LTN1_HUMAN - dbPTM
LTN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LTN1_HUMAN
UniProt AC O94822
Protein Name E3 ubiquitin-protein ligase listerin
Gene Name LTN1
Organism Homo sapiens (Human).
Sequence Length 1766
Subcellular Localization
Protein Description E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. [PubMed: 23685075]
Protein Sequence MGGKNKQRTKGNLRPSNSGRAAELLAKEQGTVPGFIGFGTSQSDLGYVPAIQGAEEIDSLVDSDFRMVLRKLSKKDVTTKLKAMQEFGTMCTERDTETVKGVLPYWPRIFCKISLDHDRRVREATQQAFEKLILKVKKQLAPYLKSLMGYWLMAQCDTYTPAAFAAKDAFEAAFPPSKQPEAIAFCKDEITSVLQDHLIKETPDTLSDPQTVPEEEREAKFYRVVTCSLLALKRLLCLLPDNELDSLEEKFKSLLSQNKFWKYGKHSVPQIRSAYFELVSALCQRIPQLMKEEASKVSPSVLLSIDDSDPIVCPALWEAVLYTLTTIEDCWLHVNAKKSVFPKLSTVIREGGRGLATVIYPYLLPFISKLPQSITNPKLDFFKNFLTSLVAGLSTERTKTSSLESSAVISAFFECLRFIMQQNLGEEEIEQMLVNDQLIPFIDAVLKDPGLQHGQLFNHLAETLSSWEAKADTEKDEKTAHNLENVLIHFWERLSEICVAKISEPEADVESVLGVSNLLQVLQKPKSSLKSSKKKNGKVRFADEILESNKENEKCVSSEGEKIEGWELTTEPSLTHNSSGLLSPLRKKPLEDLVCKLADISINYVNERKSEQHLRFLSTLLDSFSSSRVFKMLLGDEKQSIVQAKPLEIAKLVQKNPAVQFLYQKLIGWLNEDQRKDFGFLVDILYSALRCCDNDMERKKVLDDLTKVDLKWNSLLKIIEKACPSSDKHALVTPWLKGDILGEKLVNLADCLCNEDLESRVSSESHFSERWTLLSLVLSQHVKNDYLIGDVYVERIIVRLHETLFKTKKLSEAESSDSSVSFICDVAYNYFSSAKGCLLMPSSEDLLLTLFQLCAQSKEKTHLPDFLICKLKNTWLSGVNLLVHQTDSSYKESTFLHLSALWLKNQVQASSLDINSLQVLLSAVDDLLNTLLESEDSYLMGVYIGSVMPNDSEWEKMRQSLPMQWLHRPLLEGRLSLNYECFKTDFKEQDIKTLPSHLCTSALLSKMVLIALRKETVLENNELEKIIAELLYSLQWCEELDNPPIFLIGFCEILQKMNITYDNLRVLGNTSGLLQLLFNRSREHGTLWSLIIAKLILSRSISSDEVKPHYKRKESFFPLTEGNLHTIQSLCPFLSKEEKKEFSAQCIPALLGWTKKDLCSTNGGFGHLAIFNSCLQTKSIDDGELLHGILKIIISWKKEHEDIFLFSCNLSEASPEVLGVNIEIIRFLSLFLKYCSSPLAESEWDFIMCSMLAWLETTSENQALYSIPLVQLFACVSCDLACDLSAFFDSTTLDTIGNLPVNLISEWKEFFSQGIHSLLLPILVTVTGENKDVSETSFQNAMLKPMCETLTYISKEQLLSHKLPARLVADQKTNLPEYLQTLLNTLAPLLLFRARPVQIAVYHMLYKLMPELPQYDQDNLKSYGDEEEEPALSPPAALMSLLSIQEDLLENVLGCIPVGQIVTIKPLSEDFCYVLGYLLTWKLILTFFKAASSQLRALYSMYLRKTKSLNKLLYHLFRLMPENPTYAETAVEVPNKDPKTFFTEELQLSIRETTMLPYHIPHLACSVYHMTLKDLPAMVRLWWNSSEKRVFNIVDRFTSKYVSSVLSFQEISSVQTSTQLFNGMTVKARATTREVMATYTIEDIVIELIIQLPSNYPLGSIIVESGKRVGVAVQQWRNWMLQLSTYLTHQNGSIMEGLALWKNNVDKRFEGVEDCMICFSVIHGFNYSLPKKACRTCKKKFHSACLYKWFTSSNKSTCPLCRETFF
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
13PhosphorylationKQRTKGNLRPSNSGR
CCCCCCCCCCCCHHH
13.3620068231
13 (in isoform 3)Phosphorylation-13.3620068231
14PhosphorylationQRTKGNLRPSNSGRA
CCCCCCCCCCCHHHH
36.2820068231
14 (in isoform 3)Phosphorylation-36.2820068231
15PhosphorylationRTKGNLRPSNSGRAA
CCCCCCCCCCHHHHH
40.8220068231
15 (in isoform 3)Phosphorylation-40.8220068231
16PhosphorylationTKGNLRPSNSGRAAE
CCCCCCCCCHHHHHH
36.8729514088
18PhosphorylationGNLRPSNSGRAAELL
CCCCCCCHHHHHHHH
33.7120068231
18 (in isoform 3)Phosphorylation-33.7120068231
19 (in isoform 3)Phosphorylation-27.7420068231
20MethylationLRPSNSGRAAELLAK
CCCCCHHHHHHHHHH
30.37115920437
20 (in isoform 3)Phosphorylation-30.3720068231
26UbiquitinationGRAAELLAKEQGTVP
HHHHHHHHHHCCCCC
26.4321890473
64PhosphorylationIDSLVDSDFRMVLRK
HHHHCCCCHHHHHHH
30.61-
66MethylationSLVDSDFRMVLRKLS
HHCCCCHHHHHHHHC
21.20-
89PhosphorylationKAMQEFGTMCTERDT
HHHHHHHCCCCCCCH
17.8829449344
92PhosphorylationQEFGTMCTERDTETV
HHHHCCCCCCCHHHH
24.1929449344
96PhosphorylationTMCTERDTETVKGVL
CCCCCCCHHHHCCCC
39.5129449344
98PhosphorylationCTERDTETVKGVLPY
CCCCCHHHHCCCCCC
29.6129449344
126UbiquitinationRRVREATQQAFEKLI
HHHHHHHHHHHHHHH
39.39-
177UbiquitinationFEAAFPPSKQPEAIA
HHHHCCCCCCCHHHH
44.13-
191PhosphorylationAFCKDEITSVLQDHL
HCCHHHHHHHHHHHH
15.6720873877
192PhosphorylationFCKDEITSVLQDHLI
CCHHHHHHHHHHHHC
26.8820873877
224UbiquitinationREAKFYRVVTCSLLA
HHHHHHHHHHHHHHH
2.59-
228PhosphorylationFYRVVTCSLLALKRL
HHHHHHHHHHHHHHH
19.6325003641
233UbiquitinationTCSLLALKRLLCLLP
HHHHHHHHHHHHHCC
35.08-
246PhosphorylationLPDNELDSLEEKFKS
CCCCHHHHHHHHHHH
50.7523401153
246UbiquitinationLPDNELDSLEEKFKS
CCCCHHHHHHHHHHH
50.75-
259AcetylationKSLLSQNKFWKYGKH
HHHHHCCCHHHHCCC
44.9919608861
262AcetylationLSQNKFWKYGKHSVP
HHCCCHHHHCCCCHH
47.4619608861
276UbiquitinationPQIRSAYFELVSALC
HHHHHHHHHHHHHHH
6.1422817900
281UbiquitinationAYFELVSALCQRIPQ
HHHHHHHHHHHHHHH
12.6021890473
296UbiquitinationLMKEEASKVSPSVLL
HHHHHHHCCCHHHEE
54.50-
298UbiquitinationKEEASKVSPSVLLSI
HHHHHCCCHHHEEEC
18.39-
305AcetylationSPSVLLSIDDSDPIV
CHHHEEECCCCCCCC
7.4219608861
305UbiquitinationSPSVLLSIDDSDPIV
CHHHEEECCCCCCCC
7.4219608861
308AcetylationVLLSIDDSDPIVCPA
HEEECCCCCCCCCHH
41.3519608861
349UbiquitinationPKLSTVIREGGRGLA
HHHHHHHCCCCCCHH
31.9721890473
362UbiquitinationLATVIYPYLLPFISK
HHHHHHHHHHHHHHC
12.1421890473
366UbiquitinationIYPYLLPFISKLPQS
HHHHHHHHHHCCCCC
11.2622817900
387PhosphorylationDFFKNFLTSLVAGLS
HHHHHHHHHHHHHCC
18.8425690035
394PhosphorylationTSLVAGLSTERTKTS
HHHHHHCCCCCCCCC
27.5725690035
424UbiquitinationRFIMQQNLGEEEIEQ
HHHHHCCCCHHHHHH
8.75-
425UbiquitinationFIMQQNLGEEEIEQM
HHHHCCCCHHHHHHH
48.0622817900
428UbiquitinationQQNLGEEEIEQMLVN
HCCCCHHHHHHHHHH
47.7421890473
429UbiquitinationQNLGEEEIEQMLVND
CCCCHHHHHHHHHHC
5.1521890473
432UbiquitinationGEEEIEQMLVNDQLI
CHHHHHHHHHHCCHH
2.6822817900
448UbiquitinationFIDAVLKDPGLQHGQ
HHHHHHCCCCCCHHH
38.0421890473
516UbiquitinationVESVLGVSNLLQVLQ
HHHHHCHHHHHHHHH
21.69-
524UbiquitinationNLLQVLQKPKSSLKS
HHHHHHHCCHHHCCC
50.6929967540
570UbiquitinationIEGWELTTEPSLTHN
ECCEEECCCCCCCCC
59.53-
573PhosphorylationWELTTEPSLTHNSSG
EEECCCCCCCCCCCC
39.4028348404
575PhosphorylationLTTEPSLTHNSSGLL
ECCCCCCCCCCCCCC
24.2925627689
578PhosphorylationEPSLTHNSSGLLSPL
CCCCCCCCCCCCCCC
20.4125627689
579PhosphorylationPSLTHNSSGLLSPLR
CCCCCCCCCCCCCCC
38.4825627689
583PhosphorylationHNSSGLLSPLRKKPL
CCCCCCCCCCCCCCH
27.2525159151
596UbiquitinationPLEDLVCKLADISIN
CHHHHHHHHHHCCCE
38.95-
618PhosphorylationEQHLRFLSTLLDSFS
HHHHHHHHHHHHHHC
17.81-
619PhosphorylationQHLRFLSTLLDSFSS
HHHHHHHHHHHHHCC
33.22-
629PhosphorylationDSFSSSRVFKMLLGD
HHHCCHHHHHHHHCC
6.13-
633UbiquitinationSSRVFKMLLGDEKQS
CHHHHHHHHCCCCHH
5.08-
638UbiquitinationKMLLGDEKQSIVQAK
HHHHCCCCHHHHHCC
54.8321890473
644UbiquitinationEKQSIVQAKPLEIAK
CCHHHHHCCHHHHHH
12.4421890473
645UbiquitinationKQSIVQAKPLEIAKL
CHHHHHCCHHHHHHH
32.80-
651UbiquitinationAKPLEIAKLVQKNPA
CCHHHHHHHHHHCHH
55.6521890473
684UbiquitinationDFGFLVDILYSALRC
CHHHHHHHHHHHHHH
2.7921890473
697UbiquitinationRCCDNDMERKKVLDD
HHCCCHHHHHHHHHH
65.3021890473
698UbiquitinationCCDNDMERKKVLDDL
HCCCHHHHHHHHHHH
37.1422817900
701UbiquitinationNDMERKKVLDDLTKV
CHHHHHHHHHHHHHC
8.7622817900
703UbiquitinationMERKKVLDDLTKVDL
HHHHHHHHHHHHCCH
52.4321890473
706O-linked_GlycosylationKKVLDDLTKVDLKWN
HHHHHHHHHCCHHHH
35.7028510447
711UbiquitinationDLTKVDLKWNSLLKI
HHHHCCHHHHHHHHH
39.6132015554
714PhosphorylationKVDLKWNSLLKIIEK
HCCHHHHHHHHHHHH
33.6824719451
717UbiquitinationLKWNSLLKIIEKACP
HHHHHHHHHHHHHCC
47.1021890473
737UbiquitinationALVTPWLKGDILGEK
CCCCCCCCCCHHHHH
51.1521890473
744UbiquitinationKGDILGEKLVNLADC
CCCHHHHHHHHHHHH
56.81-
746UbiquitinationDILGEKLVNLADCLC
CHHHHHHHHHHHHHC
9.04-
753UbiquitinationVNLADCLCNEDLESR
HHHHHHHCCCCHHHH
7.05-
757UbiquitinationDCLCNEDLESRVSSE
HHHCCCCHHHHHCCC
5.40-
762PhosphorylationEDLESRVSSESHFSE
CCHHHHHCCCCHHHH
27.5525841592
763PhosphorylationDLESRVSSESHFSER
CHHHHHCCCCHHHHH
40.0225841592
763UbiquitinationDLESRVSSESHFSER
CHHHHHCCCCHHHHH
40.0221890473
765PhosphorylationESRVSSESHFSERWT
HHHHCCCCHHHHHHH
31.6025841592
767UbiquitinationRVSSESHFSERWTLL
HHCCCCHHHHHHHHH
12.9722817900
768PhosphorylationVSSESHFSERWTLLS
HCCCCHHHHHHHHHH
22.3425841592
769UbiquitinationSSESHFSERWTLLSL
CCCCHHHHHHHHHHH
51.8221890473
774UbiquitinationFSERWTLLSLVLSQH
HHHHHHHHHHHHHHH
2.66-
783UbiquitinationLVLSQHVKNDYLIGD
HHHHHHHCCCEECCC
41.8121890473
847UbiquitinationMPSSEDLLLTLFQLC
CCCCHHHHHHHHHHH
5.4822817900
850UbiquitinationSEDLLLTLFQLCAQS
CHHHHHHHHHHHHHC
2.3122817900
851UbiquitinationEDLLLTLFQLCAQSK
HHHHHHHHHHHHHCC
4.3721890473
906UbiquitinationSALWLKNQVQASSLD
HHHHHHCCCCCCCCC
27.41-
992UbiquitinationDFKEQDIKTLPSHLC
CCCCCCHHHHCHHHH
52.9121890473
1019UbiquitinationLRKETVLENNELEKI
HCCCHHHCCCHHHHH
54.3922817900
1024UbiquitinationVLENNELEKIIAELL
HHCCCHHHHHHHHHH
35.7121890473
1033UbiquitinationIIAELLYSLQWCEEL
HHHHHHHHHHHHHHC
17.6622817900
1038UbiquitinationLYSLQWCEELDNPPI
HHHHHHHHHCCCCCE
59.6521890473
1066UbiquitinationITYDNLRVLGNTSGL
CCCCCEEECCCHHHH
10.1421890473
1100PhosphorylationAKLILSRSISSDEVK
HHHHHHCCCCCCCCC
24.36-
1140UbiquitinationFLSKEEKKEFSAQCI
CCCHHHHHHHHHHHH
68.2421890473
1168UbiquitinationTNGGFGHLAIFNSCL
CCCCCCHHEHHHCCC
3.9122817900
1171UbiquitinationGFGHLAIFNSCLQTK
CCCHHEHHHCCCCCC
4.5922817900
1172UbiquitinationFGHLAIFNSCLQTKS
CCHHEHHHCCCCCCC
26.2121890473
1182UbiquitinationLQTKSIDDGELLHGI
CCCCCCCCCHHHHHH
51.2822817900
1185UbiquitinationKSIDDGELLHGILKI
CCCCCCHHHHHHHHH
5.3822817900
1186UbiquitinationSIDDGELLHGILKII
CCCCCHHHHHHHHHH
2.7921890473
1336O-linked_GlycosylationENKDVSETSFQNAML
CCCCCCHHHHHHHHH
27.6028510447
1337O-linked_GlycosylationNKDVSETSFQNAMLK
CCCCCHHHHHHHHHH
22.3028510447
1355UbiquitinationETLTYISKEQLLSHK
HHHHHCCHHHHHCCC
39.6621890473
1387UbiquitinationQTLLNTLAPLLLFRA
HHHHHHHHHHHHHHC
7.2321890473
1401UbiquitinationARPVQIAVYHMLYKL
CCCHHHHHHHHHHHH
3.4421890473
1408UbiquitinationVYHMLYKLMPELPQY
HHHHHHHHCCCCCCC
4.35-
1499PhosphorylationSSQLRALYSMYLRKT
HHHHHHHHHHHHHHC
7.1523663014
1500PhosphorylationSQLRALYSMYLRKTK
HHHHHHHHHHHHHCH
11.2023663014
1502PhosphorylationLRALYSMYLRKTKSL
HHHHHHHHHHHCHHH
9.4523663014
1612PhosphorylationVLSFQEISSVQTSTQ
HHCHHHHCCCCCCCH
24.5722210691
1616PhosphorylationQEISSVQTSTQLFNG
HHHCCCCCCCHHHCC
31.4222210691
1617PhosphorylationEISSVQTSTQLFNGM
HHCCCCCCCHHHCCC
9.3222210691
1747PhosphorylationKFHSACLYKWFTSSN
HCHHHHHHHHHHCCC
13.1725159151
1755UbiquitinationKWFTSSNKSTCPLCR
HHHHCCCCCCCCCCH
49.44-
1786Ubiquitination---------------------------
---------------------------
-
1793Phosphorylation----------------------------------
----------------------------------
-
1801Ubiquitination------------------------------------------
------------------------------------------
-

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 LTN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LTN1_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 LTN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
19196968
UB2D2_HUMANUBE2D2physical
19196968
DHCR7_HUMANDHCR7physical
26496610
FEN1_HUMANFEN1physical
26496610
HEMO_HUMANHPXphysical
26496610
KIF2A_HUMANKIF2Aphysical
26496610
NPAT_HUMANNPATphysical
26496610
SP100_HUMANSP100physical
26496610
TAP1_HUMANTAP1physical
26496610
CTDP1_HUMANCTDP1physical
26496610
PLD3_HUMANPLD3physical
26496610
CHM2B_HUMANCHMP2Bphysical
26496610
CLSPN_HUMANCLSPNphysical
26496610
CEP97_HUMANCEP97physical
26496610
ILKAP_HUMANILKAPphysical
26496610
PNPT1_HUMANPNPT1physical
26496610
KI18B_HUMANKIF18Bphysical
26496610
TET3_HUMANTET3physical
26496610
SC61B_HUMANSEC61Bphysical
25877867
SSRA_HUMANSSR1physical
25877867
RL6_HUMANRPL6physical
25877867

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 LTN1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-259, AND MASS SPECTROMETRY.

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