UniProt ID | RFA1_HUMAN | |
---|---|---|
UniProt AC | P27694 | |
Protein Name | Replication protein A 70 kDa DNA-binding subunit | |
Gene Name | RPA1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 616 | |
Subcellular Localization | Nucleus . Nucleus, PML body . Enriched in PML bodies in cells displaying alternative lengthening of their telomeres. | |
Protein Description | As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. [PubMed: 27723720] | |
Protein Sequence | MVGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSALM | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MVGQLSEG -------CCCCCCHH | 7.44 | 19413330 | |
6 | Phosphorylation | --MVGQLSEGAIAAI --CCCCCCHHHHHHH | 26.54 | 20068231 | |
14 | Sulfoxidation | EGAIAAIMQKGDTNI HHHHHHHHHCCCCCC | 2.63 | 21406390 | |
16 | Ubiquitination | AIAAIMQKGDTNIKP HHHHHHHCCCCCCCC | 41.18 | 23000965 | |
19 | Phosphorylation | AIMQKGDTNIKPILQ HHHHCCCCCCCCEEE | 47.73 | 30108239 | |
22 | Ubiquitination | QKGDTNIKPILQVIN HCCCCCCCCEEEEEE | 28.24 | 23000965 | |
34 | Phosphorylation | VINIRPITTGNSPPR EEECEECCCCCCCCC | 31.19 | 23898821 | |
35 | Phosphorylation | INIRPITTGNSPPRY EECEECCCCCCCCCE | 34.78 | 21712546 | |
38 | Phosphorylation | RPITTGNSPPRYRLL EECCCCCCCCCEEEE | 37.31 | 29255136 | |
42 | Phosphorylation | TGNSPPRYRLLMSDG CCCCCCCEEEECCCC | 16.04 | 23090842 | |
75 | Ubiquitination | EEQLSSNCVCQIHRF HHHHCCCCEEEEEHH | 3.32 | 33845483 | |
88 | 2-Hydroxyisobutyrylation | RFIVNTLKDGRRVVI HHHHHCCCCCCEEEE | 56.98 | - | |
88 | Acetylation | RFIVNTLKDGRRVVI HHHHHCCCCCCEEEE | 56.98 | 25953088 | |
88 | Ubiquitination | RFIVNTLKDGRRVVI HHHHHCCCCCCEEEE | 56.98 | 21906983 | |
111 | Sumoylation | SAEAVGVKIGNPVPY CCCHHCCCCCCCCCC | 38.68 | - | |
111 | Ubiquitination | SAEAVGVKIGNPVPY CCCHHCCCCCCCCCC | 38.68 | 29967540 | |
118 | Phosphorylation | KIGNPVPYNEGLGQP CCCCCCCCCCCCCCC | 26.53 | 22199227 | |
122 | Phosphorylation | PVPYNEGLGQPQVAP CCCCCCCCCCCCCCC | 4.73 | 32142685 | |
135 | Phosphorylation | APPAPAASPAASSRP CCCCCCCCCCCCCCC | 19.71 | 29255136 | |
139 | Phosphorylation | PAASPAASSRPQPQN CCCCCCCCCCCCCCC | 29.05 | 30206219 | |
140 | Phosphorylation | AASPAASSRPQPQNG CCCCCCCCCCCCCCC | 43.16 | 30206219 | |
148 | Phosphorylation | RPQPQNGSSGMGSTV CCCCCCCCCCCCHHH | 31.13 | 22199227 | |
149 | O-linked_Glycosylation | PQPQNGSSGMGSTVS CCCCCCCCCCCHHHH | 33.91 | 23301498 | |
149 | Phosphorylation | PQPQNGSSGMGSTVS CCCCCCCCCCCHHHH | 33.91 | 22199227 | |
150 | Ubiquitination | QPQNGSSGMGSTVSK CCCCCCCCCCHHHHH | 26.60 | 33845483 | |
153 | Phosphorylation | NGSSGMGSTVSKAYG CCCCCCCHHHHHHHC | 19.42 | 22199227 | |
154 | Phosphorylation | GSSGMGSTVSKAYGA CCCCCCHHHHHHHCC | 24.06 | 22199227 | |
154 | Ubiquitination | GSSGMGSTVSKAYGA CCCCCCHHHHHHHCC | 24.06 | 32015554 | |
156 | Phosphorylation | SGMGSTVSKAYGASK CCCCHHHHHHHCCCC | 16.20 | 22199227 | |
157 | Ubiquitination | GMGSTVSKAYGASKT CCCHHHHHHHCCCCC | 41.09 | 22817900 | |
159 | Phosphorylation | GSTVSKAYGASKTFG CHHHHHHHCCCCCCC | 19.57 | 26074081 | |
162 | Phosphorylation | VSKAYGASKTFGKAA HHHHHCCCCCCCCCC | 28.06 | 24719451 | |
163 | Acetylation | SKAYGASKTFGKAAG HHHHCCCCCCCCCCC | 47.54 | 19608861 | |
163 | Methylation | SKAYGASKTFGKAAG HHHHCCCCCCCCCCC | 47.54 | - | |
163 | Ubiquitination | SKAYGASKTFGKAAG HHHHCCCCCCCCCCC | 47.54 | 23000965 | |
164 | Phosphorylation | KAYGASKTFGKAAGP HHHCCCCCCCCCCCC | 34.81 | 18212344 | |
167 | Sumoylation | GASKTFGKAAGPSLS CCCCCCCCCCCCCCC | 30.76 | - | |
167 | Acetylation | GASKTFGKAAGPSLS CCCCCCCCCCCCCCC | 30.76 | 19608861 | |
167 | Methylation | GASKTFGKAAGPSLS CCCCCCCCCCCCCCC | 30.76 | 69823 | |
167 | Sumoylation | GASKTFGKAAGPSLS CCCCCCCCCCCCCCC | 30.76 | 19608861 | |
167 | Ubiquitination | GASKTFGKAAGPSLS CCCCCCCCCCCCCCC | 30.76 | 23000965 | |
172 | Phosphorylation | FGKAAGPSLSHTSGG CCCCCCCCCCCCCCC | 41.40 | 25159151 | |
174 | Phosphorylation | KAAGPSLSHTSGGTQ CCCCCCCCCCCCCCC | 29.11 | 25159151 | |
176 | Phosphorylation | AGPSLSHTSGGTQSK CCCCCCCCCCCCCCC | 26.20 | 25159151 | |
177 | Phosphorylation | GPSLSHTSGGTQSKV CCCCCCCCCCCCCCE | 29.78 | 25159151 | |
180 | Phosphorylation | LSHTSGGTQSKVVPI CCCCCCCCCCCEEEE | 32.94 | 17525332 | |
182 | Phosphorylation | HTSGGTQSKVVPIAS CCCCCCCCCEEEECC | 27.53 | 29523821 | |
183 | Acetylation | TSGGTQSKVVPIASL CCCCCCCCEEEECCC | 37.12 | 26051181 | |
183 | Ubiquitination | TSGGTQSKVVPIASL CCCCCCCCEEEECCC | 37.12 | 23000965 | |
189 | Phosphorylation | SKVVPIASLTPYQSK CCEEEECCCCCCCCC | 33.23 | 28152594 | |
191 | Phosphorylation | VVPIASLTPYQSKWT EEEECCCCCCCCCCE | 19.91 | 25159151 | |
193 | Phosphorylation | PIASLTPYQSKWTIC EECCCCCCCCCCEEE | 21.86 | 28152594 | |
195 | Phosphorylation | ASLTPYQSKWTICAR CCCCCCCCCCEEEEE | 25.07 | 25159151 | |
196 | Acetylation | SLTPYQSKWTICARV CCCCCCCCCEEEEEE | 32.60 | 25953088 | |
196 | Ubiquitination | SLTPYQSKWTICARV CCCCCCCCCEEEEEE | 32.60 | 23000965 | |
204 | Phosphorylation | WTICARVTNKSQIRT CEEEEEECCHHHCEE | 31.23 | 21406692 | |
206 | Ubiquitination | ICARVTNKSQIRTWS EEEEECCHHHCEEEE | 34.08 | 24816145 | |
207 | Phosphorylation | CARVTNKSQIRTWSN EEEECCHHHCEEEEC | 32.67 | 21406692 | |
210 | Methylation | VTNKSQIRTWSNSRG ECCHHHCEEEECCCC | 23.62 | 115491499 | |
213 | Phosphorylation | KSQIRTWSNSRGEGK HHHCEEEECCCCCCE | 25.06 | 28348404 | |
215 | Phosphorylation | QIRTWSNSRGEGKLF HCEEEECCCCCCEEE | 35.83 | 28348404 | |
220 | Ubiquitination | SNSRGEGKLFSLELV ECCCCCCEEEEEEEE | 41.90 | 26474068 | |
244 | Acetylation | AFNEQVDKFFPLIEV EEHHHHHHHEEEEEE | 50.47 | 26051181 | |
244 | Ubiquitination | AFNEQVDKFFPLIEV EEHHHHHHHEEEEEE | 50.47 | 21963094 | |
254 | Ubiquitination | PLIEVNKVYYFSKGT EEEEECEEEEECCCC | 3.85 | 32142685 | |
259 | 2-Hydroxyisobutyrylation | NKVYYFSKGTLKIAN CEEEEECCCCEEECC | 46.12 | - | |
259 | Acetylation | NKVYYFSKGTLKIAN CEEEEECCCCEEECC | 46.12 | 19608861 | |
259 | Ubiquitination | NKVYYFSKGTLKIAN CEEEEECCCCEEECC | 46.12 | 26474068 | |
263 | Acetylation | YFSKGTLKIANKQFT EECCCCEEECCCEEE | 39.34 | 25953088 | |
263 | Ubiquitination | YFSKGTLKIANKQFT EECCCCEEECCCEEE | 39.34 | 23000965 | |
267 | 2-Hydroxyisobutyrylation | GTLKIANKQFTAVKN CCEEECCCEEEEEEC | 37.45 | - | |
267 | Acetylation | GTLKIANKQFTAVKN CCEEECCCEEEEEEC | 37.45 | 88069 | |
267 | Ubiquitination | GTLKIANKQFTAVKN CCEEECCCEEEEEEC | 37.45 | 23000965 | |
273 | Ubiquitination | NKQFTAVKNDYEMTF CCEEEEEECCEEEEE | 41.45 | 23000965 | |
311 | Ubiquitination | GIDDLENKSKDSLVD CHHHHCCCCCCCHHH | 49.89 | 22817900 | |
312 | Phosphorylation | IDDLENKSKDSLVDI HHHHCCCCCCCHHHH | 53.96 | 28450419 | |
313 | 2-Hydroxyisobutyrylation | DDLENKSKDSLVDII HHHCCCCCCCHHHHH | 53.60 | - | |
313 | Ubiquitination | DDLENKSKDSLVDII HHHCCCCCCCHHHHH | 53.60 | 21963094 | |
315 | Phosphorylation | LENKSKDSLVDIIGI HCCCCCCCHHHHHHH | 33.75 | 28464451 | |
318 | Ubiquitination | KSKDSLVDIIGICKS CCCCCHHHHHHHHCC | 31.89 | 33845483 | |
324 | Ubiquitination | VDIIGICKSYEDATK HHHHHHHCCCCCCCE | 54.90 | 29967540 | |
331 | Ubiquitination | KSYEDATKITVRSNN CCCCCCCEEEECCCC | 37.79 | 33845483 | |
351 | Phosphorylation | RNIYLMDTSGKVVTA CCEEEECCCCCEEEE | 25.97 | 30576142 | |
352 | Phosphorylation | NIYLMDTSGKVVTAT CEEEECCCCCEEEEE | 32.14 | 28555341 | |
359 | Phosphorylation | SGKVVTATLWGEDAD CCCEEEEEEECCCHH | 17.43 | 30576142 | |
366 | Ubiquitination | TLWGEDADKFDGSRQ EEECCCHHHCCCCCC | 65.56 | 32015554 | |
367 | Acetylation | LWGEDADKFDGSRQP EECCCHHHCCCCCCC | 47.26 | 26051181 | |
367 | Ubiquitination | LWGEDADKFDGSRQP EECCCHHHCCCCCCC | 47.26 | 22817900 | |
371 | Phosphorylation | DADKFDGSRQPVLAI CHHHCCCCCCCEEEE | 29.59 | 30576142 | |
379 | Acetylation | RQPVLAIKGARVSDF CCCEEEEECCEECCC | 40.69 | 25953088 | |
379 | Ubiquitination | RQPVLAIKGARVSDF CCCEEEEECCEECCC | 40.69 | 32015554 | |
384 | Phosphorylation | AIKGARVSDFGGRSL EEECCEECCCCCCEE | 22.97 | 20201521 | |
390 | Phosphorylation | VSDFGGRSLSVLSSS ECCCCCCEEEECCCC | 28.42 | 29978859 | |
392 | Phosphorylation | DFGGRSLSVLSSSTI CCCCCEEEECCCCEE | 23.43 | 26657352 | |
395 | Phosphorylation | GRSLSVLSSSTIIAN CCEEEECCCCEEEEC | 21.78 | 29978859 | |
396 | Phosphorylation | RSLSVLSSSTIIANP CEEEECCCCEEEECC | 27.60 | 29978859 | |
397 | Phosphorylation | SLSVLSSSTIIANPD EEEECCCCEEEECCC | 21.90 | 29978859 | |
397 | Ubiquitination | SLSVLSSSTIIANPD EEEECCCCEEEECCC | 21.90 | 33845483 | |
398 | Phosphorylation | LSVLSSSTIIANPDI EEECCCCEEEECCCC | 20.53 | 29978859 | |
410 | Ubiquitination | PDIPEAYKLRGWFDA CCCCHHHHHCCCCCC | 38.46 | 23000965 | |
418 | Neddylation | LRGWFDAEGQALDGV HCCCCCCCCCCCCCE | 54.40 | 32015554 | |
418 | Ubiquitination | LRGWFDAEGQALDGV HCCCCCCCCCCCCCE | 54.40 | 32015554 | |
426 | Phosphorylation | GQALDGVSISDLKSG CCCCCCEEHHHHHCC | 23.15 | 22210691 | |
428 | Phosphorylation | ALDGVSISDLKSGGV CCCCEEHHHHHCCCC | 29.41 | 22210691 | |
430 | Ubiquitination | DGVSISDLKSGGVGG CCEEHHHHHCCCCCC | 3.67 | 33845483 | |
431 | Neddylation | GVSISDLKSGGVGGS CEEHHHHHCCCCCCC | 52.63 | 32015554 | |
431 | Ubiquitination | GVSISDLKSGGVGGS CEEHHHHHCCCCCCC | 52.63 | 21906983 | |
432 | Phosphorylation | VSISDLKSGGVGGSN EEHHHHHCCCCCCCC | 48.34 | 20068231 | |
438 | Phosphorylation | KSGGVGGSNTNWKTL HCCCCCCCCCCCEEE | 34.25 | 20068231 | |
440 | Phosphorylation | GGVGGSNTNWKTLYE CCCCCCCCCCEEEEE | 44.12 | 20068231 | |
443 | Methylation | GGSNTNWKTLYEVKS CCCCCCCEEEEEEEH | 30.62 | 42367465 | |
443 | Ubiquitination | GGSNTNWKTLYEVKS CCCCCCCEEEEEEEH | 30.62 | 21906983 | |
449 | Sumoylation | WKTLYEVKSENLGQG CEEEEEEEHHCCCCC | 39.86 | - | |
449 | Sumoylation | WKTLYEVKSENLGQG CEEEEEEEHHCCCCC | 39.86 | 20705237 | |
449 | Ubiquitination | WKTLYEVKSENLGQG CEEEEEEEHHCCCCC | 39.86 | 21963094 | |
450 | Phosphorylation | KTLYEVKSENLGQGD EEEEEEEHHCCCCCC | 36.57 | 20068231 | |
458 | Ubiquitination | ENLGQGDKPDYFSSV HCCCCCCCCCCHHHH | 46.76 | 21906983 | |
461 | Phosphorylation | GQGDKPDYFSSVATV CCCCCCCCHHHHEEE | 17.56 | 20068231 | |
463 | Phosphorylation | GDKPDYFSSVATVVY CCCCCCHHHHEEEEE | 20.06 | 20068231 | |
464 | Phosphorylation | DKPDYFSSVATVVYL CCCCCHHHHEEEEEE | 13.08 | 20068231 | |
467 | Phosphorylation | DYFSSVATVVYLRKE CCHHHHEEEEEEECC | 14.35 | 28152594 | |
470 | Phosphorylation | SSVATVVYLRKENCM HHHEEEEEEECCCCC | 9.10 | 28152594 | |
473 | Acetylation | ATVVYLRKENCMYQA EEEEEEECCCCCCEE | 51.16 | 26051181 | |
473 | Ubiquitination | ATVVYLRKENCMYQA EEEEEEECCCCCCEE | 51.16 | 24816145 | |
476 | Ubiquitination | VYLRKENCMYQACPT EEEECCCCCCEECCC | 2.56 | 33845483 | |
478 | Phosphorylation | LRKENCMYQACPTQD EECCCCCCEECCCCC | 8.65 | 22461510 | |
483 | Phosphorylation | CMYQACPTQDCNKKV CCCEECCCCCCCCHH | 36.60 | 22461510 | |
488 | Acetylation | CPTQDCNKKVIDQQN CCCCCCCCHHHHCCC | 55.54 | 25953088 | |
488 | Ubiquitination | CPTQDCNKKVIDQQN CCCCCCCCHHHHCCC | 55.54 | 21963094 | |
489 | Sumoylation | PTQDCNKKVIDQQNG CCCCCCCHHHHCCCC | 30.36 | - | |
489 | Acetylation | PTQDCNKKVIDQQNG CCCCCCCHHHHCCCC | 30.36 | 23749302 | |
489 | Malonylation | PTQDCNKKVIDQQNG CCCCCCCHHHHCCCC | 30.36 | 26320211 | |
489 | Sumoylation | PTQDCNKKVIDQQNG CCCCCCCHHHHCCCC | 30.36 | - | |
489 | Ubiquitination | PTQDCNKKVIDQQNG CCCCCCCHHHHCCCC | 30.36 | 27667366 | |
502 | Acetylation | NGLYRCEKCDTEFPN CCEEECCCCCCCCCC | 40.82 | 25953088 | |
502 | Ubiquitination | NGLYRCEKCDTEFPN CCEEECCCCCCCCCC | 40.82 | 23000965 | |
511 | Acetylation | DTEFPNFKYRMILSV CCCCCCCCEEEEEEE | 38.29 | 25953088 | |
511 | Ubiquitination | DTEFPNFKYRMILSV CCCCCCCCEEEEEEE | 38.29 | 21963094 | |
518 | Ubiquitination | KYRMILSVNIADFQE CEEEEEEEEEHHHCC | 5.57 | 33845483 | |
529 | Ubiquitination | DFQENQWVTCFQESA HHCCCCEEEEHHHHH | 2.11 | 33845483 | |
536 | Ubiquitination | VTCFQESAEAILGQN EEEHHHHHHHHHCCC | 14.97 | 33845483 | |
551 | Ubiquitination | AAYLGELKDKNEQAF HHHHHCCCCCCHHHH | 63.45 | 22817900 | |
553 | Acetylation | YLGELKDKNEQAFEE HHHCCCCCCHHHHHH | 61.88 | 25953088 | |
553 | Ubiquitination | YLGELKDKNEQAFEE HHHCCCCCCHHHHHH | 61.88 | 21906983 | |
564 | Ubiquitination | AFEEVFQNANFRSFI HHHHHHHCCCCHHEE | 25.95 | 33845483 | |
575 | Ubiquitination | RSFIFRVRVKVETYN HHEEEEEEEEEEECC | 20.48 | 33845483 | |
577 | Sumoylation | FIFRVRVKVETYNDE EEEEEEEEEEECCCC | 24.64 | - | |
577 | 2-Hydroxyisobutyrylation | FIFRVRVKVETYNDE EEEEEEEEEEECCCC | 24.64 | - | |
577 | Acetylation | FIFRVRVKVETYNDE EEEEEEEEEEECCCC | 24.64 | 23749302 | |
577 | Sumoylation | FIFRVRVKVETYNDE EEEEEEEEEEECCCC | 24.64 | 20705237 | |
577 | Ubiquitination | FIFRVRVKVETYNDE EEEEEEEEEEECCCC | 24.64 | 21906983 | |
580 | Phosphorylation | RVRVKVETYNDESRI EEEEEEEECCCCCCE | 30.52 | 28152594 | |
581 | Phosphorylation | VRVKVETYNDESRIK EEEEEEECCCCCCEE | 13.70 | 28152594 | |
582 | Ubiquitination | RVKVETYNDESRIKA EEEEEECCCCCCEEE | 54.73 | 33845483 | |
585 | Phosphorylation | VETYNDESRIKATVM EEECCCCCCEEEEEE | 42.01 | 28152594 | |
588 | Malonylation | YNDESRIKATVMDVK CCCCCCEEEEEECCC | 36.57 | 26320211 | |
588 | Ubiquitination | YNDESRIKATVMDVK CCCCCCEEEEEECCC | 36.57 | 21963094 | |
590 | O-linked_Glycosylation | DESRIKATVMDVKPV CCCCEEEEEECCCCC | 16.03 | 23301498 | |
590 | Phosphorylation | DESRIKATVMDVKPV CCCCEEEEEECCCCC | 16.03 | 20068231 | |
592 | Sulfoxidation | SRIKATVMDVKPVDY CCEEEEEECCCCCCH | 4.21 | 28183972 | |
595 | Sumoylation | KATVMDVKPVDYREY EEEEECCCCCCHHHH | 34.75 | - | |
595 | Acetylation | KATVMDVKPVDYREY EEEEECCCCCCHHHH | 34.75 | 25953088 | |
595 | Sumoylation | KATVMDVKPVDYREY EEEEECCCCCCHHHH | 34.75 | - | |
595 | Ubiquitination | KATVMDVKPVDYREY EEEEECCCCCCHHHH | 34.75 | 27667366 | |
599 | Phosphorylation | MDVKPVDYREYGRRL ECCCCCCHHHHHHHH | 12.94 | 20068231 |
* 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 RFA1_HUMAN !! |
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. |
loading...
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-163; LYS-167 AND LYS-259,AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASSSPECTROMETRY. | |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-191, AND MASSSPECTROMETRY. | |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, AND MASSSPECTROMETRY. | |
Sumoylation | |
Reference | PubMed |
"Regulation of DNA repair through desumoylation and sumoylation ofreplication protein A complex."; Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.; Mol. Cell 39:333-345(2010). Cited for: SUMOYLATION AT LYS-449 AND LYS-577, DESUMOYLATION BY SENP6,MUTAGENESIS OF LYS-449 AND LYS-577, AND INTERACTION WITH SENP6 ANDRAD51. |