SMCA1_HUMAN - dbPTM
SMCA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMCA1_HUMAN
UniProt AC P28370
Protein Name Probable global transcription activator SNF2L1
Gene Name SMARCA1
Organism Homo sapiens (Human).
Sequence Length 1054
Subcellular Localization Nucleus.
Protein Description Energy-transducing component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes. Both complexes facilitate the perturbation of chromatin structure in an ATP-dependent manner. Potentiates neurite outgrowth. May be involved in brain development by regulating En-1 and En-2 expression. May be involved in the development of luteal cells..
Protein Sequence MEQDTAAVAATVAAADATATIVVIEDEQPGPSTSQEEGAAAAATEATAATEKGEKKKEKNVSSFQLKLAAKAPKSEKEMDPEYEEKMKADRAKRFEFLLKQTELFAHFIQPSAQKSPTSPLNMKLGRPRIKKDEKQSLISAGDYRHRRTEQEEDEELLSESRKTSNVCIRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIVSNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREDKFLEVEFLGQREAIEAFNAPNSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQSNKLAKEEMLQMIRHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRNFRMDIEQSLYKFEGEDYREKQKLGMVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRNPDIPNPALAQREEQKKIDGAEPLTPEETEEKEKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNYTEEEDRFLICMLHKMGFDRENVYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERERAEKKKRATKTPMVKFSAFS
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
62PhosphorylationKKKEKNVSSFQLKLA
HHHCCCCCHHHHHHH		34.5221712546
63PhosphorylationKKEKNVSSFQLKLAA
HHCCCCCHHHHHHHH		16.8427134283
71AcetylationFQLKLAAKAPKSEKE
HHHHHHHHCCCCCCC		60.6625953088
83PhosphorylationEKEMDPEYEEKMKAD
CCCCCHHHHHHHHHH		34.47-
102PhosphorylationFEFLLKQTELFAHFI
HHHHHHHHHHHHHHH		32.8223403867
112PhosphorylationFAHFIQPSAQKSPTS
HHHHHCCCCCCCCCC		27.2722617229
112 (in isoform 2)Phosphorylation-27.27-
116 (in isoform 2)Phosphorylation-22.72-
116PhosphorylationIQPSAQKSPTSPLNM
HCCCCCCCCCCCCCC		22.7225159151
118 (in isoform 2)Phosphorylation-50.49-
118PhosphorylationPSAQKSPTSPLNMKL
CCCCCCCCCCCCCCC		50.4930266825
119 (in isoform 2)Phosphorylation-30.67-
119PhosphorylationSAQKSPTSPLNMKLG
CCCCCCCCCCCCCCC		30.6725159151
137PhosphorylationIKKDEKQSLISAGDY
CCHHHHHCCHHHHCC		38.4421406692
140PhosphorylationDEKQSLISAGDYRHR
HHHHCCHHHHCCCCC		31.3421406692
144PhosphorylationSLISAGDYRHRRTEQ
CCHHHHCCCCCCCCH		13.8521406692
149PhosphorylationGDYRHRRTEQEEDEE
HCCCCCCCCHHHHHH		41.8128555341
159PhosphorylationEEDEELLSESRKTSN
HHHHHHHHHHHCCCC		46.26-
161PhosphorylationDEELLSESRKTSNVC
HHHHHHHHHCCCCEE		35.38-
164PhosphorylationLLSESRKTSNVCIRF
HHHHHHCCCCEEEEE		25.1527282143
165PhosphorylationLSESRKTSNVCIRFE
HHHHHCCCCEEEEEE		30.2424076635
174PhosphorylationVCIRFEVSPSYVKGG
EEEEEEECHHHHCCC		10.8424076635
179 (in isoform 2)Ubiquitination-50.3321890473
179 (in isoform 1)Ubiquitination-50.3321890473
179UbiquitinationEVSPSYVKGGPLRDY
EECHHHHCCCCCCCC		50.3321890473
257PhosphorylationEFKRWVPSLRVICFV
HHHHHCCCCEEEEEE		21.1324719451
322UbiquitinationRIKNEKSKLSEIVRE
HHHCCHHHHHHHHHH		68.08-
374PhosphorylationDFDSWFDTKNCLGDQ
CHHHHHCCCCCCCCH		18.06-
416PhosphorylationPKKEIKIYLGLSKMQ
CHHHEEEEECCHHHH		6.9620068231
416 (in isoform 2)Phosphorylation-6.96-
420PhosphorylationIKIYLGLSKMQREWY
EEEEECCHHHHHHHH		25.0420068231
421UbiquitinationKIYLGLSKMQREWYT
EEEECCHHHHHHHHH		44.06-
427PhosphorylationSKMQREWYTKILMKD
HHHHHHHHHHHHHHH		8.0622817900
429 (in isoform 2)Ubiquitination-20.3921890473
429UbiquitinationMQREWYTKILMKDID
HHHHHHHHHHHHHHH		20.3921890473
429 (in isoform 1)Ubiquitination-20.3921890473
440PhosphorylationKDIDVLNSSGKMDKM
HHHHHHCCCCCCCHH		35.9921406692
441PhosphorylationDIDVLNSSGKMDKMR
HHHHHCCCCCCCHHH		41.1621406692
443UbiquitinationDVLNSSGKMDKMRLL
HHHCCCCCCCHHHHH		45.96-
443AcetylationDVLNSSGKMDKMRLL
HHHCCCCCCCHHHHH		45.9625953088
503PhosphorylationAKLKEQGSRVLIFSQ
HHHHHCCCEEEEEHH		20.9322210691
509PhosphorylationGSRVLIFSQMTRLLD
CCEEEEEHHHHHHHH		16.4320068231
512PhosphorylationVLIFSQMTRLLDILE
EEEEHHHHHHHHHHH		15.5520068231
565PhosphorylationEAFNAPNSSKFIFML
HHHCCCCCCCEEEEE		33.5721406692
566PhosphorylationAFNAPNSSKFIFMLS
HHCCCCCCCEEEEEE		37.9221406692
573PhosphorylationSKFIFMLSTRAGGLG
CCEEEEEECCCCCCC		12.2224719451
639UbiquitinationIVERAEIKLRLDSIV
HHHHHHHHHHHHHHE		21.04-
644PhosphorylationEIKLRLDSIVIQQGR
HHHHHHHHHEEECCC		24.2824719451
650 (in isoform 2)Ubiquitination-15.2421890473
657PhosphorylationGRLIDQQSNKLAKEE
CCCCHHHCCHHHHHH		30.2424719451
659UbiquitinationLIDQQSNKLAKEEML
CCHHHCCHHHHHHHH		55.88-
662 (in isoform 1)Ubiquitination-65.7221890473
662UbiquitinationQQSNKLAKEEMLQMI
HHCCHHHHHHHHHHH		65.7221890473
662SumoylationQQSNKLAKEEMLQMI
HHCCHHHHHHHHHHH		65.7228112733
680UbiquitinationATHVFASKESELTDE
CCEEEECCCCCCCHH		62.93-
685PhosphorylationASKESELTDEDITTI
ECCCCCCCHHHHHHH		33.04-
701 (in isoform 2)Phosphorylation-23.95-
713 (in isoform 2)Phosphorylation-29.01-
713PhosphorylationRLQKMGESSLRNFRM
HHHHHHHHHHHHHCH		29.0118691976
714PhosphorylationLQKMGESSLRNFRMD
HHHHHHHHHHHHCHH		27.3521815630
725PhosphorylationFRMDIEQSLYKFEGE
HCHHHHHHHHHHCCC		22.3717192257
727PhosphorylationMDIEQSLYKFEGEDY
HHHHHHHHHHCCCCH		20.9129759185
728SumoylationDIEQSLYKFEGEDYR
HHHHHHHHHCCCCHH		42.0828112733
739AcetylationEDYREKQKLGMVEWI
CCHHHHHHCCCEEEC		59.0625953088
739UbiquitinationEDYREKQKLGMVEWI
CCHHHHHHCCCEEEC		59.06-
750SumoylationVEWIEPPKRERKANY
EEECCCCCCHHHHHH		77.0728112733
754UbiquitinationEPPKRERKANYAVDA
CCCCCHHHHHHHHHH		35.91-
754SumoylationEPPKRERKANYAVDA
CCCCCHHHHHHHHHH		35.91-
754SumoylationEPPKRERKANYAVDA
CCCCCHHHHHHHHHH		35.91-
757PhosphorylationKRERKANYAVDAYFR
CCHHHHHHHHHHHHH		16.9228152594
758 (in isoform 2)Phosphorylation-7.79-
762PhosphorylationANYAVDAYFREALRV
HHHHHHHHHHHHHHC		9.9421406692
770PhosphorylationFREALRVSEPKIPKA
HHHHHHCCCCCCCCC		41.5725159151
814UbiquitinationYRKTIGYKVPRNPDI
HHHCCCCCCCCCCCC		40.32-
839 (in isoform 2)Ubiquitination-46.5021890473
851UbiquitinationEETEEKEKLLTQGFT
HHHHHHHHHHHCCCC		60.9221890473
851AcetylationEETEEKEKLLTQGFT
HHHHHHHHHHHCCCC		60.9230592455
851 (in isoform 1)Ubiquitination-60.9221890473
870UbiquitinationRDFNQFIKANEKYGR
HHHHHHHHHCHHHCC		46.58-
874UbiquitinationQFIKANEKYGRDDID
HHHHHCHHHCCCCHH		53.46-
932 (in isoform 2)Ubiquitination-5.0221890473
943PhosphorylationLDAKIARYKAPFHQL
HHHHHHHHCCCHHHH		11.5028152594
944 (in isoform 1)Ubiquitination-43.9921890473
944UbiquitinationDAKIARYKAPFHQLR
HHHHHHHCCCHHHHH		43.9921890473
944SumoylationDAKIARYKAPFHQLR
HHHHHHHCCCHHHHH		43.99-
944SumoylationDAKIARYKAPFHQLR
HHHHHHHCCCHHHHH		43.99-
954PhosphorylationFHQLRIQYGTSKGKN
HHHHHHCCCCCCCCC		21.7228112733
960UbiquitinationQYGTSKGKNYTEEED
CCCCCCCCCCCHHHH		50.98-
962PhosphorylationGTSKGKNYTEEEDRF
CCCCCCCCCHHHHHH		21.00-
985PhosphorylationGFDRENVYEELRQCV
CCCHHHHHHHHHHHH		18.4422817900
1009 (in isoform 2)Phosphorylation-8.39-
1018PhosphorylationEFQRRCNTLISLIEK
HHHHHHHHHHHHHHH		29.1520068231
1021PhosphorylationRRCNTLISLIEKENM
HHHHHHHHHHHHHCC		26.8020068231
1025UbiquitinationTLISLIEKENMEIEE
HHHHHHHHHCCCHHH		47.60-
1038AcetylationEERERAEKKKRATKT
HHHHHHHHHHHCCCC		63.7120167786
1039AcetylationERERAEKKKRATKTP
HHHHHHHHHHCCCCC		38.7120167786
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 SMCA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMCA1_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 SMCA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PARP1_HUMANPARP1physical
18922045
PRGR_HUMANPGRphysical
16740656
BPTF_HUMANBPTFphysical
14609955
RBBP7_HUMANRBBP7physical
14609955
RBBP4_HUMANRBBP4physical
14609955
SMCA5_HUMANSMARCA5physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SMRC1_HUMANSMARCC1physical
22939629
SMCA4_HUMANSMARCA4physical
22939629
TFPT_HUMANTFPTphysical
22939629
DPOE3_HUMANPOLE3physical
26344197
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMCA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; THR-118 ANDSER-119, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725, AND MASSSPECTROMETRY.
"Identification of the phosphotyrosine proteome from thrombinactivated platelets.";
Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,Fitzgerald D.J.;
Proteomics 2:642-648(2002).
Cited for: PHOSPHORYLATION AT TYR-954.

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