SYHM_HUMAN - dbPTM
SYHM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYHM_HUMAN
UniProt AC P49590
Protein Name Probable histidine--tRNA ligase, mitochondrial
Gene Name HARS2
Organism Homo sapiens (Human).
Sequence Length 506
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MPLLGLLPRRAWASLLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAHQEKPNFIIKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTIVQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPRLSQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQAGEEPLNVGSVAAGGRYDGLVGMFDPKGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSES
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
42 (in isoform 2)Phosphorylation-5.0029507054
52AcetylationQLKAHQEKPNFIIKT
HHHHHHCCCCEEEEC
38.4023236377
52MalonylationQLKAHQEKPNFIIKT
HHHHHHCCCCEEEEC
38.4026320211
52UbiquitinationQLKAHQEKPNFIIKT
HHHHHHCCCCEEEEC
38.40-
59PhosphorylationKPNFIIKTPKGTRDL
CCCEEEECCCCCCCC
21.5925599653
63PhosphorylationIIKTPKGTRDLSPQH
EEECCCCCCCCCHHH
27.4329514088
67PhosphorylationPKGTRDLSPQHMVVR
CCCCCCCCHHHHHHH
27.1429255136
76SumoylationQHMVVREKILDLVIS
HHHHHHHHHHHHHHH
37.70-
91SuccinylationCFKRHGAKGMDTPAF
HHHHHCCCCCCCCCC
60.4027452117
91MalonylationCFKRHGAKGMDTPAF
HHHHHCCCCCCCCCC
60.4026320211
93SulfoxidationKRHGAKGMDTPAFEL
HHHCCCCCCCCCCHH
5.2321406390
94UbiquitinationRHGAKGMDTPAFELK
HHCCCCCCCCCCHHH
59.20-
116PhosphorylationGEDSGLMYDLKDQGG
CCCCCCEEEEECCCC
24.1424961811
119UbiquitinationSGLMYDLKDQGGELL
CCCEEEEECCCCCEE
45.14-
127PhosphorylationDQGGELLSLRYDLTV
CCCCCEEEEEEEEHH
24.3521712546
130PhosphorylationGELLSLRYDLTVPFA
CCEEEEEEEEHHHHH
22.1628152594
144AcetylationARYLAMNKVKKMKRY
HHHHHHHHHHHCHHH
42.2025953088
151PhosphorylationKVKKMKRYHVGKVWR
HHHHCHHHCCCCEEC
8.71-
161PhosphorylationGKVWRRESPTIVQGR
CCEECCCCCCEEECC
26.0730266825
163PhosphorylationVWRRESPTIVQGRYR
EECCCCCCEEECCCH
42.9630266825
241AcetylationAICSSIDKLDKMAWK
HHHHCHHHHHHHHHH
57.8425953088
257SuccinylationVRHEMVVKKGLAPEV
HHHHHHHHCCCCHHH
29.7027452117
257AcetylationVRHEMVVKKGLAPEV
HHHHHHHHCCCCHHH
29.7025953088
258UbiquitinationRHEMVVKKGLAPEVA
HHHHHHHCCCCHHHH
47.77-
294UbiquitinationDPRLSQNKQALEGLG
CCCHHHCHHHHHCHH
29.3421906983
364PhosphorylationSVAAGGRYDGLVGMF
CCEECCCCCCEEECC
20.0320068231
377UbiquitinationMFDPKGHKVPCVGLS
CCCCCCCCCCEEEEE
57.45-
392PhosphorylationIGVERIFYIVEQRMK
ECHHHHHHHHHHHHC
11.1628152594
394UbiquitinationVERIFYIVEQRMKTK
HHHHHHHHHHHHCCC
3.32-
407PhosphorylationTKGEKVRTTETQVFV
CCCCCCCCCCCEEEE
31.7821406692
408PhosphorylationKGEKVRTTETQVFVA
CCCCCCCCCCEEEEE
26.8621406692
410PhosphorylationEKVRTTETQVFVATP
CCCCCCCCEEEEECC
28.1321406692
416PhosphorylationETQVFVATPQKNFLQ
CCEEEEECCCCCHHH
22.4321406692
419UbiquitinationVFVATPQKNFLQERL
EEEECCCCCHHHHHH
51.36-
419AcetylationVFVATPQKNFLQERL
EEEECCCCCHHHHHH
51.36-
419AcetylationVFVATPQKNFLQERL
EEEECCCCCHHHHHH
51.36132945
419SuccinylationVFVATPQKNFLQERL
EEEECCCCCHHHHHH
51.3623954790
444MalonylationIKAEMLYKNNPKLLT
HHHHHHHHCCHHHHH
46.4126320211
444AcetylationIKAEMLYKNNPKLLT
HHHHHHHHCCHHHHH
46.4119608861
444SuccinylationIKAEMLYKNNPKLLT
HHHHHHHHCCHHHHH
46.4127452117

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 SYHM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYHM_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 SYHM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATRAP_HUMANAGTRAPphysical
25416956
GARS_HUMANGARSphysical
26344197
SYHC_HUMANHARSphysical
28514442
CH60_HUMANHSPD1physical
28514442
SDHB_HUMANSDHBphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614926Perrault syndrome 2 (PRLTS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYHM_HUMAN

loading...

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-444, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASSSPECTROMETRY.

TOP