AIMP2_HUMAN - dbPTM
AIMP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AIMP2_HUMAN
UniProt AC Q13155
Protein Name Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Gene Name AIMP2
Organism Homo sapiens (Human).
Sequence Length 320
Subcellular Localization Cytoplasm, cytosol . Nucleus . Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus.
Protein Description Required for assembly and stability of the aminoacyl-tRNA synthase complex. [PubMed: 19131329 Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor.]
Protein Sequence MPMYQVKPYHGGGAPLRVELPTCMYRLPNVHGRSYGPAPGAGHVQEESNLSLQALESRQDDILKRLYELKAAVDGLSKMIQTPDADLDVTNIIQADEPTTLTTNALDLNSVLGKDYGALKDIVINANPASPPLSLLVLHRLLCEHFRVLSTVHTHSSVKSVPENLLKCFGEQNKKQPRQDYQLGFTLIWKNVPKTQMKFSIQTMCPIEGEGNIARFLFSLFGQKHNAVNATLIDSWVDIAIFQLKEGSSKEKAAVFRSMNSALGKSPWLAGNELTVADVVLWSVLQQIGGCSVTVPANVQRWMRSCENLAPFNTALKLLK
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 Orthologous
Protein Cluster
4Phosphorylation----MPMYQVKPYHG
----CCCEECCCCCC
12.3220068231
7Ubiquitination-MPMYQVKPYHGGGA
-CCCEECCCCCCCCC
25.0821890473
7Ubiquitination-MPMYQVKPYHGGGA
-CCCEECCCCCCCCC
25.08-
9PhosphorylationPMYQVKPYHGGGAPL
CCEECCCCCCCCCCC
13.8429496907
17MethylationHGGGAPLRVELPTCM
CCCCCCCEEECCCCE
20.8581424315
22PhosphorylationPLRVELPTCMYRLPN
CCEEECCCCEEECCC
23.6429978859
23GlutathionylationLRVELPTCMYRLPNV
CEEECCCCEEECCCC
1.8122555962
25PhosphorylationVELPTCMYRLPNVHG
EECCCCEEECCCCCC
15.9029978859
26MethylationELPTCMYRLPNVHGR
ECCCCEEECCCCCCC
19.4526494351
33MethylationRLPNVHGRSYGPAPG
ECCCCCCCCCCCCCC
16.3083445863
34PhosphorylationLPNVHGRSYGPAPGA
CCCCCCCCCCCCCCC
38.7528857561
35PhosphorylationPNVHGRSYGPAPGAG
CCCCCCCCCCCCCCC
26.2628152594
48PhosphorylationAGHVQEESNLSLQAL
CCCCCCCCCCCHHHH
42.1728555341
51PhosphorylationVQEESNLSLQALESR
CCCCCCCCHHHHHHC
23.7628555341
64UbiquitinationSRQDDILKRLYELKA
HCHHHHHHHHHHHHH
40.46-
67PhosphorylationDDILKRLYELKAAVD
HHHHHHHHHHHHHHH
24.2120068231
702-HydroxyisobutyrylationLKRLYELKAAVDGLS
HHHHHHHHHHHHHHH
23.51-
70UbiquitinationLKRLYELKAAVDGLS
HHHHHHHHHHHHHHH
23.51-
77PhosphorylationKAAVDGLSKMIQTPD
HHHHHHHHHHCCCCC
26.2120068231
82PhosphorylationGLSKMIQTPDADLDV
HHHHHCCCCCCCCCC
16.5326657352
90PhosphorylationPDADLDVTNIIQADE
CCCCCCCCCEEECCC
21.9928450419
114UbiquitinationDLNSVLGKDYGALKD
HHHHHHCCCCCCCCC
43.55-
130PhosphorylationVINANPASPPLSLLV
EECCCCCCCCHHHHH
28.4521406692
134PhosphorylationNPASPPLSLLVLHRL
CCCCCCHHHHHHHHH
25.9821406692
143S-nitrosylationLVLHRLLCEHFRVLS
HHHHHHHHHHHHHHC
4.5219483679
143S-nitrosocysteineLVLHRLLCEHFRVLS
HHHHHHHHHHHHHHC
4.52-
154PhosphorylationRVLSTVHTHSSVKSV
HHHCCCCCCCCCCCC
21.08-
156PhosphorylationLSTVHTHSSVKSVPE
HCCCCCCCCCCCCCH
37.67-
157PhosphorylationSTVHTHSSVKSVPEN
CCCCCCCCCCCCCHH
26.43-
159UbiquitinationVHTHSSVKSVPENLL
CCCCCCCCCCCHHHH
47.92-
167UbiquitinationSVPENLLKCFGEQNK
CCCHHHHHHHHHCCC
30.59-
174AcetylationKCFGEQNKKQPRQDY
HHHHHCCCCCCCHHH
53.1025953088
186PhosphorylationQDYQLGFTLIWKNVP
HHHCCCEEEEEECCC
18.6118491316
198AcetylationNVPKTQMKFSIQTMC
CCCCCEEEEEEEEEC
26.5826051181
205GlutathionylationKFSIQTMCPIEGEGN
EEEEEEECCCCCCCH
3.3122555962
219PhosphorylationNIARFLFSLFGQKHN
HHHHHHHHHHCCCCC
25.5723898821
252UbiquitinationKEGSSKEKAAVFRSM
CCCCCHHHHHHHHHH
45.44-
2522-HydroxyisobutyrylationKEGSSKEKAAVFRSM
CCCCCHHHHHHHHHH
45.44-
252MalonylationKEGSSKEKAAVFRSM
CCCCCHHHHHHHHHH
45.4426320211
252AcetylationKEGSSKEKAAVFRSM
CCCCCHHHHHHHHHH
45.4425953088
304MethylationANVQRWMRSCENLAP
HHHHHHHHHCCCCCC
31.06115480765
305PhosphorylationNVQRWMRSCENLAPF
HHHHHHHHCCCCCCH
15.0721712546
306GlutathionylationVQRWMRSCENLAPFN
HHHHHHHCCCCCCHH
2.5722555962
317UbiquitinationAPFNTALKLLK----
CCHHHHHHHHC----
49.6721890473
317AcetylationAPFNTALKLLK----
CCHHHHHHHHC----
49.6725953088

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
156SPhosphorylationKinaseMAPK14Q16539
GPS
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:16135753

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AIMP2_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 AIMP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMO3_HUMANLMO3physical
16189514
LNX1_HUMANLNX1physical
16189514
CS057_HUMANC19orf57physical
16189514
AIMP2_HUMANAIMP2physical
16189514
SYRC_HUMANRARSphysical
9878398
SYIC_HUMANIARSphysical
9878398
SYDM_HUMANDARS2physical
9878398
SYQ_HUMANQARSphysical
9878398
SYK_HUMANKARSphysical
9878398
P53_HUMANTP53physical
18695251
PRKN_HUMANPARK2physical
16135753
CHIP_HUMANSTUB1physical
16135753
HSP74_HUMANHSPA4physical
16135753
SYK_HUMANKARSphysical
21900206
DEAF1_HUMANDEAF1physical
21900206
VGFR2_HUMANKDRphysical
21900206
KLC2_HUMANKLC2physical
21900206
PSME1_HUMANPSME1physical
21900206
CE126_HUMANKIAA1377physical
21900206
MATR3_HUMANMATR3physical
21900206
BL1S4_HUMANBLOC1S4physical
21900206
ZC12A_HUMANZC3H12Aphysical
21900206
DSN1_HUMANDSN1physical
21900206
2AAA_HUMANPPP2R1Aphysical
21900206
CHD3_HUMANCHD3physical
21900206
MCF2L_HUMANMCF2Lphysical
21900206
SYDC_HUMANDARSphysical
21900206
TRM2A_HUMANTRMT2Aphysical
21900206
ACTB_HUMANACTBphysical
21900206
ICE1_HUMANICE1physical
21900206
FIBB_HUMANFGBphysical
21900206
LC7L2_HUMANLUC7L2physical
21900206
TRAF2_HUMANTRAF2physical
19584093
SYK_HUMANKARSphysical
19584093
A4_HUMANAPPphysical
21832049
SYK_HUMANKARSphysical
22939629
SYDC_HUMANDARSphysical
22939629
SYEP_HUMANEPRSphysical
22939629
SYIC_HUMANIARSphysical
22939629
SYRC_HUMANRARSphysical
22939629
SYQ_HUMANQARSphysical
22939629
SYLC_HUMANLARSphysical
22939629
SYMC_HUMANMARSphysical
22939629
MCA3_HUMANEEF1E1physical
22939629
UBA1_HUMANUBA1physical
22939629
CS057_HUMANC19orf57physical
19060904
BEX3_HUMANNGFRAP1physical
21988832
SYK_HUMANKARSphysical
21988832
FUBP1_HUMANFUBP1physical
21988832
TANK_HUMANTANKphysical
21988832
AIMP1_HUMANAIMP1physical
22863883
ROA1_HUMANHNRNPA1physical
22863883
SYIC_HUMANIARSphysical
22863883
IQGA1_HUMANIQGAP1physical
22863883
PRS10_HUMANPSMC6physical
22863883
PTBP1_HUMANPTBP1physical
22863883
AIMP1_HUMANAIMP1physical
25416956
SPF27_HUMANBCAS2physical
25416956
TFP11_HUMANTFIP11physical
25416956
MS18A_HUMANMIS18Aphysical
25416956
NECA2_HUMANNECAB2physical
25416956
CS057_HUMANC19orf57physical
25416956
PKHF2_HUMANPLEKHF2physical
25416956
NDEL1_HUMANNDEL1physical
25416956
ZGPAT_HUMANZGPATphysical
25416956
LNX1_HUMANLNX1physical
25416956
AIMP1_HUMANAIMP1physical
26344197
VATE1_HUMANATP6V1E1physical
26344197
MCA3_HUMANEEF1E1physical
26344197
SYLC_HUMANLARSphysical
26344197
PIN4_HUMANPIN4physical
26344197
PSMD4_HUMANPSMD4physical
26344197
SYQ_HUMANQARSphysical
26344197
SYRC_HUMANRARSphysical
26344197
TWF1_HUMANTWF1physical
26344197
UBA1_HUMANUBA1physical
26344197
FUBP1_HUMANFUBP1physical
12819782
SYK_HUMANKARSphysical
12819782
AIMP2_HUMANAIMP2physical
12819782
SMUF2_HUMANSMURF2physical
27197155
PRKN_HUMANPARK2physical
27197155
TRAF6_HUMANTRAF6physical
27197155
OFD1_HUMANOFD1physical
27173435
AIMP1_HUMANAIMP1physical
27173435
PARP1_HUMANPARP1physical
28383562

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
There are no disease associations of PTM sites.
Regulatory Network of AIMP2_HUMAN

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Related Literatures of Post-Translational Modification

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