S14L1_HUMAN - dbPTM
S14L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S14L1_HUMAN
UniProt AC Q92503
Protein Name SEC14-like protein 1 {ECO:0000305}
Gene Name SEC14L1
Organism Homo sapiens (Human).
Sequence Length 715
Subcellular Localization Cytoplasm . Golgi apparatus .
Protein Description May play a role in innate immunity by inhibiting the antiviral RIG-I signaling pathway. In this pathway, functions as a negative regulator of DDX58/RIG-I, the cytoplasmic sensor of viral nucleic acids. Prevents the interaction of DDX58 with MAVS/IPS1, an important step in signal propagation. [PubMed: 23843640 May also regulate the SLC18A3 and SLC5A7 cholinergic transporters]
Protein Sequence MVQKYQSPVRVYKYPFELIMAAYERRFPTCPLIPMFVGSDTVNEFKSEDGAIHVIERRCKLDVDAPRLLKKIAGVDYVYFVQKNSLNSRERTLHIEAYNETFSNRVIINEHCCYTVHPENEDWTCFEQSASLDIKSFFGFESTVEKIAMKQYTSNIKKGKEIIEYYLRQLEEEGITFVPRWSPPSITTSSETSSSSSKKQAASMAVVIPEAALKEGLSGDALSSPSAPEPVVGTPDDKLDADYIKRYLGDLTPLQESCLIRLRQWLQETHKGKIPKDEHILRFLRARDFNIDKAREIMCQSLTWRKQHQVDYILETWTPPQVLQDYYAGGWHHHDKDGRPLYVLRLGQMDTKGLVRALGEEALLRYVLSINEEGLRRCEENTKVFGRPISSWTCLVDLEGLNMRHLWRPGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIYAGNDYQGPGGLLDYIDKEIIPDFLSGECMCEVPEGGLVPKSLYRTAEELENEDLKLWTETIYQSASVFKGAPHEILIQIVDASSVITWDFDVCKGDIVFNIYHSKRSPQPPKKDSLGAHSITSPGGNNVQLIDKVWQLGRDYSMVESPLICKEGESVQGSHVTRWPGFYILQWKFHSMPACAASSLPRVDDVLASLQVSSHKCKVMYYTEVIGSEDFRGSMTSLESSHSGFSQLSAATTSSSQSHSSSMISR
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
4Ubiquitination----MVQKYQSPVRV
----CCCCCCCCCEE		33.57-
5 (in isoform 3)Phosphorylation-9.3522210691
5Phosphorylation---MVQKYQSPVRVY
---CCCCCCCCCEEE		9.35-
7 (in isoform 3)Phosphorylation-23.4422210691
12PhosphorylationYQSPVRVYKYPFELI
CCCCCEEECCCHHHH		8.34-
23PhosphorylationFELIMAAYERRFPTC
HHHHHHHHHHHCCCC		10.6322817900
60UbiquitinationHVIERRCKLDVDAPR
EEEEHHHCCCCCHHH		46.00-
71UbiquitinationDAPRLLKKIAGVDYV
CHHHHHHHHHCCCEE		37.44-
77PhosphorylationKKIAGVDYVYFVQKN
HHHHCCCEEEEEECC		8.4729978859
79PhosphorylationIAGVDYVYFVQKNSL
HHCCCEEEEEECCCC		7.5729978859
141UbiquitinationIKSFFGFESTVEKIA
HHHHHCCHHHHHHHH		45.9721890473
146UbiquitinationGFESTVEKIAMKQYT
CCHHHHHHHHHHHHH		31.28-
150UbiquitinationTVEKIAMKQYTSNIK
HHHHHHHHHHHHCHH		31.0021890473
150 (in isoform 2)Ubiquitination-31.00-
152PhosphorylationEKIAMKQYTSNIKKG
HHHHHHHHHHCHHHH		13.4530631047
157UbiquitinationKQYTSNIKKGKEIIE
HHHHHCHHHHHHHHH		60.78-
160UbiquitinationTSNIKKGKEIIEYYL
HHCHHHHHHHHHHHH		55.4021890473
160 (in isoform 2)Ubiquitination-55.40-
160UbiquitinationTSNIKKGKEIIEYYL
HHCHHHHHHHHHHHH		55.4021890473
165PhosphorylationKGKEIIEYYLRQLEE
HHHHHHHHHHHHHHH		9.4428152594
166PhosphorylationGKEIIEYYLRQLEEE
HHHHHHHHHHHHHHH		5.2128152594
193PhosphorylationITTSSETSSSSSKKQ
CCCCCCCCCCCCHHH		24.9525852190
194PhosphorylationTTSSETSSSSSKKQA
CCCCCCCCCCCHHHH		41.4825852190
195PhosphorylationTSSETSSSSSKKQAA
CCCCCCCCCCHHHHH		38.1025852190
196PhosphorylationSSETSSSSSKKQAAS
CCCCCCCCCHHHHHH		48.3925852190
197PhosphorylationSETSSSSSKKQAASM
CCCCCCCCHHHHHHE		45.9125852190
199UbiquitinationTSSSSSKKQAASMAV
CCCCCCHHHHHHEEE		47.30-
203PhosphorylationSSKKQAASMAVVIPE
CCHHHHHHEEEEECH		15.4130622161
218PhosphorylationAALKEGLSGDALSSP
HHHHCCCCCCCCCCC		45.5423927012
223PhosphorylationGLSGDALSSPSAPEP
CCCCCCCCCCCCCCC		41.7630266825
224PhosphorylationLSGDALSSPSAPEPV
CCCCCCCCCCCCCCC		24.5930266825
226PhosphorylationGDALSSPSAPEPVVG
CCCCCCCCCCCCCCC		59.4030266825
234PhosphorylationAPEPVVGTPDDKLDA
CCCCCCCCCCCCCCH		16.3730266825
238UbiquitinationVVGTPDDKLDADYIK
CCCCCCCCCCHHHHH		56.50-
243PhosphorylationDDKLDADYIKRYLGD
CCCCCHHHHHHHHCC		15.2923927012
245 (in isoform 2)Ubiquitination-28.85-
245UbiquitinationKLDADYIKRYLGDLT
CCCHHHHHHHHCCCC		28.85-
276UbiquitinationTHKGKIPKDEHILRF
HCCCCCCCHHHHHHH		78.28-
352 (in isoform 2)Ubiquitination-46.08-
352UbiquitinationRLGQMDTKGLVRALG
EECCCCHHHHHHHHC		46.0821906983
425PhosphorylationIEVVEANYPETLGRL
HHHHHHCCCHHHHHH		14.9729632367
428PhosphorylationVEANYPETLGRLLIL
HHHCCCHHHHHHHHH		29.9729632367
503UbiquitinationPEGGLVPKSLYRTAE
CCCCCCCHHHHHCHH		45.68-
518UbiquitinationELENEDLKLWTETIY
HHCCCCHHHHHHHHH		55.06-
568UbiquitinationVFNIYHSKRSPQPPK
EEEEEECCCCCCCCC		43.51-
578PhosphorylationPQPPKKDSLGAHSIT
CCCCCCCCCCCCCCC		37.2725159151
578UbiquitinationPQPPKKDSLGAHSIT
CCCCCCCCCCCCCCC		37.2721890473
583PhosphorylationKDSLGAHSITSPGGN
CCCCCCCCCCCCCCC		27.3322199227
585PhosphorylationSLGAHSITSPGGNNV
CCCCCCCCCCCCCCH		31.7025159151
586PhosphorylationLGAHSITSPGGNNVQ
CCCCCCCCCCCCCHH		21.6325159151
597UbiquitinationNNVQLIDKVWQLGRD
CCHHHHHHHHHCCCC		38.0821890473
597UbiquitinationNNVQLIDKVWQLGRD
CCHHHHHHHHHCCCC		38.0821890473
605PhosphorylationVWQLGRDYSMVESPL
HHHCCCCCCCCCCCE		9.4129083192
606PhosphorylationWQLGRDYSMVESPLI
HHCCCCCCCCCCCEE		22.2029083192
610PhosphorylationRDYSMVESPLICKEG
CCCCCCCCCEEECCC		17.3729083192
619PhosphorylationLICKEGESVQGSHVT
EEECCCCCCCCCCCC		30.5129083192
623PhosphorylationEGESVQGSHVTRWPG
CCCCCCCCCCCCCCC		9.5529083192
626PhosphorylationSVQGSHVTRWPGFYI
CCCCCCCCCCCCEEE		22.92-
640PhosphorylationILQWKFHSMPACAAS
EEEEEECCCCCHHHH		29.6023312004
647PhosphorylationSMPACAASSLPRVDD
CCCCHHHHCCCCHHH		17.5523312004
648PhosphorylationMPACAASSLPRVDDV
CCCHHHHCCCCHHHH		37.3528985074
658PhosphorylationRVDDVLASLQVSSHK
CHHHHHHHHHCCCCC		18.38-
663PhosphorylationLASLQVSSHKCKVMY
HHHHHCCCCCCEEEE		28.27-
665UbiquitinationSLQVSSHKCKVMYYT
HHHCCCCCCEEEEEE		37.38-
667UbiquitinationQVSSHKCKVMYYTEV
HCCCCCCEEEEEEEE		34.54-
686PhosphorylationDFRGSMTSLESSHSG
CCCCCCCCCCCCCCC		22.8430576142
689PhosphorylationGSMTSLESSHSGFSQ
CCCCCCCCCCCCCCC		38.3530576142
692PhosphorylationTSLESSHSGFSQLSA
CCCCCCCCCCCCCCE		43.4030576142
695PhosphorylationESSHSGFSQLSAATT
CCCCCCCCCCCEECC		33.4630576142
698PhosphorylationHSGFSQLSAATTSSS
CCCCCCCCEECCCCC		14.2830576142
701PhosphorylationFSQLSAATTSSSQSH
CCCCCEECCCCCCCC		27.2530576142
705PhosphorylationSAATTSSSQSHSSSM
CEECCCCCCCCCCCC		35.1530576142
707PhosphorylationATTSSSQSHSSSMIS
ECCCCCCCCCCCCCC		27.5630576142
709PhosphorylationTSSSQSHSSSMISR-
CCCCCCCCCCCCCC-		29.3830576142
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 S14L1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S14L1_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 S14L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of S14L1_HUMAN !!
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 S14L1_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-224 AND THR-234, ANDMASS SPECTROMETRY.

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