SNPC4_HUMAN - dbPTM
SNPC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNPC4_HUMAN
UniProt AC Q5SXM2
Protein Name snRNA-activating protein complex subunit 4
Gene Name SNAPC4 {ECO:0000312|EMBL:CAI13935.1, ECO:0000312|HGNC:HGNC:11137}
Organism Homo sapiens (Human).
Sequence Length 1469
Subcellular Localization Nucleus .
Protein Description Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box..
Protein Sequence MDVDAEREKITQEIKELERILDPGSSGSHVEISESSLESDSEADSLPSEDLDPADPPISEEERWGEASNDEDDPKDKTLPEDPETCLQLNMVYQEVIQEKLAEANLLLAQNREQQEELMRDLAGSKGTKVKDGKSLPPSTYMGHFMKPYFKDKVTGVGPPANEDTREKAAQGIKAFEELLVTKWKNWEKALLRKSVVSDRLQRLLQPKLLKLEYLHQKQSKVSSELERQALEKQGREAEKEIQDINQLPEEALLGNRLDSHDWEKISNINFEGSRSAEEIRKFWQNSEHPSINKQEWSREEEERLQAIAAAHGHLEWQKIAEELGTSRSAFQCLQKFQQHNKALKRKEWTEEEDRMLTQLVQEMRVGSHIPYRRIVYYMEGRDSMQLIYRWTKSLDPGLKKGYWAPEEDAKLLQAVAKYGEQDWFKIREEVPGRSDAQCRDRYLRRLHFSLKKGRWNLKEEEQLIELIEKYGVGHWAKIASELPHRSGSQCLSKWKIMMGKKQGLRRRRRRARHSVRWSSTSSSGSSSGSSGGSSSSSSSSSEEDEPEQAQAGEGDRALLSPQYMVPDMDLWVPARQSTSQPWRGGAGAWLGGPAASLSPPKGSSASQGGSKEASTTAAAPGEETSPVQVPARAHGPVPRSAQASHSADTRPAGAEKQALEGGRRLLTVPVETVLRVLRANTAARSCTQKEQLRQPPLPTSSPGVSSGDSVARSHVQWLRHRATQSGQRRWRHALHRRLLNRRLLLAVTPWVGDVVVPCTQASQRPAVVQTQADGLREQLQQARLASTPVFTLFTQLFHIDTAGCLEVVRERKALPPRLPQAGARDPPVHLLQASSSAQSTPGHLFPNVPAQEASKSASHKGSRRLASSRVERTLPQASLLASTGPRPKPKTVSELLQEKRLQEARAREATRGPVVLPSQLLVSSSVILQPPLPHTPHGRPAPGPTVLNVPLSGPGAPAAAKPGTSGSWQEAGTSAKDKRLSTMQALPLAPVFSEAEGTAPAASQAPALGPGQISVSCPESGLGQSQAPAASRKQGLPEAPPFLPAAPSPTPLPVQPLSLTHIGGPHVATSVPLPVTWVLTAQGLLPVPVPAVVSLPRPAGTPGPAGLLATLLPPLTETRAAQGPRAPALSSSWQPPANMNREPEPSCRTDTPAPPTHALSQSPAEADGSVAFVPGEAQVAREIPEPRTSSHADPPEAEPPWSGRLPAFGGVIPATEPRGTPGSPSGTQEPRGPLGLEKLPLRQPGPEKGALDLEKPPLPQPGPEKGALDLGLLSQEGEAATQQWLGGQRGVRVPLLGSRLPYQPPALCSLRALSGLLLHKKALEHKATSLVVGGEAERPAGALQASLGLVRGQLQDNPAYLLLRARFLAAFTLPALLATLAPQGVRTTLSVPSRVGSESEDEDLLSELELADRDGQPGCTTATCPIQGAPDSGKCSASSCLDTSNDPDDLDVLRTRHARHTRKRRRLV
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-------MDVDAERE
-------CCHHHHHH		47.20-
36PhosphorylationHVEISESSLESDSEA
CEEECHHHCCCCCCC		31.9130576142
48PhosphorylationSEADSLPSEDLDPAD
CCCCCCCHHHCCCCC		49.3830576142
59PhosphorylationDPADPPISEEERWGE
CCCCCCCCHHHHHHC		44.7430576142
68PhosphorylationEERWGEASNDEDDPK
HHHHHCCCCCCCCCC		40.2823401153
135PhosphorylationTKVKDGKSLPPSTYM
CCCCCCCCCCCCCCC		52.19-
223PhosphorylationHQKQSKVSSELERQA
HHHHHHHCHHHHHHH		23.1023312004
224PhosphorylationQKQSKVSSELERQAL
HHHHHHCHHHHHHHH		49.5423312004
240UbiquitinationKQGREAEKEIQDINQ
HHHHHHHHHHHHHHH		68.14-
411UbiquitinationWAPEEDAKLLQAVAK
CCCHHHHHHHHHHHH		63.15-
450PhosphorylationYLRRLHFSLKKGRWN
HHHHHHHHHHCCCCC		28.6521712546
501AcetylationKWKIMMGKKQGLRRR
HHHHHHCCHHHHHHH		24.837679297
519PhosphorylationARHSVRWSSTSSSGS
HHHCCEEECCCCCCC		17.1130576142
521PhosphorylationHSVRWSSTSSSGSSS
HCCEEECCCCCCCCC		27.41-
524PhosphorylationRWSSTSSSGSSSGSS
EEECCCCCCCCCCCC		42.32-
528PhosphorylationTSSSGSSSGSSGGSS
CCCCCCCCCCCCCCC		44.37-
531PhosphorylationSGSSSGSSGGSSSSS
CCCCCCCCCCCCCCC		51.18-
534PhosphorylationSSGSSGGSSSSSSSS
CCCCCCCCCCCCCCC		30.4930576142
535PhosphorylationSGSSGGSSSSSSSSS
CCCCCCCCCCCCCCC		37.2030576142
536PhosphorylationGSSGGSSSSSSSSSE
CCCCCCCCCCCCCCC		35.62-
537PhosphorylationSSGGSSSSSSSSSEE
CCCCCCCCCCCCCCC		35.87-
538PhosphorylationSGGSSSSSSSSSEED
CCCCCCCCCCCCCCC		35.87-
539PhosphorylationGGSSSSSSSSSEEDE
CCCCCCCCCCCCCCC		35.87-
541PhosphorylationSSSSSSSSSEEDEPE
CCCCCCCCCCCCCHH		43.65-
561PhosphorylationEGDRALLSPQYMVPD
CCCHHHHCCCCCCCC		15.7127251275
597PhosphorylationWLGGPAASLSPPKGS
CCCCCHHHCCCCCCC		31.3330175587
599PhosphorylationGGPAASLSPPKGSSA
CCCHHHCCCCCCCCC		36.3421712546
604PhosphorylationSLSPPKGSSASQGGS
HCCCCCCCCCCCCCC		28.9328152594
605PhosphorylationLSPPKGSSASQGGSK
CCCCCCCCCCCCCCC		40.3828152594
607PhosphorylationPPKGSSASQGGSKEA
CCCCCCCCCCCCCCC		31.1628152594
611PhosphorylationSSASQGGSKEASTTA
CCCCCCCCCCCCCCC		33.8628152594
615PhosphorylationQGGSKEASTTAAAPG
CCCCCCCCCCCCCCC		27.6423401153
616PhosphorylationGGSKEASTTAAAPGE
CCCCCCCCCCCCCCC		27.7428450419
617PhosphorylationGSKEASTTAAAPGEE
CCCCCCCCCCCCCCC		16.2928450419
625PhosphorylationAAAPGEETSPVQVPA
CCCCCCCCCCCCCCC		33.7525159151
626PhosphorylationAAPGEETSPVQVPAR
CCCCCCCCCCCCCCH		26.7625159151
657UbiquitinationTRPAGAEKQALEGGR
CCCCCHHHHHHHCCC		40.09-
700PhosphorylationLRQPPLPTSSPGVSS
HCCCCCCCCCCCCCC		49.9023312004
701PhosphorylationRQPPLPTSSPGVSSG
CCCCCCCCCCCCCCC		32.3723312004
702PhosphorylationQPPLPTSSPGVSSGD
CCCCCCCCCCCCCCC		28.3121815630
706PhosphorylationPTSSPGVSSGDSVAR
CCCCCCCCCCCHHHH		34.2230257219
707PhosphorylationTSSPGVSSGDSVARS
CCCCCCCCCCHHHHH		44.1830257219
710PhosphorylationPGVSSGDSVARSHVQ
CCCCCCCHHHHHHHH		22.6223312004
840PhosphorylationQASSSAQSTPGHLFP
ECCCCCCCCCCCCCC		35.9628555341
1095PhosphorylationVPVPAVVSLPRPAGT
CCCCEEEECCCCCCC		26.5124719451
1150PhosphorylationEPEPSCRTDTPAPPT
CCCCCCCCCCCCCCC		48.8528450419
1152PhosphorylationEPSCRTDTPAPPTHA
CCCCCCCCCCCCCCC		22.2728450419
1157PhosphorylationTDTPAPPTHALSQSP
CCCCCCCCCCCCCCC		20.7921712546
1161PhosphorylationAPPTHALSQSPAEAD
CCCCCCCCCCCCCCC		29.4228450419
1163PhosphorylationPTHALSQSPAEADGS
CCCCCCCCCCCCCCC		23.7721712546
1170PhosphorylationSPAEADGSVAFVPGE
CCCCCCCCEEECCCC		15.7228450419
1216PhosphorylationFGGVIPATEPRGTPG
CCCEECCCCCCCCCC		40.9627134283
1221PhosphorylationPATEPRGTPGSPSGT
CCCCCCCCCCCCCCC		26.2529255136
1224PhosphorylationEPRGTPGSPSGTQEP
CCCCCCCCCCCCCCC		19.6629255136
1226PhosphorylationRGTPGSPSGTQEPRG
CCCCCCCCCCCCCCC		57.0529255136
1228PhosphorylationTPGSPSGTQEPRGPL
CCCCCCCCCCCCCCC		33.8129978859
1256AcetylationKGALDLEKPPLPQPG
CCCCCCCCCCCCCCC		60.2720167786
1300MethylationRVPLLGSRLPYQPPA
CCCCCCCCCCCCCCH		37.5754559481
1315PhosphorylationLCSLRALSGLLLHKK
HHHHHHHHHHHHCHH		26.8127251275
1322UbiquitinationSGLLLHKKALEHKAT
HHHHHCHHHHCCCCC		47.67-
1388PhosphorylationLAPQGVRTTLSVPSR
HCCCCCEEEECCCCC		29.6822210691
1389PhosphorylationAPQGVRTTLSVPSRV
CCCCCEEEECCCCCC		13.3822210691
1391PhosphorylationQGVRTTLSVPSRVGS
CCCEEEECCCCCCCC		29.8624719451
1394PhosphorylationRTTLSVPSRVGSESE
EEEECCCCCCCCCCC		37.1325921289
1398PhosphorylationSVPSRVGSESEDEDL
CCCCCCCCCCCCHHH		34.7830278072
1400PhosphorylationPSRVGSESEDEDLLS
CCCCCCCCCCHHHHH		52.6330278072
1407PhosphorylationSEDEDLLSELELADR
CCCHHHHHHHHHHCC		47.6429978859
1421PhosphorylationRDGQPGCTTATCPIQ
CCCCCCCCEEECCCC		25.9424144214
1422PhosphorylationDGQPGCTTATCPIQG
CCCCCCCEEECCCCC		24.8524144214
1424PhosphorylationQPGCTTATCPIQGAP
CCCCCEEECCCCCCC		19.4024144214
1440PhosphorylationSGKCSASSCLDTSND
CCCCCHHHHCCCCCC		20.58-
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 SNPC4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNPC4_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 SNPC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNPC2_HUMANSNAPC2physical
9418884
PO2F1_HUMANPOU2F1physical
9418884
SNPC5_HUMANSNAPC5physical
11056176
SNPC1_HUMANSNAPC1physical
11056176
SNPC2_HUMANSNAPC2physical
11056176
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 SNPC4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-626, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1398 AND SER-1400, ANDMASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-626, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1157, AND MASSSPECTROMETRY.

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