SYSC_HUMAN - dbPTM
SYSC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYSC_HUMAN
UniProt AC P49591
Protein Name Serine--tRNA ligase, cytoplasmic
Gene Name SARS
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Cytoplasm . Nucleus . Predominantly cytoplasmic, but a minor proportion is also found in the nucleus.
Protein Description Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). [PubMed: 22353712]
Protein Sequence MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLSQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEPSKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA
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
1Acetylation-------MVLDLDLF
-------CCEECEEE		6.4419413330
12UbiquitinationLDLFRVDKGGDPALI
CEEEEECCCCCHHHH		63.03-
12AcetylationLDLFRVDKGGDPALI
CEEEEECCCCCHHHH		63.0325953088
12MalonylationLDLFRVDKGGDPALI
CEEEEECCCCCHHHH		63.0326320211
22PhosphorylationDPALIRETQEKRFKD
CHHHHHHHHHHHHCC		31.9830576142
25UbiquitinationLIRETQEKRFKDPGL
HHHHHHHHHHCCCCH		54.00-
282-HydroxyisobutyrylationETQEKRFKDPGLVDQ
HHHHHHHCCCCHHHH		68.02-
28UbiquitinationETQEKRFKDPGLVDQ
HHHHHHHCCCCHHHH		68.02-
38UbiquitinationGLVDQLVKADSEWRR
CHHHHHHHCCHHHHH		55.8821906983
55AcetylationFRADNLNKLKNLCSK
HHHHCHHHHHHHHHH		65.0925953088
55UbiquitinationFRADNLNKLKNLCSK
HHHHCHHHHHHHHHH		65.09-
57UbiquitinationADNLNKLKNLCSKTI
HHCHHHHHHHHHHHH		49.86-
62AcetylationKLKNLCSKTIGEKMK
HHHHHHHHHHHHHHC		43.0725953088
62MalonylationKLKNLCSKTIGEKMK
HHHHHHHHHHHHHHC		43.0726320211
62UbiquitinationKLKNLCSKTIGEKMK
HHHHHHHHHHHHHHC		43.07-
63PhosphorylationLKNLCSKTIGEKMKK
HHHHHHHHHHHHHCC		20.2321949786
67UbiquitinationCSKTIGEKMKKKEPV
HHHHHHHHHCCCCCC		51.29-
70UbiquitinationTIGEKMKKKEPVGDD
HHHHHHCCCCCCCCC		59.89-
71UbiquitinationIGEKMKKKEPVGDDE
HHHHHCCCCCCCCCC		62.83-
79PhosphorylationEPVGDDESVPENVLS
CCCCCCCCCCCCCCC		50.3926434776
99UbiquitinationADALANLKVSQIKKV
HHHHHCCCHHHHHHH		39.38-
101PhosphorylationALANLKVSQIKKVRL
HHHCCCHHHHHHHHH		25.30-
116UbiquitinationLIDEAILKCDAERIK
HHCHHHHHCCHHHHH		24.77-
1162-HydroxyisobutyrylationLIDEAILKCDAERIK
HHCHHHHHCCHHHHH		24.77-
117GlutathionylationIDEAILKCDAERIKL
HCHHHHHCCHHHHHH		5.5522555962
123UbiquitinationKCDAERIKLEAERFE
HCCHHHHHHHHHHHH		46.63-
1232-HydroxyisobutyrylationKCDAERIKLEAERFE
HCCHHHHHHHHHHHH		46.63-
123AcetylationKCDAERIKLEAERFE
HCCHHHHHHHHHHHH		46.6325953088
142PhosphorylationIGNLLHPSVPISNDE
HHHHHCCCCCCCCCC		29.7622617229
154AcetylationNDEDVDNKVERIWGD
CCCCHHHHHHHHHHC		40.8026051181
154UbiquitinationNDEDVDNKVERIWGD
CCCCHHHHHHHHHHC		40.8021890473
157MethylationDVDNKVERIWGDCTV
CHHHHHHHHHHCCHH		32.71115493327
167AcetylationGDCTVRKKYSHVDLV
HCCHHHHCCCCCCEE		41.237823055
184AcetylationVDGFEGEKGAVVAGS
ECCCCCCCCEEEEEC		64.137823063
191PhosphorylationKGAVVAGSRGYFLKG
CCEEEEECCCHHHHH		16.8823898821
231UbiquitinationYTPFFMRKEVMQEVA
CCCHHHHHHHHHHHH		42.76-
234SulfoxidationFFMRKEVMQEVAQLS
HHHHHHHHHHHHHHH		2.7030846556
241PhosphorylationMQEVAQLSQFDEELY
HHHHHHHHHCCHHHH		19.4017525332
248PhosphorylationSQFDEELYKVIGKGS
HHCCHHHHHHHCCCC		13.39-
249UbiquitinationQFDEELYKVIGKGSE
HCCHHHHHHHCCCCC		39.75-
253UbiquitinationELYKVIGKGSEKSDD
HHHHHHCCCCCCCCC		48.41-
255PhosphorylationYKVIGKGSEKSDDNS
HHHHCCCCCCCCCCC		45.39-
257UbiquitinationVIGKGSEKSDDNSYD
HHCCCCCCCCCCCCC		61.9621890473
258PhosphorylationIGKGSEKSDDNSYDE
HCCCCCCCCCCCCCC		46.2628985074
262PhosphorylationSEKSDDNSYDEKYLI
CCCCCCCCCCCCEEE		40.74-
266AcetylationDDNSYDEKYLIATSE
CCCCCCCCEEEEECC		42.3227452117
266UbiquitinationDDNSYDEKYLIATSE
CCCCCCCCEEEEECC		42.3221890473
293UbiquitinationRPEDLPIKYAGLSTC
CCCCCCCCCCCHHHH		27.40-
317MethylationRDTRGIFRVHQFEKI
CCCCCEEEEEECCEE		24.08115493319
323AcetylationFRVHQFEKIEQFVYS
EEEEECCEEEHHHHC		53.4819608861
323UbiquitinationFRVHQFEKIEQFVYS
EEEEECCEEEHHHHC		53.4819608861
329PhosphorylationEKIEQFVYSSPHDNK
CEEEHHHHCCCCCCC		12.5228152594
330PhosphorylationKIEQFVYSSPHDNKS
EEEHHHHCCCCCCCC		31.9028152594
331PhosphorylationIEQFVYSSPHDNKSW
EEHHHHCCCCCCCCH		14.4725627689
368PhosphorylationIVNIVSGSLNHAASK
HHHHHHCCCCHHHHC		20.63-
376UbiquitinationLNHAASKKLDLEAWF
CCHHHHCCCCHHHHC		44.7521890473
396PhosphorylationFRELVSCSNCTDYQA
HHHHHCCCCCCHHHH		27.6828152594
399PhosphorylationLVSCSNCTDYQARRL
HHCCCCCCHHHHHHH		41.8328152594
401PhosphorylationSCSNCTDYQARRLRI
CCCCCCHHHHHHHHH		5.9728152594
438GlutathionylationCATTRTICAILENYQ
HHHHHHHHHHHHHHC		1.5822555962
444PhosphorylationICAILENYQTEKGIT
HHHHHHHHCCCCCCC		13.8722210691
446PhosphorylationAILENYQTEKGITVP
HHHHHHCCCCCCCCC		29.3322210691
448UbiquitinationLENYQTEKGITVPEK
HHHHCCCCCCCCCHH		60.03-
451PhosphorylationYQTEKGITVPEKLKE
HCCCCCCCCCHHHHH		38.3822210691
455UbiquitinationKGITVPEKLKEFMPP
CCCCCCHHHHHHCCC		59.81-
472UbiquitinationQELIPFVKPAPIEQE
HHHCCCCCCCCCCCC		35.52-
481PhosphorylationAPIEQEPSKKQKKQH
CCCCCCCCHHHHHCC		52.3026434776
491PhosphorylationQKKQHEGSKKKAAAR
HHHCCCCHHHHHHHH		38.0126074081
501PhosphorylationKAAARDVTLENRLQN
HHHHHHCCHHHHHHH		32.4229255136
505MethylationRDVTLENRLQNMEVT
HHCCHHHHHHHCCCC		28.42115493311
512PhosphorylationRLQNMEVTDA-----
HHHHCCCCCC-----		16.9520068231
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 SYSC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYSC_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 SYSC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYTC_HUMANTARSphysical
22939629
AN32E_HUMANANP32Ephysical
22863883
U5S1_HUMANEFTUD2physical
22863883
TF2AA_HUMANGTF2A1physical
22863883
SNX5_HUMANSNX5physical
22863883
TBCD_HUMANTBCDphysical
22863883
DUS3L_HUMANDUS3Lphysical
26186194
R3HCL_HUMANR3HCC1Lphysical
26186194
CL045_HUMANC12orf45physical
26186194
ARFP1_HUMANARFIP1physical
26344197
ARFP2_HUMANARFIP2physical
26344197
TLS1_HUMANC9orf78physical
26344197
PYR1_HUMANCADphysical
26344197
CCDC6_HUMANCCDC6physical
26344197
GFPT2_HUMANGFPT2physical
26344197
SYHC_HUMANHARSphysical
26344197
SYHM_HUMANHARS2physical
26344197
HIP1R_HUMANHIP1Rphysical
26344197
HSPB1_HUMANHSPB1physical
26344197
PO210_HUMANNUP210physical
26344197
PAPOA_HUMANPAPOLAphysical
26344197
PFD2_HUMANPFDN2physical
26344197
PFKAM_HUMANPFKMphysical
26344197
PPM1G_HUMANPPM1Gphysical
26344197
PRRC1_HUMANPRRC1physical
26344197
TEBP_HUMANPTGES3physical
26344197
SEC13_HUMANSEC13physical
26344197
SNW1_HUMANSNW1physical
26344197
TRI25_HUMANTRIM25physical
26344197
SYWC_HUMANWARSphysical
26344197
DUS3L_HUMANDUS3Lphysical
28514442
R3HCL_HUMANR3HCC1Lphysical
28514442
CL045_HUMANC12orf45physical
28514442
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
DB00133L-Serine
Regulatory Network of SYSC_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-323, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.

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