SYLM_HUMAN - dbPTM
SYLM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYLM_HUMAN
UniProt AC Q15031
Protein Name Probable leucine--tRNA ligase, mitochondrial
Gene Name LARS2
Organism Homo sapiens (Human).
Sequence Length 903
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MASVWQRLGFYASLLKRQLNGGPDVIKWERRVIPGCTRSIYSATGKWTKEYTLQTRKDVEKWWHQRIKEQASKISEADKSKPKFYVLSMFPYPSGKLHMGHVRVYTISDTIARFQKMRGMQVINPMGWDAFGLPAENAAVERNLHPQSWTQSNIKHMRKQLDRLGLCFSWDREITTCLPDYYKWTQYLFIKLYEAGLAYQKEALVNWDPVDQTVLANEQVDEHGCSWRSGAKVEQKYLRQWFIKTTAYAKAMQDALADLPEWYGIKGMQAHWIGDCVGCHLDFTLKVHGQATGEKLTAYTATPEAIYGTSHVAISPSHRLLHGHSSLKEALRMALVPGKDCLTPVMAVNMLTQQEVPVVILAKADLEGSLDSKIGIPSTSSEDTILAQTLGLAYSEVIETLPDGTERLSSSAEFTGMTRQDAFLALTQKARGKRVGGDVTSDKLKDWLISRQRYWGTPIPIVHCPVCGPTPVPLEDLPVTLPNIASFTGKGGPPLAMASEWVNCSCPRCKGAAKRETDTMDTFVDSAWYYFRYTDPHNPHSPFNTAVADYWMPVDLYIGGKEHAVMHLFYARFFSHFCHDQKMVKHREPFHKLLAQGLIKGQTFRLPSGQYLQREEVDLTGSVPVHAKTKEKLEVTWEKMSKSKHNGVDPEEVVEQYGIDTIRLYILFAAPPEKDILWDVKTDALPGVLRWQQRLWTLTTRFIEARASGKSPQPQLLSNKEKAEARKLWEYKNSVISQVTTHFTEDFSLNSAISQLMGLSNALSQASQSVILHSPEFEDALCALMVMAAPLAPHVTSEIWAGLALVPRKLCAHYTWDASVLLQAWPAVDPEFLQQPEVVQMAVLINNKACGKIPVPQQVARDQDKVHEFVLQSELGVRLLQGRSIKKSFLSPRTALINFLVQD
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
13PhosphorylationQRLGFYASLLKRQLN
HHHHHHHHHHHHHHC
23.9024719451
39PhosphorylationVIPGCTRSIYSATGK
CCCCCCCCHHHHCCC
14.02-
41PhosphorylationPGCTRSIYSATGKWT
CCCCCCHHHHCCCCE
8.10-
42PhosphorylationGCTRSIYSATGKWTK
CCCCCHHHHCCCCEE
20.06-
44PhosphorylationTRSIYSATGKWTKEY
CCCHHHHCCCCEEEE
33.1024719451
52PhosphorylationGKWTKEYTLQTRKDV
CCCEEEEEECCHHHH
17.3024719451
68AcetylationKWWHQRIKEQASKIS
HHHHHHHHHHHHHHC
46.06-
85PhosphorylationDKSKPKFYVLSMFPY
HHCCCCEEEEEECCC
13.4520058876
88PhosphorylationKPKFYVLSMFPYPSG
CCCEEEEEECCCCCC
14.3420058876
108PhosphorylationHVRVYTISDTIARFQ
EEEEEEEHHHHHHHH
22.39-
110PhosphorylationRVYTISDTIARFQKM
EEEEEHHHHHHHHHH
15.11-
155AcetylationSWTQSNIKHMRKQLD
CCCHHHHHHHHHHHH
35.2825953088
155SuccinylationSWTQSNIKHMRKQLD
CCCHHHHHHHHHHHH
35.2823954790
155MalonylationSWTQSNIKHMRKQLD
CCCHHHHHHHHHHHH
35.2826320211
199PhosphorylationLYEAGLAYQKEALVN
HHHHCCCHHHHHHCC
25.7625159151
232UbiquitinationCSWRSGAKVEQKYLR
CCCCCCCCHHHHHHH
50.2424816145
236AcetylationSGAKVEQKYLRQWFI
CCCCHHHHHHHHHHH
32.5219608861
315PhosphorylationGTSHVAISPSHRLLH
CCCCEEECCCHHHHC
15.60-
328AcetylationLHGHSSLKEALRMAL
HCCCCCHHHHHHHHH
42.7823236377
343PhosphorylationVPGKDCLTPVMAVNM
CCCCCCCCHHHHHHC
21.84-
352PhosphorylationVMAVNMLTQQEVPVV
HHHHHCCCCCCCCEE
19.89-
369PhosphorylationAKADLEGSLDSKIGI
EECCCCCCCCCCCCC
21.4521406692
372PhosphorylationDLEGSLDSKIGIPST
CCCCCCCCCCCCCCC
31.3121406692
409PhosphorylationPDGTERLSSSAEFTG
CCCCCCCCCCCCCCC
28.5922210691
410PhosphorylationDGTERLSSSAEFTGM
CCCCCCCCCCCCCCC
37.8526852163
411PhosphorylationGTERLSSSAEFTGMT
CCCCCCCCCCCCCCC
28.5726852163
415PhosphorylationLSSSAEFTGMTRQDA
CCCCCCCCCCCHHHH
19.9726852163
418PhosphorylationSAEFTGMTRQDAFLA
CCCCCCCCHHHHHHH
26.9026852163
427PhosphorylationQDAFLALTQKARGKR
HHHHHHHHHHHCCCC
23.5522210691
429UbiquitinationAFLALTQKARGKRVG
HHHHHHHHHCCCCCC
34.5130230243
445UbiquitinationDVTSDKLKDWLISRQ
CCCHHHHHHHHHHCC
53.23-
450PhosphorylationKLKDWLISRQRYWGT
HHHHHHHHCCCCCCC
21.8623898821
517PhosphorylationKGAAKRETDTMDTFV
CCCCCCCCCCHHHHH
40.5825907765
519PhosphorylationAAKRETDTMDTFVDS
CCCCCCCCHHHHHHH
25.1125907765
522PhosphorylationRETDTMDTFVDSAWY
CCCCCHHHHHHHCHH
18.0925907765
526PhosphorylationTMDTFVDSAWYYFRY
CHHHHHHHCHHHCCC
18.5225907765
529PhosphorylationTFVDSAWYYFRYTDP
HHHHHCHHHCCCCCC
7.7625907765
530PhosphorylationFVDSAWYYFRYTDPH
HHHHCHHHCCCCCCC
3.2025907765
600UbiquitinationLLAQGLIKGQTFRLP
HHHHCCCCCCEEECC
50.43-
600MalonylationLLAQGLIKGQTFRLP
HHHHCCCCCCEEECC
50.4326320211
608PhosphorylationGQTFRLPSGQYLQRE
CCEEECCCCCEEEEE
43.0220068231
611PhosphorylationFRLPSGQYLQREEVD
EECCCCCEEEEEEEE
14.3420068231
628UbiquitinationGSVPVHAKTKEKLEV
CCCCCCCCCHHHEEE
45.3029967540
636PhosphorylationTKEKLEVTWEKMSKS
CHHHEEECHHHHCCC
20.6621406692
643PhosphorylationTWEKMSKSKHNGVDP
CHHHHCCCCCCCCCH
31.6627259358
657PhosphorylationPEEVVEQYGIDTIRL
HHHHHHHHCCCCEEE
11.5327259358
681UbiquitinationKDILWDVKTDALPGV
CCCCEEECCCCCCHH
37.91-
708PhosphorylationRFIEARASGKSPQPQ
HHHHHHHCCCCCCCH
41.0023186163
710UbiquitinationIEARASGKSPQPQLL
HHHHHCCCCCCCHHH
57.3727667366
711PhosphorylationEARASGKSPQPQLLS
HHHHCCCCCCCHHHC
32.0926537577
718PhosphorylationSPQPQLLSNKEKAEA
CCCCHHHCCHHHHHH
55.2223186163
720UbiquitinationQPQLLSNKEKAEARK
CCHHHCCHHHHHHHH
58.1624816145
720MalonylationQPQLLSNKEKAEARK
CCHHHCCHHHHHHHH
58.1630639696
852MalonylationINNKACGKIPVPQQV
ECCCCCCCCCCCHHH
43.6626320211
873PhosphorylationVHEFVLQSELGVRLL
HHHHHHHHHHHHHHH
30.54-
891PhosphorylationSIKKSFLSPRTALIN
CCCHHHCCCHHHHHH
15.4324719451

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 SYLM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYLM_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 SYLM_HUMAN !!

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

Oops, there are no PPI records of SYLM_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615300Perrault syndrome 4 (PRLTS4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00149L-Leucine
Regulatory Network of SYLM_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-236, AND MASS SPECTROMETRY.

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