SYNM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SYNM_HUMAN
• UniProt AC: Q96I59
• Protein Name: Probable asparagine--tRNA ligase, mitochondrial
• Gene Name: NARS2
• Organism: Homo sapiens (Human).
• Sequence Length: 477
• Subcellular Localization: Mitochondrion matrix. Mitochondrion .
• Protein Sequence: MLGVRCLLRSVRFCSSAPFPKHKPSAKLSVRDALGAQNASGERIKIQGWIRSVRSQKEVLFLHVNDGSSLESLQVVADSGLDSRELNFGSSVEVQGQLIKSPSKRQNVELKAEKIKVIGNCDAKDFPIKYKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELFQLEPSGKLKVPEENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGPQHTVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGLTEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHSCLL

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
29	O-linked_Glycosylation	HKPSAKLSVRDALGA CCCCCCCCHHHHHCC	17.88	30379171
101	Phosphorylation	VQGQLIKSPSKRQNV EEEEEECCCCCCCCE	27.67	22468782
111	Ubiquitination	KRQNVELKAEKIKVI CCCCEEEEEEEEEEE	40.78	-
111	Acetylation	KRQNVELKAEKIKVI CCCCEEEEEEEEEEE	40.78	25953088
116	Malonylation	ELKAEKIKVIGNCDA EEEEEEEEEEECCCC	38.58	26320211
116	Ubiquitination	ELKAEKIKVIGNCDA EEEEEEEEEEECCCC	38.58	-
124	Succinylation	VIGNCDAKDFPIKYK EEECCCCCCCCCCCC	46.80	23954790
124	Acetylation	VIGNCDAKDFPIKYK EEECCCCCCCCCCCC	46.80	26051181
131	Succinylation	KDFPIKYKERHPLEY CCCCCCCCCCCHHHH	43.18	23954790
138	Phosphorylation	KERHPLEYLRQYPHF CCCCHHHHHHHCCCC	18.18	28152594
149	Phosphorylation	YPHFRCRTNVLGSIL CCCCCCCCCCHHHHH	33.05	22210691
154	Phosphorylation	CRTNVLGSILRIRSE CCCCCHHHHHHHHHH	17.81	21406692
180	Phosphorylation	SGFVHIHTPIITSND CCEEEEECCEEECCC	18.64	-
202	Ubiquitination	FQLEPSGKLKVPEEN EEECCCCCCCCCHHH	49.85	-
236	Ubiquitination	SGAFTQVFTFGPTFR CCCCEEEEECCCCEE	3.17	-
300	Acetylation	EDVELCHKFIAPGQK CHHHHHHHHCCCCCH	37.15	25953088
300	Ubiquitination	EDVELCHKFIAPGQK CHHHHHHHHCCCCCH	37.15	-
307	Ubiquitination	KFIAPGQKDRLEHML HHCCCCCHHHHHHHH	51.21	-
353	Ubiquitination	DLRTEHEKYLVKHCG CCCHHHHHHHHHHHC	45.88	19608861
353	Succinylation	DLRTEHEKYLVKHCG CCCHHHHHHHHHHHC	45.88	27452117
353	Acetylation	DLRTEHEKYLVKHCG CCCHHHHHHHHHHHC	45.88	19608861
357	Succinylation	EHEKYLVKHCGNIPV HHHHHHHHHHCCCCE	30.49	23954790
357	Acetylation	EHEKYLVKHCGNIPV HHHHHHHHHHCCCCE	30.49	23954790
439	Phosphorylation	LDLRRFGSVPHGGFG HHHHHHCCCCCCCCC	29.75	-
463	Ubiquitination	ILGVDNIKDVIPFPR HHCCCCHHHCCCCCC	52.80	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SYNM_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 SYNM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYDM_HUMAN	DARS2	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 616239: Combined oxidative phosphorylation deficiency 24 (COXPD24)
• 0000269|PubMed: Note=NARS2 mutations may be the cause of deafness, autosomal recessive, 94 (DFNB94). DFNB94 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO
• 256000:
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00174: L-Asparagine

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-353, AND MASS SPECTROMETRY.
PubMed: 19608861