T131L_HUMAN - dbPTM
T131L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T131L_HUMAN
UniProt AC A2VDJ0
Protein Name Transmembrane protein 131-like {ECO:0000312|HGNC:HGNC:29146}
Gene Name TMEM131L {ECO:0000312|HGNC:HGNC:29146}
Organism Homo sapiens (Human).
Sequence Length 1609
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cytoplasm . During intrathymic development, resides in punctate cytoplasmic structures in DN1 and DN2 cells. In DN3 cells, found in large crescent-shaped membrane structures, which preferentially
Protein Description Isoform 1: Membrane-associated form that antagonizes canonical Wnt signaling by triggering lysosome-dependent degradation of Wnt-activated LRP6. Regulates thymocyte proliferation..
Protein Sequence MAGLRRPQPGCYCRTAAAVNLLLGVFQVLLPCCRPGGAQGQAIEPLPNVVELWQAEEGELLLPTQGDSEEGLEEPSQEQSFSDKLFSGKGLHFQPSVLDFGIQFLGHPVAKILHAYNPSRDSEVVVNSVFAAAGHFHVPPVPCRVIPAMGKTSFRIIFLPTEEGSIESSLFINTSSYGVLSYHVSGIGTRRISTEGSAKQLPNAYFLLPKVQSIQLSQMQAETTNTSLLQVQLECSLHNKVCQQLKGCYLESDDVLRLQMSIMVTMENFSKEFEENTQHLLDHLSIVYVATDESETSDDSAVNMYILHSGNSLIWIQDIRHFSQRDALSLQFEPVLLPTSTTNFTKIASFTCKATSCDSGIIEDVKKTTHTPTLKACLFSSVAQGYFRMDSSATQFHIETHENTSGLWSIWYRNHFDRSVVLNDVFLSKETKHMLKILNFTGPLFLPPGCWNIFSLKLAVKDIAINLFTNVFLTTNIGAIFAIPLQIYSAPTKEGSLGFEVIAHCGMHYFMGKSKAGNPNWNGSLSLDQSTWNVDSELANKLYERWKKYKNGDVCKRNVLGTTRFAHLKKSKESESFVFFLPRLIAEPGLMLNFSATALRSRMIKYFVVQNPSSWPVSLQLLPLSLYPKPEALVHLLHRWFGTDMQMINFTTGEFQLTEACPYLGTHSEESRFGILHLHLQPLEMKRVGVVFTPADYGKVTSLILIRNNLTVIDMIGVEGFGARELLKVGGRLPGAGGSLRFKVPESTLMDCRRQLKDSKQILSITKNFKVENIGPLPITVSSLKINGYNCQGYGFEVLDCHQFSLDPNTSRDISIVFTPDFTSSWVIRDLSLVTAADLEFRFTLNVTLPHHLLPLCADVVPGPSWEESFWRLTVFFVSLSLLGVILIAFQQAQYILMEFMKTRQRQNASSSSQQNNGPMDVISPHSYKSNCKNFLDTYGPSDKGRGKNCLPVNTPQSRIQNAAKRSPATYGHSQKKHKCSVYYSKHKTSTAAASSTSTTTEEKQTSPLGSSLPAAKEDICTDAMRENWISLRYASGINVNLQKNLTLPKNLLNKEENTLKNTIVFSNPSSECSMKEGIQTCMFPKETDIKTSENTAEFKERELCPLKTSKKLPENHLPRNSPQYHQPDLPEISRKNNGNNQQVPVKNEVDHCENLKKVDTKPSSEKKIHKTSREDMFSEKQDIPFVEQEDPYRKKKLQEKREGNLQNLNWSKSRTCRKNKKRGVAPVSRPPEQSDLKLVCSDFERSELSSDINVRSWCIQESTREVCKADAEIASSLPAAQREAEGYYQKPEKKCVDKFCSDSSSDCGSSSGSVRASRGSWGSWSSTSSSDGDKKPMVDAQHFLPAGDSVSQNDFPSEAPISLNLSHNICNPMTVNSLPQYAEPSCPSLPAGPTGVEEDKGLYSPGDLWPTPPVCVTSSLNCTLENGVPCVIQESAPVHNSFIDWSATCEGQFSSAYCPLELNDYNAFPEENMNYANGFPCPADVQTDFIDHNSQSTWNTPPNMPAAWGHASFISSPPYLTSTRSLSPMSGLFGSIWAPQSDVYENCCPINPTTEHSTHMENQAVVCKEYYPGFNPFRAYMNLDIWTTTANRNANFPLSRDSSYCGNV
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
12PhosphorylationRRPQPGCYCRTAAAV
CCCCCCCCHHHHHHH
7.29-
122PhosphorylationAYNPSRDSEVVVNSV
HHCCCCCCCHHHHHH
31.05-
151UbiquitinationRVIPAMGKTSFRIIF
EEECCCCCCEEEEEE
28.10-
199UbiquitinationISTEGSAKQLPNAYF
ECCCCCHHHCCCEEE
54.81-
246UbiquitinationNKVCQQLKGCYLESD
HHHHHHCCCCCCCCC
42.47-
343N-linked_GlycosylationLLPTSTTNFTKIASF
ECCCCCCCCEEEEEE
42.55UniProtKB CARBOHYD
353UbiquitinationKIASFTCKATSCDSG
EEEEEEECCCCCCCC
52.20-
353 (in isoform 3)Ubiquitination-52.20-
353 (in isoform 5)Ubiquitination-52.20-
366UbiquitinationSGIIEDVKKTTHTPT
CCCCCCHHHHCCCCH
57.64-
367 (in isoform 3)Ubiquitination-59.51-
367 (in isoform 5)Ubiquitination-59.51-
368PhosphorylationIIEDVKKTTHTPTLK
CCCCHHHHCCCCHHH
20.35-
368 (in isoform 3)Ubiquitination-20.35-
368 (in isoform 5)Ubiquitination-20.35-
369PhosphorylationIEDVKKTTHTPTLKA
CCCHHHHCCCCHHHH
32.41-
371PhosphorylationDVKKTTHTPTLKACL
CHHHHCCCCHHHHHH
18.84-
373PhosphorylationKKTTHTPTLKACLFS
HHHCCCCHHHHHHHH
41.88-
439N-linked_GlycosylationKHMLKILNFTGPLFL
HHHHHHHHCCCCCCC
35.59UniProtKB CARBOHYD
492PhosphorylationLQIYSAPTKEGSLGF
EEEEECCCCCCCCCH
41.25-
509PhosphorylationIAHCGMHYFMGKSKA
EECCCCEECCCCCCC
6.08-
522N-linked_GlycosylationKAGNPNWNGSLSLDQ
CCCCCCCCCCCCCCC
36.49UniProtKB CARBOHYD
547AcetylationNKLYERWKKYKNGDV
HHHHHHHHHHCCCCC
53.0720167786
569AcetylationTTRFAHLKKSKESES
CCCCCHHCCCCCCCC
45.1720167786
572UbiquitinationFAHLKKSKESESFVF
CCHHCCCCCCCCCEE
74.31-
574PhosphorylationHLKKSKESESFVFFL
HHCCCCCCCCCEEHH
42.1326699800
576PhosphorylationKKSKESESFVFFLPR
CCCCCCCCCEEHHHH
35.6726699800
593N-linked_GlycosylationAEPGLMLNFSATALR
CCCCEECCCCHHHHH
18.18UniProtKB CARBOHYD
614PhosphorylationFVVQNPSSWPVSLQL
EEEECCCCCCEEEEE
36.3323917254
618PhosphorylationNPSSWPVSLQLLPLS
CCCCCCEEEEEEEHH
13.3023917254
625PhosphorylationSLQLLPLSLYPKPEA
EEEEEEHHHCCCHHH
24.7423917254
627PhosphorylationQLLPLSLYPKPEALV
EEEEHHHCCCHHHHH
13.0623917254
686UbiquitinationHLQPLEMKRVGVVFT
ECCCCCCCEEEEEEC
34.26-
699UbiquitinationFTPADYGKVTSLILI
ECHHHHCCEEEEEEE
35.79-
702PhosphorylationADYGKVTSLILIRNN
HHHCCEEEEEEEECC
19.1924719451
709N-linked_GlycosylationSLILIRNNLTVIDMI
EEEEEECCCEEEECC
27.52UniProtKB CARBOHYD
728UbiquitinationFGARELLKVGGRLPG
CCHHHHHHCCCCCCC
52.00-
729 (in isoform 5)Ubiquitination-11.23-
743UbiquitinationAGGSLRFKVPESTLM
CCCCCEEECCHHHHH
50.90-
757UbiquitinationMDCRRQLKDSKQILS
HHHHHHHCCHHHHHH
52.17-
760UbiquitinationRRQLKDSKQILSITK
HHHHCCHHHHHHHCC
52.03-
764PhosphorylationKDSKQILSITKNFKV
CCHHHHHHHCCCEEE
29.8224719451
767UbiquitinationKQILSITKNFKVENI
HHHHHHCCCEEEEEC
59.73-
770UbiquitinationLSITKNFKVENIGPL
HHHCCCEEEEECCCC
59.02-
846N-linked_GlycosylationLEFRFTLNVTLPHHL
EEEEEEEEEECCCHH
22.97UniProtKB CARBOHYD
903PhosphorylationILMEFMKTRQRQNAS
HHHHHHHHHHHHHCC
21.9022210691
933AcetylationHSYKSNCKNFLDTYG
CHHHHCCCCHHHHCC
55.7919820777
933UbiquitinationHSYKSNCKNFLDTYG
CHHHHCCCCHHHHCC
55.79-
938PhosphorylationNCKNFLDTYGPSDKG
CCCCHHHHCCCCCCC
32.3128796482
939PhosphorylationCKNFLDTYGPSDKGR
CCCHHHHCCCCCCCC
27.0628796482
940PhosphorylationKNFLDTYGPSDKGRG
CCHHHHCCCCCCCCC
19.8227642862
942PhosphorylationFLDTYGPSDKGRGKN
HHHHCCCCCCCCCCC
47.8228796482
944UbiquitinationDTYGPSDKGRGKNCL
HHCCCCCCCCCCCCC
55.64-
955PhosphorylationKNCLPVNTPQSRIQN
CCCCCCCCCHHHHHH
23.9625159151
967PhosphorylationIQNAAKRSPATYGHS
HHHHHHHCCCCCCCC
20.4129978859
970PhosphorylationAAKRSPATYGHSQKK
HHHHCCCCCCCCCCC
33.1629978859
971PhosphorylationAKRSPATYGHSQKKH
HHHCCCCCCCCCCCE
18.2329978859
972PhosphorylationKRSPATYGHSQKKHK
HHCCCCCCCCCCCEE
15.0427642862
974PhosphorylationSPATYGHSQKKHKCS
CCCCCCCCCCCEECE
39.0529978859
981PhosphorylationSQKKHKCSVYYSKHK
CCCCEECEEEECCCC
20.25-
983PhosphorylationKKHKCSVYYSKHKTS
CCEECEEEECCCCCC
5.92-
989PhosphorylationVYYSKHKTSTAAASS
EEECCCCCCCCCCCC
30.91-
990PhosphorylationYYSKHKTSTAAASST
EECCCCCCCCCCCCC
22.35-
991PhosphorylationYSKHKTSTAAASSTS
ECCCCCCCCCCCCCC
26.08-
1004UbiquitinationTSTTTEEKQTSPLGS
CCCCCCCCCCCCCCC
53.28-
1007PhosphorylationTTEEKQTSPLGSSLP
CCCCCCCCCCCCCCC
18.6825159151
1017UbiquitinationGSSLPAAKEDICTDA
CCCCCCHHHHHCCHH
59.01-
1022PhosphorylationAAKEDICTDAMRENW
CHHHHHCCHHHHHCH
27.4228674151
1036PhosphorylationWISLRYASGINVNLQ
HHHEEECCCCCCEEC
31.1328555341
1044UbiquitinationGINVNLQKNLTLPKN
CCCCEECCCCCCCHH
58.03-
1055UbiquitinationLPKNLLNKEENTLKN
CCHHHCCCCCCCCCC
67.39-
1059PhosphorylationLLNKEENTLKNTIVF
HCCCCCCCCCCEEEE
42.25-
1076UbiquitinationPSSECSMKEGIQTCM
CCCCCCCCCCCCCCC
36.17-
1092PhosphorylationPKETDIKTSENTAEF
CCCCCCCCCCCCHHH
41.4229449344
1093PhosphorylationKETDIKTSENTAEFK
CCCCCCCCCCCHHHH
24.6929449344
1096PhosphorylationDIKTSENTAEFKERE
CCCCCCCCHHHHHHH
24.4229449344
1112UbiquitinationCPLKTSKKLPENHLP
CCCCCCCCCCCCCCC
69.87-
1122PhosphorylationENHLPRNSPQYHQPD
CCCCCCCCCCCCCCC
18.0525159151
1123PhosphorylationNHLPRNSPQYHQPDL
CCCCCCCCCCCCCCC
42.1527642862
1125PhosphorylationLPRNSPQYHQPDLPE
CCCCCCCCCCCCCHH
13.0528796482
1126PhosphorylationPRNSPQYHQPDLPEI
CCCCCCCCCCCCHHH
27.7027642862
1212PhosphorylationNLQNLNWSKSRTCRK
CCCCCCCCCCHHHCC
21.4925159151
1242PhosphorylationSDLKLVCSDFERSEL
CCCEEEECHHCHHHC
37.54-
1269UbiquitinationESTREVCKADAEIAS
HHHHHHHHHHHHHHH
55.25-
1276PhosphorylationKADAEIASSLPAAQR
HHHHHHHHCCCHHHH
37.7623322592
1277PhosphorylationADAEIASSLPAAQRE
HHHHHHHCCCHHHHH
29.3829978859
1288PhosphorylationAQREAEGYYQKPEKK
HHHHHCCCCCCCCCH
8.3328796482
1289PhosphorylationQREAEGYYQKPEKKC
HHHHCCCCCCCCCHH
22.4028796482
1290PhosphorylationREAEGYYQKPEKKCV
HHHCCCCCCCCCHHH
46.4727642862
1302PhosphorylationKCVDKFCSDSSSDCG
HHHHHHCCCCCCCCC
43.5926471730
1304PhosphorylationVDKFCSDSSSDCGSS
HHHHCCCCCCCCCCC
18.5627251275
1305PhosphorylationDKFCSDSSSDCGSSS
HHHCCCCCCCCCCCC
34.8827251275
1306PhosphorylationKFCSDSSSDCGSSSG
HHCCCCCCCCCCCCC
40.6526471730
1307PhosphorylationFCSDSSSDCGSSSGS
HCCCCCCCCCCCCCC
42.6227251275
1310PhosphorylationDSSSDCGSSSGSVRA
CCCCCCCCCCCCCEE
27.8826471730
1311PhosphorylationSSSDCGSSSGSVRAS
CCCCCCCCCCCCEEC
24.8127251275
1312PhosphorylationSSDCGSSSGSVRASR
CCCCCCCCCCCEECC
36.4627251275
1321PhosphorylationSVRASRGSWGSWSST
CCEECCCCCCCCCCC
27.4425159151
1324PhosphorylationASRGSWGSWSSTSSS
ECCCCCCCCCCCCCC
19.9519690332
1327PhosphorylationGSWGSWSSTSSSDGD
CCCCCCCCCCCCCCC
26.50-
1328PhosphorylationSWGSWSSTSSSDGDK
CCCCCCCCCCCCCCC
27.4119690332
1330PhosphorylationGSWSSTSSSDGDKKP
CCCCCCCCCCCCCCC
32.3219690332
1331PhosphorylationSWSSTSSSDGDKKPM
CCCCCCCCCCCCCCC
45.4319690332
1524PhosphorylationSPPYLTSTRSLSPMS
CCCCCCCCCCCCCCC
21.0226074081
1526PhosphorylationPYLTSTRSLSPMSGL
CCCCCCCCCCCCCCC
33.0326074081
1528PhosphorylationLTSTRSLSPMSGLFG
CCCCCCCCCCCCCCC
21.5826074081
1571PhosphorylationQAVVCKEYYPGFNPF
CEEEECCCCCCCCHH
10.6428796482
1572PhosphorylationAVVCKEYYPGFNPFR
EEEECCCCCCCCHHH
9.6628796482
1600PhosphorylationRNANFPLSRDSSYCG
CCCCCCCCCCCCCCC
33.9930108239

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 T131L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T131L_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 T131L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of T131L_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 T131L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-1122, AND MASSSPECTROMETRY.

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