SAFB2_MOUSE - dbPTM
SAFB2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAFB2_MOUSE
UniProt AC Q80YR5
Protein Name Scaffold attachment factor B2
Gene Name Safb2
Organism Mus musculus (Mouse).
Sequence Length 991
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation (By similarity)..
Protein Sequence MAEPGTGSGDPAFGPGASESGTRRLSDLRVIDLRAELKKRNLDTGGNKSVLMERLRKAFKEEGQEPEEVGISWGAVSKRAVKRNTKGSKMEEEGSEDNGLEEDSRYGQDGVVILQSSQDRDTMDTGVPDGMEAEDLSVPCLGKADTVNQILHAFDDSKEYVAAQLGQLPAQLLKHAVDEEVFKNTLEASVSDLKVTLADEEAPMEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEDQEEEQEEEGDLALASSSKSESPSTRCQWSEADAPLAVVKRELADAPGGGGGTRHRRKRKRRRKHQAQAEALGTGGGAGMNCEPVGLEEPVEQSSTAAQLPEATSQELVRAPTAALSPEPQDSKEDVKKFAFDACNDVPAPPKESSASEGADQKMSSVKEEQDIKPVIKDEKGRASCSSGRNLWVSGLSSSTRAADLKSLFSKHGKVIGAKVVTNARSPGARCYGFVTMSTSDEATKCISHLHRTELHGRMISVEKAKNEPSEKKSSDRRACDQKEKVPGPDRPHPVKIKTEKTVIKKEEKLERKEEKGPEDIKKEKDQDELTPGAAGHSRVTKSGSRGMERTVVMDKSKGEPVISVKATSRSKDRSSKSQDRKSEGREKRDILSFDKIKEQRERERQRQREREIRETERRREREQREREQRLDAFQERREKARLQRERMQLQCQRQRLERERLERERLERERMRVERERRKEQQRIMREREELRRQQEQLRAEQERRALRRPYDLDARRDDGYWPEGKRAALEDRYRDFPRPDHRFHDFDHRDRGHYQEHVIDRRDGSRTRVEERDGQYYPDDQHSHGRLLEHHAWDSGDGWHGYSSDKKLNEGQGLPPPPRVSREWAEHSSQLEEQQVPVWHSAVDTNMTGHEHIRWRGAERGLAGGPGHGHVAAGRGGMAGQGSFAHGGHSQGYIVPSGRLEGGGMASQDQGGRVPNPHPHPHFTRRY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAEPGTGSG
------CCCCCCCCC		31.52-
26PhosphorylationESGTRRLSDLRVIDL
CCCCCCHHHCEEEEH		32.5624704852
44PhosphorylationLKKRNLDTGGNKSVL
HHHCCCCCCCCHHHH		50.5918779572
48AcetylationNLDTGGNKSVLMERL
CCCCCCCHHHHHHHH		45.2622826441
49PhosphorylationLDTGGNKSVLMERLR
CCCCCCHHHHHHHHH		25.2025521595
77PhosphorylationGISWGAVSKRAVKRN
CCCHHHHHHHHHHHC		18.8518779572
88PhosphorylationVKRNTKGSKMEEEGS
HHHCCCCCCCCCCCC		30.3129514104
95PhosphorylationSKMEEEGSEDNGLEE
CCCCCCCCCCCCCCC		45.0925521595
104PhosphorylationDNGLEEDSRYGQDGV
CCCCCCCHHCCCCCE		30.59-
116PhosphorylationDGVVILQSSQDRDTM
CCEEEEECCCCCCCC		26.9029233185
117PhosphorylationGVVILQSSQDRDTMD
CEEEEECCCCCCCCC		24.1221743459
146PhosphorylationPCLGKADTVNQILHA
CCCCCCHHHHHHHHH		26.6427600695
157PhosphorylationILHAFDDSKEYVAAQ
HHHHHCCCHHHHHHH		29.2728285833
185PhosphorylationDEEVFKNTLEASVSD
CHHHHHHHHHHHHHH		26.9418779572
189PhosphorylationFKNTLEASVSDLKVT
HHHHHHHHHHHCEEE		16.8725266776
191PhosphorylationNTLEASVSDLKVTLA
HHHHHHHHHCEEEEC		34.4328066266
196PhosphorylationSVSDLKVTLADEEAP
HHHHCEEEECCCCCC		18.03-
218PhosphorylationILDILGETCKSEPVK
HHHHHHHHHCCCCCC		24.3630352176
221PhosphorylationILGETCKSEPVKEEG
HHHHHHCCCCCCCCC		49.6427087446
229PhosphorylationEPVKEEGSELEQPFA
CCCCCCCCCCCCHHH		42.1425521595
239PhosphorylationEQPFAQATSSVGPDR
CCHHHHHHCCCCCCH		14.9525521595
240PhosphorylationQPFAQATSSVGPDRK
CHHHHHHCCCCCCHH		26.4925159016
241PhosphorylationPFAQATSSVGPDRKL
HHHHHHCCCCCCHHH		27.0925521595
257PhosphorylationEEEDLFESCGHPEEE
HHHHHHHHCCCCHHH		20.3319060867
286PhosphorylationEGDLALASSSKSESP
HCHHHHHCCCCCCCC		35.6722668510
288PhosphorylationDLALASSSKSESPST
HHHHHCCCCCCCCCC		37.3922668510
290PhosphorylationALASSSKSESPSTRC
HHHCCCCCCCCCCCC		45.3024453211
292PhosphorylationASSSKSESPSTRCQW
HCCCCCCCCCCCCCC		31.1027818261
294PhosphorylationSSKSESPSTRCQWSE
CCCCCCCCCCCCCCC		37.4526745281
295PhosphorylationSKSESPSTRCQWSEA
CCCCCCCCCCCCCCC		38.5624453211
300PhosphorylationPSTRCQWSEADAPLA
CCCCCCCCCCCCCEE		9.3125521595
344PhosphorylationAQAEALGTGGGAGMN
HHHHHHCCCCCCCCC		33.2422705319
365PhosphorylationEEPVEQSSTAAQLPE
CCCCCCCCCCCCCCC		23.0422705319
374PhosphorylationAAQLPEATSQELVRA
CCCCCCCCCHHHHHC		29.3121149613
375PhosphorylationAQLPEATSQELVRAP
CCCCCCCCHHHHHCC		28.8017525332
383PhosphorylationQELVRAPTAALSPEP
HHHHHCCCHHCCCCC		24.4725521595
387PhosphorylationRAPTAALSPEPQDSK
HCCCHHCCCCCCCCH		23.6124925903
393PhosphorylationLSPEPQDSKEDVKKF
CCCCCCCCHHHHHHH		32.4724925903
399UbiquitinationDSKEDVKKFAFDACN
CCHHHHHHHHHHHHC		41.60-
399AcetylationDSKEDVKKFAFDACN
CCHHHHHHHHHHHHC		41.6023806337
413UbiquitinationNDVPAPPKESSASEG
CCCCCCCCCCCCCCC		69.99-
415PhosphorylationVPAPPKESSASEGAD
CCCCCCCCCCCCCCC		37.0122006019
416PhosphorylationPAPPKESSASEGADQ
CCCCCCCCCCCCCCH		36.5827087446
418PhosphorylationPPKESSASEGADQKM
CCCCCCCCCCCCHHH		38.2127087446
459PhosphorylationNLWVSGLSSSTRAAD
CEEEECCCCCCCHHH		26.2615851034
461PhosphorylationWVSGLSSSTRAADLK
EEECCCCCCCHHHHH		20.6618779572
462PhosphorylationVSGLSSSTRAADLKS
EECCCCCCCHHHHHH		26.6918779572
481MalonylationHGKVIGAKVVTNARS
CCCEEEEEEEECCCC		31.8326320211
484PhosphorylationVIGAKVVTNARSPGA
EEEEEEEECCCCCCC		26.5827087446
488PhosphorylationKVVTNARSPGARCYG
EEEECCCCCCCEEEE		25.8525521595
494PhosphorylationRSPGARCYGFVTMST
CCCCCEEEEEEEECC		14.1927149854
498PhosphorylationARCYGFVTMSTSDEA
CEEEEEEEECCCHHH		11.8027149854
500PhosphorylationCYGFVTMSTSDEATK
EEEEEEECCCHHHHH		18.5227149854
501PhosphorylationYGFVTMSTSDEATKC
EEEEEECCCHHHHHH		29.4027149854
502PhosphorylationGFVTMSTSDEATKCI
EEEEECCCHHHHHHH		26.5827149854
506PhosphorylationMSTSDEATKCISHLH
ECCCHHHHHHHHHHH		25.1327149854
526MalonylationGRMISVEKAKNEPSE
CCCCCHHHHCCCCCC		63.6126320211
593PhosphorylationEKDQDELTPGAAGHS
HHCCCCCCCCCCCCC		20.0325159016
605PhosphorylationGHSRVTKSGSRGMER
CCCCCCCCCCCCCEE		32.4123684622
607PhosphorylationSRVTKSGSRGMERTV
CCCCCCCCCCCEEEE		32.5223684622
613PhosphorylationGSRGMERTVVMDKSK
CCCCCEEEEEEECCC		12.2623375375
638PhosphorylationSRSKDRSSKSQDRKS
CCCCCCCCCCCCCHH		36.9018779572
640PhosphorylationSKDRSSKSQDRKSEG
CCCCCCCCCCCHHCC		38.9823375375
645PhosphorylationSKSQDRKSEGREKRD
CCCCCCHHCCHHHHH		46.2923684622
655PhosphorylationREKRDILSFDKIKEQ
HHHHHHHCHHHHHHH		31.5626824392
658AcetylationRDILSFDKIKEQRER
HHHHCHHHHHHHHHH		54.3823806337
829PhosphorylationVIDRRDGSRTRVEER
EEECCCCCCCEEEEC		34.4625266776
831PhosphorylationDRRDGSRTRVEERDG
ECCCCCCCEEEECCC		40.5425266776
847PhosphorylationYYPDDQHSHGRLLEH
CCCCCCCCCCCCCCE		23.2323684622
939MethylationHGHVAAGRGGMAGQG
CCCCCCCCCCCCCCC		33.4924129315
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
387SPhosphorylationKinaseMAPK1P63085
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAFB2_MOUSE !!
Disease-associated PTM Sites based on SAP

* 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 SAFB2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SAFB2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAFB2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASSSPECTROMETRY.

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