SRFB1_HUMAN - dbPTM
SRFB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRFB1_HUMAN
UniProt AC Q8NEF9
Protein Name Serum response factor-binding protein 1
Gene Name SRFBP1 {ECO:0000312|EMBL:AAH31222.1}
Organism Homo sapiens (Human).
Sequence Length 429
Subcellular Localization Cytoplasm, perinuclear region .
Protein Description May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity)..
Protein Sequence MAQPGTLNLNNEVVKMRKEVKRIRVLVIRKLVRSVGRLKSKKGTEDALLKNQRRAQRLLEEIHAMKELKPDIVTKSALGDDINFEKIFKKPDSTATERAIARLAVHPLLKKKIDVLKAAVQAFKEARQNVAEVESSKNASEDNHSENTLYSNDNGSNLQREATVISEQKVKETKILAKKPIHNSKEKIAKMEHGPKAVTIANSPSKPSEKDSVVSLESQKTPADPKLKTLSQTKKNKGSDSSLSGNSDGGEEFCEEEKEYFDDSTEERFYKQSSMSEDSDSGDDFFIGKVRRTRKKESSCHSSVKEQKPLEKVFLKEDTGETHGDTRNDKIKPSTETRKLESVFFHSLSGSKSSRRNFKEQAPKTRSLDFPQNEPQIKNQFNKKLSGRLENTKQQLQLPLHPSWEASRRRKEQQSNIAVFQGKKITFDD
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------MAQPGTLNL
------CCCCCCCCC		25.0322814378
6Phosphorylation--MAQPGTLNLNNEV
--CCCCCCCCCCHHH		21.1129978859
50UbiquitinationGTEDALLKNQRRAQR
CCHHHHHHHHHHHHH		52.4633845483
86UbiquitinationGDDINFEKIFKKPDS
CCCCCHHHHHCCCCC		49.6721890473
89UbiquitinationINFEKIFKKPDSTAT
CCHHHHHCCCCCCHH		67.8623000965
90UbiquitinationNFEKIFKKPDSTATE
CHHHHHCCCCCCHHH		43.2223000965
111AcetylationAVHPLLKKKIDVLKA
HHHHHHHHHHHHHHH		55.7330584007
112AcetylationVHPLLKKKIDVLKAA
HHHHHHHHHHHHHHH		42.4230584013
117AcetylationKKKIDVLKAAVQAFK
HHHHHHHHHHHHHHH		33.8630584019
122UbiquitinationVLKAAVQAFKEARQN
HHHHHHHHHHHHHHH		15.7521890473
124AcetylationKAAVQAFKEARQNVA
HHHHHHHHHHHHHHH		54.1826051181
125UbiquitinationAAVQAFKEARQNVAE
HHHHHHHHHHHHHHH		42.5023000965
126UbiquitinationAVQAFKEARQNVAEV
HHHHHHHHHHHHHHH		20.9623000965
140PhosphorylationVESSKNASEDNHSEN
HHCCCCCCCCCCCCC		55.6828450419
145PhosphorylationNASEDNHSENTLYSN
CCCCCCCCCCCEECC		38.5028450419
148PhosphorylationEDNHSENTLYSNDNG
CCCCCCCCEECCCCC		24.0328450419
150PhosphorylationNHSENTLYSNDNGSN
CCCCCCEECCCCCCC		11.9121406692
151PhosphorylationHSENTLYSNDNGSNL
CCCCCEECCCCCCCC		40.6021406692
163PhosphorylationSNLQREATVISEQKV
CCCEEEEEEEEHHHH		17.3920860994
166PhosphorylationQREATVISEQKVKET
EEEEEEEEHHHHHHH		29.6425159151
173PhosphorylationSEQKVKETKILAKKP
EHHHHHHHHHHCCCC		20.05-
178AcetylationKETKILAKKPIHNSK
HHHHHHCCCCCCCCH		56.4925953088
184PhosphorylationAKKPIHNSKEKIAKM
CCCCCCCCHHHHHCC		28.2028985074
190SumoylationNSKEKIAKMEHGPKA
CCHHHHHCCCCCCCE		48.5828112733
190SumoylationNSKEKIAKMEHGPKA
CCHHHHHCCCCCCCE		48.58-
199PhosphorylationEHGPKAVTIANSPSK
CCCCCEEEECCCCCC		21.1630266825
203PhosphorylationKAVTIANSPSKPSEK
CEEEECCCCCCCCCC		22.8729255136
205PhosphorylationVTIANSPSKPSEKDS
EEECCCCCCCCCCCC		57.9522167270
206AcetylationTIANSPSKPSEKDSV
EECCCCCCCCCCCCE		56.8226051181
208PhosphorylationANSPSKPSEKDSVVS
CCCCCCCCCCCCEEE		62.1030266825
212PhosphorylationSKPSEKDSVVSLESQ
CCCCCCCCEEECCCC		35.1723927012
215PhosphorylationSEKDSVVSLESQKTP
CCCCCEEECCCCCCC		25.0230266825
218PhosphorylationDSVVSLESQKTPADP
CCEEECCCCCCCCCH		42.1230266825
221PhosphorylationVSLESQKTPADPKLK
EECCCCCCCCCHHHH		18.9730266825
2262-HydroxyisobutyrylationQKTPADPKLKTLSQT
CCCCCCHHHHHHHHH		64.26-
229PhosphorylationPADPKLKTLSQTKKN
CCCHHHHHHHHHCCC		41.9228060719
231PhosphorylationDPKLKTLSQTKKNKG
CHHHHHHHHHCCCCC		40.8228060719
233PhosphorylationKLKTLSQTKKNKGSD
HHHHHHHHCCCCCCC		40.3828060719
239PhosphorylationQTKKNKGSDSSLSGN
HHCCCCCCCCCCCCC		35.6128450419
241PhosphorylationKKNKGSDSSLSGNSD
CCCCCCCCCCCCCCC		34.5728450419
242PhosphorylationKNKGSDSSLSGNSDG
CCCCCCCCCCCCCCC		31.3928450419
244PhosphorylationKGSDSSLSGNSDGGE
CCCCCCCCCCCCCHH		37.5730576142
247PhosphorylationDSSLSGNSDGGEEFC
CCCCCCCCCCHHHHH		40.9530576142
260PhosphorylationFCEEEKEYFDDSTEE
HHHHHHHHCCCCHHH		24.3123403867
264PhosphorylationEKEYFDDSTEERFYK
HHHHCCCCHHHHHHH		39.2929255136
265PhosphorylationKEYFDDSTEERFYKQ
HHHCCCCHHHHHHHH		49.1929255136
270PhosphorylationDSTEERFYKQSSMSE
CCHHHHHHHHHCCCC		17.8422115753
273PhosphorylationEERFYKQSSMSEDSD
HHHHHHHHCCCCCCC		24.6928102081
274PhosphorylationERFYKQSSMSEDSDS
HHHHHHHCCCCCCCC		24.6728102081
276PhosphorylationFYKQSSMSEDSDSGD
HHHHHCCCCCCCCCC		39.9528102081
279PhosphorylationQSSMSEDSDSGDDFF
HHCCCCCCCCCCCCC		29.6225159151
281PhosphorylationSMSEDSDSGDDFFIG
CCCCCCCCCCCCCHH		48.3421082442
293O-linked_GlycosylationFIGKVRRTRKKESSC
CHHHHHCCCCCCCCC		35.9530379171
298O-linked_GlycosylationRRTRKKESSCHSSVK
HCCCCCCCCCCCCCC		47.3330379171
302PhosphorylationKKESSCHSSVKEQKP
CCCCCCCCCCCCCCC		40.9525367160
303PhosphorylationKESSCHSSVKEQKPL
CCCCCCCCCCCCCCH		17.3425367160
316SumoylationPLEKVFLKEDTGETH
CHHHEEECCCCCCCC		41.9228112733
334PhosphorylationRNDKIKPSTETRKLE
CCCCCCCCHHHHHHH		33.6030631047
342PhosphorylationTETRKLESVFFHSLS
HHHHHHHHHHHHHCC		34.3623403867
347PhosphorylationLESVFFHSLSGSKSS
HHHHHHHHCCCCHHH		21.0525159151
349PhosphorylationSVFFHSLSGSKSSRR
HHHHHHCCCCHHHCC		43.9925159151
351PhosphorylationFFHSLSGSKSSRRNF
HHHHCCCCHHHCCCH		26.4525159151
352AcetylationFHSLSGSKSSRRNFK
HHHCCCCHHHCCCHH		56.8530584001
353PhosphorylationHSLSGSKSSRRNFKE
HHCCCCHHHCCCHHH		30.6728509920
354PhosphorylationSLSGSKSSRRNFKEQ
HCCCCHHHCCCHHHH		38.7128509920
365PhosphorylationFKEQAPKTRSLDFPQ
HHHHCCCCCCCCCCC		25.1623401153
367PhosphorylationEQAPKTRSLDFPQNE
HHCCCCCCCCCCCCC		37.2123401153
378UbiquitinationPQNEPQIKNQFNKKL
CCCCHHHHHHHHHHH		39.18-
386PhosphorylationNQFNKKLSGRLENTK
HHHHHHHHHHHCCHH		30.6528555341
407PhosphorylationLHPSWEASRRRKEQQ
CCCCHHHHHHHHHHH		18.1427080861
423UbiquitinationNIAVFQGKKITFDD-
CEEEECCCCCCCCC-		30.1633845483
423AcetylationNIAVFQGKKITFDD-
CEEEECCCCCCCCC-		30.1623954790
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 SRFB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRFB1_HUMAN !!
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 SRFB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX10_HUMANDDX10physical
26186194
FBXW5_HUMANFBXW5physical
26186194
FBXW5_HUMANFBXW5physical
28514442
DDX10_HUMANDDX10physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRFB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-273; SER-274; SER-276;SER-279 AND SER-281, 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-203; TYR-270; SER-273;SER-274; SER-276 AND SER-281, AND MASS SPECTROMETRY.

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