SYCM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SYCM_HUMAN
• UniProt AC: Q9HA77
• Protein Name: Probable cysteine--tRNA ligase, mitochondrial
• Gene Name: CARS2
• Organism: Homo sapiens (Human).
• Sequence Length: 564
• Subcellular Localization: Mitochondrion matrix.
• Protein Sequence: MLRTTRGPGLGPPLLQAALGLGRAGWHWPAGRAASGGRGRAWLQPTGRETGVQVYNSLTGRKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVFGCSIVMVMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGIIARGNAYSTAKGNVYFDLKSRGDKYGKLVGVVPGPVGEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHAKGKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLQAQQLLLGLGSFLEDARAYMKGQLACGSVREAMLWERLSSTKRAVKAALADDFDTPRVVDAILGLAHHGNGQLRASLKEPEGPRSPAVFGAIISYFEQFFETVGISLANQQYVSGDGSEATLHGVVDELVRFRQKVRQFALAMPEATGDARRQQLLERQPLLEACDTLRRGLTAHGINIKDRSSTTSTWELLDQRTKDQKSAG

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
46	Phosphorylation	GRAWLQPTGRETGVQ CCEEECCCCCCCCEE	35.59	21406692
111	Phosphorylation	LTKVFGCSIVMVMGI HHHHHCCEEEEECCC	20.71	-
160	Phosphorylation	ALKVLPPTVYLRVTE HHHCCCCEEEEEECC	21.61	27251275
194	Phosphorylation	STAKGNVYFDLKSRG CCCCCEEEEEECCCC	8.72	-
198	Acetylation	GNVYFDLKSRGDKYG CEEEEEECCCCCCCC	39.69	26822725
198	Succinylation	GNVYFDLKSRGDKYG CEEEEEECCCCCCCC	39.69	23954790
198	Malonylation	GNVYFDLKSRGDKYG CEEEEEECCCCCCCC	39.69	26320211
206	Ubiquitination	SRGDKYGKLVGVVPG CCCCCCCEEEEEECC	36.59	-
223	Ubiquitination	GEPADSDKRHASDFA CCCCCCCCCCHHHHH	50.46	-
223	2-Hydroxyisobutyrylation	GEPADSDKRHASDFA CCCCCCCCCCHHHHH	50.46	-
223	Acetylation	GEPADSDKRHASDFA CCCCCCCCCCHHHHH	50.46	25953088
233	Succinylation	ASDFALWKAAKPQEV HHHHHHHHHCCCHHE	39.04	23954790
319	Phosphorylation	KGKEEKMSKSLKNYI CCCHHHHCHHHHHCE	30.11	28258704
321	Phosphorylation	KEEKMSKSLKNYITI CHHHHCHHHHHCEEH	36.95	28258704
323	Succinylation	EKMSKSLKNYITIKD HHHCHHHHHCEEHHH	55.59	23954790
323	Acetylation	EKMSKSLKNYITIKD HHHCHHHHHCEEHHH	55.59	25953088
323	Malonylation	EKMSKSLKNYITIKD HHHCHHHHHCEEHHH	55.59	26320211
325	Phosphorylation	MSKSLKNYITIKDFL HCHHHHHCEEHHHHH	9.61	29449344
327	Phosphorylation	KSLKNYITIKDFLKT HHHHHCEEHHHHHHH	16.18	29449344
329	Acetylation	LKNYITIKDFLKTFS HHHCEEHHHHHHHCC	33.50	19608861
351	Phosphorylation	CLRSSYRSAIDYSDS HHCCHHHCCCCCCHH	22.73	25332170
358	Phosphorylation	SAIDYSDSAMLQAQQ CCCCCCHHHHHHHHH	15.05	25332170
401	Phosphorylation	MLWERLSSTKRAVKA HHHHHHHHCHHHHHH	42.41	-
407	Succinylation	SSTKRAVKAALADDF HHCHHHHHHHHCCCC	27.27	23954790
407	Acetylation	SSTKRAVKAALADDF HHCHHHHHHHHCCCC	27.27	26822725
407	Malonylation	SSTKRAVKAALADDF HHCHHHHHHHHCCCC	27.27	26320211
407	Ubiquitination	SSTKRAVKAALADDF HHCHHHHHHHHCCCC	27.27	-
416	Phosphorylation	ALADDFDTPRVVDAI HHCCCCCCHHHHHHH	17.00	-
534	Phosphorylation	DTLRRGLTAHGINIK HHHHHHHHHCCCCCC	21.31	20068231
544	Phosphorylation	GINIKDRSSTTSTWE CCCCCCCCCCCCHHH	42.02	28450419
545	Phosphorylation	INIKDRSSTTSTWEL CCCCCCCCCCCHHHH	36.28	28450419
546	Phosphorylation	NIKDRSSTTSTWELL CCCCCCCCCCHHHHH	26.47	28450419
547	Phosphorylation	IKDRSSTTSTWELLD CCCCCCCCCHHHHHH	26.55	28450419
548	Phosphorylation	KDRSSTTSTWELLDQ CCCCCCCCHHHHHHH	31.45	28450419
549	Phosphorylation	DRSSTTSTWELLDQR CCCCCCCHHHHHHHH	22.36	28450419

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SYCM_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SYCM_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SYCM_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SYCM_HUMAN !!

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
• DB00151: L-Cysteine

Related Literatures of Post-Translational Modification

Acetylation

"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-329, AND MASS SPECTROMETRY.
PubMed: 19608861