UniProt ID | MCM2_HUMAN | |
---|---|---|
UniProt AC | P49736 | |
Protein Name | DNA replication licensing factor MCM2 | |
Gene Name | MCM2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 904 | |
Subcellular Localization | Nucleus . | |
Protein Description | Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division. Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis.. | |
Protein Sequence | MAESSESFTMASSPAQRRRGNDPLTSSPGRSSRRTDALTSSPGRDLPPFEDESEGLLGTEGPLEEEEDGEELIGDGMERDYRAIPELDAYEAEGLALDDEDVEELTASQREAAERAMRQRDREAGRGLGRMRRGLLYDSDEEDEERPARKRRQVERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLPQLSMVKYNCNKCNFVLGPFCQSQNQEVKPGSCPECQSAGPFEVNMEETIYQNYQRIRIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTANGFPVFATVILANHVAKKDNKVAVGELTDEDVKMITSLSKDQQIGEKIFASIAPSIYGHEDIKRGLALALFGGEPKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYIEKVSSRAIFTTGQGASAVGLTAYVQRHPVSREWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSLTFSENVDLTEPIISRFDILCVVRDTVDPVQDEMLARFVVGSHVRHHPSNKEEEGLANGSAAEPAMPNTYGVEPLPQEVLKKYIIYAKERVHPKLNQMDQDKVAKMYSDLRKESMATGSIPITVRHIESMIRMAEAHARIHLRDYVIEDDVNMAIRVMLESFIDTQKFSVMRSMRKTFARYLSFRRDNNELLLFILKQLVAEQVTYQRNRFGAQQDTIEVPEKDLVDKARQINIHNLSAFYDSELFRMNKFSHDLKRKMILQQF | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAESSESFT ------CCCCCCCCC | 25.94 | 20068231 | |
4 | Phosphorylation | ----MAESSESFTMA ----CCCCCCCCCCC | 29.84 | 23401153 | |
5 | Phosphorylation | ---MAESSESFTMAS ---CCCCCCCCCCCC | 28.85 | 23401153 | |
7 | Phosphorylation | -MAESSESFTMASSP -CCCCCCCCCCCCCH | 28.15 | 29255136 | |
9 | Phosphorylation | AESSESFTMASSPAQ CCCCCCCCCCCCHHH | 22.55 | 29255136 | |
12 | Phosphorylation | SESFTMASSPAQRRR CCCCCCCCCHHHHHC | 26.49 | 29255136 | |
13 | Phosphorylation | ESFTMASSPAQRRRG CCCCCCCCHHHHHCC | 18.08 | 29255136 | |
25 | Phosphorylation | RRGNDPLTSSPGRSS HCCCCCCCCCCCCCC | 32.33 | 29255136 | |
26 | Phosphorylation | RGNDPLTSSPGRSSR CCCCCCCCCCCCCCC | 42.07 | 29255136 | |
27 | O-linked_Glycosylation | GNDPLTSSPGRSSRR CCCCCCCCCCCCCCC | 26.58 | 28510447 | |
27 | Phosphorylation | GNDPLTSSPGRSSRR CCCCCCCCCCCCCCC | 26.58 | 19664994 | |
31 | Phosphorylation | LTSSPGRSSRRTDAL CCCCCCCCCCCCCCC | 33.83 | 23401153 | |
32 | Phosphorylation | TSSPGRSSRRTDALT CCCCCCCCCCCCCCC | 25.15 | 22167270 | |
35 | Phosphorylation | PGRSSRRTDALTSSP CCCCCCCCCCCCCCC | 25.23 | 23927012 | |
39 | Phosphorylation | SRRTDALTSSPGRDL CCCCCCCCCCCCCCC | 28.95 | 29255136 | |
40 | Phosphorylation | RRTDALTSSPGRDLP CCCCCCCCCCCCCCC | 35.07 | 29255136 | |
41 | Phosphorylation | RTDALTSSPGRDLPP CCCCCCCCCCCCCCC | 26.58 | 29255136 | |
53 | Phosphorylation | LPPFEDESEGLLGTE CCCCCCCCCCCCCCC | 49.65 | 21955146 | |
59 | Phosphorylation | ESEGLLGTEGPLEEE CCCCCCCCCCCCCCC | 37.42 | 21955146 | |
81 | Phosphorylation | GDGMERDYRAIPELD CCCCCCCCCCCCCCC | 14.25 | 21406692 | |
90 | Phosphorylation | AIPELDAYEAEGLAL CCCCCCHHHCCCCCC | 18.48 | 28176443 | |
106 | Phosphorylation | DEDVEELTASQREAA HHHHHHHHHHHHHHH | 27.78 | 30266825 | |
108 | Phosphorylation | DVEELTASQREAAER HHHHHHHHHHHHHHH | 25.24 | 19664994 | |
126 | Methylation | QRDREAGRGLGRMRR HHHHHHHHCCCCCCC | 44.18 | 54557289 | |
137 | Phosphorylation | RMRRGLLYDSDEEDE CCCCCCCCCCCCCCC | 20.60 | 22167270 | |
139 | Phosphorylation | RRGLLYDSDEEDEER CCCCCCCCCCCCCCC | 33.11 | 19664994 | |
158 | Phosphorylation | RRQVERATEDGEEDE HHHHHHHCCCCCHHH | 40.61 | 27422710 | |
167 | Sulfoxidation | DGEEDEEMIESIENL CCCHHHHHHHHHHCH | 3.76 | 21406390 | |
170 | Phosphorylation | EDEEMIESIENLEDL HHHHHHHHHHCHHHH | 25.03 | 23401153 | |
178 | 2-Hydroxyisobutyrylation | IENLEDLKGHSVREW HHCHHHHCCCCHHHH | 67.89 | - | |
178 | Sumoylation | IENLEDLKGHSVREW HHCHHHHCCCCHHHH | 67.89 | 28112733 | |
178 | Ubiquitination | IENLEDLKGHSVREW HHCHHHHCCCCHHHH | 67.89 | 21906983 | |
200 | Ubiquitination | LEIHHRFKNFLRTHV EEEEHHHHHHHHHHH | 46.90 | - | |
209 | Phosphorylation | FLRTHVDSHGHNVFK HHHHHHHHCCCHHHH | 30.22 | - | |
216 | 2-Hydroxyisobutyrylation | SHGHNVFKERISDMC HCCCHHHHHHHHHHH | 41.63 | - | |
216 | Acetylation | SHGHNVFKERISDMC HCCCHHHHHHHHHHH | 41.63 | 19608861 | |
216 | Ubiquitination | SHGHNVFKERISDMC HCCCHHHHHHHHHHH | 41.63 | 33845483 | |
220 | Phosphorylation | NVFKERISDMCKENR HHHHHHHHHHHHHCH | 26.05 | 22817900 | |
224 | Acetylation | ERISDMCKENRESLV HHHHHHHHHCHHHEE | 51.92 | 25953088 | |
224 | Ubiquitination | ERISDMCKENRESLV HHHHHHHHHCHHHEE | 51.92 | 33845483 | |
229 | Phosphorylation | MCKENRESLVVNYED HHHHCHHHEECCHHH | 24.19 | 30108239 | |
234 | Phosphorylation | RESLVVNYEDLAARE HHHEECCHHHHHHHH | 10.14 | 28152594 | |
307 | Methylation | LHLNQLIRTSGVVTS HHHHHHHHHHCCCCC | 31.28 | 115482819 | |
313 | Phosphorylation | IRTSGVVTSCTGVLP HHHHCCCCCCCCCHH | 18.71 | 27080861 | |
314 | Phosphorylation | RTSGVVTSCTGVLPQ HHHCCCCCCCCCHHH | 9.70 | 27080861 | |
316 | Phosphorylation | SGVVTSCTGVLPQLS HCCCCCCCCCHHHHH | 30.05 | 27080861 | |
323 | Phosphorylation | TGVLPQLSMVKYNCN CCCHHHHHHEEECCC | 19.11 | 27080861 | |
324 | Sulfoxidation | GVLPQLSMVKYNCNK CCHHHHHHEEECCCC | 4.02 | 21406390 | |
326 | Acetylation | LPQLSMVKYNCNKCN HHHHHHEEECCCCCC | 23.31 | 26051181 | |
326 | Ubiquitination | LPQLSMVKYNCNKCN HHHHHHEEECCCCCC | 23.31 | - | |
381 | Phosphorylation | QRIRIQESPGKVAAG HEEEEECCCCCCCCC | 23.68 | 30266825 | |
384 | 2-Hydroxyisobutyrylation | RIQESPGKVAAGRLP EEECCCCCCCCCCCC | 31.89 | - | |
384 | Acetylation | RIQESPGKVAAGRLP EEECCCCCCCCCCCC | 31.89 | 25953088 | |
384 | Ubiquitination | RIQESPGKVAAGRLP EEECCCCCCCCCCCC | 31.89 | 24816145 | |
394 | Ubiquitination | AGRLPRSKDAILLAD CCCCCCCCCEEEHHH | 53.08 | 29967540 | |
418 | Phosphorylation | EIELTGIYHNNYDGS EEEEEEEEECCCCCC | 10.39 | 22817900 | |
422 | Phosphorylation | TGIYHNNYDGSLNTA EEEEECCCCCCCCCC | 27.31 | 22817900 | |
447 | Acetylation | LANHVAKKDNKVAVG HHHHHCCCCCCEEEE | 57.72 | 25953088 | |
447 | Ubiquitination | LANHVAKKDNKVAVG HHHHHCCCCCCEEEE | 57.72 | 29967540 | |
450 | Sumoylation | HVAKKDNKVAVGELT HHCCCCCCEEEEECC | 41.53 | - | |
450 | Ubiquitination | HVAKKDNKVAVGELT HHCCCCCCEEEEECC | 41.53 | 29967540 | |
457 | Phosphorylation | KVAVGELTDEDVKMI CEEEEECCHHHHHHH | 32.80 | 27067055 | |
462 | Acetylation | ELTDEDVKMITSLSK ECCHHHHHHHHHCCC | 36.59 | 25953088 | |
462 | Sumoylation | ELTDEDVKMITSLSK ECCHHHHHHHHHCCC | 36.59 | - | |
462 | Ubiquitination | ELTDEDVKMITSLSK ECCHHHHHHHHHCCC | 36.59 | 21906983 | |
466 | Phosphorylation | EDVKMITSLSKDQQI HHHHHHHHCCCCHHH | 21.52 | 22496350 | |
469 | Acetylation | KMITSLSKDQQIGEK HHHHHCCCCHHHHHH | 65.92 | 25953088 | |
469 | Ubiquitination | KMITSLSKDQQIGEK HHHHHCCCCHHHHHH | 65.92 | 22817900 | |
476 | Ubiquitination | KDQQIGEKIFASIAP CCHHHHHHHHHHHCH | 37.60 | 21906983 | |
484 | Phosphorylation | IFASIAPSIYGHEDI HHHHHCHHHHCCHHH | 21.30 | 28112733 | |
492 | Sumoylation | IYGHEDIKRGLALAL HHCCHHHHHHHHHHH | 53.38 | - | |
492 | Ubiquitination | IYGHEDIKRGLALAL HHCCHHHHHHHHHHH | 53.38 | 22817900 | |
505 | Ubiquitination | ALFGGEPKNPGGKHK HHHCCCCCCCCCCCC | 72.04 | 24816145 | |
527 | Phosphorylation | LLCGDPGTAKSQFLK EECCCCCCHHHHHHH | 35.98 | 20068231 | |
529 | 2-Hydroxyisobutyrylation | CGDPGTAKSQFLKYI CCCCCCHHHHHHHHH | 44.63 | - | |
529 | Ubiquitination | CGDPGTAKSQFLKYI CCCCCCHHHHHHHHH | 44.63 | 29967540 | |
534 | 2-Hydroxyisobutyrylation | TAKSQFLKYIEKVSS CHHHHHHHHHHHHCC | 45.53 | - | |
534 | Acetylation | TAKSQFLKYIEKVSS CHHHHHHHHHHHHCC | 45.53 | 26822725 | |
535 | Phosphorylation | AKSQFLKYIEKVSSR HHHHHHHHHHHHCCC | 19.23 | 20068231 | |
538 | Acetylation | QFLKYIEKVSSRAIF HHHHHHHHHCCCEEE | 37.55 | 25953088 | |
538 | Succinylation | QFLKYIEKVSSRAIF HHHHHHHHHCCCEEE | 37.55 | 23954790 | |
538 | Ubiquitination | QFLKYIEKVSSRAIF HHHHHHHHHCCCEEE | 37.55 | - | |
540 | Phosphorylation | LKYIEKVSSRAIFTT HHHHHHHCCCEEEEC | 25.77 | 20068231 | |
541 | Phosphorylation | KYIEKVSSRAIFTTG HHHHHHCCCEEEECC | 28.81 | 20068231 | |
546 | Phosphorylation | VSSRAIFTTGQGASA HCCCEEEECCCCCCC | 24.73 | 20068231 | |
547 | Phosphorylation | SSRAIFTTGQGASAV CCCEEEECCCCCCCE | 19.43 | 20068231 | |
552 | Phosphorylation | FTTGQGASAVGLTAY EECCCCCCCEECEEH | 30.25 | 20068231 | |
557 | Phosphorylation | GASAVGLTAYVQRHP CCCCEECEEHHHHCC | 15.26 | 28152594 | |
559 | Phosphorylation | SAVGLTAYVQRHPVS CCEECEEHHHHCCCC | 7.59 | 28152594 | |
566 | Phosphorylation | YVQRHPVSREWTLEA HHHHCCCCCCEEHHH | 29.00 | 20873877 | |
591 | Acetylation | CLIDEFDKMNDQDRT EEECCHHHCCCCCCH | 44.94 | 26822725 | |
591 | Ubiquitination | CLIDEFDKMNDQDRT EEECCHHHCCCCCCH | 44.94 | 21906983 | |
598 | Phosphorylation | KMNDQDRTSIHEAME HCCCCCCHHHHHHHH | 40.08 | 28348404 | |
599 | Phosphorylation | MNDQDRTSIHEAMEQ CCCCCCHHHHHHHHH | 23.88 | 28348404 | |
604 | Sulfoxidation | RTSIHEAMEQQSISI CHHHHHHHHHHCCCE | 4.32 | 28183972 | |
610 | Phosphorylation | AMEQQSISISKAGIV HHHHHCCCEEHHCHH | 26.51 | 24719451 | |
613 | Ubiquitination | QQSISISKAGIVTSL HHCCCEEHHCHHHHH | 49.30 | 21963094 | |
623 | Methylation | IVTSLQARCTVIAAA HHHHHHHHHEEEEEE | 12.04 | 115482803 | |
624 | Glutathionylation | VTSLQARCTVIAAAN HHHHHHHHEEEEEEC | 3.90 | 22555962 | |
674 | Sulfoxidation | VDPVQDEMLARFVVG CCHHCHHHHHHHHHC | 4.82 | 21406390 | |
677 | Methylation | VQDEMLARFVVGSHV HCHHHHHHHHHCCCC | 22.41 | 115385713 | |
691 | Acetylation | VRHHPSNKEEEGLAN CCCCCCCHHHCCCCC | 71.49 | 26051181 | |
721 | Ubiquitination | PLPQEVLKKYIIYAK CCCHHHHHHHHHHHH | 49.02 | - | |
722 | Ubiquitination | LPQEVLKKYIIYAKE CCHHHHHHHHHHHHH | 37.20 | 29967540 | |
728 | 2-Hydroxyisobutyrylation | KKYIIYAKERVHPKL HHHHHHHHHCCCHHH | 29.14 | - | |
728 | Ubiquitination | KKYIIYAKERVHPKL HHHHHHHHHCCCHHH | 29.14 | 29967540 | |
734 | 2-Hydroxyisobutyrylation | AKERVHPKLNQMDQD HHHCCCHHHCCCCHH | 45.23 | - | |
734 | Acetylation | AKERVHPKLNQMDQD HHHCCCHHHCCCCHH | 45.23 | 25953088 | |
734 | Ubiquitination | AKERVHPKLNQMDQD HHHCCCHHHCCCCHH | 45.23 | 24816145 | |
742 | 2-Hydroxyisobutyrylation | LNQMDQDKVAKMYSD HCCCCHHHHHHHHHH | 38.16 | - | |
742 | Acetylation | LNQMDQDKVAKMYSD HCCCCHHHHHHHHHH | 38.16 | 26822725 | |
742 | Ubiquitination | LNQMDQDKVAKMYSD HCCCCHHHHHHHHHH | 38.16 | 29967540 | |
745 | 2-Hydroxyisobutyrylation | MDQDKVAKMYSDLRK CCHHHHHHHHHHHHH | 41.16 | - | |
745 | Acetylation | MDQDKVAKMYSDLRK CCHHHHHHHHHHHHH | 41.16 | 25953088 | |
745 | Ubiquitination | MDQDKVAKMYSDLRK CCHHHHHHHHHHHHH | 41.16 | 29967540 | |
751 | Methylation | AKMYSDLRKESMATG HHHHHHHHHHHHHCC | 45.76 | 115482811 | |
752 | 2-Hydroxyisobutyrylation | KMYSDLRKESMATGS HHHHHHHHHHHHCCC | 62.53 | - | |
752 | Ubiquitination | KMYSDLRKESMATGS HHHHHHHHHHHHCCC | 62.53 | 24816145 | |
754 | Phosphorylation | YSDLRKESMATGSIP HHHHHHHHHHCCCCC | 19.42 | 20068231 | |
755 | Sulfoxidation | SDLRKESMATGSIPI HHHHHHHHHCCCCCE | 3.97 | 21406390 | |
757 | Phosphorylation | LRKESMATGSIPITV HHHHHHHCCCCCEEH | 23.87 | 20068231 | |
759 | Phosphorylation | KESMATGSIPITVRH HHHHHCCCCCEEHHH | 22.34 | 21406692 | |
763 | Phosphorylation | ATGSIPITVRHIESM HCCCCCEEHHHHHHH | 13.21 | 20068231 | |
769 | Phosphorylation | ITVRHIESMIRMAEA EEHHHHHHHHHHHHH | 20.93 | 21406692 | |
793 | Sulfoxidation | VIEDDVNMAIRVMLE CCCCCHHHHHHHHHH | 3.09 | 30846556 | |
798 | Sulfoxidation | VNMAIRVMLESFIDT HHHHHHHHHHHHHCH | 2.17 | 28183972 | |
801 | Phosphorylation | AIRVMLESFIDTQKF HHHHHHHHHHCHHCH | 24.44 | 20044836 | |
805 | Phosphorylation | MLESFIDTQKFSVMR HHHHHHCHHCHHHHH | 28.92 | 20068231 | |
807 | 2-Hydroxyisobutyrylation | ESFIDTQKFSVMRSM HHHHCHHCHHHHHHH | 41.52 | - | |
809 | Phosphorylation | FIDTQKFSVMRSMRK HHCHHCHHHHHHHHH | 23.26 | 29978859 | |
813 | Phosphorylation | QKFSVMRSMRKTFAR HCHHHHHHHHHHHHH | 12.58 | 29978859 | |
821 | Phosphorylation | MRKTFARYLSFRRDN HHHHHHHHHHHCCCC | 11.85 | 22210691 | |
845 | Phosphorylation | QLVAEQVTYQRNRFG HHHHHHHHHHHHCCC | 17.40 | 28152594 | |
846 | Phosphorylation | LVAEQVTYQRNRFGA HHHHHHHHHHHCCCC | 13.45 | 28152594 | |
857 | Phosphorylation | RFGAQQDTIEVPEKD CCCCCCCEEECCHHH | 18.07 | - | |
863 | Acetylation | DTIEVPEKDLVDKAR CEEECCHHHHHHHHH | 50.74 | 26822725 | |
863 | Ubiquitination | DTIEVPEKDLVDKAR CEEECCHHHHHHHHH | 50.74 | 29967540 | |
868 | Acetylation | PEKDLVDKARQINIH CHHHHHHHHHHCCCC | 37.68 | 26051181 | |
868 | Ubiquitination | PEKDLVDKARQINIH CHHHHHHHHHHCCCC | 37.68 | 24816145 | |
878 | Phosphorylation | QINIHNLSAFYDSEL HCCCCCHHHHCCHHH | 22.96 | 27050516 | |
890 | Ubiquitination | SELFRMNKFSHDLKR HHHHHHCCCCHHHHH | 38.61 | 24816145 | |
896 | Acetylation | NKFSHDLKRKMILQQ CCCCHHHHHHHHHHC | 56.90 | 19608861 | |
896 | Ubiquitination | NKFSHDLKRKMILQQ CCCCHHHHHHHHHHC | 56.90 | 33845483 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
4 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
4 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
5 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
5 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
7 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
7 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
13 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
13 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
13 | S | Phosphorylation | Kinase | CDK1 | P06493 | GPS |
13 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
27 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
27 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
27 | S | Phosphorylation | Kinase | CDK1 | P06493 | GPS |
27 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
27 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
31 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
40 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
40 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
40 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
40 | S | Phosphorylation | Kinase | CDC7 | O00311 | Uniprot |
41 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
41 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
41 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
41 | S | Phosphorylation | Kinase | CDK1 | P06493 | GPS |
41 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
53 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
53 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
53 | S | Phosphorylation | Kinase | CDC7 | O00311 | Uniprot |
53 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
59 | T | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
108 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
108 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
108 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
108 | S | Phosphorylation | Kinase | ATR | Q13535 | Uniprot |
108 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
139 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
139 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
139 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
139 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
139 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
220 | S | Phosphorylation | Kinase | CDC7 | O00311 | PSP |
220 | S | Phosphorylation | Kinase | AURKA | O14965 | GPS |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
857 | Phosphorylation | 858 (1) | I ⇒ T | rs144122212 |
| 28090653 |
863 | Acetylation | 858 (5) | I ⇒ T | rs144122212 |
| 28090653 |
868 | Acetylation | 858 (10) | I ⇒ T | rs144122212 |
| 28090653 |
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. |
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Acetylation | |
Reference | PubMed |
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4; SER-5; SER-7; SER-13; THR-25; SER-26;SER-27; SER-32 AND SER-139, AND MASS SPECTROMETRY. | |
"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-216 AND LYS-896, AND MASSSPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; THR-59;SER-108 AND SER-139, AND MASS SPECTROMETRY. | |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4; SER-5; SER-7; SER-13; THR-25; SER-26;SER-27; SER-32 AND SER-139, AND MASS SPECTROMETRY. | |
"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 THR-25; SER-26; SER-27;THR-39; SER-40; SER-41; SER-53; SER-139 AND SER-381, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-139, ANDMASS SPECTROMETRY. | |
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASSSPECTROMETRY. | |
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-139, AND MASSSPECTROMETRY. | |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, 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 SER-108, AND MASSSPECTROMETRY. | |
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASSSPECTROMETRY. | |
"Cdc7 is an active kinase in human cancer cells undergoing replicationstress."; Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C.,Santocanale C.; J. Biol. Chem. 282:208-215(2007). Cited for: PHOSPHORYLATION AT SER-40 AND SER-53. | |
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASSSPECTROMETRY. | |
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-41, AND MASSSPECTROMETRY. | |
"Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in theinitiation of DNA replication in mammalian cells."; Tsuji T., Ficarro S.B., Jiang W.; Mol. Biol. Cell 17:4459-4472(2006). Cited for: PHOSPHORYLATION AT SER-27; SER-41; SER-53; SER-108 AND SER-139,MUTAGENESIS OF SER-27; SER-41 AND SER-139, IDENTIFICATION IN THEMCM2-7 COMPLEX, AND ATPASE ACTIVITY OF THE MCM2-7 COMPLEX. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-27; THR-39;SER-40; SER-41 AND SER-139, AND MASS SPECTROMETRY. | |
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-139, AND MASSSPECTROMETRY. | |
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41 AND THR-106,AND MASS SPECTROMETRY. | |
"Minichromosome maintenance proteins are direct targets of the ATM andATR checkpoint kinases."; Cortez D., Glick G., Elledge S.J.; Proc. Natl. Acad. Sci. U.S.A. 101:10078-10083(2004). Cited for: PHOSPHORYLATION AT SER-108, AND MUTAGENESIS OF SER-108. |