SYK_HUMAN - dbPTM
SYK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYK_HUMAN
UniProt AC Q15046
Protein Name Lysine--tRNA ligase
Gene Name KARS
Organism Homo sapiens (Human).
Sequence Length 597
Subcellular Localization Isoform Cytoplasmic: Cytoplasm, cytosol . Cytoplasm . Nucleus . Cell membrane
Peripheral membrane protein . Secreted . Secretion is induced by TNF-alpha (PubMed:15851690). Cytosolic in quiescent mast cells. Translocates into the nucleus in response
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. [PubMed: 9278442]
Protein Sequence MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTTDNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
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------MAAVQAAEV
------CCCCEEEEE
19.1522223895
3 (in isoform 2)Phosphorylation-7.8325072903
8UbiquitinationMAAVQAAEVKVDGSE
CCCCEEEEEECCCCC
45.9824816145
102-HydroxyisobutyrylationAVQAAEVKVDGSEPK
CCEEEEEECCCCCCC
26.55-
10UbiquitinationAVQAAEVKVDGSEPK
CCEEEEEECCCCCCC
26.55-
14PhosphorylationAEVKVDGSEPKLSKN
EEEECCCCCCCCCHH
46.3824850871
17UbiquitinationKVDGSEPKLSKNELK
ECCCCCCCCCHHHHH
62.4324816145
17 (in isoform 2)Phosphorylation-62.4321406692
18 (in isoform 2)Phosphorylation-14.9521406692
202-HydroxyisobutyrylationGSEPKLSKNELKRRL
CCCCCCCHHHHHHHH
65.95-
31AcetylationKRRLKAEKKVAEKEA
HHHHHHHHHHHHHHH
58.3630589629
34UbiquitinationLKAEKKVAEKEAKQK
HHHHHHHHHHHHHHH
30.9027667366
44PhosphorylationEAKQKELSEKQLSQA
HHHHHHHCHHHHHHH
43.7924719451
49PhosphorylationELSEKQLSQATAAAT
HHCHHHHHHHHHHHH
18.4428348404
52PhosphorylationEKQLSQATAAATNHT
HHHHHHHHHHHHCCC
14.8028348404
56PhosphorylationSQATAAATNHTTDNG
HHHHHHHHCCCCCCC
23.8628348404
59PhosphorylationTAAATNHTTDNGVGP
HHHHHCCCCCCCCCC
37.6028348404
60PhosphorylationAAATNHTTDNGVGPE
HHHHCCCCCCCCCCC
21.6628348404
78AcetylationVDPNQYYKIRSQAIH
CCHHHHHEEHHHHHE
27.0626051181
78UbiquitinationVDPNQYYKIRSQAIH
CCHHHHHEEHHHHHE
27.0622817900
78 (in isoform 1)Ubiquitination-27.0621890473
81PhosphorylationNQYYKIRSQAIHQLK
HHHHEEHHHHHEEEE
27.6928857561
88AcetylationSQAIHQLKVNGEDPY
HHHHEEEEECCCCCC
27.3819608861
88MethylationSQAIHQLKVNGEDPY
HHHHEEEEECCCCCC
27.3822640393
95PhosphorylationKVNGEDPYPHKFHVD
EECCCCCCCCCCEEE
30.2328152594
106UbiquitinationFHVDISLTDFIQKYS
CEEEEEHHHHHHHHC
23.2921890473
106 (in isoform 2)Ubiquitination-23.2921890473
111AcetylationSLTDFIQKYSHLQPG
EHHHHHHHHCCCCCC
43.8525038526
112PhosphorylationLTDFIQKYSHLQPGD
HHHHHHHHCCCCCCC
5.7328152594
113PhosphorylationTDFIQKYSHLQPGDH
HHHHHHHCCCCCCCC
25.4228152594
116AcetylationIQKYSHLQPGDHLTD
HHHHCCCCCCCCHHH
34.2119608861
1272-HydroxyisobutyrylationHLTDITLKVAGRIHA
CHHHHHHEECCEEEE
22.76-
127AcetylationHLTDITLKVAGRIHA
CHHHHHHEECCEEEE
22.7625953088
127UbiquitinationHLTDITLKVAGRIHA
CHHHHHHEECCEEEE
22.7632015554
135UbiquitinationVAGRIHAKRASGGKL
ECCEEEEEECCCCEE
34.0423000965
1412-HydroxyisobutyrylationAKRASGGKLIFYDLR
EEECCCCEEEEEECC
41.77-
141AcetylationAKRASGGKLIFYDLR
EEECCCCEEEEEECC
41.7719608861
141MalonylationAKRASGGKLIFYDLR
EEECCCCEEEEEECC
41.7726320211
141SuccinylationAKRASGGKLIFYDLR
EEECCCCEEEEEECC
41.7727452117
141UbiquitinationAKRASGGKLIFYDLR
EEECCCCEEEEEECC
41.7723000965
148MethylationKLIFYDLRGEGVKLQ
EEEEEECCCCCEEEE
37.91115480819
149UbiquitinationLIFYDLRGEGVKLQV
EEEEECCCCCEEEEE
43.2223000965
153AcetylationDLRGEGVKLQVMANS
ECCCCCEEEEEEECC
44.0225953088
155UbiquitinationRGEGVKLQVMANSRN
CCCCEEEEEEECCCC
19.7532015554
163UbiquitinationVMANSRNYKSEEEFI
EEECCCCCCCHHHEE
18.1223000965
164AcetylationMANSRNYKSEEEFIH
EECCCCCCCHHHEEE
55.7425038526
164UbiquitinationMANSRNYKSEEEFIH
EECCCCCCCHHHEEE
55.7424816145
169AcetylationNYKSEEEFIHINNKL
CCCCHHHEEECCCCC
5.8019608861
169UbiquitinationNYKSEEEFIHINNKL
CCCCHHHEEECCCCC
5.8023000965
169 (in isoform 2)Malonylation-5.8026320211
169 (in isoform 2)Ubiquitination-5.80-
1752-HydroxyisobutyrylationEFIHINNKLRRGDII
HEEECCCCCCCCCEE
38.59-
175AcetylationEFIHINNKLRRGDII
HEEECCCCCCCCCEE
38.5923954790
175UbiquitinationEFIHINNKLRRGDII
HEEECCCCCCCCCEE
38.5929967540
190UbiquitinationGVQGNPGKTKKGELS
EECCCCCCCCCCEEE
59.4327667366
192UbiquitinationQGNPGKTKKGELSII
CCCCCCCCCCEEEEC
63.3724816145
203UbiquitinationLSIIPYEITLLSPCL
EEECCEEEHHHHHHH
2.4429967540
207PhosphorylationPYEITLLSPCLHMLP
CEEEHHHHHHHHHHH
19.3819524539
207UbiquitinationPYEITLLSPCLHMLP
CEEEHHHHHHHHHHH
19.3821890473
218UbiquitinationHMLPHLHFGLKDKET
HHHHHHCCCCCCHHH
18.0427667366
2492-HydroxyisobutyrylationQKFIIRSKIITYIRS
HHHHHHHHHHHHHHH
28.42-
249UbiquitinationQKFIIRSKIITYIRS
HHHHHHHHHHHHHHH
28.42-
251UbiquitinationFIIRSKIITYIRSFL
HHHHHHHHHHHHHHH
2.4833845483
265UbiquitinationLDELGFLEIETPMMN
HHHHCCCEEECCCEE
36.2023000965
274UbiquitinationETPMMNIIPGGAVAK
ECCCEECCCCCCCCC
1.8921963094
305UbiquitinationIAPELYHKMLVVGGI
HCHHHHHHHHHHCCC
22.0023000965
305 (in isoform 1)Ubiquitination-22.0021890473
314MethylationLVVGGIDRVYEIGRQ
HHHCCCHHHHHHHHH
30.88115480827
333UbiquitinationGIDLTHNPEFTTCEF
CCCCCCCCCCCCEEE
30.4023000965
333 (in isoform 2)Ubiquitination-30.4021890473
336UbiquitinationLTHNPEFTTCEFYMA
CCCCCCCCCEEEEEE
28.9521890473
361UbiquitinationTEKMVSGMVKHITGS
HHHHHHHHHHHHCCE
2.5633845483
363AcetylationKMVSGMVKHITGSYK
HHHHHHHHHHCCEEE
22.0125953088
363UbiquitinationKMVSGMVKHITGSYK
HHHHHHHHHHCCEEE
22.0122817900
363 (in isoform 1)Ubiquitination-22.0121890473
366PhosphorylationSGMVKHITGSYKVTY
HHHHHHHCCEEEEEE
21.5722210691
368PhosphorylationMVKHITGSYKVTYHP
HHHHHCCEEEEEECC
17.0922210691
391UbiquitinationDVDFTPPFRRINMVE
ECCCCCCCCCCCHHH
9.6221890473
391 (in isoform 2)Ubiquitination-9.6221890473
396SulfoxidationPPFRRINMVEELEKA
CCCCCCCHHHHHHHH
3.6021406390
402AcetylationNMVEELEKALGMKLP
CHHHHHHHHHCCCCC
62.6319608861
402UbiquitinationNMVEELEKALGMKLP
CHHHHHHHHHCCCCC
62.6329967540
407UbiquitinationLEKALGMKLPETNLF
HHHHHCCCCCCCCCC
60.1233845483
4212-HydroxyisobutyrylationFETEETRKILDDICV
CCCHHHHHHHHHHHH
55.85-
421UbiquitinationFETEETRKILDDICV
CCCHHHHHHHHHHHH
55.8523000965
421 (in isoform 1)Ubiquitination-55.8521890473
422UbiquitinationETEETRKILDDICVA
CCHHHHHHHHHHHHH
4.6133845483
423UbiquitinationTEETRKILDDICVAK
CHHHHHHHHHHHHHH
5.6233845483
427GlutathionylationRKILDDICVAKAVEC
HHHHHHHHHHHHCCC
2.9122555962
4302-HydroxyisobutyrylationLDDICVAKAVECPPP
HHHHHHHHHCCCCCC
32.35-
430AcetylationLDDICVAKAVECPPP
HHHHHHHHHCCCCCC
32.3526051181
430UbiquitinationLDDICVAKAVECPPP
HHHHHHHHHCCCCCC
32.3521963094
435UbiquitinationVAKAVECPPPRTTAR
HHHHCCCCCCHHHHH
28.5532015554
449UbiquitinationRLLDKLVGEFLEVTC
HHHHHHHHHHHEEEE
30.3023000965
449 (in isoform 2)Ubiquitination-30.3021890473
458UbiquitinationFLEVTCINPTFICDH
HHEEEECCCEEECCC
31.5421963094
460PhosphorylationEVTCINPTFICDHPQ
EEEECCCEEECCCHH
22.5725850435
470PhosphorylationCDHPQIMSPLAKWHR
CCCHHHHCHHHHHHH
20.5625850435
4922-HydroxyisobutyrylationRFELFVMKKEICNAY
HHHEHHHHHHHHHHH
41.79-
492AcetylationRFELFVMKKEICNAY
HHHEHHHHHHHHHHH
41.7925953088
492UbiquitinationRFELFVMKKEICNAY
HHHEHHHHHHHHHHH
41.7921890473
492 (in isoform 1)Ubiquitination-41.7921890473
4932-HydroxyisobutyrylationFELFVMKKEICNAYT
HHEHHHHHHHHHHHH
33.93-
493AcetylationFELFVMKKEICNAYT
HHEHHHHHHHHHHHH
33.9326051181
493UbiquitinationFELFVMKKEICNAYT
HHEHHHHHHHHHHHH
33.9329967540
496GlutathionylationFVMKKEICNAYTELN
HHHHHHHHHHHHHHC
2.2122555962
506SulfoxidationYTELNDPMRQRQLFE
HHHHCCHHHHHHHHH
6.7721406390
517AcetylationQLFEEQAKAKAAGDD
HHHHHHHHHHHCCCC
50.5525953088
517UbiquitinationQLFEEQAKAKAAGDD
HHHHHHHHHHHCCCC
50.5533845483
520UbiquitinationEEQAKAKAAGDDEAM
HHHHHHHHCCCCCCE
22.8721890473
520 (in isoform 2)Ubiquitination-22.8721890473
521UbiquitinationEQAKAKAAGDDEAMF
HHHHHHHCCCCCCEE
22.6529967540
545UbiquitinationEYGLPPTAGWGMGID
HHCCCCCCCCCCCCC
19.9533845483
556SulfoxidationMGIDRVAMFLTDSNN
CCCCEEEEEEECCCC
2.3021406390
561PhosphorylationVAMFLTDSNNIKEVL
EEEEEECCCCCEEEE
26.9221712546
573SulfoxidationEVLLFPAMKPEDKKE
EEEEEECCCCCCCCC
8.2921406390
5742-HydroxyisobutyrylationVLLFPAMKPEDKKEN
EEEEECCCCCCCCCC
47.57-
574AcetylationVLLFPAMKPEDKKEN
EEEEECCCCCCCCCC
47.5725038526
578UbiquitinationPAMKPEDKKENVATT
ECCCCCCCCCCCCCC
61.3932015554
579UbiquitinationAMKPEDKKENVATTD
CCCCCCCCCCCCCCC
67.8333845483
584PhosphorylationDKKENVATTDTLEST
CCCCCCCCCCCCCCC
22.4130257219
585PhosphorylationKKENVATTDTLESTT
CCCCCCCCCCCCCCC
19.7627251275
587PhosphorylationENVATTDTLESTTVG
CCCCCCCCCCCCCCC
30.2729970186
590PhosphorylationATTDTLESTTVGTSV
CCCCCCCCCCCCCCC
32.2729514088
591PhosphorylationTTDTLESTTVGTSV-
CCCCCCCCCCCCCC-
19.0030266825
592PhosphorylationTDTLESTTVGTSV--
CCCCCCCCCCCCC--
26.6429514088
595PhosphorylationLESTTVGTSV-----
CCCCCCCCCC-----
23.2130266825
596PhosphorylationESTTVGTSV------
CCCCCCCCC------
21.6530266825
606Ubiquitination----------------
----------------
32015554
607Ubiquitination-----------------
-----------------
33845483

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
49SPhosphorylationKinaseP38AQ16539
PSP
52TPhosphorylationKinaseMAPK14Q16539
GPS
207SPhosphorylationKinaseMAPK3P27361
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYK_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 SYK_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AIMP2_HUMANAIMP2physical
16189514
LIS1_HUMANPAFAH1B1physical
16169070
ADT3_HUMANSLC25A6physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
RSSA_HUMANRPSAphysical
22751010
AIMP2_HUMANAIMP2physical
22751010
MK01_HUMANMAPK1physical
22751010
SYLC_HUMANLARSphysical
22939629
SYQ_HUMANQARSphysical
22939629
SYRC_HUMANRARSphysical
22939629
SYMC_HUMANMARSphysical
22939629
UBA1_HUMANUBA1physical
22939629
SYNC_HUMANNARSphysical
22939629
UBE2S_HUMANUBE2Sphysical
22939629
TXLNA_HUMANTXLNAphysical
22939629
TRM1_HUMANTRMT1physical
22939629
TCPQ_HUMANCCT8physical
22939629
SYKM_YEASTMSK1genetic
22539966
SYCC_HUMANCARSphysical
22863883
IPO7_HUMANIPO7physical
22863883
AIMP2_HUMANAIMP2physical
25416956
AIMP1_HUMANAIMP1physical
26344197
AIMP2_HUMANAIMP2physical
26344197
SYDC_HUMANDARSphysical
26344197
SYDM_HUMANDARS2physical
26344197
MCA3_HUMANEEF1E1physical
26344197
SYEP_HUMANEPRSphysical
26344197
SYIC_HUMANIARSphysical
26344197
MSH3_HUMANMSH3physical
26344197
SYQ_HUMANQARSphysical
26344197
SAMD9_HUMANSAMD9physical
26344197
SNX8_HUMANSNX8physical
26344197
XPP1_HUMANXPNPEP1physical
26344197
SYRC_HUMANRARSphysical
28514442
SYTC2_HUMANTARSL2physical
28514442
SDCG8_HUMANSDCCAG8physical
28514442
AIMP2_HUMANAIMP2physical
28514442
AIMP1_HUMANAIMP1physical
28514442
SYDC_HUMANDARSphysical
28514442
SYEP_HUMANEPRSphysical
28514442
MCA3_HUMANEEF1E1physical
28514442
SYIC_HUMANIARSphysical
28514442
SYLC_HUMANLARSphysical
28514442
SYMC_HUMANMARSphysical
28514442
SYQ_HUMANQARSphysical
28514442
LRRF2_HUMANLRRFIP2physical
28514442

Drug and Disease Associations
Kegg Disease
H00264 Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
OMIM Disease
613641Charcot-Marie-Tooth disease, recessive, intermediate type, B (CMTRIB)
613916Deafness, autosomal recessive, 89 (DFNB89)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00123L-Lysine
Regulatory Network of SYK_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM CYTOPLASMIC),PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND MASSSPECTROMETRY.
"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-88; LYS-141 AND LYS-402, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM CYTOPLASMIC),PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-587, AND MASSSPECTROMETRY.

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