MD13L_MOUSE - dbPTM
MD13L_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MD13L_MOUSE
UniProt AC Q6JPI3
Protein Name Mediator of RNA polymerase II transcription subunit 13-like
Gene Name Med13l
Organism Mus musculus (Mouse).
Sequence Length 2207
Subcellular Localization Nucleus .
Protein Description Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway (By similarity)..
Protein Sequence MTAAANWVANGASLEDCHSNLFSLAELTGIKWRRYNFGGHGDCGPIISAPAQDDPILLSFIRCLQANLLCVWRRDVKPDCKELWIFWWGDEPNLVGVIHHELQVVEEGLWENGLSYECRTLLFKAIHNLLERCLMDKNFVRIGKWFVRPYDKDEKPVNKSEHLSCAFTFFLHGESNVCTSVEIAQHQPIYLINEEHLHMAQSSPAPFQVLVSPYGLNGTLTGHAYKMSDPAARKLIEEWHCFYPMVLRKREEPREEAELGYDDDFPVAVEVIVGGVRMVYPSAFVLVSQNDIPVPQSGHGTVAQQGLGSVKDPSNCGMPLTPPTSPEQVVIGESGGVQSAASHLGSQDGGMSTMHSPKRSRKTPPKLHSHMVRRVWRECILSRAQSKRSQMSTPTREEEAAHSPAAWDFVDPTQRVSCSCSRHKLLKRCAVGPSRPPAISQPGFSAGLPSSSSLPPPASSKHKTTERQEKGDKLQKRPLVPFHHRPSVAEELCVEQDAPGQKLGLAGIDASLEVSNTRKYDKQMAVPSRNTSKQMNLNPMDSPHSPISPLPPTLSPQPRGQEAESLDPPSVPVNPALYGNGLDLQQLSTIEDRTVLVGQRLPLMAEASETALYSGLRPSYTESSDRWWQSFRLPSSEDAEFRPPELQGERFDTALDLNPESTALQRLLAQPNKRFKIWQDEQPQVQPLPFLDPSPLSQQPGDTLGEVNDPYTFEDGDIKYIFTANKKCKQGTEKDSLKKNKSEDGFGTKDVTTPGHSTPVPDGKNAMSIFSSATKTDVRQDSAAGRAGSGSLTQVTDLAPSLHDLDNIFDNSDDDELGAVSPALRSSKMPTVGTEERPPGKDGRAAGPYPPTVADLQRMFPTPPSLEQHPAFSPVMNYKDGVSSETVTALGMMESPVVSMVPTHLTEFRMEVEDGLGSPKPEEIKDFSYVHKVPQFQPFVGSSMFAPLKTLPSHCLLPLKTPDACLFRPSWAVPPKMEQLPMPPAASSIRDGYNNVPSVGSLADPDYVNTPQMNTPVTLNSAAPASNSGAGVLPSPATPRFSVPTPRTPRTPRTPRGGGTASGQGSVKYDSTDQGSPASTPSTTRPLNSVEPATMQPIPEAHSLYVTLILSDSVMNVFKDRNFDSCCICACNMNIKGADVGLYIPDSSKEDQYRCTCGFSAIVNRKLGYNSGLFLEDELDIFGKNSDIGQAAERRLMMCQSSGQSTLLPQVEGARKAPEPPVSLLLLLQNQHTQPFASLSFLDYISSANRHALPCVSWTYDRVQADNNDYWTECFNALEQGRQYVDNPTGGKVDEALVRSATVHCWPHSNVLDTSMLSSQDVVRMLLSLQPFLQDAIQKKRTGRTWENIQHVQGPLTWQQFHKMAGRGTYGSEESPEPLPIPTLLVGYDKEFLTISPFSLPFWERLLLEPYGGHRDVAYIVVCPENEALLEGAKTFFRDLSAVYEMCRLGQHKPICKVLRDGIMRVGKTVAQKLTEELVSEWFNQPWSSEESDNHSRLKLYAQVCRHHLAPYLATLQLDSGLLMPPKHQSPPAEAQGQATPGNAGSLPSNSGSGAPPAGSAFNPTSSSSANPTTSSSSASSGPPGSSAASAPGITQMNTTSSSGFGGGVGGQNPSAGGSSTDRTPGNVACGDTEPGQSCTQSSQDGQDSVTERERIGIPTEPDSADSHAYPPAVVIYMVDPFTYTAEEDSSSGNFWLLSLMRCYTEMLDHLPEHMRSSFILQIVPCQYMLQTMKDEHVFYIQYLKSMAFSVYCQCRRPLPTQIHIKSLTGFGPAASIEMTLKNPERPSPIQLYSPPFILAPIKDKQTEPGETFGEASQKYNVLFVGYCLSHDQRWLLASCTDLHGELLETCVVNIALPSRSRKSKVSARKVGLQKLWEWCLGIVQMTSLPWRVVIGRLGRLGHGELKDWSILLGECSLQTISKQLKDVCRMCGISAADSPSILSACLVAMEPQGSFVVMPDAVTMGSVFGRSTALNMQSSQLNTPQDASCTHILVFPTSSTIQVAPANYPNEDGFSPNNDDMFVDLPFPDDMDNDIGILMTGNLHSSPNSSPVPSPGSPSGIGVGSHFQHSRSQGERLLSREAPEELKQQPLALGYFVSTAKAENLPQWFWSSCPQARNQCPLFLKASLHHHISVAQTDELLPARTSQRAPHPLDSKTTSDVLRFVLEQYNALSWLTCNPATQDRTSCLPVHFVVLTQLYNAIMNML
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
35PhosphorylationTGIKWRRYNFGGHGD
HCCCEEEECCCCCCC		13.2819854140
48PhosphorylationGDCGPIISAPAQDDP
CCCCCCCCCCCCCCH		28.9919854140
148MethylationRIGKWFVRPYDKDEK
EEEEEECCCCCCCCC		18.0030989539
356PhosphorylationGGMSTMHSPKRSRKT
CCCCCCCCCCCCCCC		22.6923384938
389PhosphorylationSRAQSKRSQMSTPTR
HHHHHHHHCCCCCCH		33.6926643407
392PhosphorylationQSKRSQMSTPTREEE
HHHHHCCCCCCHHHH		24.4925777480
393PhosphorylationSKRSQMSTPTREEEA
HHHHCCCCCCHHHHH		24.2825777480
395PhosphorylationRSQMSTPTREEEAAH
HHCCCCCCHHHHHHC		51.2926643407
403PhosphorylationREEEAAHSPAAWDFV
HHHHHHCCCCCHHCC		16.1126643407
413PhosphorylationAWDFVDPTQRVSCSC
CHHCCCCCCCEECCC		25.2525777480
542PhosphorylationMNLNPMDSPHSPISP
CCCCCCCCCCCCCCC		20.4724759943
545PhosphorylationNPMDSPHSPISPLPP
CCCCCCCCCCCCCCC		27.5824759943
548PhosphorylationDSPHSPISPLPPTLS
CCCCCCCCCCCCCCC		24.6224759943
555PhosphorylationSPLPPTLSPQPRGQE
CCCCCCCCCCCCCCC		24.7824759943
570PhosphorylationAESLDPPSVPVNPAL
CCCCCCCCCCCCHHH		44.4325338131
608PhosphorylationLPLMAEASETALYSG
HHHCHHHHHHHHHCC		27.3019854140
610PhosphorylationLMAEASETALYSGLR
HCHHHHHHHHHCCCC		21.3319854140
613PhosphorylationEASETALYSGLRPSY
HHHHHHHHCCCCCCC		9.7619854140
727UbiquitinationYIFTANKKCKQGTEK
EEEECCCCCCCCCCC		46.61-
729UbiquitinationFTANKKCKQGTEKDS
EECCCCCCCCCCCHH		61.72-
738UbiquitinationGTEKDSLKKNKSEDG
CCCCHHCCCCCCCCC		59.25-
742PhosphorylationDSLKKNKSEDGFGTK
HHCCCCCCCCCCCCC		50.76-
749AcetylationSEDGFGTKDVTTPGH
CCCCCCCCCCCCCCC		51.0523806337
752PhosphorylationGFGTKDVTTPGHSTP
CCCCCCCCCCCCCCC		37.0925338131
753PhosphorylationFGTKDVTTPGHSTPV
CCCCCCCCCCCCCCC		27.4123984901
757PhosphorylationDVTTPGHSTPVPDGK
CCCCCCCCCCCCCCC		40.0826643407
758PhosphorylationVTTPGHSTPVPDGKN
CCCCCCCCCCCCCCC		23.7226643407
764AcetylationSTPVPDGKNAMSIFS
CCCCCCCCCHHHHHH		49.2522826441
772PhosphorylationNAMSIFSSATKTDVR
CHHHHHHHCCCCCCC		29.2522006019
801PhosphorylationQVTDLAPSLHDLDNI
EHHHCCCCHHHHHHC		32.5021149613
812PhosphorylationLDNIFDNSDDDELGA
HHHCCCCCCCCHHHC		44.2421149613
821PhosphorylationDDELGAVSPALRSSK
CCHHHCCCHHHHHCC		12.1526745281
873PhosphorylationLEQHPAFSPVMNYKD
HHHCCCCCCCCCCCC		20.7727180971
918PhosphorylationEVEDGLGSPKPEEIK
ECCCCCCCCCHHHHC		34.4926824392
928PhosphorylationPEEIKDFSYVHKVPQ
HHHHCCCCCEECCCC		36.0625777480
929PhosphorylationEEIKDFSYVHKVPQF
HHHCCCCCEECCCCC		13.4325777480
1042PhosphorylationSPATPRFSVPTPRTP
CCCCCCCCCCCCCCC		28.5929472430
1045PhosphorylationTPRFSVPTPRTPRTP
CCCCCCCCCCCCCCC		24.2129472430
1048PhosphorylationFSVPTPRTPRTPRTP
CCCCCCCCCCCCCCC		20.5123684622
1051PhosphorylationPTPRTPRTPRTPRGG
CCCCCCCCCCCCCCC		20.5123684622
1054PhosphorylationRTPRTPRTPRGGGTA
CCCCCCCCCCCCCCC		20.6723684622
1071PhosphorylationQGSVKYDSTDQGSPA
CCCEEECCCCCCCCC		30.6928066266
1072PhosphorylationGSVKYDSTDQGSPAS
CCEEECCCCCCCCCC		29.4628066266
1076PhosphorylationYDSTDQGSPASTPST
ECCCCCCCCCCCCCC		16.2028066266
1079PhosphorylationTDQGSPASTPSTTRP
CCCCCCCCCCCCCCC		44.2128066266
1080PhosphorylationDQGSPASTPSTTRPL
CCCCCCCCCCCCCCC		24.3028066266
1082PhosphorylationGSPASTPSTTRPLNS
CCCCCCCCCCCCCCC		42.3628066266
1083PhosphorylationSPASTPSTTRPLNSV
CCCCCCCCCCCCCCC		28.2028066266
1732PhosphorylationPCQYMLQTMKDEHVF
CHHHHHHHCCCCCEE		23.4028576409
1769PhosphorylationQIHIKSLTGFGPAAS
EEEEEECCCCCCCEE		37.2426239621
1776PhosphorylationTGFGPAASIEMTLKN
CCCCCCEEEEEEECC		22.6126239621
1780PhosphorylationPAASIEMTLKNPERP
CCEEEEEEECCCCCC		23.0726239621
2080PhosphorylationSQGERLLSREAPEEL
HHHHHHHHCCCCHHH		32.4426824392
2156PhosphorylationRAPHPLDSKTTSDVL
CCCCCCCCCCHHHHH		39.3223984901
2158PhosphorylationPHPLDSKTTSDVLRF
CCCCCCCCHHHHHHH		35.1723984901
2159PhosphorylationHPLDSKTTSDVLRFV
CCCCCCCHHHHHHHH		27.0223984901
2160PhosphorylationPLDSKTTSDVLRFVL
CCCCCCHHHHHHHHH		30.8423984901
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 MD13L_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MD13L_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 MD13L_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MD13L_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MD13L_MOUSE

loading...

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-918, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory