dbPTM

AIMP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AIMP1_HUMAN
UniProt AC	Q12904
Protein Name	Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
Gene Name	AIMP1
Organism	Homo sapiens (Human).
Sequence Length	312
Subcellular Localization	Nucleus . Cytoplasm, cytosol . Secreted . Endoplasmic reticulum . Golgi apparatus . Enriched in secretory vesicles of pancreatic alpha cells and secreted from the pancreas in response to low glucose levels (By similarity). Secreted in response to hyp
Protein Description	Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. [PubMed: 10358004 Binds tRNA. Possesses inflammatory cytokine activity]
Protein Sequence	MANNDAVLKRLEQKGAEADQIIEYLKQQVSLLKEKAILQATLREEKKLRVENAKLKKEIEELKQELIQAEIQNGVKQIPFPSGTPLHANSMVSENVIQSTAVTTVSSGTKEQIKGGTGDEKKAKEKIEKKGEKKEKKQQSIAGSADSKPIDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCASSPEKIEILAPPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNDECVATYKGVPFEVKGKGVCRAQTMSNSGIK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MANNDAVLK ------CCCHHHHHH	24.43	22223895
9	Ubiquitination	ANNDAVLKRLEQKGA CCHHHHHHHHHHCCC	48.62	-
9	Acetylation	ANNDAVLKRLEQKGA CCHHHHHHHHHHCCC	48.62	25953088
24	Ubiquitination	EADQIIEYLKQQVSL CHHHHHHHHHHHHHH	14.59	-
24 (in isoform 2)	Ubiquitination	-	14.59	21139048
24	Ubiquitination	EADQIIEYLKQQVSL CHHHHHHHHHHHHHH	14.59	21890473
24	Phosphorylation	EADQIIEYLKQQVSL CHHHHHHHHHHHHHH	14.59	-
26	Ubiquitination	DQIIEYLKQQVSLLK HHHHHHHHHHHHHHH	37.47	-
30	Phosphorylation	EYLKQQVSLLKEKAI HHHHHHHHHHHHHHH	24.52	24719451
33	Acetylation	KQQVSLLKEKAILQA HHHHHHHHHHHHHHH	63.56	23236377
33	Ubiquitination	KQQVSLLKEKAILQA HHHHHHHHHHHHHHH	63.56	-
35	Acetylation	QVSLLKEKAILQATL HHHHHHHHHHHHHHH	38.86	25953088
35	Ubiquitination	QVSLLKEKAILQATL HHHHHHHHHHHHHHH	38.86	-
41	Phosphorylation	EKAILQATLREEKKL HHHHHHHHHHHHHHH	17.25	21406692
46	Malonylation	QATLREEKKLRVENA HHHHHHHHHHHHHHH	52.97	26320211
46	Acetylation	QATLREEKKLRVENA HHHHHHHHHHHHHHH	52.97	25953088
48	Phosphorylation	TLREEKKLRVENAKL HHHHHHHHHHHHHHH	12.58	-
54	Acetylation	KLRVENAKLKKEIEE HHHHHHHHHHHHHHH	72.86	25953088
57	Ubiquitination	VENAKLKKEIEELKQ HHHHHHHHHHHHHHH	74.49	-
57	Acetylation	VENAKLKKEIEELKQ HHHHHHHHHHHHHHH	74.49	19608861
59	Ubiquitination	NAKLKKEIEELKQEL HHHHHHHHHHHHHHH	7.37	-
63	Acetylation	KKEIEELKQELIQAE HHHHHHHHHHHHHHH	45.03	23954790
63	Succinylation	KKEIEELKQELIQAE HHHHHHHHHHHHHHH	45.03	23954790
65	Phosphorylation	EIEELKQELIQAEIQ HHHHHHHHHHHHHHH	46.37	-
70 (in isoform 2)	Malonylation	-	28.82	26320211
82	Phosphorylation	VKQIPFPSGTPLHAN CCCCCCCCCCCCCCC	56.53	20068231
84	Phosphorylation	QIPFPSGTPLHANSM CCCCCCCCCCCCCCC	27.32	20068231
87	Ubiquitination	FPSGTPLHANSMVSE CCCCCCCCCCCCCCC	24.86	-
87	Acetylation	FPSGTPLHANSMVSE CCCCCCCCCCCCCCC	24.86	-
90	Phosphorylation	GTPLHANSMVSENVI CCCCCCCCCCCCCEE	22.73	20068231
93	Phosphorylation	LHANSMVSENVIQST CCCCCCCCCCEEECE	18.14	20068231
99	Phosphorylation	VSENVIQSTAVTTVS CCCCEEECEEEEEEC	13.75	20068231
100	Phosphorylation	SENVIQSTAVTTVSS CCCEEECEEEEEECC	14.58	27251275
103	Phosphorylation	VIQSTAVTTVSSGTK EEECEEEEEECCCCH	21.00	20068231
104	Phosphorylation	IQSTAVTTVSSGTKE EECEEEEEECCCCHH	16.28	20068231
106	Phosphorylation	STAVTTVSSGTKEQI CEEEEEECCCCHHHH	22.43	20068231
107	Phosphorylation	TAVTTVSSGTKEQIK EEEEEECCCCHHHHC	46.26	20068231
108	Phosphorylation	AVTTVSSGTKEQIKG EEEEECCCCHHHHCC	33.04	24719451
109	Phosphorylation	VTTVSSGTKEQIKGG EEEECCCCHHHHCCC	33.10	20068231
114	Phosphorylation	SGTKEQIKGGTGDEK CCCHHHHCCCCCCHH	51.48	27251275
137	Sumoylation	KGEKKEKKQQSIAGS HCHHHHHHHHHHCCC	55.45	25114211
140	Phosphorylation	KKEKKQQSIAGSADS HHHHHHHHHCCCCCC	16.35	29255136
144	Phosphorylation	KQQSIAGSADSKPID HHHHHCCCCCCCCCC	21.63	28450419
147	Phosphorylation	SIAGSADSKPIDVSR HHCCCCCCCCCCHHH	39.79	26434776
148	Acetylation	IAGSADSKPIDVSRL HCCCCCCCCCCHHHC	46.68	23236377
148	Malonylation	IAGSADSKPIDVSRL HCCCCCCCCCCHHHC	46.68	26320211
161	S-palmitoylation	RLDLRIGCIITARKH HCEEEEEEEEEEECC	1.57	29575903
161	Sumoylation	RLDLRIGCIITARKH HCEEEEEEEEEEECC	1.57	-
161	S-nitrosocysteine	RLDLRIGCIITARKH HCEEEEEEEEEEECC	1.57	-
161 (in isoform 2)	Malonylation	-	1.57	32601280
161	Glutathionylation	RLDLRIGCIITARKH HCEEEEEEEEEEECC	1.57	22555962
161	S-nitrosylation	RLDLRIGCIITARKH HCEEEEEEEEEEECC	1.57	19483679
164	Phosphorylation	LRIGCIITARKHPDA EEEEEEEEEECCCCC	10.66	24719451
167	Acetylation	GCIITARKHPDADSL EEEEEEECCCCCCCE	57.96	26051181
168	Phosphorylation	CIITARKHPDADSLY EEEEEECCCCCCCEE	21.66	-
172 (in isoform 2)	Malonylation	-	46.70	26320211
173	Phosphorylation	RKHPDADSLYVEEVD ECCCCCCCEEEEEEC	24.26	28348404
175	Phosphorylation	HPDADSLYVEEVDVG CCCCCCEEEEEECCC	15.12	-
187	Methylation	DVGEIAPRTVVSGLV CCCCCCCHHHHHCCC	31.00	115493435
188	Phosphorylation	VGEIAPRTVVSGLVN CCCCCCHHHHHCCCC	24.97	25693802
191	Phosphorylation	IAPRTVVSGLVNHVP CCCHHHHHCCCCCCC	23.29	25693802
197	Phosphorylation	VSGLVNHVPLEQMQN HHCCCCCCCHHHHHH	4.96	-
199	Phosphorylation	GLVNHVPLEQMQNRM CCCCCCCHHHHHHCE	7.50	-
205	Methylation	PLEQMQNRMVILLCN CHHHHHHCEEEEHHC	12.12	115493443
211	Methylation	NRMVILLCNLKPAKM HCEEEEHHCCCHHHH	5.13	-
214	Malonylation	VILLCNLKPAKMRGV EEEHHCCCHHHHHCH	29.01	26320211
214	Acetylation	VILLCNLKPAKMRGV EEEHHCCCHHHHHCH	29.01	25953088
217	Acetylation	LCNLKPAKMRGVLSQ HHCCCHHHHHCHHHH	37.34	25953088
223	Phosphorylation	AKMRGVLSQAMVMCA HHHHCHHHHHHHHHC	17.31	20068231
229	Glutathionylation	LSQAMVMCASSPEKI HHHHHHHHCCCCCCE	1.95	22555962
229	Methylation	LSQAMVMCASSPEKI HHHHHHHHCCCCCCE	1.95	-
231	Phosphorylation	QAMVMCASSPEKIEI HHHHHHCCCCCCEEE	41.31	25159151
232	Phosphorylation	AMVMCASSPEKIEIL HHHHHCCCCCCEEEE	20.67	25159151
238 (in isoform 2)	Malonylation	-	4.53	26320211
247	Phosphorylation	APPNGSVPGDRITFD CCCCCCCCCCEEEEE	40.44	-
250	Methylation	NGSVPGDRITFDAFP CCCCCCCEEEEECCC	35.44	115493427
262	Acetylation	AFPGEPDKELNPKKK CCCCCCCCCCCCCHH	74.86	23954790
267	Acetylation	PDKELNPKKKIWEQI CCCCCCCCHHHHHHH	66.67	29323409
269	Succinylation	KELNPKKKIWEQIQP CCCCCCHHHHHHHCC	60.21	-
269	Succinylation	KELNPKKKIWEQIQP CCCCCCHHHHHHHCC	60.21	-
269	Malonylation	KELNPKKKIWEQIQP CCCCCCHHHHHHHCC	60.21	26320211
274	Methylation	KKKIWEQIQPDLHTN CHHHHHHHCCCCCCC	4.32	-
284	Glutathionylation	DLHTNDECVATYKGV CCCCCCCEEEEECCC	2.55	22555962
286	Acetylation	HTNDECVATYKGVPF CCCCCEEEEECCCCE	19.50	-
289	Acetylation	DECVATYKGVPFEVK CCEEEEECCCCEEEC	49.42	26051181
291 (in isoform 2)	Malonylation	-	4.25	32601280
293 (in isoform 2)	Malonylation	-	18.32	26320211
293	Ubiquitination	ATYKGVPFEVKGKGV EEECCCCEEECCCCE	18.32	-
312	Ubiquitination	TMSNSGIK------- ECCCCCCC-------	58.79	-
336	Ubiquitination	------------------------------- -------------------------------		-

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
140	S	Phosphorylation	Kinase	MAPK8	P45983	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AIMP1_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 AIMP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYRC_HUMAN	RARS	physical	10358004
SMUF2_HUMAN	SMURF2	physical	18448069
PSA7_HUMAN	PSMA7	physical	19362550
A4_HUMAN	APP	physical	21832049
SYRC_HUMAN	RARS	physical	22939629
SYK_HUMAN	KARS	physical	22939629
AIMP2_HUMAN	AIMP2	physical	22939629
SYIC_HUMAN	IARS	physical	22939629
SYQ_HUMAN	QARS	physical	22939629
SYEP_HUMAN	EPRS	physical	22939629
SYMC_HUMAN	MARS	physical	22939629
SYLC_HUMAN	LARS	physical	22939629
SYDC_HUMAN	DARS	physical	22939629
MCA3_HUMAN	EEF1E1	physical	22939629
IQGA1_HUMAN	IQGAP1	physical	22863883
SYK_HUMAN	KARS	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
RL17_HUMAN	RPL17	physical	22863883
HOME1_HUMAN	HOMER1	physical	26344197
SYIC_HUMAN	IARS	physical	26344197
SYMC_HUMAN	MARS	physical	26344197
MCFD2_HUMAN	MCFD2	physical	26344197
SYQ_HUMAN	QARS	physical	26344197
OPTN_HUMAN	OPTN	physical	28514442
SYTC2_HUMAN	TARSL2	physical	28514442
AIMP2_HUMAN	AIMP2	physical	28514442
SYIC_HUMAN	IARS	physical	28514442
MCA3_HUMAN	EEF1E1	physical	28514442
SYEP_HUMAN	EPRS	physical	28514442
SYDC_HUMAN	DARS	physical	28514442
SYMC_HUMAN	MARS	physical	28514442
GCC2_HUMAN	GCC2	physical	28514442
OFD1_HUMAN	OFD1	physical	27173435
TRAP1_HUMAN	TRAP1	physical	27173435
SND1_HUMAN	SND1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
260600	Leukodystrophy, hypomyelinating, 3 (HLD3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AIMP1_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-33, AND MASS SPECTROMETRY.	19608861 [Abstract]