SMRCD_MOUSE - dbPTM
SMRCD_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMRCD_MOUSE
UniProt AC Q04692
Protein Name SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1
Gene Name Smarcad1
Organism Mus musculus (Mouse).
Sequence Length 1021
Subcellular Localization Nucleus . Chromosome. Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage (By similarity)..
Protein Description DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing (By similarity)..
Protein Sequence MNLFNLDRFRFEKRSKIEEAPEAAPQPSQARPSSPISLSAEEENAEGEGSRANTPDSDVTEKTEDSSVPEPPDNERKASLSCFQNQRAIQEYIDLSSDTEDVSPNCSSTVQEKKFSKDTVIIVSEPSEDEESHDLPSVTRRNDSSELEDLSELEDLKDAKLQTLKELFPQRSDSDLLKLIESTSTMDGAIAAALLMFGDAGGGPRKRKLSSSSEEDDVNDDQSVKQPRGDRGEESNESAEASSNWEKQESIVLKLQKEFPNFDKQELREVLKEHEWMYTEALESLKVFAEDQDVQCASQSEVTNGKEVARNQNYSKNATKIKMKQKISVKPQNGFNKKRKKNVFNPKKAVEDSEYDSGSDAGSSLDEDYSSCEEVMEDGYKGKILHFLQVSSIAELTLIPKCSQKKAQKITELRPFNNWEALFTKMSKINGLSEDLIWNCKTVIQERDVVIRLMNKCEDISNKLTKQVTMLTGNGGGWNREQPSLLNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLCYYGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTKPADEQSIYEKERIAHAKQIIKPFILRRVKEEVLKLLPPKKDRIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQYYTPEKLKEMSQLMLKEPTHCEANPDLIFEDMEVMTDFELHVLCKQYQHINSYQLDMDLILDSGKFRALGCILSELKQKGDRVVLFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLEQDMTTVDEADEGSMPADIATLLKTSMGL
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
1Acetylation-------MNLFNLDR
-------CCCCCHHH		42.81-
15PhosphorylationRFRFEKRSKIEEAPE
HHHHHCHHCCCCCCC		49.4025777480
28PhosphorylationPEAAPQPSQARPSSP
CCCCCCCCCCCCCCC		31.0925619855
33PhosphorylationQPSQARPSSPISLSA
CCCCCCCCCCCCCCC		43.1025619855
34PhosphorylationPSQARPSSPISLSAE
CCCCCCCCCCCCCCH		29.0027087446
37PhosphorylationARPSSPISLSAEEEN
CCCCCCCCCCCHHHC		21.4725619855
39PhosphorylationPSSPISLSAEEENAE
CCCCCCCCCHHHCCC		27.1825619855
50PhosphorylationENAEGEGSRANTPDS
HCCCCCCCCCCCCCC		24.7425619855
54PhosphorylationGEGSRANTPDSDVTE
CCCCCCCCCCCCCCC		27.7325521595
57PhosphorylationSRANTPDSDVTEKTE
CCCCCCCCCCCCCCC		34.8725521595
60PhosphorylationNTPDSDVTEKTEDSS
CCCCCCCCCCCCCCC		36.4328066266
63PhosphorylationDSDVTEKTEDSSVPE
CCCCCCCCCCCCCCC		38.5025293948
66PhosphorylationVTEKTEDSSVPEPPD
CCCCCCCCCCCCCCC		27.3125293948
67PhosphorylationTEKTEDSSVPEPPDN
CCCCCCCCCCCCCCC		54.7525293948
79PhosphorylationPDNERKASLSCFQNQ
CCCCCHHHHHHHHHH		24.6926824392
81PhosphorylationNERKASLSCFQNQRA
CCCHHHHHHHHHHHH		15.4725619855
92PhosphorylationNQRAIQEYIDLSSDT
HHHHHHHHHHCCCCC		5.3725619855
96PhosphorylationIQEYIDLSSDTEDVS
HHHHHHCCCCCCCCC		23.5521082442
97PhosphorylationQEYIDLSSDTEDVSP
HHHHHCCCCCCCCCC		56.7127087446
99PhosphorylationYIDLSSDTEDVSPNC
HHHCCCCCCCCCCCC		35.7127087446
103PhosphorylationSSDTEDVSPNCSSTV
CCCCCCCCCCCCCCC		23.7927087446
107PhosphorylationEDVSPNCSSTVQEKK
CCCCCCCCCCCCCCC		35.3725619855
108PhosphorylationDVSPNCSSTVQEKKF
CCCCCCCCCCCCCCC		34.4925619855
109PhosphorylationVSPNCSSTVQEKKFS
CCCCCCCCCCCCCCC		15.2025619855
116PhosphorylationTVQEKKFSKDTVIIV
CCCCCCCCCCEEEEE		38.2025367039
119PhosphorylationEKKFSKDTVIIVSEP
CCCCCCCEEEEEECC		19.8325619855
124PhosphorylationKDTVIIVSEPSEDEE
CCEEEEEECCCCCCC		33.1227087446
127PhosphorylationVIIVSEPSEDEESHD
EEEEECCCCCCCCCC		54.3427087446
132PhosphorylationEPSEDEESHDLPSVT
CCCCCCCCCCCCCCC		21.9127087446
137PhosphorylationEESHDLPSVTRRNDS
CCCCCCCCCCCCCCC		43.3421082442
139PhosphorylationSHDLPSVTRRNDSSE
CCCCCCCCCCCCCHH		28.4022802335
144PhosphorylationSVTRRNDSSELEDLS
CCCCCCCCHHCCCHH		29.3027087446
145PhosphorylationVTRRNDSSELEDLSE
CCCCCCCHHCCCHHH		49.4127087446
151PhosphorylationSSELEDLSELEDLKD
CHHCCCHHHHHHHHH		53.0826824392
172PhosphorylationKELFPQRSDSDLLKL
HHHCCCCCHHHHHHH		35.9025266776
174PhosphorylationLFPQRSDSDLLKLIE
HCCCCCHHHHHHHHH		31.2526643407
210PhosphorylationGPRKRKLSSSSEEDD
CCCCCCCCCCCCCCC		31.0727087446
211PhosphorylationPRKRKLSSSSEEDDV
CCCCCCCCCCCCCCC		48.6027087446
212PhosphorylationRKRKLSSSSEEDDVN
CCCCCCCCCCCCCCC		38.0927087446
213PhosphorylationKRKLSSSSEEDDVND
CCCCCCCCCCCCCCC		47.1327087446
235PhosphorylationRGDRGEESNESAEAS
CCCCCCCCCCCCCHH		41.4123429704
238PhosphorylationRGEESNESAEASSNW
CCCCCCCCCCHHCCH		35.3423429704
242PhosphorylationSNESAEASSNWEKQE
CCCCCCHHCCHHHHH		18.7321149613
243PhosphorylationNESAEASSNWEKQES
CCCCCHHCCHHHHHH		53.6721149613
298PhosphorylationDQDVQCASQSEVTNG
CCCCCCCCHHHCCCH		41.6930635358
300PhosphorylationDVQCASQSEVTNGKE
CCCCCCHHHCCCHHH		31.3830635358
303PhosphorylationCASQSEVTNGKEVAR
CCCHHHCCCHHHHHH		33.9130635358
403PhosphorylationLTLIPKCSQKKAQKI
HHCCCCCCHHHCHHH		51.6817203969
411PhosphorylationQKKAQKITELRPFNN
HHHCHHHHHCCCCCC		35.6820469934
641PhosphorylationIRYQHLMTINARNRL
EEEEEEEEECCCCCE		19.8928576409
746PhosphorylationSEKQEQLYSGLFNRL
CHHHHHHHHHHHHHH		10.6125777480
747PhosphorylationEKQEQLYSGLFNRLK
HHHHHHHHHHHHHHH		37.3025777480
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 SMRCD_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMRCD_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 SMRCD_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, 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-137; SER-144 ANDSER-145, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-132; SER-210;SER-211; SER-212 AND SER-213, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND MASSSPECTROMETRY.

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