SMRD2_HUMAN - dbPTM
SMRD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMRD2_HUMAN
UniProt AC Q92925
Protein Name SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2
Gene Name SMARCD2
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization Nucleus .
Protein Description Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. [PubMed: 22952240]
Protein Sequence MSGRGAGGFPLPPLSPGGGAVAAALGAPPPPAGPGMLPGPALRGPGPAGGVGGPGAAAFRPMGPAGPAAQYQRPGMSPGNRMPMAGLQVGPPAGSPFGAAAPLRPGMPPTMMDPFRKRLLVPQAQPPMPAQRRGLKRRKMADKVLPQRIRELVPESQAYMDLLAFERKLDQTIARKRMEIQEAIKKPLTQKRKLRIYISNTFSPSKAEGDSAGTAGTPGGTPAGDKVASWELRVEGKLLDDPSKQKRKFSSFFKSLVIELDKELYGPDNHLVEWHRMPTTQETDGFQVKRPGDLNVKCTLLLMLDHQPPQYKLDPRLARLLGVHTQTRAAIMQALWLYIKHNQLQDGHEREYINCNRYFRQIFSCGRLRFSEIPMKLAGLLQHPDPIVINHVISVDPNDQKKTACYDIDVEVDDPLKAQMSNFLASTTNQQEIASLDVKIHETIESINQLKTQRDFMLSFSTDPQDFIQEWLRSQRRDLKIITDVIGNPEEERRAAFYHQPWAQEAVGRHIFAKVQQRRQELEQVLGIRLT
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
4Methylation----MSGRGAGGFPL
----CCCCCCCCCCC		25.20115387975
15PhosphorylationGFPLPPLSPGGGAVA
CCCCCCCCCCCCHHH		27.5426074081
50 (in isoform 2)Phosphorylation-19.6022210691
73DimethylationGPAAQYQRPGMSPGN
CCCHHCCCCCCCCCC		25.46-
73MethylationGPAAQYQRPGMSPGN
CCCHHCCCCCCCCCC		25.4658855407
81Asymmetric dimethylargininePGMSPGNRMPMAGLQ
CCCCCCCCCCCCCCE		36.17-
81MethylationPGMSPGNRMPMAGLQ
CCCCCCCCCCCCCCE		36.1724129315
81 (in isoform 2)Phosphorylation-36.1722210691
83 (in isoform 2)Phosphorylation-13.2622210691
95PhosphorylationQVGPPAGSPFGAAAP
EECCCCCCCCCCCCC		21.1126074081
104Asymmetric dimethylarginineFGAAAPLRPGMPPTM
CCCCCCCCCCCCCCC		25.35-
104MethylationFGAAAPLRPGMPPTM
CCCCCCCCCCCCCCC		25.3524129315
110PhosphorylationLRPGMPPTMMDPFRK
CCCCCCCCCCCHHHH		21.1824719451
116MethylationPTMMDPFRKRLLVPQ
CCCCCHHHHHCCCCC		28.6830688373
116DimethylationPTMMDPFRKRLLVPQ
CCCCCHHHHHCCCCC		28.68-
118MethylationMMDPFRKRLLVPQAQ
CCCHHHHHCCCCCCC		29.06115917221
131 (in isoform 1)Ubiquitination-29.7221890473
139UbiquitinationRRGLKRRKMADKVLP
HHCHHHHHHHHHHHH		42.34-
142PhosphorylationLKRRKMADKVLPQRI
HHHHHHHHHHHHHHH		37.7918669648
143UbiquitinationKRRKMADKVLPQRIR
HHHHHHHHHHHHHHH		35.81-
143AcetylationKRRKMADKVLPQRIR
HHHHHHHHHHHHHHH		35.8125953088
150 (in isoform 2)Ubiquitination-33.1321890473
151 (in isoform 1)Ubiquitination-52.3121890473
159PhosphorylationLVPESQAYMDLLAFE
HCCHHHHHHHHHHHH		5.41-
162 (in isoform 1)Ubiquitination-1.8021890473
168SumoylationDLLAFERKLDQTIAR
HHHHHHHHHHHHHHH		49.57-
168UbiquitinationDLLAFERKLDQTIAR
HHHHHHHHHHHHHHH		49.57-
168SumoylationDLLAFERKLDQTIAR
HHHHHHHHHHHHHHH		49.57-
169 (in isoform 1)Ubiquitination-8.0621890473
170 (in isoform 2)Ubiquitination-46.7621890473
181 (in isoform 2)Ubiquitination-22.2921890473
185 (in isoform 2)Ubiquitination-56.22-
185AcetylationMEIQEAIKKPLTQKR
HHHHHHHHCCCCCCC		56.2225953088
185UbiquitinationMEIQEAIKKPLTQKR
HHHHHHHHCCCCCCC		56.2219608861
186UbiquitinationEIQEAIKKPLTQKRK
HHHHHHHCCCCCCCC		38.86-
188 (in isoform 2)Ubiquitination-12.4521890473
197PhosphorylationQKRKLRIYISNTFSP
CCCCEEEEEECCCCC		7.5830278072
199PhosphorylationRKLRIYISNTFSPSK
CCEEEEEECCCCCCC		16.9130278072
201PhosphorylationLRIYISNTFSPSKAE
EEEEEECCCCCCCCC		20.7830278072
203PhosphorylationIYISNTFSPSKAEGD
EEEECCCCCCCCCCC		26.6530278072
205 (in isoform 2)Ubiquitination-43.21-
205PhosphorylationISNTFSPSKAEGDSA
EECCCCCCCCCCCCC		43.2130266825
206UbiquitinationSNTFSPSKAEGDSAG
ECCCCCCCCCCCCCC		54.57-
211PhosphorylationPSKAEGDSAGTAGTP
CCCCCCCCCCCCCCC		39.1830266825
214PhosphorylationAEGDSAGTAGTPGGT
CCCCCCCCCCCCCCC		22.9430266825
214UbiquitinationAEGDSAGTAGTPGGT
CCCCCCCCCCCCCCC		22.9421890473
217PhosphorylationDSAGTAGTPGGTPAG
CCCCCCCCCCCCCCC		19.1219664994
221PhosphorylationTAGTPGGTPAGDKVA
CCCCCCCCCCCCCEE		18.8430266825
226SumoylationGGTPAGDKVASWELR
CCCCCCCCEEEEEEE		38.4928112733
226UbiquitinationGGTPAGDKVASWELR
CCCCCCCCEEEEEEE		38.49-
229PhosphorylationPAGDKVASWELRVEG
CCCCCEEEEEEEEEC		24.8724719451
237UbiquitinationWELRVEGKLLDDPSK
EEEEEECEECCCHHH		32.16-
244UbiquitinationKLLDDPSKQKRKFSS
EECCCHHHHHHHHHH		66.29-
246UbiquitinationLDDPSKQKRKFSSFF
CCCHHHHHHHHHHHH		62.38-
248UbiquitinationDPSKQKRKFSSFFKS
CHHHHHHHHHHHHHH		57.54-
262UbiquitinationSLVIELDKELYGPDN
HHHHHHHHHHHCCCC		63.3421890473
262UbiquitinationSLVIELDKELYGPDN
HHHHHHHHHHHCCCC		63.34-
262UbiquitinationSLVIELDKELYGPDN
HHHHHHHHHHHCCCC		63.3421890473
268 (in isoform 2)Ubiquitination-51.31-
289AcetylationETDGFQVKRPGDLNV
CCCCCEECCCCCCCC		41.9326051181
289UbiquitinationETDGFQVKRPGDLNV
CCCCCEECCCCCCCC		41.93-
297UbiquitinationRPGDLNVKCTLLLML
CCCCCCCEEEEEEEE		22.04-
299O-linked_GlycosylationGDLNVKCTLLLMLDH
CCCCCEEEEEEEECC		18.0929351928
301 (in isoform 1)Ubiquitination-1.1021890473
312UbiquitinationDHQPPQYKLDPRLAR
CCCCCHHCCCHHHHH		40.96-
320 (in isoform 2)Ubiquitination-3.9821890473
325PhosphorylationARLLGVHTQTRAAIM
HHHHCCCHHHHHHHH		29.27-
326 (in isoform 1)Ubiquitination-17.7021890473
327PhosphorylationLLGVHTQTRAAIMQA
HHCCCHHHHHHHHHH		24.35-
338PhosphorylationIMQALWLYIKHNQLQ
HHHHHHHHHHHCCCC		9.0620068231
345 (in isoform 2)Ubiquitination-44.8921890473
352PhosphorylationQDGHEREYINCNRYF
CCCCCCCCCCHHHHH		12.0329496907
364PhosphorylationRYFRQIFSCGRLRFS
HHHHHHHCCCCEEHH		19.7930631047
376AcetylationRFSEIPMKLAGLLQH
EHHHCCHHHHHHCCC		29.8123236377
376 (in isoform 1)Ubiquitination-29.8121890473
376UbiquitinationRFSEIPMKLAGLLQH
EHHHCCHHHHHHCCC		29.81-
395 (in isoform 2)Ubiquitination-11.0221890473
401AcetylationSVDPNDQKKTACYDI
EECCCCCCCCEEEEE		55.7625953088
401UbiquitinationSVDPNDQKKTACYDI
EECCCCCCCCEEEEE		55.76-
402UbiquitinationVDPNDQKKTACYDID
ECCCCCCCCEEEEEE		35.40-
403UbiquitinationDPNDQKKTACYDIDV
CCCCCCCCEEEEEEC		29.0621890473
405 (in isoform 1)Ubiquitination-3.6721890473
408PhosphorylationKKTACYDIDVEVDDP
CCCEEEEEECEECCH		2.3017081983
424 (in isoform 2)Ubiquitination-4.2721890473
430 (in isoform 2)Ubiquitination-39.94-
439 (in isoform 1)Ubiquitination-37.7021890473
451UbiquitinationIESINQLKTQRDFML
HHHHHHHHHCHHHHH		32.61-
451UbiquitinationIESINQLKTQRDFML
HHHHHHHHHCHHHHH		32.6121890473
451UbiquitinationIESINQLKTQRDFML
HHHHHHHHHCHHHHH		32.6121890473
458 (in isoform 2)Ubiquitination-4.7621890473
459 (in isoform 2)Ubiquitination-12.83-
480UbiquitinationRSQRRDLKIITDVIG
HHCCCCCCHHHHCCC		36.03-
483PhosphorylationRRDLKIITDVIGNPE
CCCCCHHHHCCCCHH		27.9019060867
498PhosphorylationEERRAAFYHQPWAQE
HHHHHHHHCCHHHHH		8.5329496907
514UbiquitinationVGRHIFAKVQQRRQE
HHHHHHHHHHHHHHH		29.81-
529MethylationLEQVLGIRLT-----
HHHHHCCCCC-----		30.4054559413
531PhosphorylationQVLGIRLT-------
HHHCCCCC-------		27.0730108239
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 SMRD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMRD2_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 SMRD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNF5_HUMANSMARCB1physical
22939629
TOP2B_HUMANTOP2Bphysical
22939629
NT2NL_HUMANNOTCH2NLphysical
25416956
ACL6A_HUMANACTL6Aphysical
26344197
ARI1A_HUMANARID1Aphysical
26344197
ARI1B_HUMANARID1Bphysical
26344197
BCL7A_HUMANBCL7Aphysical
26344197
REQU_HUMANDPF2physical
26344197
SMCA4_HUMANSMARCA4physical
26344197
SSXT_HUMANSS18physical
26344197
TBL1R_HUMANTBL1XR1physical
26344197
RENT2_HUMANUPF2physical
26344197
FANCA_HUMANFANCAphysical
28215707
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 SMRD2_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 THR-217, AND MASSSPECTROMETRY.
"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 THR-217, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND MASSSPECTROMETRY.
"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 THR-483, AND MASSSPECTROMETRY.

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