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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
4 | Ubiquitination | ----MADKLTRIAIV ----CCCCCEEEEEE | 42.07 | - | |
15 | Ubiquitination | IAIVNHDKCKPKKCR EEEECCCCCCCHHHH | 36.29 | 29967540 | |
17 | Ubiquitination | IVNHDKCKPKKCRQE EECCCCCCCHHHHHH | 66.66 | 29967540 | |
19 | Ubiquitination | NHDKCKPKKCRQECK CCCCCCCHHHHHHHH | 50.42 | - | |
27 | Ubiquitination | KCRQECKKSCPVVRM HHHHHHHHHCCEEEE | 69.79 | 27667366 | |
36 | Ubiquitination | CPVVRMGKLCIEVTP CCEEEECCEEEEECC | 30.73 | - | |
36 | Acetylation | CPVVRMGKLCIEVTP CCEEEECCEEEEECC | 30.73 | 25953088 | |
42 | Phosphorylation | GKLCIEVTPQSKIAW CCEEEEECCCCHHHH | 11.65 | 25159151 | |
45 | Phosphorylation | CIEVTPQSKIAWISE EEEECCCCHHHHHHC | 27.51 | 21815630 | |
63 | Ubiquitination | IGCGICIKKCPFGAL CCCCCEEECCCCCCE | 43.86 | 22817900 | |
64 | Ubiquitination | GCGICIKKCPFGALS CCCCEEECCCCCCEE | 27.51 | 22817900 | |
65 | S-palmitoylation | CGICIKKCPFGALSI CCCEEECCCCCCEEE | 2.61 | 29575903 | |
71 | Phosphorylation | KCPFGALSIVNLPSN CCCCCCEEEECCCCC | 24.77 | 27050516 | |
81 | Ubiquitination | NLPSNLEKETTHRYC CCCCCCCHHCCHHHH | 64.62 | 21963094 | |
87 | Phosphorylation | EKETTHRYCANAFKL CHHCCHHHHHCCHHH | 6.57 | 29496907 | |
93 | Acetylation | RYCANAFKLHRLPIP HHHHCCHHHCCCCCC | 40.76 | 25953088 | |
93 | Ubiquitination | RYCANAFKLHRLPIP HHHHCCHHHCCCCCC | 40.76 | 25015289 | |
93 | Methylation | RYCANAFKLHRLPIP HHHHCCHHHCCCCCC | 40.76 | - | |
111 | Phosphorylation | EVLGLVGTNGIGKST CEEEEEECCCCCHHH | 23.85 | 46156877 | |
116 | Ubiquitination | VGTNGIGKSTALKIL EECCCCCHHHHHHHH | 42.59 | 21906983 | |
117 | Phosphorylation | GTNGIGKSTALKILA ECCCCCHHHHHHHHC | 17.44 | 68734809 | |
121 | Malonylation | IGKSTALKILAGKQK CCHHHHHHHHCCCCC | 32.96 | 26320211 | |
121 | Ubiquitination | IGKSTALKILAGKQK CCHHHHHHHHCCCCC | 32.96 | 21906983 | |
121 | Acetylation | IGKSTALKILAGKQK CCHHHHHHHHCCCCC | 32.96 | 19608861 | |
126 | Ubiquitination | ALKILAGKQKPNLGK HHHHHCCCCCCCCCC | 49.93 | 22817900 | |
126 | Acetylation | ALKILAGKQKPNLGK HHHHHCCCCCCCCCC | 49.93 | 25953088 | |
128 | Ubiquitination | KILAGKQKPNLGKYD HHHCCCCCCCCCCCC | 39.08 | 21906983 | |
133 | Ubiquitination | KQKPNLGKYDDPPDW CCCCCCCCCCCCCCH | 48.98 | 21963094 | |
155 | Nitration | RGSELQNYFTKILED CHHHHHHHHHHHHHH | 10.32 | - | |
155 | Phosphorylation | RGSELQNYFTKILED CHHHHHHHHHHHHHH | 10.32 | 28152594 | |
157 | Phosphorylation | SELQNYFTKILEDDL HHHHHHHHHHHHHHH | 13.55 | 28152594 | |
158 | Ubiquitination | ELQNYFTKILEDDLK HHHHHHHHHHHHHHH | 35.08 | 21906983 | |
158 | Acetylation | ELQNYFTKILEDDLK HHHHHHHHHHHHHHH | 35.08 | 129683 | |
165 | Acetylation | KILEDDLKAIIKPQY HHHHHHHHHHHCHHH | 44.53 | 25953088 | |
165 | Ubiquitination | KILEDDLKAIIKPQY HHHHHHHHHHHCHHH | 44.53 | 21906983 | |
169 | Ubiquitination | DDLKAIIKPQYVDQI HHHHHHHCHHHHHHC | 21.69 | 27667366 | |
172 | Phosphorylation | KAIIKPQYVDQIPKA HHHHCHHHHHHCCHH | 17.96 | 28152594 | |
178 | Acetylation | QYVDQIPKAAKGTVG HHHHHCCHHCCCCHH | 63.71 | 25953088 | |
178 | Ubiquitination | QYVDQIPKAAKGTVG HHHHHCCHHCCCCHH | 63.71 | 21906983 | |
178 | Malonylation | QYVDQIPKAAKGTVG HHHHHCCHHCCCCHH | 63.71 | 32601280 | |
181 | 2-Hydroxyisobutyrylation | DQIPKAAKGTVGSIL HHCCHHCCCCHHHHH | 61.03 | - | |
181 | Ubiquitination | DQIPKAAKGTVGSIL HHCCHHCCCCHHHHH | 61.03 | 21906983 | |
181 | Malonylation | DQIPKAAKGTVGSIL HHCCHHCCCCHHHHH | 61.03 | 26320211 | |
183 | Phosphorylation | IPKAAKGTVGSILDR CCHHCCCCHHHHHCC | 22.46 | 20068231 | |
186 | Phosphorylation | AAKGTVGSILDRKDE HCCCCHHHHHCCCCC | 18.68 | 20068231 | |
191 | Ubiquitination | VGSILDRKDETKTQA HHHHHCCCCCHHHHE | 60.63 | 22817900 | |
191 | Malonylation | VGSILDRKDETKTQA HHHHHCCCCCHHHHE | 60.63 | 26320211 | |
191 | Acetylation | VGSILDRKDETKTQA HHHHHCCCCCHHHHE | 60.63 | 23954790 | |
195 | Ubiquitination | LDRKDETKTQAIVCQ HCCCCCHHHHEEEEE | 36.27 | 22817900 | |
210 | Acetylation | QLDLTHLKERNVEDL HHCCHHHHHCCHHHC | 47.20 | 23749302 | |
210 | Malonylation | QLDLTHLKERNVEDL HHCCHHHHHCCHHHC | 47.20 | 26320211 | |
210 | Ubiquitination | QLDLTHLKERNVEDL HHCCHHHHHCCHHHC | 47.20 | 27667366 | |
210 | 2-Hydroxyisobutyrylation | QLDLTHLKERNVEDL HHCCHHHHHCCHHHC | 47.20 | - | |
218 | Phosphorylation | ERNVEDLSGGELQRF HCCHHHCCHHHHHHH | 58.01 | 46156859 | |
227 | S-palmitoylation | GELQRFACAVVCIQK HHHHHHHEEEEEEEE | 2.44 | 29575903 | |
231 | S-palmitoylation | RFACAVVCIQKADIF HHHEEEEEEEECCEE | 1.88 | 29575903 | |
239 | Sulfoxidation | IQKADIFMFDEPSSY EEECCEEEECCCHHH | 4.17 | 30846556 | |
250 | Ubiquitination | PSSYLDVKQRLKAAI CHHHCCHHHHHHHHH | 29.39 | 21963094 | |
254 | Ubiquitination | LDVKQRLKAAITIRS CCHHHHHHHHHHHHH | 37.65 | 22817900 | |
325 | Methylation | PTENLRFRDASLVFK CCCCCCCCHHHHEEE | 31.95 | - | |
328 | Phosphorylation | NLRFRDASLVFKVAE CCCCCHHHHEEEEEC | 29.38 | 22617229 | |
332 | Ubiquitination | RDASLVFKVAETANE CHHHHEEEEECCCCH | 32.81 | 21906983 | |
343 | Acetylation | TANEEEVKKMCMYKY CCCHHHHHHHHHHCC | 37.76 | 23749302 | |
343 | Ubiquitination | TANEEEVKKMCMYKY CCCHHHHHHHHHHCC | 37.76 | 21906983 | |
344 | Ubiquitination | ANEEEVKKMCMYKYP CCHHHHHHHHHHCCC | 42.37 | 22817900 | |
349 | Acetylation | VKKMCMYKYPGMKKK HHHHHHHCCCCHHHC | 20.34 | 19608861 | |
349 | Ubiquitination | VKKMCMYKYPGMKKK HHHHHHHCCCCHHHC | 20.34 | 19608861 | |
372 | Phosphorylation | VAGEFTDSEIMVMLG EEEECCCCEEEEEEC | 26.43 | 22210691 | |
397 | Ubiquitination | RMLAGRLKPDEGGEV HHHCCCCCCCCCCCC | 49.41 | 21906983 | |
410 | Phosphorylation | EVPVLNVSYKPQKIS CCCEEEEEECCCCCC | 26.77 | 28152594 | |
411 | Phosphorylation | VPVLNVSYKPQKISP CCEEEEEECCCCCCC | 23.54 | 28152594 | |
412 | Ubiquitination | PVLNVSYKPQKISPK CEEEEEECCCCCCCC | 33.20 | 21906983 | |
415 | Ubiquitination | NVSYKPQKISPKSTG EEEECCCCCCCCCCC | 54.39 | 29967540 | |
417 | Phosphorylation | SYKPQKISPKSTGSV EECCCCCCCCCCCHH | 33.05 | 21406692 | |
419 | Ubiquitination | KPQKISPKSTGSVRQ CCCCCCCCCCCHHHH | 54.59 | 29967540 | |
419 | Acetylation | KPQKISPKSTGSVRQ CCCCCCCCCCCHHHH | 54.59 | 27452117 | |
420 | Phosphorylation | PQKISPKSTGSVRQL CCCCCCCCCCHHHHH | 41.19 | 21406692 | |
421 | Phosphorylation | QKISPKSTGSVRQLL CCCCCCCCCHHHHHH | 39.33 | 21406692 | |
423 | Phosphorylation | ISPKSTGSVRQLLHE CCCCCCCHHHHHHHH | 17.76 | 21406692 | |
431 | Ubiquitination | VRQLLHEKIRDAYTH HHHHHHHHHHHHHCC | 32.09 | 24816145 | |
431 | Acetylation | VRQLLHEKIRDAYTH HHHHHHHHHHHHHCC | 32.09 | 23749302 | |
447 | Ubiquitination | QFVTDVMKPLQIENI HHHCCCCCCCCHHHH | 42.28 | 29967540 | |
478 | Ubiquitination | ALALCLGKPADVYLI HHHHHHCCCCCEEEE | 24.88 | 29967540 | |
478 | Acetylation | ALALCLGKPADVYLI HHHHHHCCCCCEEEE | 24.88 | 26051181 | |
512 | 2-Hydroxyisobutyrylation | KRFILHAKKTAFVVE HHHHHHHHCCEEEEE | 39.65 | - | |
541 | Ubiquitination | VFDGVPSKNTVANSP EECCCCCCCCCCCCH | 51.04 | 21906983 | |
547 | Phosphorylation | SKNTVANSPQTLLAG CCCCCCCCHHHHHHH | 14.51 | 25159151 | |
550 | Phosphorylation | TVANSPQTLLAGMNK CCCCCHHHHHHHHHH | 27.42 | 23186163 | |
560 | Phosphorylation | AGMNKFLSQLEITFR HHHHHHHHHHHEEEC | 35.53 | 22210691 | |
579 | Ubiquitination | NYRPRINKLNSIKDV CCCCCCCCCCCCCCH | 46.83 | 22817900 | |
582 | Phosphorylation | PRINKLNSIKDVEQK CCCCCCCCCCCHHHH | 41.26 | 28450419 | |
584 | Ubiquitination | INKLNSIKDVEQKKS CCCCCCCCCHHHHHC | 56.39 | 21906983 | |
584 | Acetylation | INKLNSIKDVEQKKS CCCCCCCCCHHHHHC | 56.39 | 23749302 | |
589 | Ubiquitination | SIKDVEQKKSGNYFF CCCCHHHHHCCCCEE | 35.09 | 22817900 | |
590 | Ubiquitination | IKDVEQKKSGNYFFL CCCHHHHHCCCCEEC | 64.39 | 22817900 | |
591 | Phosphorylation | KDVEQKKSGNYFFLD CCHHHHHCCCCEECC | 39.03 | 28796482 | |
594 | Nitration | EQKKSGNYFFLDD-- HHHHCCCCEECCC-- | 10.15 | - | |
594 | Phosphorylation | EQKKSGNYFFLDD-- HHHHCCCCEECCC-- | 10.15 | 28796482 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ABCE1_HUMAN !! |
* 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 !! |
Kegg Disease | ||||||
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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. |
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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-121; LYS-191; LYS-210;LYS-349 AND LYS-431, AND MASS SPECTROMETRY. |