SAFB1_RAT - dbPTM
SAFB1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAFB1_RAT
UniProt AC O88453
Protein Name Scaffold attachment factor B1
Gene Name Safb
Organism Rattus norvegicus (Rat).
Sequence Length 931
Subcellular Localization Nucleus.
Protein Description 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. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity)..
Protein Sequence MAETLSGLGDSGAASAAAVSSAASETGTRRLSDLRVIDLRAELRKRNLTSSGNKSVLMERLKKAIEEEGGNPDEIEVISEGNKKMPKRPSKGKKPEDEGVEDNGLEENSGDGQEDVETSLENLQDMDMMDISVLDEADIDNGSVADCVEEEEEATLPEGLGLLRIGRLQSKGLPEQLQELAIDDKEAINNVDTSSSDFTILQEMEEASLEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEEEQEEEQEEEGDLALASSSKSESSSTRCQWSEADALLAVVKREPAEAPGGGTGMDREPVGLEEPVEQSSTAAQLPETTSQELVRAPTAAPSPEPRDSKDDVKKFAFDACNDVPAAPKESSASEGADQKMSSVEDDSDTKRLSREEKGRSSCGRNFWVSGLSSTTRATDLKNLFSRYGKVVGAKVVTNARSPGARCYGFVTMSTAEEATKCINHLHKTELHGKMISVEKAKSEPAGKRVPDRRDGDSKKEKTSTSDRSANLKREEKGDRKDDAKKTDDGSTEKSKDADDQKPGPSERSRTTKSGSRGTERTVVMDKSKGVPVISVKTSGSKERASKSQDRKSVSREKRSVVSFDKVKESRKSRDSESRRERERERSEREQRLQAQWEREERERLEIARERLAFHRHRLERERMERERLERERMHVEQERRREQERIHREREELRRQQELRYEQERRPAVRRPYEVDGRRDDAYWPEAKRAALDDRYHSDFSRQDRFHDFDHRDRGRYPNHSVDRREGSRSMMGDREGQHYPERHGGPERHGRDSRDGWGYGSNKRLSEGRGLPLLPRRDWGEHARRLEDDRAWQGTADGGMMERDQQRWQGGERSMSGHSGPGHMMNRGGMSGRGSFAPGGASRRHVIPRGGMQAGFGGTEPGQQTQ
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------MAETLSGLG
------CCCCCCCCC		20.62-
4Phosphorylation----MAETLSGLGDS
----CCCCCCCCCCC		19.3826022182
6Phosphorylation--MAETLSGLGDSGA
--CCCCCCCCCCCHH		39.1226022182
11PhosphorylationTLSGLGDSGAASAAA
CCCCCCCCHHHHHHH		28.6527097102
15PhosphorylationLGDSGAASAAAVSSA
CCCCHHHHHHHHHHH		20.2223984901
20PhosphorylationAASAAAVSSAASETG
HHHHHHHHHHHHHHC		14.9923984901
21PhosphorylationASAAAVSSAASETGT
HHHHHHHHHHHHHCC		22.6623984901
24PhosphorylationAAVSSAASETGTRRL
HHHHHHHHHHCCCCH		35.0927097102
26PhosphorylationVSSAASETGTRRLSD
HHHHHHHHCCCCHHH		41.1627097102
28PhosphorylationSAASETGTRRLSDLR
HHHHHHCCCCHHHCE		21.7527097102
32PhosphorylationETGTRRLSDLRVIDL
HHCCCCHHHCEEEEH		32.5622673903
55PhosphorylationLTSSGNKSVLMERLK
CCCCCCHHHHHHHHH		25.20-
79PhosphorylationPDEIEVISEGNKKMP
HHHEEEEECCCCCCC		44.6328432305
83AcetylationEVISEGNKKMPKRPS
EEEECCCCCCCCCCC		62.4025786129
193PhosphorylationEAINNVDTSSSDFTI
HHHHCCCCCCCCCHH		26.6527097102
194PhosphorylationAINNVDTSSSDFTIL
HHHCCCCCCCCCHHH		24.3127097102
195PhosphorylationINNVDTSSSDFTILQ
HHCCCCCCCCCHHHH		35.7027097102
196PhosphorylationNNVDTSSSDFTILQE
HCCCCCCCCCHHHHH		36.1927097102
199PhosphorylationDTSSSDFTILQEMEE
CCCCCCCHHHHHHHH		26.2627097102
208PhosphorylationLQEMEEASLEPENEK
HHHHHHHCCCCCCHH		36.2227097102
223PhosphorylationILDILGETCKSEPVK
HHHHHHHHHCCCCCC		24.3625575281
226PhosphorylationILGETCKSEPVKEEG
HHHHHHCCCCCCCCC		49.6427097102
234PhosphorylationEPVKEEGSELEQPFA
CCCCCCCCCCCCHHH		42.1423712012
244PhosphorylationEQPFAQATSSVGPDR
CCHHHHHHCCCCCCH		14.9527097102
245PhosphorylationQPFAQATSSVGPDRK
CHHHHHHCCCCCCHH		26.4927097102
246PhosphorylationPFAQATSSVGPDRKL
HHHHHHCCCCCCHHH		27.0927097102
262PhosphorylationEEEDLFESCGHPEEE
HHHHHHHHCCCCHHH		20.3328689409
352PhosphorylationTAAQLPETTSQELVR
CCCCCCCCCCHHHHH		29.7927097102
353PhosphorylationAAQLPETTSQELVRA
CCCCCCCCCHHHHHC		27.1027097102
354PhosphorylationAQLPETTSQELVRAP
CCCCCCCCHHHHHCC		29.1327097102
362PhosphorylationQELVRAPTAAPSPEP
HHHHHCCCCCCCCCC		34.1729779826
366PhosphorylationRAPTAAPSPEPRDSK
HCCCCCCCCCCCCCH		36.8523712012
372PhosphorylationPSPEPRDSKDDVKKF
CCCCCCCCHHHHHHH		38.9823984901
394PhosphorylationVPAAPKESSASEGAD
CCCCCCCCCCCCCCC		37.0125575281
395PhosphorylationPAAPKESSASEGADQ
CCCCCCCCCCCCCCH		36.5829779826
397PhosphorylationAPKESSASEGADQKM
CCCCCCCCCCCCHHH		38.2128689409
405PhosphorylationEGADQKMSSVEDDSD
CCCCHHHHCCCCCHH		37.9628432305
406PhosphorylationGADQKMSSVEDDSDT
CCCHHHHCCCCCHHH		26.4828432305
411PhosphorylationMSSVEDDSDTKRLSR
HHCCCCCHHHHCCCH		60.5528432305
413PhosphorylationSVEDDSDTKRLSREE
CCCCCHHHHCCCHHH		23.2428432305
433PhosphorylationCGRNFWVSGLSSTTR
CCCCCCCCCCCCCCC		25.3127097102
436PhosphorylationNFWVSGLSSTTRATD
CCCCCCCCCCCCHHH		29.2123984901
437PhosphorylationFWVSGLSSTTRATDL
CCCCCCCCCCCHHHH		38.5523984901
438PhosphorylationWVSGLSSTTRATDLK
CCCCCCCCCCHHHHH		19.5423984901
439PhosphorylationVSGLSSTTRATDLKN
CCCCCCCCCHHHHHH		21.9123984901
445AcetylationTTRATDLKNLFSRYG
CCCHHHHHHHHHHHC		55.1822902405
461PhosphorylationVVGAKVVTNARSPGA
EECCEEEECCCCCCC		26.5823984901
465PhosphorylationKVVTNARSPGARCYG
EEEECCCCCCCEEEE		25.8522668510
497AcetylationHKTELHGKMISVEKA
HHHCCCCEEEEHHHH		23.4722902405
577PhosphorylationERSRTTKSGSRGTER
CCCCCCCCCCCCCEE		39.6529779826
582PhosphorylationTKSGSRGTERTVVMD
CCCCCCCCEEEEEEE		22.6029779826
590AcetylationERTVVMDKSKGVPVI
EEEEEEECCCCCEEE		35.6530596085
602PhosphorylationPVISVKTSGSKERAS
EEEEEEECCCHHHHC		35.0428689409
604PhosphorylationISVKTSGSKERASKS
EEEEECCCHHHHCCC		30.9828689409
623PhosphorylationSVSREKRSVVSFDKV
HHCHHHHHHCCHHHH		37.6323712012
626PhosphorylationREKRSVVSFDKVKES
HHHHHHCCHHHHHHH		26.1023712012
629AcetylationRSVVSFDKVKESRKS
HHHCCHHHHHHHHHC		53.8722902405
831PhosphorylationYGSNKRLSEGRGLPL
CCCCCCCCCCCCCCC		41.8822673903
834MethylationNKRLSEGRGLPLLPR
CCCCCCCCCCCCCCC		39.15-
892Asymmetric dimethylarginineGPGHMMNRGGMSGRG
CCCCCCCCCCCCCCC		25.75-
892MethylationGPGHMMNRGGMSGRG
CCCCCCCCCCCCCCC		25.75-
898MethylationNRGGMSGRGSFAPGG
CCCCCCCCCCCCCCC		30.21-
898Asymmetric dimethylarginineNRGGMSGRGSFAPGG
CCCCCCCCCCCCCCC		30.21-
908MethylationFAPGGASRRHVIPRG
CCCCCCCCCCEECCC		31.99-
908Asymmetric dimethylarginineFAPGGASRRHVIPRG
CCCCCCCCCCEECCC		31.99-
914MethylationSRRHVIPRGGMQAGF
CCCCEECCCCCCCCC		43.08-
914Asymmetric dimethylarginineSRRHVIPRGGMQAGF
CCCCEECCCCCCCCC		43.08-
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

Oops, there are no upstream regulatory protein records of SAFB1_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAFB1_RAT !!
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 SAFB1_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KHDR3_RATKhdrbs3physical
11118435
SRSF9_HUMANSRSF9physical
9671816
TRA2B_HUMANTRA2Bphysical
9671816
SRSF1_HUMANSRSF1physical
9671816
U2AF1_HUMANU2AF1physical
9671816
SRSF6_HUMANSRSF6physical
9671816
CLK2_MOUSEClk2physical
9671816
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAFB1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASSSPECTROMETRY.

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