SYSM_HUMAN - dbPTM
SYSM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYSM_HUMAN
UniProt AC Q9NP81
Protein Name Serine--tRNA ligase, mitochondrial
Gene Name SARS2
Organism Homo sapiens (Human).
Sequence Length 518
Subcellular Localization Mitochondrion matrix .
Protein Description Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)..
Protein Sequence MAASMARRLWPLLTRRGFRPRGGCISNDSPRRSFTTEKRNRNLLYEYAREGYSALPQLDIERFCACPEEAAHALELRKGELRSADLPAIISTWQELRQLQEQIRSLEEEKAAVTEAVRALLANQDSGEVQQDPKYQGLRARGREIRKELVHLYPREAQLEEQFYLQALKLPNQTHPDVPVGDESQARVLHMVGDKPVFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPARFKDLNLAGTAEVGLAGYFMDHTVAFRDLPVRMVCSSTCYRAETNTGQEPRGLYRVHHFTKVEMFGVTGPGLEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVTSASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPALQSYLGTDRITAPTHVPLQYIGPNQPRKPGLPGQPAVS
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
4Phosphorylation----MAASMARRLWP
----CHHHHHHHHHH
11.9328509920
14PhosphorylationRRLWPLLTRRGFRPR
HHHHHHHHCCCCCCC
26.4628509920
52PhosphorylationYEYAREGYSALPQLD
HHHHHHCCCCCCCCC
5.9928152594
53PhosphorylationEYAREGYSALPQLDI
HHHHHCCCCCCCCCH
33.9028152594
110AcetylationIRSLEEEKAAVTEAV
HHHHHHHHHHHHHHH
44.9523954790
110SuccinylationIRSLEEEKAAVTEAV
HHHHHHHHHHHHHHH
44.9523954790
110MalonylationIRSLEEEKAAVTEAV
HHHHHHHHHHHHHHH
44.9526320211
126PhosphorylationALLANQDSGEVQQDP
HHHHCCCCCCCCCCC
27.3929507054
134AcetylationGEVQQDPKYQGLRAR
CCCCCCCCHHHHHHH
59.5023236377
134UbiquitinationGEVQQDPKYQGLRAR
CCCCCCCCHHHHHHH
59.5029967540
1342-HydroxyisobutyrylationGEVQQDPKYQGLRAR
CCCCCCCCHHHHHHH
59.50-
135PhosphorylationEVQQDPKYQGLRARG
CCCCCCCHHHHHHHH
17.1329083192
147MalonylationARGREIRKELVHLYP
HHHHHHHHHHHHHCC
62.1526320211
184O-linked_GlycosylationDVPVGDESQARVLHM
CCCCCCHHHHEEEEE
33.6023301498
195AcetylationVLHMVGDKPVFSFQP
EEEEECCCCCEEECC
36.8325953088
195MalonylationVLHMVGDKPVFSFQP
EEEEECCCCCEEECC
36.8326320211
195SuccinylationVLHMVGDKPVFSFQP
EEEEECCCCCEEECC
36.83-
195UbiquitinationVLHMVGDKPVFSFQP
EEEEECCCCCEEECC
36.8321890473
195SuccinylationVLHMVGDKPVFSFQP
EEEEECCCCCEEECC
36.83-
197UbiquitinationHMVGDKPVFSFQPRG
EEECCCCCEEECCCC
8.4821890473
197UbiquitinationHMVGDKPVFSFQPRG
EEECCCCCEEECCCC
8.4821890473
211MalonylationGHLEIGEKLDIIRQK
CCCCHHHHHHHHHHH
46.3726320211
211AcetylationGHLEIGEKLDIIRQK
CCCCHHHHHHHHHHH
46.3725953088
221PhosphorylationIIRQKRLSHVSGHRS
HHHHHCHHCCCCCHH
26.3523312004
224PhosphorylationQKRLSHVSGHRSYYL
HHCHHCCCCCHHHCH
24.3723312004
256PhosphorylationKLLRRGFTPMTVPDL
HHHHCCCCCCCHHHH
18.2521406692
259PhosphorylationRRGFTPMTVPDLLRG
HCCCCCCCHHHHHCC
30.0421406692
325PhosphorylationLPVRMVCSSTCYRAE
CCCEEEEECEEEEEE
19.7825219547
326PhosphorylationPVRMVCSSTCYRAET
CCEEEEECEEEEEEC
19.8525219547
327PhosphorylationVRMVCSSTCYRAETN
CEEEEECEEEEEECC
9.3925219547
329PhosphorylationMVCSSTCYRAETNTG
EEEECEEEEEECCCC
16.9725219547
343PhosphorylationGQEPRGLYRVHHFTK
CCCCCCEEEEEEEEE
17.26-
401PhosphorylationQELGLPAYRKFDIEA
HHCCCCCHHCCCEEE
16.6430576142
500PhosphorylationPTHVPLQYIGPNQPR
CCCCCCCCCCCCCCC
18.61-
518PhosphorylationLPGQPAVS-------
CCCCCCCC-------
36.2920068231

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 SYSM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYSM_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 SYSM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYHM_HUMANHARS2physical
26344197
SBDS_HUMANSBDSphysical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613845Hyperuricemia, pulmonary hypertension, renal failure, and alkalosis syndrome (HUPRAS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYSM_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-110, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY.

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