SYK_MOUSE - dbPTM
SYK_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYK_MOUSE
UniProt AC Q99MN1
Protein Name Lysine--tRNA ligase
Gene Name Kars
Organism Mus musculus (Mouse).
Sequence Length 595
Subcellular Localization Cytoplasm, cytosol . Cytoplasm . Nucleus . Cell membrane
Peripheral membrane protein . Secreted . Secretion is induced by TNF-alpha. Cytosolic in quiescent mast cells. Translocates into the nucleus in response to mast cell activation by immunoglobu
Protein Description Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity..
Protein Sequence MATLQESEVKVDGEQKLSKNELKRRLKAEKKLAEKEAKQKELSEKQLNQTASAPNHTADNGVGAEEETLDPNQYYKIRSQAVQQLKVTGEDPYPHKFHVDISLTQFIQEYSHLQPGDHLTDVTLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIIPQEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIVRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVKSITGSYKITYHPDGPEGQAYEVDFTPPFRRISMVEELEKALGVKLPETSLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFPAMKPEDKKETAATTETPESTEASPSV
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
2Acetylation------MATLQESEV
------CCCCCCCEE		19.61-
16MalonylationVKVDGEQKLSKNELK
EECCCCCCCCHHHHH		50.8826320211
19MalonylationDGEQKLSKNELKRRL
CCCCCCCHHHHHHHH		65.9526320211
43PhosphorylationEAKQKELSEKQLNQT
HHHHHHHCHHHHHHH		43.79-
76UbiquitinationLDPNQYYKIRSQAVQ
CCHHHHHHHHHHHHH		27.06-
86AcetylationSQAVQQLKVTGEDPY
HHHHHHCCCCCCCCC		33.15-
125UbiquitinationHLTDVTLKVAGRIHA
CCCHHHHEEECEEEE		22.22-
139AcetylationAKRASGGKLIFYDLR
EEECCCCEEEEEECC		41.77-
139MalonylationAKRASGGKLIFYDLR
EEECCCCEEEEEECC		41.7726320211
205PhosphorylationPQEITLLSPCLHMLP
CCHHHHHHHHHHHHH		19.38-
247UbiquitinationQKFIVRSKIITYIRS
HHHHHHHHHHHHHHH		27.80-
303UbiquitinationIAPELYHKMLVVGGI
HCHHHHHHHHHHCCC		22.00-
357PhosphorylationEITEKMLSGMVKSIT
HHHHHHHHCHHHHHC		22.7326643407
361UbiquitinationKMLSGMVKSITGSYK
HHHHCHHHHHCCEEE		27.52-
362PhosphorylationMLSGMVKSITGSYKI
HHHCHHHHHCCEEEE		17.6126643407
364PhosphorylationSGMVKSITGSYKITY
HCHHHHHCCEEEEEE		27.4526643407
366PhosphorylationMVKSITGSYKITYHP
HHHHHCCEEEEEECC		18.0126643407
367PhosphorylationVKSITGSYKITYHPD
HHHHCCEEEEEECCC		14.0426643407
381PhosphorylationDGPEGQAYEVDFTPP
CCCCCCEEEEECCCC		14.4818563927
393PhosphorylationTPPFRRISMVEELEK
CCCCCCCHHHHHHHH		18.2425521595
405UbiquitinationLEKALGVKLPETSLF
HHHHHCCCCCCCCCC		57.43-
410PhosphorylationGVKLPETSLFETEET
CCCCCCCCCCCCHHH		29.42-
419UbiquitinationFETEETRKILDDICV
CCCHHHHHHHHHHHH		55.85-
453PhosphorylationVGEFLEVTCISPTFI
HHHHHEEEECCCCEE		8.5126745281
456PhosphorylationFLEVTCISPTFICDH
HHEEEECCCCEECCC		21.7526745281
458PhosphorylationEVTCISPTFICDHPQ
EEEECCCCEECCCHH		20.8826643407
468PhosphorylationCDHPQIMSPLAKWHR
CCCHHHHCHHHHHHH		20.5626643407
477AcetylationLAKWHRSKEGLTERF
HHHHHHCCCCCHHHH		56.6219857957
490UbiquitinationRFELFVMKKEICNAY
HHHEHHHHHHHHHHH		41.79-
491UbiquitinationFELFVMKKEICNAYT
HHEHHHHHHHHHHHH		33.93-
557PhosphorylationDRLTMFLTDSNNIKE
HEEEEEEECCCCCEE		26.56-
563UbiquitinationLTDSNNIKEVLLFPA
EECCCCCEEEEEEEC		43.84-
576UbiquitinationPAMKPEDKKETAATT
ECCCCCCCCCCCCCC		51.34-
579PhosphorylationKPEDKKETAATTETP
CCCCCCCCCCCCCCC		30.3925619855
582PhosphorylationDKKETAATTETPEST
CCCCCCCCCCCCCCC		23.7726239621
583PhosphorylationKKETAATTETPESTE
CCCCCCCCCCCCCCC		32.8925619855
585PhosphorylationETAATTETPESTEAS
CCCCCCCCCCCCCCC		30.2025521595
588PhosphorylationATTETPESTEASPSV
CCCCCCCCCCCCCCC		32.5225521595
589PhosphorylationTTETPESTEASPSV-
CCCCCCCCCCCCCC-		33.6327087446
592PhosphorylationTPESTEASPSV----
CCCCCCCCCCC----		16.1025521595
594PhosphorylationESTEASPSV------
CCCCCCCCC------		37.6525521595
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 SYK_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYK_MOUSE !!
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 SYK_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SYK_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYK_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASSSPECTROMETRY.

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