Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Scaffold attachment factor B2  

UniProtKB / Swiss-Prot ID :  SAFB2_HUMAN

Gene Name (Synonyms) : 
SAFB2, KIAA0138  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation. 

Protein Sequence MAETLPGSGDSGPGTASLGPGVAETGTRRLSELRVIDLRAELKKRNLDTGGNKSVLMERLKKAVKEEGQD...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHEEEEHHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHCCC...
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.---MAETLP
---CCCCCC
20.62UniProtKB
Link-
4Phosphothreonine-MAETLPGS
-CCCCCCCC
28.81HPRD
Link-
4Phosphothreonine-MAETLPGS
-CCCCCCCC
28.81Phosphositeplus
Link-
8PhosphoserineTLPGSGDSG
CCCCCCCCC
37.17HPRD
Link-
31PhosphoserineTRRLSELRV
HHHHHHEEE
32.54HPRD
Link-
31Phosphoserine.TRRLSELRV
HHHHHHEEE
32.54UniProtKB
Link-
54PhosphoserineGGNKSVLME
CCCHHHHHH
25.20HPRD
Link-
109PhosphoserineLEDDSRDGQ
CCCCCCCCH
44.59HPRD
Link-
109PhosphoserineLEDDSRDGQ
CCCCCCCCH
44.59PhosphoELM
Link-
109PhosphoserineLEDDSRDGQ
CCCCCCCCH
44.59Phosphositeplus
Link-
109PhosphoserineLEDDSRDGQ
CCCCCCCCH
44.59SysPTM
Link-
109Phosphoserine.LEDDSRDGQ
CCCCCCCCH
44.59UniProtKB
Link-
194PhosphoserineTLETSSLNF
HHHHCCCCC
24.37HPRD
Link-
194PhosphoserineTLETSSLNF
HHHHCCCCC
24.37Phosphositeplus
Link-
195PhosphoserineLETSSLNFK
HHHCCCCCE
34.45HPRD
Link-
195PhosphoserineLETSSLNFK
HHHCCCCCE
34.45PhosphoELM
Link-
195PhosphoserineLETSSLNFK
HHHCCCCCE
34.45Phosphositeplus
Link-
195Phosphoserine.LETSSLNFK
HHHCCCCCE
34.45UniProtKB
Link-
201PhosphothreonineNFKVTPDIE
CCEECHHHH
18.81HPRD
Link-
201PhosphothreonineNFKVTPDIE
CCEECHHHH
18.81Phosphositeplus
Link-
201Phosphothreonine.NFKVTPDIE
CCEECHHHH
18.81UniProtKB
Link-
207PhosphoserineDIEESLLEP
HHHCCCCCC
26.01HPRD
Link-
207PhosphoserineDIEESLLEP
HHHCCCCCC
26.01PhosphoELM
Link-
207PhosphoserineDIEESLLEP
HHHCCCCCC
26.01Phosphositeplus
Link-
207PhosphoserineDIEESLLEP
HHHCCCCCC
26.01SysPTM
Link-
207Phosphoserine.DIEESLLEP
HHHCCCCCC
26.01UniProtKB
Link-
226PhosphoserineETCKSEPVK
HHHHCHHHH
49.64HPRD
Link-
226PhosphoserineETCKSEPVK
HHHHCHHHH
49.64PhosphoELM
Link-
230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).SEPVKEESS
CHHHHHHHH
67.49UniProtKB
Link-
233PhosphoserineVKEESSELE
HHHHHHHHH
30.15HPRD
Link-
233PhosphoserineVKEESSELE
HHHHHHHHH
30.15PhosphoELM
Link-
234PhosphoserineKEESSELEQ
HHHHHHHHC
49.86HPRD
Link-
234PhosphoserineKEESSELEQ
HHHHHHHHC
49.86PhosphoELM
Link-
234PhosphoserineKEESSELEQ
HHHHHHHHC
49.86Phosphositeplus
Link-
244PhosphothreonineFAQDTSSVG
CCHHHHHHC
15.72HPRD
Link-
244PhosphothreonineFAQDTSSVG
CCHHHHHHC
15.72PhosphoELM
Link-
245PhosphoserineAQDTSSVGP
CHHHHHHCC
31.17HPRD
Link-
245PhosphoserineAQDTSSVGP
CHHHHHHCC
31.17PhosphoELM
Link-
245PhosphoserineAQDTSSVGP
CHHHHHHCC
31.17Phosphositeplus
Link-
246PhosphoserineQDTSSVGPD
HHHHHHCCC
32.93HPRD
Link-
246PhosphoserineQDTSSVGPD
HHHHHHCCC
32.93PhosphoELM
Link-
246PhosphoserineQDTSSVGPD
HHHHHHCCC
32.93Phosphositeplus
Link-
261Caspase cleavage aspartic acidEDLFDSAHP
CCCCCCCCH
52.81Phosphositeplus
Link-
287PhosphoserineSKADSLLAV
CCCCCHHHH
30.09HPRD
Link-
287PhosphoserineSKADSLLAV
CCCCCHHHH
30.09PhosphoELM
Link-
287PhosphoserineSKADSLLAV
CCCCCHHHH
30.09SysPTM
Link-
287Phosphoserine.SKADSLLAV
CCCCCHHHH
30.09UniProtKB
Link-
293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).LAVVKREPA
HHHHHHCCC
44.43UniProtKB
Link-
293N6-acetyllysineLAVVKREPA
HHHHHHCCC
44.43HPRD
Link-
293N6-acetyllysineLAVVKREPA
HHHHHHCCC
44.43Phosphositeplus
Link-
293N6-acetyllysine.LAVVKREPA
HHHHHHCCC
44.43UniProtKB
Link-
330PhosphoserineLAEASSEEL
CCCCCCCCC
29.77HPRD
Link-
330PhosphoserineLAEASSEEL
CCCCCCCCC
29.77PhosphoELM
Link-
331PhosphoserineAEASSEELA
CCCCCCCCC
41.98HPRD
Link-
331PhosphoserineAEASSEELA
CCCCCCCCC
41.98PhosphoELM
Link-
339PhosphothreonineAEAPTEAPS
CCCCCCCCC
52.40Phosphositeplus
Link-
343PhosphoserineTEAPSPEAR
CCCCCCCCC
42.28HPRD
Link-
343PhosphoserineTEAPSPEAR
CCCCCCCCC
42.28PhosphoELM
Link-
343PhosphoserineTEAPSPEAR
CCCCCCCCC
42.28Phosphositeplus
Link-
343PhosphoserineTEAPSPEAR
CCCCCCCCC
42.28SysPTM
Link-
343Phosphoserine.TEAPSPEAR
CCCCCCCCC
42.28UniProtKB
Link-
349PhosphoserineEARDSKEDG
CCCCCCCCC
32.18HPRD
Link-
349PhosphoserineEARDSKEDG
CCCCCCCCC
32.18PhosphoELM
Link-
349PhosphoserineEARDSKEDG
CCCCCCCCC
32.18Phosphositeplus
Link-
391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)EKDIKPIIK
CCCCCCCCC
40.05Phosphositeplus
Link-
424N6-acetyllysineATDLKNLFS
HHHHHHHHH
55.18HPRD
Link-
424N6-acetyllysine.ATDLKNLFS
HHHHHHHHH
55.18UniProtKB
Link-
429N6-acetyllysineNLFSKYGKV
HHHHHCCCE
51.17HPRD
Link-
429N6-acetyllysine.NLFSKYGKV
HHHHHCCCE
51.17UniProtKB
Link-
444PhosphoserineTNARSPGAR
EECCCCCCC
25.85HPRD
Link-
444PhosphoserineTNARSPGAR
EECCCCCCC
25.85Phosphositeplus
Link-
506PhosphoserineKEKLSSVDR
HCCCCCCCC
39.11HPRD
Link-
513PhosphoserineDRHHSVEIK
CCCCCCCCH
18.47HPRD
Link-
513PhosphoserineDRHHSVEIK
CCCCCCCCH
18.47PhosphoELM
Link-
513PhosphoserineDRHHSVEIK
CCCCCCCCH
18.47Phosphositeplus
Link-
513PhosphoserineDRHHSVEIK
CCCCCCCCH
18.47SysPTM
Link-
513Phosphoserine.DRHHSVEIK
CCCCCCCCH
18.47UniProtKB
Link-
517Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)SVEIKIEKT
CCCCHHHHH
31.16Phosphositeplus
Link-
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)KTVIKKEEK
HHHHHHHHH
50.20Phosphositeplus
Link-
613PhosphoserineRDILSFDKI
HCCCCHHHH
31.56HPRD
Link-
613PhosphoserineRDILSFDKI
HCCCCHHHH
31.56PhosphoELM
Link-
613PhosphoserineRDILSFDKI
HCCCCHHHH
31.56Phosphositeplus
Link-
613PhosphoserineRDILSFDKI
HCCCCHHHH
31.56SysPTM
Link-
613Phosphoserine.RDILSFDKI
HCCCCHHHH
31.56UniProtKB
Link-
616N6-acetyllysineLSFDKIKEQ
CCHHHHHHH
54.38HPRD
Link-
616N6-acetyllysineLSFDKIKEQ
CCHHHHHHH
54.38Phosphositeplus
Link-
616N6-acetyllysine.LSFDKIKEQ
CCHHHHHHH
54.38UniProtKB
Link-
741PhosphotyrosineRDDAYWPEG
CCCCCCCCH
28.61Phosphositeplus
Link-
832PhosphoserineDKRLSEGRG
CCCCCCCCC
41.88HPRD
Link-
832PhosphoserineDKRLSEGRG
CCCCCCCCC
41.88PhosphoELM
Link-
832PhosphoserineDKRLSEGRG
CCCCCCCCC
41.88Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SCG1_HUMANphysical interactionMINT-64171MINT16169070
SCG1_HUMANphysical interactionEBI-735726
intact16169070
ESR1_HUMANin vitro
in vivo
HPRD:06424HPRD12660241
SAFB1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:06424HPRD12660241
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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-195 AND THR-201, 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-293; LYS-424; LYS-429 ANDLYS-616, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.
"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-207; SER-287; SER-343AND SER-613, 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-195 AND THR-201, 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-195 AND SER-207, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.
"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-109; SER-343 ANDSER-513, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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-207, AND MASSSPECTROMETRY.
"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-343, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"Co-repressor activity of scaffold attachment factor B1 requiressumoylation.";
Garee J.P., Meyer R., Oesterreich S.;
Biochem. Biophys. Res. Commun. 408:516-522(2011).
Cited for: SUMOYLATION AT LYS-230 AND LYS-293.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures