dbPTM

SYFB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYFB_HUMAN
UniProt AC	Q9NSD9
Protein Name	Phenylalanine--tRNA ligase beta subunit
Gene Name	FARSB
Organism	Homo sapiens (Human).
Sequence Length	589
Subcellular Localization	Cytoplasm.
Protein Description
Protein Sequence	MPTVSVKRDLLFQALGRTYTDEEFDELCFEFGLELDEITSEKEIISKEQGNVKAAGASDVVLYKIDVPANRYDLLCLEGLVRGLQVFKERIKAPVYKRVMPDGKIQKLIITEETAKIRPFAVAAVLRNIKFTKDRYDSFIELQEKLHQNICRKRALVAIGTHDLDTLSGPFTYTAKRPSDIKFKPLNKTKEYTACELMNIYKTDNHLKHYLHIIENKPLYPVIYDSNGVVLSMPPIINGDHSRITVNTRNIFIECTGTDFTKAKIVLDIIVTMFSEYCENQFTVEAAEVVFPNGKSHTFPELAYRKEMVRADLINKKVGIRETPENLAKLLTRMYLKSEVIGDGNQIEIEIPPTRADIIHACDIVEDAAIAYGYNNIQMTLPKTYTIANQFPLNKLTELLRHDMAAAGFTEALTFALCSQEDIADKLGVDISATKAVHISNPKTAEFQVARTTLLPGLLKTIAANRKMPLPLKLFEISDIVIKDSNTDVGAKNYRHLCAVYYNKNPGFEIIHGLLDRIMQLLDVPPGEDKGGYVIKASEGPAFFPGRCAEIFARGQSVGKLGVLHPDVITKFELTMPCSSLEINVGPFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPTVSVKRDL -----CCCCCCCHHH	24.90	23403867
5	Phosphorylation	---MPTVSVKRDLLF ---CCCCCCCHHHHH	25.13	23403867
7	2-Hydroxyisobutyrylation	-MPTVSVKRDLLFQA -CCCCCCCHHHHHHH	32.46	-
46	Phosphorylation	TSEKEIISKEQGNVK CCHHHHHCHHHCCEE	35.48	-
47	Acetylation	SEKEIISKEQGNVKA CHHHHHCHHHCCEEE	43.58	7704535
47	Ubiquitination	SEKEIISKEQGNVKA CHHHHHCHHHCCEEE	43.58	32015554
53	Ubiquitination	SKEQGNVKAAGASDV CHHHCCEEECCCCCE	36.20	21906983
63	Phosphorylation	GASDVVLYKIDVPAN CCCCEEEEEEECCCC	8.35	17053785
64	Ubiquitination	ASDVVLYKIDVPANR CCCEEEEEEECCCCH	28.41	22817900
64	Ubiquitination	ASDVVLYKIDVPANR CCCEEEEEEECCCCH	28.41	21890473
64	Ubiquitination	ASDVVLYKIDVPANR CCCEEEEEEECCCCH	28.41	21890473
64	Ubiquitination	ASDVVLYKIDVPANR CCCEEEEEEECCCCH	28.41	21890473
71	Methylation	KIDVPANRYDLLCLE EEECCCCHHHHHHHH	28.57	-
72	Phosphorylation	IDVPANRYDLLCLEG EECCCCHHHHHHHHH	15.68	17053785
88	Methylation	VRGLQVFKERIKAPV HHHHHHHHHHHCCCC	47.42	-
88	Ubiquitination	VRGLQVFKERIKAPV HHHHHHHHHHHCCCC	47.42	24816145
88	2-Hydroxyisobutyrylation	VRGLQVFKERIKAPV HHHHHHHHHHHCCCC	47.42	-
92	Ubiquitination	QVFKERIKAPVYKRV HHHHHHHCCCCEEEE	53.51	33845483
92	Malonylation	QVFKERIKAPVYKRV HHHHHHHCCCCEEEE	53.51	32601280
97	Ubiquitination	RIKAPVYKRVMPDGK HHCCCCEEEECCCCC	38.46	27667366
97	Acetylation	RIKAPVYKRVMPDGK HHCCCCEEEECCCCC	38.46	25953088
104	Ubiquitination	KRVMPDGKIQKLIIT EEECCCCCEEEEEEE	49.71	32015554
104	Acetylation	KRVMPDGKIQKLIIT EEECCCCCEEEEEEE	49.71	25953088
107	Acetylation	MPDGKIQKLIITEET CCCCCEEEEEEECCC	45.16	23749302
107	Ubiquitination	MPDGKIQKLIITEET CCCCCEEEEEEECCC	45.16	29967540
107	Malonylation	MPDGKIQKLIITEET CCCCCEEEEEEECCC	45.16	26320211
116	Acetylation	IITEETAKIRPFAVA EEECCCCCCCHHHHH	46.82	25953088
136	Phosphorylation	IKFTKDRYDSFIELQ CCCCHHHHHHHHHHH	26.52	28152594
138	Phosphorylation	FTKDRYDSFIELQEK CCHHHHHHHHHHHHH	21.13	28152594
145	Ubiquitination	SFIELQEKLHQNICR HHHHHHHHHHHHHHH	38.00	32015554
145	Acetylation	SFIELQEKLHQNICR HHHHHHHHHHHHHHH	38.00	25953088
161	Phosphorylation	RALVAIGTHDLDTLS HCEEEEECCCHHCCC	13.20	21406692
166	Phosphorylation	IGTHDLDTLSGPFTY EECCCHHCCCCCCEE	30.07	21406692
168	Phosphorylation	THDLDTLSGPFTYTA CCCHHCCCCCCEEEC	46.65	21406692
172	Phosphorylation	DTLSGPFTYTAKRPS HCCCCCCEEECCCCC	24.09	21406692
173	Phosphorylation	TLSGPFTYTAKRPSD CCCCCCEEECCCCCC	12.70	21406692
174	Phosphorylation	LSGPFTYTAKRPSDI CCCCCEEECCCCCCC	23.73	21406692
182	Ubiquitination	AKRPSDIKFKPLNKT CCCCCCCCCCCCCCC	52.94	29967540
188	Acetylation	IKFKPLNKTKEYTAC CCCCCCCCCCCEEHH	69.52	25953088
190	Ubiquitination	FKPLNKTKEYTACEL CCCCCCCCCEEHHHH	50.78	29967540
190	Malonylation	FKPLNKTKEYTACEL CCCCCCCCCEEHHHH	50.78	32601280
190	Acetylation	FKPLNKTKEYTACEL CCCCCCCCCEEHHHH	50.78	26051181
192	Phosphorylation	PLNKTKEYTACELMN CCCCCCCEEHHHHEE	10.95	-
193	Phosphorylation	LNKTKEYTACELMNI CCCCCCEEHHHHEEE	26.39	29507054
202	Ubiquitination	CELMNIYKTDNHLKH HHHEEEEECCCCHHH	45.68	29967540
202	Acetylation	CELMNIYKTDNHLKH HHHEEEEECCCCHHH	45.68	26822725
218	Ubiquitination	LHIIENKPLYPVIYD HHHHHCCCCCEEEEC	49.02	24816145
224	Phosphorylation	KPLYPVIYDSNGVVL CCCCEEEECCCCEEE	17.35	24719451
226	Phosphorylation	LYPVIYDSNGVVLSM CCEEEECCCCEEEEC	20.64	24719451
230	Ubiquitination	IYDSNGVVLSMPPII EECCCCEEEECCCEE	3.29	21890473
262	Ubiquitination	CTGTDFTKAKIVLDI EECCCHHHHHHHHHH	47.91	32015554
262	Acetylation	CTGTDFTKAKIVLDI EECCCHHHHHHHHHH	47.91	26051181
316	Ubiquitination	VRADLINKKVGIRET HHHHHHCCCCCCCCC	41.67	29967540
316	Acetylation	VRADLINKKVGIRET HHHHHHCCCCCCCCC	41.67	25953088
317	Ubiquitination	RADLINKKVGIRETP HHHHHCCCCCCCCCH	41.00	24816145
329	Acetylation	ETPENLAKLLTRMYL CCHHHHHHHHHHHHH	47.39	19608861
329	Ubiquitination	ETPENLAKLLTRMYL CCHHHHHHHHHHHHH	47.39	27667366
329	Ubiquitination	ETPENLAKLLTRMYL CCHHHHHHHHHHHHH	47.39	21890473
329	Ubiquitination	ETPENLAKLLTRMYL CCHHHHHHHHHHHHH	47.39	21890473
329	Ubiquitination	ETPENLAKLLTRMYL CCHHHHHHHHHHHHH	47.39	21890473
335	Phosphorylation	AKLLTRMYLKSEVIG HHHHHHHHHHHEEEC	14.00	26546556
354	Phosphorylation	IEIEIPPTRADIIHA EEEECCCCHHHHHHH	32.89	26546556
361	Ubiquitination	TRADIIHACDIVEDA CHHHHHHHCHHHHHH	5.14	22817900
368	Ubiquitination	ACDIVEDAAIAYGYN HCHHHHHHHHHHCCC	6.30	27667366
384	Phosphorylation	IQMTLPKTYTIANQF EEEECCCEEEECCCC	24.77	28152594
385	Phosphorylation	QMTLPKTYTIANQFP EEECCCEEEECCCCC	11.41	28152594
386	Phosphorylation	MTLPKTYTIANQFPL EECCCEEEECCCCCH	20.88	25072903
393	Ubiquitination	TIANQFPLNKLTELL EECCCCCHHHHHHHH	10.49	27667366
395	Ubiquitination	ANQFPLNKLTELLRH CCCCCHHHHHHHHHH	65.55	30230243
397	Phosphorylation	QFPLNKLTELLRHDM CCCHHHHHHHHHHHH	26.62	25072903
435	Ubiquitination	GVDISATKAVHISNP CCCCEECEEEEECCC	48.40	32015554
437	Ubiquitination	DISATKAVHISNPKT CCEECEEEEECCCCC	4.37	27667366
440	Phosphorylation	ATKAVHISNPKTAEF ECEEEEECCCCCHHH	32.00	26437602
443	Ubiquitination	AVHISNPKTAEFQVA EEEECCCCCHHHHHH	65.70	29967540
443	2-Hydroxyisobutyrylation	AVHISNPKTAEFQVA EEEECCCCCHHHHHH	65.70	-
443	Malonylation	AVHISNPKTAEFQVA EEEECCCCCHHHHHH	65.70	26320211
443	Acetylation	AVHISNPKTAEFQVA EEEECCCCCHHHHHH	65.70	25953088
460	Ubiquitination	TLLPGLLKTIAANRK HCHHHHHHHHHHCCC	42.82	21906983
460	Acetylation	TLLPGLLKTIAANRK HCHHHHHHHHHHCCC	42.82	26051181
461	Ubiquitination	LLPGLLKTIAANRKM CHHHHHHHHHHCCCC	18.80	21890473
467	Ubiquitination	KTIAANRKMPLPLKL HHHHHCCCCCCCEEE	44.68	27667366
473	Acetylation	RKMPLPLKLFEISDI CCCCCCEEEEEEEEE	49.55	156495
473	Ubiquitination	RKMPLPLKLFEISDI CCCCCCEEEEEEEEE	49.55	32015554
478	Phosphorylation	PLKLFEISDIVIKDS CEEEEEEEEEEEECC	17.68	-
483	Ubiquitination	EISDIVIKDSNTDVG EEEEEEEECCCCCCC	44.18	29967540
485	Phosphorylation	SDIVIKDSNTDVGAK EEEEEECCCCCCCCC	36.31	28348404
487	Phosphorylation	IVIKDSNTDVGAKNY EEEECCCCCCCCCCH	35.69	28348404
492	Ubiquitination	SNTDVGAKNYRHLCA CCCCCCCCCHHEEEE	48.89	33845483
501	Phosphorylation	YRHLCAVYYNKNPGF HHEEEEEEECCCCCH	5.25	28152594
502	Phosphorylation	RHLCAVYYNKNPGFE HEEEEEEECCCCCHH	17.05	28152594
504	Acetylation	LCAVYYNKNPGFEII EEEEEECCCCCHHHH	48.69	26051181
517	Methylation	IIHGLLDRIMQLLDV HHHHHHHHHHHHHCC	26.67	-
530	Ubiquitination	DVPPGEDKGGYVIKA CCCCCCCCCCEEEEC	50.35	-
536	Ubiquitination	DKGGYVIKASEGPAF CCCCEEEECCCCCCC	35.50	32015554
536	2-Hydroxyisobutyrylation	DKGGYVIKASEGPAF CCCCEEEECCCCCCC	35.50	-
560	Ubiquitination	ARGQSVGKLGVLHPD HCCCCCCCCCCCCHH	39.65	23000965
560	Ubiquitination	ARGQSVGKLGVLHPD HCCCCCCCCCCCCHH	39.65	21890473
560	Ubiquitination	ARGQSVGKLGVLHPD HCCCCCCCCCCCCHH	39.65	21890473
560	Ubiquitination	ARGQSVGKLGVLHPD HCCCCCCCCCCCCHH	39.65	21890473
560	Acetylation	ARGQSVGKLGVLHPD HCCCCCCCCCCCCHH	39.65	25953088
570	Phosphorylation	VLHPDVITKFELTMP CCCHHHEEEEEEECC	29.54	25867546

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 SYFB_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYIC_HUMAN	IARS	physical	22939629
UBP8_HUMAN	USP8	physical	22939629
PUR2_HUMAN	GART	physical	22863883
HS105_HUMAN	HSPH1	physical	22863883
PUR6_HUMAN	PAICS	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
RL24_HUMAN	RPL24	physical	22863883
RLA0_HUMAN	RPLP0	physical	22863883
RLA1_HUMAN	RPLP1	physical	22863883
SET_HUMAN	SET	physical	22863883
SF01_HUMAN	SF1	physical	22863883
SPT5H_HUMAN	SUPT5H	physical	22863883
SWP70_HUMAN	SWAP70	physical	22863883
SYFA_HUMAN	FARSA	physical	26344197
SYIC_HUMAN	IARS	physical	26344197
OGT1_HUMAN	OGT	physical	26344197

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 SYFB_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63 AND TYR-72, AND MASSSPECTROMETRY.	17053785 [Abstract]