SYCC_HUMAN - dbPTM
SYCC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYCC_HUMAN
UniProt AC P49589
Protein Name Cysteine--tRNA ligase, cytoplasmic
Gene Name CARS
Organism Homo sapiens (Human).
Sequence Length 748
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MADSSGQQGKGRRVQPQWSPPAGTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITDIDDKIIKRARQNHLFEQYREKRPEAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQHAVQLATEPLEKAVQSRLTGEEVNSCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSEKHSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVDITGQFEKWGEEEAELNKNFYDKKTAIHKALCDNVDTRTVMEEMRALVSQCNLYMAARKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATVMPYLQVLSEFREGVRKIAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPTVVKLVDRNTLLKEREEKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDKYSKFDENGLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ
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------MADSSGQQG
------CCCCCCCCC		25.9522814378
19PhosphorylationRRVQPQWSPPAGTQP
CCCCCCCCCCCCCCC		18.7630266825
24PhosphorylationQWSPPAGTQPCRLHL
CCCCCCCCCCCEEEE		31.2930266825
32PhosphorylationQPCRLHLYNSLTRNK
CCCEEEEECCCCCCC		7.6130266825
34PhosphorylationCRLHLYNSLTRNKEV
CEEEEECCCCCCCCE		19.9830266825
36PhosphorylationLHLYNSLTRNKEVFI
EEEECCCCCCCCEEE		31.8330266825
39UbiquitinationYNSLTRNKEVFIPQD
ECCCCCCCCEEECCC		52.55-
48AcetylationVFIPQDGKKVTWYCC
EEECCCCCEEEEEEE		52.9725953088
48UbiquitinationVFIPQDGKKVTWYCC
EEECCCCCEEEEEEE		52.97-
49AcetylationFIPQDGKKVTWYCCG
EECCCCCEEEEEEEC		50.887673993
51PhosphorylationPQDGKKVTWYCCGPT
CCCCCEEEEEEECCE		21.4225348954
53PhosphorylationDGKKVTWYCCGPTVY
CCCEEEEEEECCEEE		2.9026356563
58PhosphorylationTWYCCGPTVYDASHM
EEEEECCEEECCCHH		19.5825348954
60PhosphorylationYCCGPTVYDASHMGH
EEECCEEECCCHHCC		14.3127259358
63PhosphorylationGPTVYDASHMGHARS
CCEEECCCHHCCHHH		15.8827259358
71PhosphorylationHMGHARSYISFDILR
HHCCHHHHHHHHHHH		8.6023071622
79 (in isoform 3)Phosphorylation-34.3730266825
82UbiquitinationDILRRVLKDYFKFDV
HHHHHHHHHHHCCCE		47.74-
102 (in isoform 3)Phosphorylation-6.0529116813
115PhosphorylationQNHLFEQYREKRPEA
HHHHHHHHHHHCHHH		17.3427251275
122 (in isoform 3)Ubiquitination-11.82-
131 (in isoform 3)Ubiquitination-18.01-
134UbiquitinationEDVQAALKPFSVKLN
HHHHHHHCCCCEECC		39.01-
137PhosphorylationQAALKPFSVKLNETT
HHHHCCCCEECCCCC		27.2023186163
143PhosphorylationFSVKLNETTDPDKKQ
CCEECCCCCCHHHHH		35.1120068231
148AcetylationNETTDPDKKQMLERI
CCCCCHHHHHHHHHH		50.7423749302
165 (in isoform 3)Ubiquitination-41.27-
168UbiquitinationLATEPLEKAVQSRLT
HHHHHHHHHHHHCCC		62.63-
213PhosphorylationVTDNSIFSKLPKFWE
CCCCCHHHCCCCHHC		31.4524719451
214UbiquitinationTDNSIFSKLPKFWEG
CCCCHHHCCCCHHCC		59.04-
217AcetylationSIFSKLPKFWEGDFH
CHHHCCCCHHCCCCC		73.8125953088
217UbiquitinationSIFSKLPKFWEGDFH
CHHHCCCCHHCCCCC		73.81-
227SulfoxidationEGDFHRDMEALNVLP
CCCCCCCHHHHCCCC		3.0730846556
231 (in isoform 3)Ubiquitination-40.08-
232 (in isoform 3)Ubiquitination-9.87-
239PhosphorylationVLPPDVLTRVSEYVP
CCCHHHHHHHHHHHH		28.9520068231
251 (in isoform 3)Ubiquitination-4.22-
260PhosphorylationQKIVDNGYGYVSNGS
HHHHHCCCCCCCCCE		16.1328152594
262PhosphorylationIVDNGYGYVSNGSVY
HHHCCCCCCCCCEEE		7.6928152594
264PhosphorylationDNGYGYVSNGSVYFD
HCCCCCCCCCEEEEC		27.3023401153
280AcetylationAKFASSEKHSYGKLV
CHHCCCCCCCCCCCC		39.5425953088
280UbiquitinationAKFASSEKHSYGKLV
CHHCCCCCCCCCCCC		39.54-
285UbiquitinationSEKHSYGKLVPEAVG
CCCCCCCCCCCCHHC		37.77-
295 (in isoform 1)Ubiquitination-56.6621906983
295 (in isoform 2)Ubiquitination-56.6621906983
295UbiquitinationPEAVGDQKALQEGEG
CCHHCCHHHHHCCCC		56.6621906983
300 (in isoform 3)Ubiquitination-31.09-
305PhosphorylationQEGEGDLSISADRLS
HCCCCCCCEEHHHHC		21.1629255136
307PhosphorylationGEGDLSISADRLSEK
CCCCCCEEHHHHCCC		22.2719664994
312PhosphorylationSISADRLSEKRSPND
CEEHHHHCCCCCCCC		41.8025159151
324UbiquitinationPNDFALWKASKPGEP
CCCCCCCCCCCCCCC		43.57-
327UbiquitinationFALWKASKPGEPSWP
CCCCCCCCCCCCCCC		63.00-
363 (in isoform 3)Ubiquitination-25.28-
368 (in isoform 3)Ubiquitination-39.96-
378 (in isoform 3)Ubiquitination-7.06-
407 (in isoform 3)Ubiquitination-7.68-
410PhosphorylationAGCKMSKSLKNFITI
CCCCCCHHHHCCEEH		36.9530576142
412AcetylationCKMSKSLKNFITIKD
CCCCHHHHCCEEHHH		57.8325953088
412UbiquitinationCKMSKSLKNFITIKD
CCCCHHHHCCEEHHH		57.83-
418UbiquitinationLKNFITIKDALKKHS
HHCCEEHHHHHHHCC		28.44-
444PhosphorylationSWKDTLDYSSNTMES
HHHHHHCCCCCHHHH		19.6722210691
445PhosphorylationWKDTLDYSSNTMESA
HHHHHCCCCCHHHHH		19.4422210691
449SulfoxidationLDYSSNTMESALQYE
HCCCCCHHHHHHHHH		4.4830846556
455PhosphorylationTMESALQYEKFLNEF
HHHHHHHHHHHHHHH		23.1822210691
482 (in isoform 1)Ubiquitination-62.8821906983
482 (in isoform 2)Ubiquitination-62.8821906983
482UbiquitinationDITGQFEKWGEEEAE
CCCCCHHHHCHHHHH		62.882190698
492UbiquitinationEEEAELNKNFYDKKT
HHHHHHHHHCCCHHH		62.14-
503AcetylationDKKTAIHKALCDNVD
CHHHHHHHHHHCCCC		36.6219608861
503UbiquitinationDKKTAIHKALCDNVD
CHHHHHHHHHHCCCC		36.6219608861
503MalonylationDKKTAIHKALCDNVD
CHHHHHHHHHHCCCC		36.6226320211
506 (in isoform 3)Ubiquitination-4.23-
528PhosphorylationLVSQCNLYMAARKAV
HHHHHHHHHHHHHHH		3.18-
583O-linked_GlycosylationTSLSLEATVMPYLQV
CCCCHHHHHHHHHHH		14.15OGP
586 (in isoform 3)Ubiquitination-23.50-
586AcetylationSLEATVMPYLQVLSE
CHHHHHHHHHHHHHH		23.5019608861
606UbiquitinationRKIAREQKVPEILQL
HHHHHHCCCCHHHHH		55.81-
640UbiquitinationEGLPTVVKLVDRNTL
CCCCCCEEHHCCCCH		38.16-
672AcetylationKEEAARRKQEQEAAK
HHHHHHHHHHHHHHH		53.277338357
689 (in isoform 3)Ubiquitination-39.46-
706 (in isoform 2)Phosphorylation-7.15-
711SulfoxidationNGLPTHDMEGKELSK
CCCCCCCCCCCCCCH		5.9321406390
723 (in isoform 3)Ubiquitination-69.43-
726MalonylationGQAKKLKKLFEAQEK
HHHHHHHHHHHHHHH		69.6926320211
733AcetylationKLFEAQEKLYKEYLQ
HHHHHHHHHHHHHHH		45.0723236377
746PhosphorylationLQMAQNGSFQ-----
HHHHHHCCCC-----		28.2025159151
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 SYCC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYCC_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 SYCC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1G_HUMANEEF1Gphysical
10908348
A4_HUMANAPPphysical
21832049
HSP74_HUMANHSPA4physical
22863883
SC24D_HUMANSEC24Dphysical
22863883
THUM3_HUMANTHUMPD3physical
22863883
SYLC_HUMANLARSphysical
26344197
MCFD2_HUMANMCFD2physical
26344197
PLPHP_HUMANPROSCphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00151L-Cysteine
Regulatory Network of SYCC_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-503, AND MASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-260, AND MASSSPECTROMETRY.

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