SYHC_HUMAN - dbPTM
SYHC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYHC_HUMAN
UniProt AC P12081
Protein Name Histidine--tRNA ligase, cytoplasmic
Gene Name HARS
Organism Homo sapiens (Human).
Sequence Length 509
Subcellular Localization Cytoplasm.
Protein Description Cytoplasmic histidine--tRNA ligase (Probable). Plays a role in axon guidance..
Protein Sequence MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAGGRYDGLVGMFDPKGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRRTGQPLCIC
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
57AcetylationSKQKFVLKTPKGTRD
HHCCEEEECCCCCCC
58.4425953088
106AcetylationLKETLMGKYGEDSKL
HHHHHCCCCCCCCEE
35.8027452117
143AcetylationARYLAMNKLTNIKRY
HHHHHHHHCCCCCHH
43.5325953088
224GlutathionylationLDGMFAICGVSDSKF
EEECEEEECCCHHHH
3.8522555962
235GlutathionylationDSKFRTICSSVDKLD
HHHHHHHHHCCCCCC
2.1622555962
240AcetylationTICSSVDKLDKVSWE
HHHHCCCCCCCCCHH
57.3325953088
253UbiquitinationWEEVKNEMVGEKGLA
HHHHHHHHCCCCCCC
7.0221890473
253UbiquitinationWEEVKNEMVGEKGLA
HHHHHHHHCCCCCCC
7.0221890473
383AcetylationKVPCVGLSIGVERIF
CCCEEEEECCHHHHH
16.0319608861
403AcetylationRLEALEEKIRTTETQ
HHHHHHHHHCCCHHH
28.2819608861
418AcetylationVLVASAQKKLLEERL
HHHHHHHHHHHHHHH
45.1425953088
423AcetylationAQKKLLEERLKLVSE
HHHHHHHHHHHHHHH
64.3819608861

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 SYHC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYHC_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 SYHC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AASD1_HUMANAARSD1physical
22863883
CALU_HUMANCALUphysical
22863883
U5S1_HUMANEFTUD2physical
22863883
FEN1_HUMANFEN1physical
22863883
IPO7_HUMANIPO7physical
22863883
PFD1_HUMANPFDN1physical
22863883
RUSD2_HUMANRPUSD2physical
22863883
SNF8_HUMANSNF8physical
22863883
THG1_HUMANTHG1Lphysical
22863883
CKAP5_HUMANCKAP5physical
26344197
DTD1_HUMANDTD1physical
26344197
GCN1_HUMANGCN1L1physical
26344197
HNRPF_HUMANHNRNPFphysical
26344197
PLST_HUMANPLS3physical
26344197
PRRC1_HUMANPRRC1physical
26344197
SYWC_HUMANWARSphysical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614504Usher syndrome 3B (USH3B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00117L-Histidine
Regulatory Network of SYHC_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, AND MASS SPECTROMETRY.
"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-443, AND MASS SPECTROMETRY.

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