SYYM_HUMAN - dbPTM
SYYM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYYM_HUMAN
UniProt AC Q9Y2Z4
Protein Name Tyrosine--tRNA ligase, mitochondrial
Gene Name YARS2
Organism Homo sapiens (Human).
Sequence Length 477
Subcellular Localization Mitochondrion matrix .
Protein Description Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr)..
Protein Sequence MAAPILRSFSWGRWSGTLNLSVLLPLGLRKAHSGAQGLLAAQKARGLFKDFFPETGTKIELPELFDRGTASFPQTIYCGFDPTADSLHVGHLLALLGLFHLQRAGHNVIALVGGATARLGDPSGRTKEREALETERVRANARALRLGLEALAANHQQLFTDGRSWGSFTVLDNSAWYQKQHLVDFLAAVGGHFRMGTLLSRQSVQLRLKSPEGMSLAEFFYQVLQAYDFYYLFQRYGCRVQLGGSDQLGNIMSGYEFINKLTGEDVFGITVPLITSTTGAKLGKSAGNAVWLNRDKTSPFELYQFFVRQPDDSVERYLKLFTFLPLPEIDHIMQLHVKEPERRGPQKRLAAEVTKLVHGREGLDSAKRCTQALYHSSIDALEVMSDQELKELFKEAPFSEFFLDPGTSVLDTCRKANAIPDGPRGYRMITEGGVSINHQQVTNPESVLIVGQHILKNGLSLLKIGKRNFYIIKWLQL
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
8PhosphorylationMAAPILRSFSWGRWS
CCCCCEECCCCCCCC		21.8624043423
10PhosphorylationAPILRSFSWGRWSGT
CCCEECCCCCCCCCE		29.8424043423
15PhosphorylationSFSWGRWSGTLNLSV
CCCCCCCCCEEEEEE		22.1224043423
17PhosphorylationSWGRWSGTLNLSVLL
CCCCCCCEEEEEEEH		13.6324043423
21PhosphorylationWSGTLNLSVLLPLGL
CCCEEEEEEEHCCCC		15.0524043423
43UbiquitinationQGLLAAQKARGLFKD
HHHHHHHHHHHHHHH		35.0123503661
49AcetylationQKARGLFKDFFPETG
HHHHHHHHHHCCCCC		59.6823954790
49SuccinylationQKARGLFKDFFPETG
HHHHHHHHHHCCCCC		59.6823954790
49UbiquitinationQKARGLFKDFFPETG
HHHHHHHHHHCCCCC		59.6823503661
58UbiquitinationFFPETGTKIELPELF
HCCCCCCEEECCHHH		35.2123503661
164PhosphorylationQLFTDGRSWGSFTVL
HHCCCCCCCCCEEEE		41.1229083192
167PhosphorylationTDGRSWGSFTVLDNS
CCCCCCCCEEEECCC		16.1029083192
169PhosphorylationGRSWGSFTVLDNSAW
CCCCCCEEEECCCHH		23.1229083192
203PhosphorylationGTLLSRQSVQLRLKS
HHHHCCCEEEEEECC		15.6629978859
210PhosphorylationSVQLRLKSPEGMSLA
EEEEEECCCCCCCHH		32.5429978859
215PhosphorylationLKSPEGMSLAEFFYQ
ECCCCCCCHHHHHHH		34.9729978859
221PhosphorylationMSLAEFFYQVLQAYD
CCHHHHHHHHHHHHH		11.7529978859
227PhosphorylationFYQVLQAYDFYYLFQ
HHHHHHHHHHHHHHH		8.1429978859
230PhosphorylationVLQAYDFYYLFQRYG
HHHHHHHHHHHHHHC		9.0729978859
231PhosphorylationLQAYDFYYLFQRYGC
HHHHHHHHHHHHHCC		10.8829978859
245PhosphorylationCRVQLGGSDQLGNIM
CEEECCCCCHHHCHH		22.0124719451
253PhosphorylationDQLGNIMSGYEFINK
CHHHCHHHHHHHHHH		34.1324719451
255PhosphorylationLGNIMSGYEFINKLT
HHCHHHHHHHHHHHH		10.6024719451
281UbiquitinationITSTTGAKLGKSAGN
EEECCCCCCCCCCCC		60.1523503661
284UbiquitinationTTGAKLGKSAGNAVW
CCCCCCCCCCCCCEE		47.7927667366
296UbiquitinationAVWLNRDKTSPFELY
CEEECCCCCCCCEEH		47.9021963094
297PhosphorylationVWLNRDKTSPFELYQ
EEECCCCCCCCEEHH		46.0226270265
298PhosphorylationWLNRDKTSPFELYQF
EECCCCCCCCEEHHH		33.0726270265
303PhosphorylationKTSPFELYQFFVRQP
CCCCCEEHHHHHCCC		8.97-
308MethylationELYQFFVRQPDDSVE
EEHHHHHCCCCCHHH		36.84115920181
354O-linked_GlycosylationKRLAAEVTKLVHGRE
HHHHHHHHHHHHCCC		15.3430379171
355AcetylationRLAAEVTKLVHGREG
HHHHHHHHHHHCCCC		54.4019608861
355UbiquitinationRLAAEVTKLVHGREG
HHHHHHHHHHHCCCC		54.4019608861
355SuccinylationRLAAEVTKLVHGREG
HHHHHHHHHHHCCCC		54.4027452117
355MalonylationRLAAEVTKLVHGREG
HHHHHHHHHHHCCCC		54.4026320211
367SuccinylationREGLDSAKRCTQALY
CCCHHHHHHHHHHHH		52.5423954790
367AcetylationREGLDSAKRCTQALY
CCCHHHHHHHHHHHH		52.5425953088
367UbiquitinationREGLDSAKRCTQALY
CCCHHHHHHHHHHHH		52.5424816145
370PhosphorylationLDSAKRCTQALYHSS
HHHHHHHHHHHHHCC		22.4026471730
374PhosphorylationKRCTQALYHSSIDAL
HHHHHHHHHCCCCHH		11.5926471730
376PhosphorylationCTQALYHSSIDALEV
HHHHHHHCCCCHHHH		18.5526471730
377PhosphorylationTQALYHSSIDALEVM
HHHHHHCCCCHHHHC		15.9227251275
413GlutathionylationGTSVLDTCRKANAIP
CCCHHHHHHHHCCCC		4.1322555962
415UbiquitinationSVLDTCRKANAIPDG
CHHHHHHHHCCCCCC		48.4129967540
426PhosphorylationIPDGPRGYRMITEGG
CCCCCCCEEEEEECC		9.7822817900
435PhosphorylationMITEGGVSINHQQVT
EEEECCEEECCCCCC		22.4322817900
460PhosphorylationHILKNGLSLLKIGKR
HHHHCCHHHEEECCC		32.8124719451
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 SYYM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYYM_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 SYYM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAM9B_HUMANFAM9Bphysical
25416956
ADA12_HUMANADAM12physical
26344197
LYRM2_HUMANLYRM2physical
28514442
UQCC2_HUMANUQCC2physical
28514442
HNRPK_HUMANHNRNPKphysical
28514442
CH60_HUMANHSPD1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613561Myopathy with lactic acidosis and sideroblastic anemia 2 (MLASA2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00135L-Tyrosine
Regulatory Network of SYYM_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-355, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426 AND SER-435, ANDMASS SPECTROMETRY.

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