dbPTM

SYFA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYFA_HUMAN
UniProt AC	Q9Y285
Protein Name	Phenylalanine--tRNA ligase alpha subunit
Gene Name	FARSA
Organism	Homo sapiens (Human).
Sequence Length	508
Subcellular Localization	Cytoplasm .
Protein Description
Protein Sequence	MADGQVAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIPPEGLAQSELMRLPSGKVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLVRGGQAEKLGEKERSELRKRKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEALQLPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEARKNLLRTHTTSASARALYRLAQKKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVNLQMVYDSPLCRLDAEPRPPPTQEAA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADGQVAEL ------CCCHHHHHH	29.64	19413330
12	Methylation	QVAELLLRRLEASDG HHHHHHHHHHHHCCC	40.90	-
32	Sulfoxidation	ELAAELGMEHQAVVG HHHHHHCCHHHHHHH	6.94	30846556
43	Phosphorylation	AVVGAVKSLQALGEV HHHHHHHHHHHHHHH	21.08	21712546
59	Ubiquitination	EAELRSTKHWELTAE HHHHHCCCCEEEEEC	48.22	21890473
59	Ubiquitination	EAELRSTKHWELTAE HHHHHCCCCEEEEEC	48.22	-
59	Acetylation	EAELRSTKHWELTAE HHHHHCCCCEEEEEC	48.22	25953088
99	Phosphorylation	SELMRLPSGKVGFSK HHHHCCCCCCCCCCH	56.70	24719451
101	Ubiquitination	LMRLPSGKVGFSKAM HHCCCCCCCCCCHHH	43.45	-
101	Ubiquitination	LMRLPSGKVGFSKAM HHCCCCCCCCCCHHH	43.45	-
101	Malonylation	LMRLPSGKVGFSKAM HHCCCCCCCCCCHHH	43.45	26320211
101	Acetylation	LMRLPSGKVGFSKAM HHCCCCCCCCCCHHH	43.45	25953088
106	Ubiquitination	SGKVGFSKAMSNKWI CCCCCCCHHHCCCEE	45.94	-
106	Ubiquitination	SGKVGFSKAMSNKWI CCCCCCCHHHCCCEE	45.94	-
106	Malonylation	SGKVGFSKAMSNKWI CCCCCCCHHHCCCEE	45.94	26320211
106	Acetylation	SGKVGFSKAMSNKWI CCCCCCCHHHCCCEE	45.94	25953088
109	Phosphorylation	VGFSKAMSNKWIRVD CCCCHHHCCCEEEEE	39.87	28857561
111	Ubiquitination	FSKAMSNKWIRVDKS CCHHHCCCEEEEECC	36.37	-
111	Ubiquitination	FSKAMSNKWIRVDKS CCHHHCCCEEEEECC	36.37	-
111	Acetylation	FSKAMSNKWIRVDKS CCHHHCCCEEEEECC	36.37	25953088
117	Acetylation	NKWIRVDKSAADGPR CCEEEEECCCCCCCC	38.85	23749302
117	Ubiquitination	NKWIRVDKSAADGPR CCEEEEECCCCCCCC	38.85	21890473
117	Acetylation	NKWIRVDKSAADGPR CCEEEEECCCCCCCC	38.85	-
117	Ubiquitination	NKWIRVDKSAADGPR CCEEEEECCCCCCCC	38.85	-
117	2-Hydroxyisobutyrylation	NKWIRVDKSAADGPR CCEEEEECCCCCCCC	38.85	-
118	Phosphorylation	KWIRVDKSAADGPRV CEEEEECCCCCCCCE	24.99	-
124	Methylation	KSAADGPRVFRVVDS CCCCCCCCEEEEECC	45.82	-
132	Sulfoxidation	VFRVVDSMEDEVQRR EEEEECCCHHHHHHH	6.96	21406390
144	Methylation	QRRLQLVRGGQAEKL HHHHHHHHCCHHHHH	52.71	-
150	Ubiquitination	VRGGQAEKLGEKERS HHCCHHHHHCHHHHH	65.88	21890473
150	Ubiquitination	VRGGQAEKLGEKERS HHCCHHHHHCHHHHH	65.88	-
150	Acetylation	VRGGQAEKLGEKERS HHCCHHHHHCHHHHH	65.88	25953088
154	Ubiquitination	QAEKLGEKERSELRK HHHHHCHHHHHHHHH	57.54	-
154	Ubiquitination	QAEKLGEKERSELRK HHHHHCHHHHHHHHH	57.54	-
157	Phosphorylation	KLGEKERSELRKRKL HHCHHHHHHHHHHHH	41.91	28634120
163	Ubiquitination	RSELRKRKLLAEVTL HHHHHHHHHHHEEEE	51.38	-
177	Ubiquitination	LKTYWVSKGSAFSTS EEEEEEECCCCCCCC	47.46	21890473
177	Ubiquitination	LKTYWVSKGSAFSTS EEEEEEECCCCCCCC	47.46	-
177	Acetylation	LKTYWVSKGSAFSTS EEEEEEECCCCCCCC	47.46	26051181
179	Phosphorylation	TYWVSKGSAFSTSIS EEEEECCCCCCCCCC	29.85	27080861
182	Phosphorylation	VSKGSAFSTSISKQE EECCCCCCCCCCHHC	22.44	23090842
183	Phosphorylation	SKGSAFSTSISKQET ECCCCCCCCCCHHCC	24.51	22199227
184	Phosphorylation	KGSAFSTSISKQETE CCCCCCCCCCHHCCC	24.54	29507054
186	Phosphorylation	SAFSTSISKQETELS CCCCCCCCHHCCCCC	28.22	29514088
187	Ubiquitination	AFSTSISKQETELSP CCCCCCCHHCCCCCH	50.94	21890473
187	Acetylation	AFSTSISKQETELSP CCCCCCCHHCCCCCH	50.94	26051181
190	Phosphorylation	TSISKQETELSPEMI CCCCHHCCCCCHHHH	39.47	30108239
193	Phosphorylation	SKQETELSPEMISSG CHHCCCCCHHHHHCC	16.75	25159151
198	Phosphorylation	ELSPEMISSGSWRDR CCCHHHHHCCCCCCC	27.60	30108239
198	Ubiquitination	ELSPEMISSGSWRDR CCCHHHHHCCCCCCC	27.60	-
199	Phosphorylation	LSPEMISSGSWRDRP CCHHHHHCCCCCCCC	26.39	29396449
201	Phosphorylation	PEMISSGSWRDRPFK HHHHHCCCCCCCCCC	22.38	29396449
208	Ubiquitination	SWRDRPFKPYNFLAH CCCCCCCCCCCEEEC	49.64	-
208	Acetylation	SWRDRPFKPYNFLAH CCCCCCCCCCCEEEC	49.64	26051181
210	Phosphorylation	RDRPFKPYNFLAHGV CCCCCCCCCEEECEE	21.09	28796482
244	Phosphorylation	IFLEMGFTEMPTDNF HHHHCCCCCCCCCCC	26.16	26074081
248	Phosphorylation	MGFTEMPTDNFIESS CCCCCCCCCCCHHHC	42.12	26074081
254	Phosphorylation	PTDNFIESSFWNFDA CCCCCHHHCCCCHHH	26.47	26074081
255	Phosphorylation	TDNFIESSFWNFDAL CCCCHHHCCCCHHHC	22.84	26074081
280	Ubiquitination	QHDTFFLRDPAEALQ CCCCCEECCHHHHHC	42.59	-
284	Ubiquitination	FFLRDPAEALQLPMD CEECCHHHHHCCCHH	56.13	21890473
292	Phosphorylation	ALQLPMDYVQRVKRT HHCCCHHHHHHHHHH	7.70	-
292	Nitration	ALQLPMDYVQRVKRT HHCCCHHHHHHHHHH	7.70	-
297	Acetylation	MDYVQRVKRTHSQGG HHHHHHHHHHHHCCC	54.49	7663211
299	Phosphorylation	YVQRVKRTHSQGGYG HHHHHHHHHHCCCCC	21.84	25159151
301	Phosphorylation	QRVKRTHSQGGYGSQ HHHHHHHHCCCCCCC	29.88	23401153
305	Phosphorylation	RTHSQGGYGSQGYKY HHHHCCCCCCCCCCE	22.04	23403867
307	Phosphorylation	HSQGGYGSQGYKYNW HHCCCCCCCCCCEEC	16.37	28152594
310	Phosphorylation	GGYGSQGYKYNWKLD CCCCCCCCCEECCHH	11.58	28152594
311	Acetylation	GYGSQGYKYNWKLDE CCCCCCCCEECCHHH	38.64	19608861
311	Sumoylation	GYGSQGYKYNWKLDE CCCCCCCCEECCHHH	38.64	-
311	Ubiquitination	GYGSQGYKYNWKLDE CCCCCCCCEECCHHH	38.64	21906983
311	Sumoylation	GYGSQGYKYNWKLDE CCCCCCCCEECCHHH	38.64	19608861
311	Ubiquitination	GYGSQGYKYNWKLDE CCCCCCCCEECCHHH	38.64	-
312	Ubiquitination	YGSQGYKYNWKLDEA CCCCCCCEECCHHHH	20.12	-
315	Ubiquitination	QGYKYNWKLDEARKN CCCCEECCHHHHHHH	42.28	21890473
315	Acetylation	QGYKYNWKLDEARKN CCCCEECCHHHHHHH	42.28	25953088
318	Ubiquitination	KYNWKLDEARKNLLR CEECCHHHHHHHHHH	61.89	21890473
326	Phosphorylation	ARKNLLRTHTTSASA HHHHHHHHHCCCHHH	24.44	27080861
328	Phosphorylation	KNLLRTHTTSASARA HHHHHHHCCCHHHHH	23.10	27080861
342	Ubiquitination	ALYRLAQKKPFTPVK HHHHHHHCCCCCCCE	57.73	-
343	Ubiquitination	LYRLAQKKPFTPVKY HHHHHHCCCCCCCEE	33.03	21890473
343	2-Hydroxyisobutyrylation	LYRLAQKKPFTPVKY HHHHHHCCCCCCCEE	33.03	-
346	Phosphorylation	LAQKKPFTPVKYFSI HHHCCCCCCCEEEEE	35.38	21712546
349	Acetylation	KKPFTPVKYFSIDRV CCCCCCCEEEEEEEE	41.61	88315
349	Ubiquitination	KKPFTPVKYFSIDRV CCCCCCCEEEEEEEE	41.61	21890473
355	Methylation	VKYFSIDRVFRNETL CEEEEEEEEECCCCC	28.01	-
366	Ubiquitination	NETLDATHLAEFHQI CCCCCHHHHHHHHCC	25.43	-
375	Ubiquitination	AEFHQIEGVVADHGL HHHHCCCEEEECCCC	22.34	21890473
396	Ubiquitination	GVLREFFTKLGITQL HHHHHHHHHHCCEEC	30.58	-
397	Ubiquitination	VLREFFTKLGITQLR HHHHHHHHHCCEECE	39.29	21890473
397	Ubiquitination	VLREFFTKLGITQLR HHHHHHHHHCCEECE	39.29	-
397	Acetylation	VLREFFTKLGITQLR HHHHHHHHHCCEECE	39.29	26051181
406	Ubiquitination	GITQLRFKPAYNPYT CCEECEEECCCCCCC	23.46	21890473
406	Acetylation	GITQLRFKPAYNPYT CCEECEEECCCCCCC	23.46	26051181
412	Phosphorylation	FKPAYNPYTEPSMEV EECCCCCCCCCCCEE	21.79	29496907
427	Ubiquitination	FSYHQGLKKWVEVGN EEECCCHHHHHHCCC	51.95	-
437	Ubiquitination	VEVGNSGVFRPEMLL HHCCCCCCCCHHHHC	3.55	21890473
450	Ubiquitination	LLPMGLPENVSVIAW HCCCCCCCCEEEEEE	75.26	21890473
468	Ubiquitination	LERPTMIKYGINNIR CCCCHHHHHCCCCHH	26.97	21890473
469	Phosphorylation	ERPTMIKYGINNIRE CCCHHHHHCCCCHHH	16.59	28152594
481	Ubiquitination	IRELVGHKVNLQMVY HHHHHCCCCEEEEEE	27.22	21890473
481	Acetylation	IRELVGHKVNLQMVY HHHHHCCCCEEEEEE	27.22	25953088
486	Sulfoxidation	GHKVNLQMVYDSPLC CCCCEEEEEECCCCC	3.21	21406390
488	Phosphorylation	KVNLQMVYDSPLCRL CCEEEEEECCCCCCC	12.83	21945579
490	Phosphorylation	NLQMVYDSPLCRLDA EEEEEECCCCCCCCC	11.33	21945579
493	S-palmitoylation	MVYDSPLCRLDAEPR EEECCCCCCCCCCCC	4.63	29575903
504	Phosphorylation	AEPRPPPTQEAA--- CCCCCCCCCCCC---	44.83	21815630

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
301	S	Phosphorylation	Kinase	ATR	Q13535	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SYFA_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 SYFA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ECSIT_HUMAN	ECSIT	physical	21163940
SYFB_HUMAN	FARSB	physical	22939629
TDGF1_HUMAN	TDGF1	physical	21988832
GORAB_HUMAN	GORAB	physical	21988832
RLA0_HUMAN	RPLP0	physical	22863883
ABI3_HUMAN	ABI3	physical	25416956
SYFB_HUMAN	FARSB	physical	26186194
TCPW_HUMAN	CCT6B	physical	26186194
SYFB_HUMAN	FARSB	physical	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
DB00120	L-Phenylalanine

Regulatory Network of SYFA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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.	19413330 [Abstract]
"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-311, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASSSPECTROMETRY.	18691976 [Abstract]