LYRIC_HUMAN - dbPTM
LYRIC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LYRIC_HUMAN
UniProt AC Q86UE4
Protein Name Protein LYRIC
Gene Name MTDH
Organism Homo sapiens (Human).
Sequence Length 582
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein. Nucleus membrane
Single-pass membrane protein. Cell junction, tight junction. Nucleus, nucleolus. Cytoplasm, perinuclear region. In epithelial cells, recruited to tight junctions (TJ) dur
Protein Description Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance..
Protein Sequence MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKTRPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET
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
452-HydroxyisobutyrylationLDLGLEPKRYPGWVI
CCCCCCCCCCCCEEE
56.01-
84PhosphorylationGARKKRRSPPRKREE
HHHHHCCCCCCHHHH
43.2030576142
88UbiquitinationKRRSPPRKREEAAAV
HCCCCCCHHHHHHCC
70.68-
107UbiquitinationPDDLALLKNLRSEEQ
HHHHHHHHHHCCHHH
55.5821890473
111PhosphorylationALLKNLRSEEQKKKN
HHHHHHCCHHHHHHH
48.9625159151
121UbiquitinationQKKKNRKKLSEKPKP
HHHHHHHHHCCCCCC
54.75-
125UbiquitinationNRKKLSEKPKPNGRT
HHHHHCCCCCCCCCE
55.77-
127UbiquitinationKKLSEKPKPNGRTVE
HHHCCCCCCCCCEEE
63.28-
132PhosphorylationKPKPNGRTVEVAEGE
CCCCCCCEEEEEECC
23.5528176443
143PhosphorylationAEGEAVRTPQSVTAK
EECCEEECCCCCCCC
21.0529255136
146PhosphorylationEAVRTPQSVTAKQPP
CEEECCCCCCCCCCC
23.7330266825
148PhosphorylationVRTPQSVTAKQPPEI
EECCCCCCCCCCCCC
33.1228176443
150UbiquitinationTPQSVTAKQPPEIDK
CCCCCCCCCCCCCCC
54.7121890473
170AcetylationKKNKKKSKSDAKAVQ
HHCHHCCHHHHHHHH
62.327676495
171PhosphorylationKNKKKSKSDAKAVQN
HCHHCCHHHHHHHHH
50.3024425749
1742-HydroxyisobutyrylationKKSKSDAKAVQNSSR
HCCHHHHHHHHHHCC
54.82-
174AcetylationKKSKSDAKAVQNSSR
HCCHHHHHHHHHHCC
54.827676507
174UbiquitinationKKSKSDAKAVQNSSR
HCCHHHHHHHHHHCC
54.8221890473
179PhosphorylationDAKAVQNSSRHDGKE
HHHHHHHHCCCCCCC
16.2028450419
180PhosphorylationAKAVQNSSRHDGKEV
HHHHHHHCCCCCCCC
40.9823927012
185AcetylationNSSRHDGKEVDEGAW
HHCCCCCCCCCCCHH
61.7026051181
185UbiquitinationNSSRHDGKEVDEGAW
HHCCCCCCCCCCCHH
61.7021890473
194PhosphorylationVDEGAWETKISHREK
CCCCHHHHHCCHHHH
23.9923186163
1952-HydroxyisobutyrylationDEGAWETKISHREKR
CCCHHHHHCCHHHHH
30.60-
195AcetylationDEGAWETKISHREKR
CCCHHHHHCCHHHHH
30.6027452117
195UbiquitinationDEGAWETKISHREKR
CCCHHHHHCCHHHHH
30.60-
197PhosphorylationGAWETKISHREKRQQ
CHHHHHCCHHHHHHH
20.3223401153
212PhosphorylationRKRDKVLTDSGSLDS
HHHHHCCCCCCCCCC
30.9823663014
214PhosphorylationRDKVLTDSGSLDSTI
HHHCCCCCCCCCCCC
25.6630278072
216PhosphorylationKVLTDSGSLDSTIPG
HCCCCCCCCCCCCCC
32.7130278072
219PhosphorylationTDSGSLDSTIPGIEN
CCCCCCCCCCCCCCC
33.2623663014
220PhosphorylationDSGSLDSTIPGIENT
CCCCCCCCCCCCCCE
30.7523663014
227PhosphorylationTIPGIENTITVTTEQ
CCCCCCCEEEEEHHH
12.7723663014
229PhosphorylationPGIENTITVTTEQLT
CCCCCEEEEEHHHEE
15.1223663014
231PhosphorylationIENTITVTTEQLTTA
CCCEEEEEHHHEEEE
18.9023663014
232PhosphorylationENTITVTTEQLTTAS
CCEEEEEHHHEEEEE
19.8723663014
236PhosphorylationTVTTEQLTTASFPVG
EEEHHHEEEEECCCC
21.7323663014
237PhosphorylationVTTEQLTTASFPVGS
EEHHHEEEEECCCCC
28.9723663014
239PhosphorylationTEQLTTASFPVGSKK
HHHEEEEECCCCCCC
28.1726434776
244PhosphorylationTASFPVGSKKNKGDS
EEECCCCCCCCCCCC
40.4626434776
246MalonylationSFPVGSKKNKGDSHL
ECCCCCCCCCCCCCE
66.6430639696
248MalonylationPVGSKKNKGDSHLNV
CCCCCCCCCCCCEEE
73.3326320211
248UbiquitinationPVGSKKNKGDSHLNV
CCCCCCCCCCCCEEE
73.33-
251PhosphorylationSKKNKGDSHLNVQVS
CCCCCCCCCEEEEEE
38.2425159151
258PhosphorylationSHLNVQVSNFKSGKG
CCEEEEEEECCCCCC
21.3225159151
261MethylationNVQVSNFKSGKGDST
EEEEEECCCCCCCCE
63.65-
262PhosphorylationVQVSNFKSGKGDSTL
EEEEECCCCCCCCEE
41.4127251275
264AcetylationVSNFKSGKGDSTLQV
EEECCCCCCCCEEEE
67.64-
264MethylationVSNFKSGKGDSTLQV
EEECCCCCCCCEEEE
67.64115972663
267PhosphorylationFKSGKGDSTLQVSSG
CCCCCCCCEEEEECC
39.4227251275
268PhosphorylationKSGKGDSTLQVSSGL
CCCCCCCEEEEECCC
26.4227251275
272PhosphorylationGDSTLQVSSGLNENL
CCCEEEEECCCCCCE
13.01-
273PhosphorylationDSTLQVSSGLNENLT
CCEEEEECCCCCCEE
48.74-
280PhosphorylationSGLNENLTVNGGGWN
CCCCCCEEEECCCCC
24.41-
289UbiquitinationNGGGWNEKSVKLSSQ
ECCCCCHHHEECCCC
58.29-
292UbiquitinationGWNEKSVKLSSQISA
CCCHHHEECCCCCCC
50.14-
294PhosphorylationNEKSVKLSSQISAGE
CHHHEECCCCCCCCH
17.9329255136
295PhosphorylationEKSVKLSSQISAGEE
HHHEECCCCCCCCHH
41.8030266825
298PhosphorylationVKLSSQISAGEEKWN
EECCCCCCCCHHHHC
23.6829255136
303AcetylationQISAGEEKWNSVSPA
CCCCCHHHHCCCCHH
47.5826051181
303UbiquitinationQISAGEEKWNSVSPA
CCCCCHHHHCCCCHH
47.58-
306PhosphorylationAGEEKWNSVSPASAG
CCHHHHCCCCHHHCC
23.9030266825
308PhosphorylationEEKWNSVSPASAGKR
HHHHCCCCHHHCCCC
17.9919664994
311PhosphorylationWNSVSPASAGKRKTE
HCCCCHHHCCCCCCC
40.7222167270
3142-HydroxyisobutyrylationVSPASAGKRKTEPSA
CCHHHCCCCCCCCCC
50.90-
314AcetylationVSPASAGKRKTEPSA
CCHHHCCCCCCCCCC
50.9025953088
314MethylationVSPASAGKRKTEPSA
CCHHHCCCCCCCCCC
50.9012430023
314UbiquitinationVSPASAGKRKTEPSA
CCHHHCCCCCCCCCC
50.90-
323PhosphorylationKTEPSAWSQDTGDAN
CCCCCCCCCCCCCCC
20.2125159151
326PhosphorylationPSAWSQDTGDANTNG
CCCCCCCCCCCCCCC
29.3523186163
331PhosphorylationQDTGDANTNGKDWGR
CCCCCCCCCCCCCCC
47.2530108239
334AcetylationGDANTNGKDWGRSWS
CCCCCCCCCCCCCCC
52.9926051181
334UbiquitinationGDANTNGKDWGRSWS
CCCCCCCCCCCCCCC
52.99-
338MethylationTNGKDWGRSWSDRSI
CCCCCCCCCCCCCCC
30.60115482437
339PhosphorylationNGKDWGRSWSDRSIF
CCCCCCCCCCCCCCC
27.3025159151
341PhosphorylationKDWGRSWSDRSIFSG
CCCCCCCCCCCCCCC
25.1323898821
344PhosphorylationGRSWSDRSIFSGIGS
CCCCCCCCCCCCCCC
32.7321082442
347PhosphorylationWSDRSIFSGIGSTAE
CCCCCCCCCCCCCCC
28.0328464451
351PhosphorylationSIFSGIGSTAEPVSQ
CCCCCCCCCCCCCCC
23.6428450419
352PhosphorylationIFSGIGSTAEPVSQS
CCCCCCCCCCCCCCC
29.8128464451
357PhosphorylationGSTAEPVSQSTTSDY
CCCCCCCCCCCCCCC
29.1826552605
359PhosphorylationTAEPVSQSTTSDYQW
CCCCCCCCCCCCCCE
26.5827251275
360PhosphorylationAEPVSQSTTSDYQWD
CCCCCCCCCCCCCEE
23.7627251275
361PhosphorylationEPVSQSTTSDYQWDV
CCCCCCCCCCCCEEC
25.5029978859
362PhosphorylationPVSQSTTSDYQWDVS
CCCCCCCCCCCEECC
34.1229978859
364PhosphorylationSQSTTSDYQWDVSRN
CCCCCCCCCEECCCC
15.9828796482
369PhosphorylationSDYQWDVSRNQPYID
CCCCEECCCCCCCCC
24.0429978859
411PhosphorylationWVDEERASLLKSQEP
CCCHHHHHHHHCCCC
40.2228258704
415PhosphorylationERASLLKSQEPIPDD
HHHHHHHCCCCCCCC
39.4825159151
426PhosphorylationIPDDQKVSDDDKEKG
CCCCCCCCCCCCCCC
42.2129255136
439PhosphorylationKGEGALPTGKSKKKK
CCCCCCCCCCCCHHH
59.0824732914
441AcetylationEGALPTGKSKKKKKK
CCCCCCCCCCHHHHH
62.6730585989
451UbiquitinationKKKKKKKKQGEDNST
HHHHHCCCCCCCCCC
72.86-
457PhosphorylationKKQGEDNSTAQDTEE
CCCCCCCCCHHCHHH
37.1228355574
458PhosphorylationKQGEDNSTAQDTEEL
CCCCCCCCHHCHHHH
34.2929255136
462PhosphorylationDNSTAQDTEELEKEI
CCCCHHCHHHHHHHH
21.1930108239
477PhosphorylationREDLPVNTSKTRPKQ
HHHCCCCCCCCCCCC
31.6629255136
478PhosphorylationEDLPVNTSKTRPKQE
HHCCCCCCCCCCCCH
27.1629255136
479AcetylationDLPVNTSKTRPKQEK
HCCCCCCCCCCCCHH
46.6525953088
489PhosphorylationPKQEKAFSLKTISTS
CCCHHCEECEEECCC
33.5424719451
491AcetylationQEKAFSLKTISTSDP
CHHCEECEEECCCCH
42.4825953088
491MethylationQEKAFSLKTISTSDP
CHHCEECEEECCCCH
42.4824659541
491UbiquitinationQEKAFSLKTISTSDP
CHHCEECEEECCCCH
42.4821890473
492PhosphorylationEKAFSLKTISTSDPA
HHCEECEEECCCCHH
26.0030266825
494PhosphorylationAFSLKTISTSDPAEV
CEECEEECCCCHHHH
27.3923401153
495PhosphorylationFSLKTISTSDPAEVL
EECEEECCCCHHHHE
33.0430266825
496O-linked_GlycosylationSLKTISTSDPAEVLV
ECEEECCCCHHHHEE
34.5031373491
496PhosphorylationSLKTISTSDPAEVLV
ECEEECCCCHHHHEE
34.5030266825
506PhosphorylationAEVLVKNSQPIKTLP
HHHEEECCCCCCCCC
31.4529214152
510UbiquitinationVKNSQPIKTLPPATS
EECCCCCCCCCCCCC
51.17-
511PhosphorylationKNSQPIKTLPPATST
ECCCCCCCCCCCCCC
45.2628555341
516O-linked_GlycosylationIKTLPPATSTEPSVI
CCCCCCCCCCCCEEE
41.7931373491
517PhosphorylationKTLPPATSTEPSVIL
CCCCCCCCCCCEEEE
32.6422468782
518PhosphorylationTLPPATSTEPSVILS
CCCCCCCCCCEEEEE
47.7822468782
521PhosphorylationPATSTEPSVILSKSD
CCCCCCCEEEEECCC
18.6328555341
525PhosphorylationTEPSVILSKSDSDKS
CCCEEEEECCCCCCC
20.9928348404
527PhosphorylationPSVILSKSDSDKSSS
CEEEEECCCCCCCCC
38.6830266825
529PhosphorylationVILSKSDSDKSSSQV
EEEECCCCCCCCCCC
54.7726657352
532PhosphorylationSKSDSDKSSSQVPPI
ECCCCCCCCCCCCCH
39.9723663014
533PhosphorylationKSDSDKSSSQVPPIL
CCCCCCCCCCCCCHH
30.4523663014
534PhosphorylationSDSDKSSSQVPPILQ
CCCCCCCCCCCCHHH
42.1423663014
543PhosphorylationVPPILQETDKSKSNT
CCCHHHHCCCCCCCC
35.4523312004
546PhosphorylationILQETDKSKSNTKQN
HHHHCCCCCCCCCCC
44.0921712546
548PhosphorylationQETDKSKSNTKQNSV
HHCCCCCCCCCCCCC
57.7421712546
550PhosphorylationTDKSKSNTKQNSVPP
CCCCCCCCCCCCCCH
40.8921712546
558PhosphorylationKQNSVPPSQTKSETS
CCCCCCHHHCCCCCC
44.40-
560PhosphorylationNSVPPSQTKSETSWE
CCCCHHHCCCCCCCC
40.66-
562PhosphorylationVPPSQTKSETSWESP
CCHHHCCCCCCCCCH
49.8723927012
564PhosphorylationPSQTKSETSWESPKQ
HHHCCCCCCCCCHHH
46.3523927012
565PhosphorylationSQTKSETSWESPKQI
HHCCCCCCCCCHHHH
25.4623927012
568PhosphorylationKSETSWESPKQIKKK
CCCCCCCCHHHHHHH
31.0122167270
570UbiquitinationETSWESPKQIKKKKK
CCCCCCHHHHHHHHH
74.14-
582PhosphorylationKKKARRET-------
HHHHHHCC-------
41.94-

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 LYRIC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYRIC_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 LYRIC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT16_HUMANZBTB16physical
19648967
PLEC_HUMANPLECphysical
22939629
CBP_HUMANCREBBPphysical
18316612
TOPRS_HUMANTOPORSphysical
24529480
CBP_HUMANCREBBPphysical
26141861
SND1_HUMANSND1physical
28514442
ZY11B_HUMANZYG11Bphysical
28514442
JUN_HUMANJUNphysical
27956703
EP300_HUMANEP300physical
27956703

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 LYRIC_HUMAN

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Related Literatures of Post-Translational Modification
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-298; SER-344 ANDSER-369, AND MASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-308 ANDSER-426, AND MASS SPECTROMETRY.
"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-143; SER-298; SER-308;SER-311; SER-426; THR-458 AND SER-568, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-426, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, 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 SER-111; SER-298; SER-308;SER-311; SER-415 AND SER-426, AND MASS SPECTROMETRY.

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