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 B1  

UniProtKB / Swiss-Prot ID :  SAFB1_HUMAN

Gene Name (Synonyms) : 
SAFB, HAP, HET, SAFB1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Can function as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity). Can inhibit cell proliferation. 

Protein Sequence MAETLSGLGDSGAAGAAALSSASSETGTRRLSDLRVIDLRAELRKRNVDSSGNKSVLMERLKKAIEDEGG...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHEEEEHHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHCC...
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.---MAETLS
---CCCCCC
20.62UniProtKB
Link-
4Phosphothreonine-MAETLSGL
-CCCCCCCC
19.38HPRD
Link-
4Phosphothreonine-MAETLSGL
-CCCCCCCC
19.38Phosphositeplus
Link-
6PhosphoserineAETLSGLGD
CCCCCCCCC
39.12HPRD
Link-
6PhosphoserineAETLSGLGD
CCCCCCCCC
39.12Phosphositeplus
Link-
11PhosphoserineGLGDSGAAG
CCCCCCCCC
28.65HPRD
Link-
11PhosphoserineGLGDSGAAG
CCCCCCCCC
28.65Phosphositeplus
Link-
20PhosphoserineAAALSSASS
CCCCCCCCC
21.09HPRD
Link-
20PhosphoserineAAALSSASS
CCCCCCCCC
21.09PhosphoELM
Link-
20PhosphoserineAAALSSASS
CCCCCCCCC
21.09Phosphositeplus
Link-
21PhosphoserineAALSSASSE
CCCCCCCCH
32.78HPRD
Link-
21PhosphoserineAALSSASSE
CCCCCCCCH
32.78PhosphoELM
Link-
23PhosphoserineLSSASSETG
CCCCCCHHH
30.56HPRD
Link-
23PhosphoserineLSSASSETG
CCCCCCHHH
30.56PhosphoELM
Link-
24PhosphoserineSSASSETGT
CCCCCHHHH
38.60HPRD
Link-
24PhosphoserineSSASSETGT
CCCCCHHHH
38.60Phosphositeplus
Link-
26PhosphothreonineASSETGTRR
CCCHHHHHH
45.89HPRD
Link-
26PhosphothreonineASSETGTRR
CCCHHHHHH
45.89Phosphositeplus
Link-
28PhosphothreonineSETGTRRLS
CHHHHHHHH
21.75HPRD
Link-
32PhosphoserineTRRLSDLRV
HHHHHHEEE
32.56HPRD
Link-
32PhosphoserineTRRLSDLRV
HHHHHHEEE
32.56PhosphoELM
Link-
32PhosphoserineTRRLSDLRV
HHHHHHEEE
32.56Phosphositeplus
Link-
55PhosphoserineSGNKSVLME
CCCHHHHHH
25.20HPRD
Link-
55PhosphoserineSGNKSVLME
CCCHHHHHH
25.20PhosphoELM
Link-
55PhosphoserineSGNKSVLME
CCCHHHHHH
25.20Phosphositeplus
Link-
55PhosphoserineSGNKSVLME
CCCHHHHHH
25.20SysPTM
Link-
55Phosphoserine.SGNKSVLME
CCCHHHHHH
25.20UniProtKB
Link-
83Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SEGNKKTSK
ECCCCCCCC
69.18Phosphositeplus
Link-
188PhosphothreonineEDKETINNL
CCCHHHCCC
34.44Phosphositeplus
Link-
194PhosphothreonineNNLDTSSSD
CCCCCCCCC
33.40HPRD
Link-
194PhosphothreonineNNLDTSSSD
CCCCCCCCC
33.40PhosphoELM
Link-
194Phosphothreonine.NNLDTSSSD
CCCCCCCCC
33.40UniProtKB
Link-
195PhosphoserineNLDTSSSDF
CCCCCCCCC
27.75HPRD
Link-
195PhosphoserineNLDTSSSDF
CCCCCCCCC
27.75Phosphositeplus
Link-
195PhosphoserineNLDTSSSDF
CCCCCCCCC
27.75SysPTM
Link-
196PhosphoserineLDTSSSDFT
CCCCCCCCE
35.70HPRD
Link-
196PhosphoserineLDTSSSDFT
CCCCCCCCE
35.70Phosphositeplus
Link-
196PhosphoserineLDTSSSDFT
CCCCCCCCE
35.70SysPTM
Link-
197PhosphoserineDTSSSDFTI
CCCCCCCEE
36.19HPRD
Link-
197PhosphoserineDTSSSDFTI
CCCCCCCEE
36.19PhosphoELM
Link-
197PhosphoserineDTSSSDFTI
CCCCCCCEE
36.19Phosphositeplus
Link-
197PhosphoserineDTSSSDFTI
CCCCCCCEE
36.19SysPTM
Link-
200PhosphothreonineSSDFTILQE
CCCCEECHH
26.26HPRD
Link-
200PhosphothreonineSSDFTILQE
CCCCEECHH
26.26PhosphoELM
Link-
200PhosphothreonineSSDFTILQE
CCCCEECHH
26.26Phosphositeplus
Link-
200PhosphothreonineSSDFTILQE
CCCCEECHH
26.26SysPTM
Link-
231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)SEPVKEESS
CHHHHHHHH
67.49Phosphositeplus
Link-
231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).SEPVKEESS
CHHHHHHHH
67.49UniProtKB
Link-
234PhosphoserineVKEESSELE
HHHHHHHHC
30.15HPRD
Link-
234PhosphoserineVKEESSELE
HHHHHHHHC
30.15PhosphoELM
Link-
235PhosphoserineKEESSELEQ
HHHHHHHCC
49.86HPRD
Link-
235PhosphoserineKEESSELEQ
HHHHHHHCC
49.86Phosphositeplus
Link-
235Phosphoserine.KEESSELEQ
HHHHHHHCC
49.86UniProtKB
Link-
245PhosphothreonineFAQDTSSVG
CCCCCCCCC
15.72HPRD
Link-
246PhosphoserineAQDTSSVGP
CCCCCCCCC
31.17HPRD
Link-
246PhosphoserineAQDTSSVGP
CCCCCCCCC
31.17Phosphositeplus
Link-
247PhosphoserineQDTSSVGPD
CCCCCCCCH
32.93HPRD
Link-
247PhosphoserineQDTSSVGPD
CCCCCCCCH
32.93Phosphositeplus
Link-
247Phosphoserine.QDTSSVGPD
CCCCCCCCH
32.93UniProtKB
Link-
288PhosphoserineSKADSLLAV
CCCHHHHHH
30.09HPRD
Link-
288PhosphoserineSKADSLLAV
CCCHHHHHH
30.09PhosphoELM
Link-
288PhosphoserineSKADSLLAV
CCCHHHHHH
30.09Phosphositeplus
Link-
288PhosphoserineSKADSLLAV
CCCHHHHHH
30.09SysPTM
Link-
288Phosphoserine.SKADSLLAV
CCCHHHHHH
30.09UniProtKB
Link-
294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)LAVVKREPA
HHHHHHCCC
44.43Phosphositeplus
Link-
294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).LAVVKREPA
HHHHHHCCC
44.43UniProtKB
Link-
294N6-acetyllysineLAVVKREPA
HHHHHHCCC
44.43Phosphositeplus
Link-
331PhosphoserineLAEASSEEL
CCCCCCCCC
29.77HPRD
Link-
332PhosphoserineAEASSEELA
CCCCCCCCC
41.98HPRD
Link-
340PhosphothreonineAEAPTEAPS
CCCCCCCCC
52.40Phosphositeplus
Link-
344PhosphoserineTEAPSPEAR
CCCCCCCCC
42.28HPRD
Link-
344PhosphoserineTEAPSPEAR
CCCCCCCCC
42.28PhosphoELM
Link-
344PhosphoserineTEAPSPEAR
CCCCCCCCC
42.28Phosphositeplus
Link-
350PhosphoserineEARDSKEDG
CCCCCCCCC
32.18Phosphositeplus
Link-
373PhosphoserinePKESSTSEG
CCCCCCCCC
36.72HPRD
Link-
373PhosphoserinePKESSTSEG
CCCCCCCCC
36.72PhosphoELM
Link-
373PhosphoserinePKESSTSEG
CCCCCCCCC
36.72SysPTM
Link-
373Phosphoserine.PKESSTSEG
CCCCCCCCC
36.72UniProtKB
Link-
383PhosphoserineDQKMSSPED
CCCCCCCCC
50.18HPRD
Link-
383PhosphoserineDQKMSSPED
CCCCCCCCC
50.18PhosphoELM
Link-
383PhosphoserineDQKMSSPED
CCCCCCCCC
50.18Phosphositeplus
Link-
383PhosphoserineDQKMSSPED
CCCCCCCCC
50.18SysPTM
Link-
383Phosphoserine.DQKMSSPED
CCCCCCCCC
50.18UniProtKB
Link-
384PhosphoserineQKMSSPEDD
CCCCCCCCC
28.89HPRD
Link-
384PhosphoserineQKMSSPEDD
CCCCCCCCC
28.89PhosphoELM
Link-
384PhosphoserineQKMSSPEDD
CCCCCCCCC
28.89Phosphositeplus
Link-
384PhosphoserineQKMSSPEDD
CCCCCCCCC
28.89SysPTM
Link-
384Phosphoserine.QKMSSPEDD
CCCCCCCCC
28.89UniProtKB
Link-
389PhosphoserinePEDDSDTKR
CCCCCCCCC
60.55HPRD
Link-
389PhosphoserinePEDDSDTKR
CCCCCCCCC
60.55Phosphositeplus
Link-
395PhosphoserineTKRLSKEEK
CCCCCCCCC
41.89HPRD
Link-
395PhosphoserineTKRLSKEEK
CCCCCCCCC
41.89Phosphositeplus
Link-
415PhosphoserineSGLSSTTRA
ECCCCCCCH
38.55HPRD
Link-
415PhosphoserineSGLSSTTRA
ECCCCCCCH
38.55Phosphositeplus
Link-
416PhosphothreonineGLSSTTRAT
CCCCCCCHH
19.54HPRD
Link-
416PhosphothreonineGLSSTTRAT
CCCCCCCHH
19.54PhosphoELM
Link-
416PhosphothreonineGLSSTTRAT
CCCCCCCHH
19.54Phosphositeplus
Link-
443PhosphoserineTNARSPGAR
ECCCCCCCC
25.85Phosphositeplus
Link-
475N6-acetyllysineELHGKMISV
EECCEEEEE
23.47HPRD
Link-
475N6-acetyllysineELHGKMISV
EECCEEEEE
23.47Phosphositeplus
Link-
475N6-acetyllysine.ELHGKMISV
EECCEEEEE
23.47UniProtKB
Link-
504PhosphoserineKKEKSSNSD
HHHHCCCCC
35.52HPRD
Link-
504PhosphoserineKKEKSSNSD
HHHHCCCCC
35.52Phosphositeplus
Link-
507PhosphoserineKSSNSDRST
HCCCCCCCC
36.03HPRD
Link-
507PhosphoserineKSSNSDRST
HCCCCCCCC
36.03Phosphositeplus
Link-
555PhosphoserineRATKSGSRG
CCCCCCCCC
37.33HPRD
Link-
555PhosphoserineRATKSGSRG
CCCCCCCCC
37.33PhosphoELM
Link-
555PhosphoserineRATKSGSRG
CCCCCCCCC
37.33Phosphositeplus
Link-
555Phosphoserine.RATKSGSRG
CCCCCCCCC
37.33UniProtKB
Link-
557PhosphoserineTKSGSRGTE
CCCCCCCCH
34.33HPRD
Link-
557PhosphoserineTKSGSRGTE
CCCCCCCCH
34.33PhosphoELM
Link-
557PhosphoserineTKSGSRGTE
CCCCCCCCH
34.33Phosphositeplus
Link-
557PhosphoserineTKSGSRGTE
CCCCCCCCH
34.33SysPTM
Link-
557Phosphoserine.TKSGSRGTE
CCCCCCCCH
34.33UniProtKB
Link-
560PhosphothreonineGSRGTERTV
CCCCCHHHH
22.60HPRD
Link-
560PhosphothreonineGSRGTERTV
CCCCCHHHH
22.60SysPTM
Link-
576PhosphoserineVPVISVKTS
CCEEECCCC
20.14HPRD
Link-
576PhosphoserineVPVISVKTS
CCEEECCCC
20.14Phosphositeplus
Link-
579PhosphothreonineISVKTSGSK
EECCCCCCC
35.84HPRD
Link-
579PhosphothreonineISVKTSGSK
EECCCCCCC
35.84Phosphositeplus
Link-
580PhosphoserineSVKTSGSKE
ECCCCCCCC
35.04HPRD
Link-
580PhosphoserineSVKTSGSKE
ECCCCCCCC
35.04Phosphositeplus
Link-
582PhosphoserineKTSGSKERA
CCCCCCCCC
30.98HPRD
Link-
582PhosphoserineKTSGSKERA
CCCCCCCCC
30.98Phosphositeplus
Link-
589PhosphoserineRASKSQDRK
CCCHHHHHH
34.51HPRD
Link-
589PhosphoserineRASKSQDRK
CCCHHHHHH
34.51PhosphoELM
Link-
589PhosphoserineRASKSQDRK
CCCHHHHHH
34.51SysPTM
Link-
589Phosphoserine.RASKSQDRK
CCCHHHHHH
34.51UniProtKB
Link-
601PhosphoserineREKRSVVSF
CCCCCCCCC
37.63HPRD
Link-
601PhosphoserineREKRSVVSF
CCCCCCCCC
37.63PhosphoELM
Link-
601PhosphoserineREKRSVVSF
CCCCCCCCC
37.63Phosphositeplus
Link-
601PhosphoserineREKRSVVSF
CCCCCCCCC
37.63SysPTM
Link-
601Phosphoserine.REKRSVVSF
CCCCCCCCC
37.63UniProtKB
Link-
604PhosphoserineRSVVSFDKV
CCCCCCCCC
26.10HPRD
Link-
604PhosphoserineRSVVSFDKV
CCCCCCCCC
26.10PhosphoELM
Link-
604PhosphoserineRSVVSFDKV
CCCCCCCCC
26.10Phosphositeplus
Link-
604PhosphoserineRSVVSFDKV
CCCCCCCCC
26.10SysPTM
Link-
604Phosphoserine.RSVVSFDKV
CCCCCCCCC
26.10UniProtKB
Link-
607N6-acetyllysineVSFDKVKEP
CCCCCCCHH
53.87HPRD
Link-
607N6-acetyllysineVSFDKVKEP
CCCCCCCHH
53.87Phosphositeplus
Link-
607N6-acetyllysine.VSFDKVKEP
CCCCCCCHH
53.87UniProtKB
Link-
617PhosphoserineKSRDSESHS
HHCCCCCCC
39.63HPRD
Link-
617PhosphoserineKSRDSESHS
HHCCCCCCC
39.63SysPTM
Link-
619PhosphoserineRDSESHSRV
CCCCCCCCC
30.62HPRD
Link-
619PhosphoserineRDSESHSRV
CCCCCCCCC
30.62SysPTM
Link-
621PhosphoserineSESHSRVRE
CCCCCCCHH
41.57HPRD
Link-
621PhosphoserineSESHSRVRE
CCCCCCCHH
41.57PhosphoELM
Link-
621PhosphoserineSESHSRVRE
CCCCCCCHH
41.57SysPTM
Link-
723PhosphotyrosineRDDAYWPEA
CCCCCCCCH
28.61Phosphositeplus
Link-
808PhosphoserineDKRMSEGRG
CCCCCCCCC
40.72HPRD
Link-
808PhosphoserineDKRMSEGRG
CCCCCCCCC
40.72PhosphoELM
Link-
808PhosphoserineDKRMSEGRG
CCCCCCCCC
40.72Phosphositeplus
Link-
808Phosphoserine.DKRMSEGRG
CCCCCCCCC
40.72UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
BAT5_HUMANphysical interactionMINT-62607MINT14667819
BAT5_HUMANphysical interactionMINT-62705MINT14667819
CHD3_HUMANphysical interactionEBI-730735
intact16169070
CYC_HUMANin vivoHPRD:04205HPRD11784858
ESR1_HUMANin vitro
in vivo
HPRD:04205HPRD10707955
ROA1_HUMANin vitroHPRD:04205HPRD10212141
CHD3_HUMANyeast 2-hybridHPRD:04205HPRD16169070
HNRPD_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04205HPRD10933876
CHD1_HUMANin vitro
yeast 2-hybrid
HPRD:04205HPRD12890497
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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 THR-194; SER-288; SER-383 AND SER-384, AND MASSSPECTROMETRY.
"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-475 AND LYS-607, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-288; SER-601 ANDSER-604, 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-604, 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-555 AND SER-557, ANDMASS 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-55; SER-373; SER-383;SER-384; SER-601 AND SER-604, 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 THR-194; SER-288; SER-383 AND SER-384, 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-235; SER-247 ANDSER-288, AND MASS 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-384; SER-589; SER-604AND SER-808, AND MASS SPECTROMETRY.
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-231 AND LYS-294.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures