ABCE1_HUMAN - dbPTM
ABCE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCE1_HUMAN
UniProt AC P61221
Protein Name ATP-binding cassette sub-family E member 1
Gene Name ABCE1
Organism Homo sapiens (Human).
Sequence Length 599
Subcellular Localization Cytoplasm . Mitochondrion . Localized to clusters of virus formation at the plasma membrane.
Protein Description Antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) by RNase L through direct interaction with RNase L and therefore inhibits its endoribonuclease activity. May play a central role in the regulation of mRNA turnover. Antagonizes the anti-viral effect of the interferon-regulated 2-5A/RNase L pathway. May act as a chaperone for post-translational events during HIV-1 capsid assembly..
Protein Sequence MADKLTRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSNLEKETTHRYCANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLKAIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYVPTENLRFRDASLVFKVAETANEEEVKKMCMYKYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQKISPKSTGSVRQLLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEITFRRDPNNYRPRINKLNSIKDVEQKKSGNYFFLDD
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
4Ubiquitination----MADKLTRIAIV
----CCCCCEEEEEE
42.07-
15UbiquitinationIAIVNHDKCKPKKCR
EEEECCCCCCCHHHH
36.2929967540
17UbiquitinationIVNHDKCKPKKCRQE
EECCCCCCCHHHHHH
66.6629967540
19UbiquitinationNHDKCKPKKCRQECK
CCCCCCCHHHHHHHH
50.42-
27UbiquitinationKCRQECKKSCPVVRM
HHHHHHHHHCCEEEE
69.7927667366
36UbiquitinationCPVVRMGKLCIEVTP
CCEEEECCEEEEECC
30.73-
36AcetylationCPVVRMGKLCIEVTP
CCEEEECCEEEEECC
30.7325953088
42PhosphorylationGKLCIEVTPQSKIAW
CCEEEEECCCCHHHH
11.6525159151
45PhosphorylationCIEVTPQSKIAWISE
EEEECCCCHHHHHHC
27.5121815630
63UbiquitinationIGCGICIKKCPFGAL
CCCCCEEECCCCCCE
43.8622817900
64UbiquitinationGCGICIKKCPFGALS
CCCCEEECCCCCCEE
27.5122817900
65S-palmitoylationCGICIKKCPFGALSI
CCCEEECCCCCCEEE
2.6129575903
71PhosphorylationKCPFGALSIVNLPSN
CCCCCCEEEECCCCC
24.7727050516
81UbiquitinationNLPSNLEKETTHRYC
CCCCCCCHHCCHHHH
64.6221963094
87PhosphorylationEKETTHRYCANAFKL
CHHCCHHHHHCCHHH
6.5729496907
93AcetylationRYCANAFKLHRLPIP
HHHHCCHHHCCCCCC
40.7625953088
93UbiquitinationRYCANAFKLHRLPIP
HHHHCCHHHCCCCCC
40.7625015289
93MethylationRYCANAFKLHRLPIP
HHHHCCHHHCCCCCC
40.76-
111PhosphorylationEVLGLVGTNGIGKST
CEEEEEECCCCCHHH
23.8546156877
116UbiquitinationVGTNGIGKSTALKIL
EECCCCCHHHHHHHH
42.5921906983
117PhosphorylationGTNGIGKSTALKILA
ECCCCCHHHHHHHHC
17.4468734809
121MalonylationIGKSTALKILAGKQK
CCHHHHHHHHCCCCC
32.9626320211
121UbiquitinationIGKSTALKILAGKQK
CCHHHHHHHHCCCCC
32.9621906983
121AcetylationIGKSTALKILAGKQK
CCHHHHHHHHCCCCC
32.9619608861
126UbiquitinationALKILAGKQKPNLGK
HHHHHCCCCCCCCCC
49.9322817900
126AcetylationALKILAGKQKPNLGK
HHHHHCCCCCCCCCC
49.9325953088
128UbiquitinationKILAGKQKPNLGKYD
HHHCCCCCCCCCCCC
39.0821906983
133UbiquitinationKQKPNLGKYDDPPDW
CCCCCCCCCCCCCCH
48.9821963094
155NitrationRGSELQNYFTKILED
CHHHHHHHHHHHHHH
10.32-
155PhosphorylationRGSELQNYFTKILED
CHHHHHHHHHHHHHH
10.3228152594
157PhosphorylationSELQNYFTKILEDDL
HHHHHHHHHHHHHHH
13.5528152594
158UbiquitinationELQNYFTKILEDDLK
HHHHHHHHHHHHHHH
35.0821906983
158AcetylationELQNYFTKILEDDLK
HHHHHHHHHHHHHHH
35.08129683
165AcetylationKILEDDLKAIIKPQY
HHHHHHHHHHHCHHH
44.5325953088
165UbiquitinationKILEDDLKAIIKPQY
HHHHHHHHHHHCHHH
44.5321906983
169UbiquitinationDDLKAIIKPQYVDQI
HHHHHHHCHHHHHHC
21.6927667366
172PhosphorylationKAIIKPQYVDQIPKA
HHHHCHHHHHHCCHH
17.9628152594
178AcetylationQYVDQIPKAAKGTVG
HHHHHCCHHCCCCHH
63.7125953088
178UbiquitinationQYVDQIPKAAKGTVG
HHHHHCCHHCCCCHH
63.7121906983
178MalonylationQYVDQIPKAAKGTVG
HHHHHCCHHCCCCHH
63.7132601280
1812-HydroxyisobutyrylationDQIPKAAKGTVGSIL
HHCCHHCCCCHHHHH
61.03-
181UbiquitinationDQIPKAAKGTVGSIL
HHCCHHCCCCHHHHH
61.0321906983
181MalonylationDQIPKAAKGTVGSIL
HHCCHHCCCCHHHHH
61.0326320211
183PhosphorylationIPKAAKGTVGSILDR
CCHHCCCCHHHHHCC
22.4620068231
186PhosphorylationAAKGTVGSILDRKDE
HCCCCHHHHHCCCCC
18.6820068231
191UbiquitinationVGSILDRKDETKTQA
HHHHHCCCCCHHHHE
60.6322817900
191MalonylationVGSILDRKDETKTQA
HHHHHCCCCCHHHHE
60.6326320211
191AcetylationVGSILDRKDETKTQA
HHHHHCCCCCHHHHE
60.6323954790
195UbiquitinationLDRKDETKTQAIVCQ
HCCCCCHHHHEEEEE
36.2722817900
210AcetylationQLDLTHLKERNVEDL
HHCCHHHHHCCHHHC
47.2023749302
210MalonylationQLDLTHLKERNVEDL
HHCCHHHHHCCHHHC
47.2026320211
210UbiquitinationQLDLTHLKERNVEDL
HHCCHHHHHCCHHHC
47.2027667366
2102-HydroxyisobutyrylationQLDLTHLKERNVEDL
HHCCHHHHHCCHHHC
47.20-
218PhosphorylationERNVEDLSGGELQRF
HCCHHHCCHHHHHHH
58.0146156859
227S-palmitoylationGELQRFACAVVCIQK
HHHHHHHEEEEEEEE
2.4429575903
231S-palmitoylationRFACAVVCIQKADIF
HHHEEEEEEEECCEE
1.8829575903
239SulfoxidationIQKADIFMFDEPSSY
EEECCEEEECCCHHH
4.1730846556
250UbiquitinationPSSYLDVKQRLKAAI
CHHHCCHHHHHHHHH
29.3921963094
254UbiquitinationLDVKQRLKAAITIRS
CCHHHHHHHHHHHHH
37.6522817900
325MethylationPTENLRFRDASLVFK
CCCCCCCCHHHHEEE
31.95-
328PhosphorylationNLRFRDASLVFKVAE
CCCCCHHHHEEEEEC
29.3822617229
332UbiquitinationRDASLVFKVAETANE
CHHHHEEEEECCCCH
32.8121906983
343AcetylationTANEEEVKKMCMYKY
CCCHHHHHHHHHHCC
37.7623749302
343UbiquitinationTANEEEVKKMCMYKY
CCCHHHHHHHHHHCC
37.7621906983
344UbiquitinationANEEEVKKMCMYKYP
CCHHHHHHHHHHCCC
42.3722817900
349AcetylationVKKMCMYKYPGMKKK
HHHHHHHCCCCHHHC
20.3419608861
349UbiquitinationVKKMCMYKYPGMKKK
HHHHHHHCCCCHHHC
20.3419608861
372PhosphorylationVAGEFTDSEIMVMLG
EEEECCCCEEEEEEC
26.4322210691
397UbiquitinationRMLAGRLKPDEGGEV
HHHCCCCCCCCCCCC
49.4121906983
410PhosphorylationEVPVLNVSYKPQKIS
CCCEEEEEECCCCCC
26.7728152594
411PhosphorylationVPVLNVSYKPQKISP
CCEEEEEECCCCCCC
23.5428152594
412UbiquitinationPVLNVSYKPQKISPK
CEEEEEECCCCCCCC
33.2021906983
415UbiquitinationNVSYKPQKISPKSTG
EEEECCCCCCCCCCC
54.3929967540
417PhosphorylationSYKPQKISPKSTGSV
EECCCCCCCCCCCHH
33.0521406692
419UbiquitinationKPQKISPKSTGSVRQ
CCCCCCCCCCCHHHH
54.5929967540
419AcetylationKPQKISPKSTGSVRQ
CCCCCCCCCCCHHHH
54.5927452117
420PhosphorylationPQKISPKSTGSVRQL
CCCCCCCCCCHHHHH
41.1921406692
421PhosphorylationQKISPKSTGSVRQLL
CCCCCCCCCHHHHHH
39.3321406692
423PhosphorylationISPKSTGSVRQLLHE
CCCCCCCHHHHHHHH
17.7621406692
431UbiquitinationVRQLLHEKIRDAYTH
HHHHHHHHHHHHHCC
32.0924816145
431AcetylationVRQLLHEKIRDAYTH
HHHHHHHHHHHHHCC
32.0923749302
447UbiquitinationQFVTDVMKPLQIENI
HHHCCCCCCCCHHHH
42.2829967540
478UbiquitinationALALCLGKPADVYLI
HHHHHHCCCCCEEEE
24.8829967540
478AcetylationALALCLGKPADVYLI
HHHHHHCCCCCEEEE
24.8826051181
5122-HydroxyisobutyrylationKRFILHAKKTAFVVE
HHHHHHHHCCEEEEE
39.65-
541UbiquitinationVFDGVPSKNTVANSP
EECCCCCCCCCCCCH
51.0421906983
547PhosphorylationSKNTVANSPQTLLAG
CCCCCCCCHHHHHHH
14.5125159151
550PhosphorylationTVANSPQTLLAGMNK
CCCCCHHHHHHHHHH
27.4223186163
560PhosphorylationAGMNKFLSQLEITFR
HHHHHHHHHHHEEEC
35.5322210691
579UbiquitinationNYRPRINKLNSIKDV
CCCCCCCCCCCCCCH
46.8322817900
582PhosphorylationPRINKLNSIKDVEQK
CCCCCCCCCCCHHHH
41.2628450419
584UbiquitinationINKLNSIKDVEQKKS
CCCCCCCCCHHHHHC
56.3921906983
584AcetylationINKLNSIKDVEQKKS
CCCCCCCCCHHHHHC
56.3923749302
589UbiquitinationSIKDVEQKKSGNYFF
CCCCHHHHHCCCCEE
35.0922817900
590UbiquitinationIKDVEQKKSGNYFFL
CCCHHHHHCCCCEEC
64.3922817900
591PhosphorylationKDVEQKKSGNYFFLD
CCHHHHHCCCCEECC
39.0328796482
594NitrationEQKKSGNYFFLDD--
HHHHCCCCEECCC--
10.15-
594PhosphorylationEQKKSGNYFFLDD--
HHHHCCCCEECCC--
10.1528796482

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 ABCE1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCE1_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 ABCE1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RN5A_HUMANRNASELphysical
7539425
UBS3A_HUMANUBASH3Aphysical
18006034
AP1B1_HUMANAP1B1physical
22863883
DBLOH_HUMANDIABLOphysical
22863883
PDIA3_HUMANPDIA3physical
22863883
STAU1_HUMANSTAU1physical
23125841
ABCF1_HUMANABCF1physical
25659154
FUBP3_HUMANFUBP3physical
25659154
CBX3_HUMANCBX3physical
25659154
ODPA_HUMANPDHA1physical
25659154
ABLM1_HUMANABLIM1physical
25659154
CNIH4_HUMANCNIH4physical
25659154
NAA10_HUMANNAA10physical
25659154
PSMD4_HUMANPSMD4physical
25659154
COR1C_HUMANCORO1Cphysical
25659154
MK01_HUMANMAPK1physical
25659154
SRP09_HUMANSRP9physical
25659154
TIM21_HUMANTIMM21physical
25659154
SNP23_HUMANSNAP23physical
25659154
H12_HUMANHIST1H1Cphysical
25659154
E41L3_HUMANEPB41L3physical
25659154
CUL4A_HUMANCUL4Aphysical
25659154
ZN207_HUMANZNF207physical
25659154
PCP_HUMANPRCPphysical
25659154
TTC29_HUMANTTC29physical
25659154
WDR1_HUMANWDR1physical
25659154
EIF3D_HUMANEIF3Dphysical
25659154
EWS_HUMANEWSR1physical
25659154
PAK3_HUMANPAK3physical
25659154
TIM23_HUMANTIMM23physical
25659154
PFD2_HUMANPFDN2physical
25659154
H3C_HUMANH3F3Cphysical
25659154
H2B2F_HUMANHIST2H2BFphysical
25659154
FLNB_HUMANFLNBphysical
25659154
SAE1_HUMANSAE1physical
25659154
TEBP_HUMANPTGES3physical
25659154
PSD13_HUMANPSMD13physical
25659154
STRAP_HUMANSTRAPphysical
25659154
MEP50_HUMANWDR77physical
25659154
TPP1_HUMANTPP1physical
25659154
GNS_HUMANGNSphysical
25659154
2ABA_HUMANPPP2R2Aphysical
25659154
CD44_HUMANCD44physical
25659154
VATA_HUMANATP6V1Aphysical
25659154
INO1_HUMANISYNA1physical
25659154
ERF1_HUMANETF1physical
25659154
CCNY_HUMANCCNYphysical
25659154
MIC60_HUMANIMMTphysical
25659154
CP096_HUMANC16orf96physical
25659154
RRP1B_HUMANRRP1Bphysical
25659154
RFC4_HUMANRFC4physical
25659154
RL32_HUMANRPL32physical
25659154
PEBP1_HUMANPEBP1physical
25659154
TFAM_HUMANTFAMphysical
25659154
ELOC_HUMANTCEB1physical
25659154
FLOT2_HUMANFLOT2physical
25659154
SSFA2_HUMANSSFA2physical
25659154
ERF3A_HUMANGSPT1physical
25659154
NAT10_HUMANNAT10physical
25659154
SYAC_HUMANAARSphysical
25659154
MAP4_HUMANMAP4physical
25659154
MYO6_HUMANMYO6physical
25659154
FLNA_HUMANFLNAphysical
25659154
RAVR1_HUMANRAVER1physical
25659154
RBBP7_HUMANRBBP7physical
25659154
ASNS_HUMANASNSphysical
25659154
FPPS_HUMANFDPSphysical
25659154
RRP12_HUMANRRP12physical
25659154
SYK_HUMANKARSphysical
25659154
41_HUMANEPB41physical
25659154
SFXN4_HUMANSFXN4physical
25659154
TSN_HUMANTSNphysical
25659154
RPR1B_HUMANRPRD1Bphysical
25659154
CD59_HUMANCD59physical
25659154
ORAV1_HUMANORAOV1physical
25659154
SRRM2_HUMANSRRM2physical
25659154
SMCA5_HUMANSMARCA5physical
25659154
RPA2_HUMANPOLR1Bphysical
25659154
SAFB1_HUMANSAFBphysical
25659154
RAB35_HUMANRAB35physical
25659154
SUCB2_HUMANSUCLG2physical
25659154
MED23_HUMANMED23physical
25659154
VDAC3_HUMANVDAC3physical
25659154
PPM1G_HUMANPPM1Gphysical
25659154
MFGM_HUMANMFGE8physical
25659154
DDX18_HUMANDDX18physical
25659154
HAX1_HUMANHAX1physical
25659154
NDUA4_HUMANNDUFA4physical
25659154
PSDE_HUMANPSMD14physical
25659154
PPP6_HUMANPPP6Cphysical
25659154
SURF4_HUMANSURF4physical
25659154
ARPC5_HUMANARPC5physical
25659154
E41L2_HUMANEPB41L2physical
25659154
DKC1_HUMANDKC1physical
25659154
PSIP1_HUMANPSIP1physical
25659154
XRP2_HUMANRP2physical
25659154
CBR3_HUMANCBR3physical
25659154
FLOT1_HUMANFLOT1physical
25659154
CIAO1_HUMANCIAO1physical
25659154
UFL1_HUMANUFL1physical
25659154
AIFM1_HUMANAIFM1physical
25659154
PNPH_HUMANPNPphysical
25659154
LMNA_HUMANLMNAphysical
25659154
CYTB_HUMANCSTBphysical
25659154
P53_HUMANTP53physical
25659154
FYN_HUMANFYNphysical
25659154
HEXB_HUMANHEXBphysical
25659154
LYN_HUMANLYNphysical
25659154
VIME_HUMANVIMphysical
25659154
PTPRF_HUMANPTPRFphysical
25659154
PPGB_HUMANCTSAphysical
25659154
RALA_HUMANRALAphysical
25659154
MPRI_HUMANIGF2Rphysical
25659154
ADT1_HUMANSLC25A4physical
25659154
SRC_HUMANSRCphysical
25659154
KAP2_HUMANPRKAR2Aphysical
25659154
PLAK_HUMANJUPphysical
25659154
BGAL_HUMANGLB1physical
25659154
KAPCA_HUMANPRKACAphysical
25659154
PFKAL_HUMANPFKLphysical
25659154
RL35A_HUMANRPL35Aphysical
25659154
GNAZ_HUMANGNAZphysical
25659154
SPEE_HUMANSRMphysical
25659154
LMNB1_HUMANLMNB1physical
25659154
SDHB_HUMANSDHBphysical
25659154
FBRL_HUMANFBLphysical
25659154
THIL_HUMANACAT1physical
25659154
RS12_HUMANRPS12physical
25659154
PSA2_HUMANPSMA2physical
25659154
MOES_HUMANMSNphysical
25659154
APEX1_HUMANAPEX1physical
25659154
PSA5_HUMANPSMA5physical
25659154
GNA11_HUMANGNA11physical
25659154
KINH_HUMANKIF5Bphysical
25659154
DUT_HUMANDUTphysical
25659154
PRS7_HUMANPSMC2physical
25659154
PP1G_HUMANPPP1CCphysical
25659154
IF4A3_HUMANEIF4A3physical
25659154
LAP2A_HUMANTMPOphysical
25659154
LAP2B_HUMANTMPOphysical
25659154
RS27_HUMANRPS27physical
25659154
VDAC2_HUMANVDAC2physical
25659154
CBX5_HUMANCBX5physical
25659154
RL21_HUMANRPL21physical
25659154
MAP1B_HUMANMAP1Bphysical
25659154
IQGA1_HUMANIQGAP1physical
25659154
PSMD8_HUMANPSMD8physical
25659154
PSB3_HUMANPSMB3physical
25659154
GNAQ_HUMANGNAQphysical
25659154
CA2D1_HUMANCACNA2D1physical
25659154
KAD2_HUMANAK2physical
25659154
S10AA_HUMANS100A10physical
25659154
ABCE1_HUMANABCE1physical
25659154
RAP2B_HUMANRAP2Bphysical
25659154
CH10_HUMANHSPE1physical
25659154
PP1B_HUMANPPP1CBphysical
25659154
RS29_HUMANRPS29physical
25659154
RUXF_HUMANSNRPFphysical
25659154
RS25_HUMANRPS25physical
25659154
GBB1_HUMANGNB1physical
25659154
DYL1_HUMANDYNLL1physical
25659154
GBG5_HUMANGNG5physical
25659154
ANK2_HUMANANK2physical
25659154
LMNB2_HUMANLMNB2physical
25659154
1433F_HUMANYWHAHphysical
25659154
TWF1_HUMANTWF1physical
25659154
DSG2_HUMANDSG2physical
25659154
SMC1A_HUMANSMC1Aphysical
25659154
NUMA1_HUMANNUMA1physical
25659154
EBP_HUMANEBPphysical
25659154
TOM20_HUMANTOMM20physical
25659154
SF3A1_HUMANSF3A1physical
25659154
MARE1_HUMANMAPRE1physical
25659154
NDUA5_HUMANNDUFA5physical
25659154
CN166_HUMANC14orf166physical
25659154
AIF1L_HUMANAIF1Lphysical
25659154
ULBP3_HUMANULBP3physical
25659154
TTC37_HUMANTTC37physical
25659154
DDX46_HUMANDDX46physical
25659154
DCXR_HUMANDCXRphysical
25659154
DNJC7_HUMANDNAJC7physical
25659154
PEG10_HUMANPEG10physical
25659154
GA2L3_HUMANGAS2L3physical
25659154
G45IP_HUMANGADD45GIP1physical
25659154
CIP2A_HUMANKIAA1524physical
25659154
HM13_HUMANHM13physical
25659154
MAIP1_HUMANC2orf47physical
25659154
ATX2L_HUMANATXN2Lphysical
25659154
UBP7_HUMANUSP7physical
25659154
MACF1_HUMANMACF1physical
25659154
MMS19_HUMANMMS19physical
25659154
PSMD1_HUMANPSMD1physical
25659154
CAB45_HUMANSDF4physical
25659154
TBCD_HUMANTBCDphysical
25659154
CPVL_HUMANCPVLphysical
25659154
GBB4_HUMANGNB4physical
25659154
EXOS4_HUMANEXOSC4physical
25659154
YAED1_HUMANYAE1D1physical
25659154
SMC4_HUMANSMC4physical
25659154
MDN1_HUMANMDN1physical
25659154
FANCI_HUMANFANCIphysical
25659154
TECR_HUMANTECRphysical
25659154
CISD1_HUMANCISD1physical
25659154
NDUF4_HUMANNDUFAF4physical
25659154
NDUAD_HUMANNDUFA13physical
25659154
STAR9_HUMANSTARD9physical
25659154
ATX10_HUMANATXN10physical
25659154
CPSF3_HUMANCPSF3physical
25659154
RL36_HUMANRPL36physical
25659154
SP16H_HUMANSUPT16Hphysical
25659154
RL4_HUMANRPL4physical
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
There are no disease associations of PTM sites.
Regulatory Network of ABCE1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-121; LYS-191; LYS-210;LYS-349 AND LYS-431, AND MASS SPECTROMETRY.

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