKP
42.63Phosphositeplus
Link-
1024N6-acetyllysineGSGFKPFKG
53.74HPRD
Link-
1024N6-acetyllysineGSGFKPFKG
53.74Phosphositeplus
Link-
1024N6-acetyllysine.GSGFKPFKG
53.74UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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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-289, 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-401; LYS-406 AND LYS-1024,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-289, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1002, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-289; SER-553 ANDSER-1002, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-550; SER-551;SER-553; SER-1002 AND SER-1014, AND MASS SPECTROMETRY.
"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-289, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-550; SER-553AND SER-748, AND MASS SPECTROMETRY.
"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-1002 AND SER-1014, 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 SER-93; SER-97; SER-289;SER-421; SER-551; SER-553; SER-590 AND SER-1002, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures