PUR2_HUMAN - dbPTM
PUR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUR2_HUMAN
UniProt AC P22102
Protein Name Trifunctional purine biosynthetic protein adenosine-3
Gene Name GART
Organism Homo sapiens (Human).
Sequence Length 1010
Subcellular Localization
Protein Description
Protein Sequence MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEAQALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKDVGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLPHLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTRIYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEGHLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKNLIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE
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
2Acetylation------MAARVLIIG
------CCEEEEEEC
18.4519413330
10PhosphorylationARVLIIGSGGREHTL
EEEEEECCCCHHHHH
27.8930108239
13MethylationLIIGSGGREHTLAWK
EEECCCCHHHHHHHH
35.73-
16PhosphorylationGSGGREHTLAWKLAQ
CCCCHHHHHHHHHHH
17.2628857561
20MethylationREHTLAWKLAQSHHV
HHHHHHHHHHHCCCC
28.47-
20UbiquitinationREHTLAWKLAQSHHV
HHHHHHHHHHHCCCC
28.47-
28AcetylationLAQSHHVKQVLVAPG
HHHCCCCEEEEECCC
30.2723749302
28UbiquitinationLAQSHHVKQVLVAPG
HHHCCCCEEEEECCC
30.27-
41S-nitrosylationPGNAGTACSEKISNT
CCCCCHHCCHHHHCC
5.6122178444
42PhosphorylationGNAGTACSEKISNTA
CCCCHHCCHHHHCCC
39.1921712546
44AcetylationAGTACSEKISNTAIS
CCHHCCHHHHCCCEE
34.8325953088
44UbiquitinationAGTACSEKISNTAIS
CCHHCCHHHHCCCEE
34.83-
62GlutathionylationHTALAQFCKEKKIEF
HHHHHHHHHHCCCEE
3.5622555962
63UbiquitinationTALAQFCKEKKIEFV
HHHHHHHHHCCCEEE
74.07-
65UbiquitinationLAQFCKEKKIEFVVV
HHHHHHHCCCEEEEE
44.54-
66AcetylationAQFCKEKKIEFVVVG
HHHHHHCCCEEEEEC
48.8626051181
66UbiquitinationAQFCKEKKIEFVVVG
HHHHHHCCCEEEEEC
48.8621906983
66 (in isoform 1)Ubiquitination-48.8621890473
66 (in isoform 2)Ubiquitination-48.8621906983
93GlutathionylationLRSAGVQCFGPTAEA
HHHCCCCEECCHHHH
3.8522555962
93S-nitrosylationLRSAGVQCFGPTAEA
HHHCCCCEECCHHHH
3.852212679
97PhosphorylationGVQCFGPTAEAAQLE
CCCEECCHHHHHHHH
37.1928857561
105PhosphorylationAEAAQLESSKRFAKE
HHHHHHHHHHHHHHH
50.1528857561
106PhosphorylationEAAQLESSKRFAKEF
HHHHHHHHHHHHHHH
20.6224719451
107AcetylationAAQLESSKRFAKEFM
HHHHHHHHHHHHHHH
61.9026051181
107UbiquitinationAAQLESSKRFAKEFM
HHHHHHHHHHHHHHH
61.9021906983
107 (in isoform 1)Ubiquitination-61.9021890473
107 (in isoform 2)Ubiquitination-61.9021906983
111AcetylationESSKRFAKEFMDRHG
HHHHHHHHHHHHHHC
49.0926822725
111UbiquitinationESSKRFAKEFMDRHG
HHHHHHHHHHHHHHC
49.0921906983
111 (in isoform 1)Ubiquitination-49.0921890473
111 (in isoform 2)Ubiquitination-49.0921906983
116MethylationFAKEFMDRHGIPTAQ
HHHHHHHHHCCCHHH
20.39-
121PhosphorylationMDRHGIPTAQWKAFT
HHHHCCCHHHHEEEC
29.5620068231
125MethylationGIPTAQWKAFTKPEE
CCCHHHHEEECCHHH
22.88-
125UbiquitinationGIPTAQWKAFTKPEE
CCCHHHHEEECCHHH
22.88-
129UbiquitinationAQWKAFTKPEEACSF
HHHEEECCHHHHHHH
43.93-
134GlutathionylationFTKPEEACSFILSAD
ECCHHHHHHHHHCCC
3.7422555962
148UbiquitinationDFPALVVKASGLAAG
CCCEEEEECCCCCCC
29.38-
1562-HydroxyisobutyrylationASGLAAGKGVIVAKS
CCCCCCCCCEEEECC
45.32-
156AcetylationASGLAAGKGVIVAKS
CCCCCCCCCEEEECC
45.3226051181
156MalonylationASGLAAGKGVIVAKS
CCCCCCCCCEEEECC
45.3226320211
156UbiquitinationASGLAAGKGVIVAKS
CCCCCCCCCEEEECC
45.32-
156 (in isoform 1)Ubiquitination-45.3221890473
156 (in isoform 2)Ubiquitination-45.3221906983
162AcetylationGKGVIVAKSKEEACK
CCCEEEECCHHHHHH
51.6825953088
162UbiquitinationGKGVIVAKSKEEACK
CCCEEEECCHHHHHH
51.68-
164AcetylationGVIVAKSKEEACKAV
CEEEECCHHHHHHHH
59.8925953088
168GlutathionylationAKSKEEACKAVQEIM
ECCHHHHHHHHHHHH
3.0822555962
169AcetylationKSKEEACKAVQEIMQ
CCHHHHHHHHHHHHH
59.6525953088
169UbiquitinationKSKEEACKAVQEIMQ
CCHHHHHHHHHHHHH
59.65-
175SulfoxidationCKAVQEIMQEKAFGA
HHHHHHHHHHHCCCC
4.0730846556
212SulfoxidationDGKTVAPMPPAQDHK
CCCEECCCCCHHHCC
4.4730846556
2192-HydroxyisobutyrylationMPPAQDHKRLLEGDG
CCCHHHCCHHHCCCC
53.70-
219AcetylationMPPAQDHKRLLEGDG
CCCHHHCCHHHCCCC
53.7030588885
219UbiquitinationMPPAQDHKRLLEGDG
CCCHHHCCHHHCCCC
53.7021906983
219 (in isoform 1)Ubiquitination-53.7021890473
219 (in isoform 2)Ubiquitination-53.7021906983
230PhosphorylationEGDGGPNTGGMGAYC
CCCCCCCCCCCCCCC
37.9420860994
237GlutathionylationTGGMGAYCPAPQVSN
CCCCCCCCCCCCCCC
1.9922555962
249AcetylationVSNDLLLKIKDTVLQ
CCCCHHHHHHHHHHH
47.9126051181
249UbiquitinationVSNDLLLKIKDTVLQ
CCCCHHHHHHHHHHH
47.91-
2512-HydroxyisobutyrylationNDLLLKIKDTVLQRT
CCHHHHHHHHHHHHH
45.84-
251UbiquitinationNDLLLKIKDTVLQRT
CCHHHHHHHHHHHHH
45.8421906983
251 (in isoform 1)Ubiquitination-45.8421890473
251 (in isoform 2)Ubiquitination-45.8421906983
258PhosphorylationKDTVLQRTVDGMQQE
HHHHHHHHHCCCCCC
15.2424043423
267PhosphorylationDGMQQEGTPYTGILY
CCCCCCCCCCCCEEE
16.6324043423
269PhosphorylationMQQEGTPYTGILYAG
CCCCCCCCCCEEEEE
19.8924043423
270PhosphorylationQQEGTPYTGILYAGI
CCCCCCCCCEEEEEE
20.9624043423
274PhosphorylationTPYTGILYAGIMLTK
CCCCCEEEEEEEEEC
10.8124043423
280PhosphorylationLYAGIMLTKNGPKVL
EEEEEEEECCCCEEE
12.7024043423
281UbiquitinationYAGIMLTKNGPKVLE
EEEEEEECCCCEEEE
56.8121906983
281 (in isoform 1)Ubiquitination-56.8121890473
281 (in isoform 2)Ubiquitination-56.8121906983
285AcetylationMLTKNGPKVLEFNCR
EEECCCCEEEEEECC
61.9327452117
285UbiquitinationMLTKNGPKVLEFNCR
EEECCCCEEEEEECC
61.93-
298S-nitrosocysteineCRFGDPECQVILPLL
CCCCCCCCCHHHHHH
4.82-
298GlutathionylationCRFGDPECQVILPLL
CCCCCCCCCHHHHHH
4.8222555962
298S-nitrosylationCRFGDPECQVILPLL
CCCCCCCCCHHHHHH
4.8219483679
298S-palmitoylationCRFGDPECQVILPLL
CCCCCCCCCHHHHHH
4.8226865113
341PhosphorylationALTVVMASKGYPGDY
EEEEEEECCCCCCCC
14.4426074081
344PhosphorylationVVMASKGYPGDYTKG
EEEECCCCCCCCCCC
14.0526356563
348PhosphorylationSKGYPGDYTKGVEIT
CCCCCCCCCCCEEEC
19.1027155012
349PhosphorylationKGYPGDYTKGVEITG
CCCCCCCCCCEEECC
26.5128152594
350AcetylationGYPGDYTKGVEITGF
CCCCCCCCCEEECCC
55.5219608861
350UbiquitinationGYPGDYTKGVEITGF
CCCCCCCCCEEECCC
55.5219608861
350 (in isoform 1)Ubiquitination-55.5221890473
350 (in isoform 2)Ubiquitination-55.5221906983
355PhosphorylationYTKGVEITGFPEAQA
CCCCEEECCCHHHHH
21.1826074081
375AcetylationFHAGTALKNGKVVTH
EECCCEEECCEEEEE
62.2825953088
375UbiquitinationFHAGTALKNGKVVTH
EECCCEEECCEEEEE
62.2821906983
375 (in isoform 1)Ubiquitination-62.2821890473
375 (in isoform 2)Ubiquitination-62.2821906983
378UbiquitinationGTALKNGKVVTHGGR
CCEEECCEEEEECCE
42.8121906983
378 (in isoform 1)Ubiquitination-42.8121890473
378 (in isoform 2)Ubiquitination-42.8121906983
381PhosphorylationLKNGKVVTHGGRVLA
EECCEEEEECCEEEE
20.1421949786
390PhosphorylationGGRVLAVTAIRENLI
CCEEEEHHHHHHHHH
15.6820068231
398PhosphorylationAIRENLISALEEAKK
HHHHHHHHHHHHHHH
29.9321712546
404AcetylationISALEEAKKGLAAIK
HHHHHHHHHHHCEEE
51.1326051181
404SuccinylationISALEEAKKGLAAIK
HHHHHHHHHHHCEEE
51.1323954790
404UbiquitinationISALEEAKKGLAAIK
HHHHHHHHHHHCEEE
51.13-
404 (in isoform 1)Ubiquitination-51.1321890473
404 (in isoform 2)Ubiquitination-51.1321906983
405UbiquitinationSALEEAKKGLAAIKF
HHHHHHHHHHCEEEE
67.23-
411UbiquitinationKKGLAAIKFEGAIYR
HHHHCEEEECCCEEE
32.4121906983
411 (in isoform 1)Ubiquitination-32.4121890473
411 (in isoform 2)Ubiquitination-32.4121906983
417NitrationIKFEGAIYRKDVGFR
EEECCCEEECCCCCH
15.86-
417PhosphorylationIKFEGAIYRKDVGFR
EEECCCEEECCCCCH
15.8625159151
419UbiquitinationFEGAIYRKDVGFRAI
ECCCEEECCCCCHHE
39.53-
433MethylationIAFLQQPRSLTYKES
EEECCCCCCCCCCCC
39.70-
434PhosphorylationAFLQQPRSLTYKESG
EECCCCCCCCCCCCC
31.5723312004
436PhosphorylationLQQPRSLTYKESGVD
CCCCCCCCCCCCCCE
33.5223312004
437PhosphorylationQQPRSLTYKESGVDI
CCCCCCCCCCCCCEE
20.3223186163
438UbiquitinationQPRSLTYKESGVDIA
CCCCCCCCCCCCEEC
39.9221906983
438 (in isoform 1)Ubiquitination-39.9221890473
440PhosphorylationRSLTYKESGVDIAAG
CCCCCCCCCCEECCC
39.7123917254
449SulfoxidationVDIAAGNMLVKKIQP
CEECCCCHHHHHHHH
4.4421406390
452AcetylationAAGNMLVKKIQPLAK
CCCCHHHHHHHHHHH
39.9525953088
452UbiquitinationAAGNMLVKKIQPLAK
CCCCHHHHHHHHHHH
39.9521890473
452 (in isoform 1)Ubiquitination-39.9521890473
453UbiquitinationAGNMLVKKIQPLAKA
CCCHHHHHHHHHHHH
38.81-
4592-HydroxyisobutyrylationKKIQPLAKATSRSGC
HHHHHHHHHHCCCCC
60.94-
459AcetylationKKIQPLAKATSRSGC
HHHHHHHHHHCCCCC
60.9425953088
459UbiquitinationKKIQPLAKATSRSGC
HHHHHHHHHHCCCCC
60.9421890473
459 (in isoform 1)Ubiquitination-60.9421890473
464PhosphorylationLAKATSRSGCKVDLG
HHHHHCCCCCEEECC
48.5924719451
466GlutathionylationKATSRSGCKVDLGGF
HHHCCCCCEEECCCC
4.0222555962
467UbiquitinationATSRSGCKVDLGGFA
HHCCCCCEEECCCCC
42.16-
480MethylationFAGLFDLKAAGFKDP
CCCCCCHHHCCCCCC
37.73-
480UbiquitinationFAGLFDLKAAGFKDP
CCCCCCHHHCCCCCC
37.7321890473
480 (in isoform 1)Ubiquitination-37.7321890473
485AcetylationDLKAAGFKDPLLASG
CHHHCCCCCCCCCCC
58.4825953088
485UbiquitinationDLKAAGFKDPLLASG
CHHHCCCCCCCCCCC
58.4821890473
485 (in isoform 1)Ubiquitination-58.4821890473
498PhosphorylationSGTDGVGTKLKIAQL
CCCCCCCHHHHHHHH
30.6921815630
499UbiquitinationGTDGVGTKLKIAQLC
CCCCCCHHHHHHHHC
41.68-
5012-HydroxyisobutyrylationDGVGTKLKIAQLCNK
CCCCHHHHHHHHCCC
37.24-
501UbiquitinationDGVGTKLKIAQLCNK
CCCCHHHHHHHHCCC
37.24-
511PhosphorylationQLCNKHDTIGQDLVA
HHCCCCCCCCHHHHH
27.0826074081
546PhosphorylationSCGKLDLSVTEAVVA
ECCCCCCHHHHHHHH
27.0228348404
548PhosphorylationGKLDLSVTEAVVAGI
CCCCCHHHHHHHHHH
18.1728348404
557UbiquitinationAVVAGIAKACGKAGC
HHHHHHHHHHCCCCC
42.14-
561UbiquitinationGIAKACGKAGCALLG
HHHHHHCCCCCHHCC
41.30-
598AcetylationGAMERDQKLPHLERI
HHHHCCCCCCCHHHC
69.1725953088
598UbiquitinationGAMERDQKLPHLERI
HHHHCCCCCCCHHHC
69.17-
616PhosphorylationDVVVGIASSGLHSNG
CEEEEEECCCCCCCC
24.0225850435
617PhosphorylationVVVGIASSGLHSNGF
EEEEEECCCCCCCCH
36.0324719451
621PhosphorylationIASSGLHSNGFSLVR
EECCCCCCCCHHHHH
43.6325850435
625PhosphorylationGLHSNGFSLVRKIVA
CCCCCCHHHHHHHHH
27.6125850435
633UbiquitinationLVRKIVAKSSLQYSS
HHHHHHHHCCCCCCC
29.68-
646GlutathionylationSSPAPDGCGDQTLGD
CCCCCCCCCCCCHHH
7.6722555962
657PhosphorylationTLGDLLLTPTRIYSH
CHHHHHCCCCEEECC
23.6824719451
662PhosphorylationLLTPTRIYSHSLLPV
HCCCCEEECCCHHHH
9.3128152594
663PhosphorylationLTPTRIYSHSLLPVL
CCCCEEECCCHHHHH
12.2928152594
665PhosphorylationPTRIYSHSLLPVLRS
CCEEECCCHHHHHHC
26.1728152594
672PhosphorylationSLLPVLRSGHVKAFA
CHHHHHHCCCCEEEE
29.14-
676UbiquitinationVLRSGHVKAFAHITG
HHHCCCCEEEEEECC
31.92-
682PhosphorylationVKAFAHITGGGLLEN
CEEEEEECCCHHHHC
21.6528450419
697UbiquitinationIPRVLPEKLGVDLDA
CCCCCHHHHCCCCCC
48.9121890473
697 (in isoform 1)Ubiquitination-48.9121890473
714PhosphorylationWRIPRVFSWLQQEGH
CCHHHHHHHHHHCCC
24.82-
723PhosphorylationLQQEGHLSEEEMART
HHHCCCCCHHHHHHH
36.97-
730PhosphorylationSEEEMARTFNCGVGA
CHHHHHHHCCCCCCE
15.0620068231
733GlutathionylationEMARTFNCGVGAVLV
HHHHHCCCCCCEEEE
4.0022555962
743UbiquitinationGAVLVVSKEQTEQIL
CEEEEECHHHHHHHH
42.08-
7572-HydroxyisobutyrylationLRDIQQHKEEAWVIG
HHHHHHHHHHHEEEH
53.57-
757AcetylationLRDIQQHKEEAWVIG
HHHHHHHHHHHEEEH
53.5725953088
757UbiquitinationLRDIQQHKEEAWVIG
HHHHHHHHHHHEEEH
53.57-
773PhosphorylationVVARAEGSPRVKVKN
HHHHCCCCCCEEEHH
10.8823403867
779UbiquitinationGSPRVKVKNLIESMQ
CCCCEEEHHHHHHHE
40.0821890473
779 (in isoform 1)Ubiquitination-40.0821890473
784PhosphorylationKVKNLIESMQINGSV
EEHHHHHHHEECCEE
14.7023186163
790PhosphorylationESMQINGSVLKNGSL
HHHEECCEEECCCCC
21.5628555341
796PhosphorylationGSVLKNGSLTNHFSF
CEEECCCCCCCCCCC
41.2223401153
798PhosphorylationVLKNGSLTNHFSFEK
EECCCCCCCCCCCCC
28.4823927012
802PhosphorylationGSLTNHFSFEKKKAR
CCCCCCCCCCCCCCE
25.5823401153
805UbiquitinationTNHFSFEKKKARVAV
CCCCCCCCCCCEEEE
58.52-
806UbiquitinationNHFSFEKKKARVAVL
CCCCCCCCCCEEEEE
44.46-
815PhosphorylationARVAVLISGTGSNLQ
CEEEEEEECCCHHHH
26.5827080861
817PhosphorylationVAVLISGTGSNLQAL
EEEEEECCCHHHHHH
30.5520068231
819PhosphorylationVLISGTGSNLQALID
EEEECCCHHHHHHHH
33.9220068231
827PhosphorylationNLQALIDSTREPNSS
HHHHHHHCCCCCCCC
23.5220068231
828PhosphorylationLQALIDSTREPNSSA
HHHHHHCCCCCCCCC
34.9927080861
844AcetylationIDIVISNKAAVAGLD
EEEEECCHHHHCCCC
30.8219811569
8522-HydroxyisobutyrylationAAVAGLDKAERAGIP
HHHCCCCHHHHCCCC
58.13-
852AcetylationAAVAGLDKAERAGIP
HHHCCCCHHHHCCCC
58.1323749302
852MalonylationAAVAGLDKAERAGIP
HHHCCCCHHHHCCCC
58.1326320211
852UbiquitinationAAVAGLDKAERAGIP
HHHCCCCHHHHCCCC
58.13-
855MethylationAGLDKAERAGIPTRV
CCCCHHHHCCCCHHH
42.87-
860PhosphorylationAERAGIPTRVINHKL
HHHCCCCHHHCCCHH
35.33-
866AcetylationPTRVINHKLYKNRVE
CHHHCCCHHHCCCCC
49.3625953088
866UbiquitinationPTRVINHKLYKNRVE
CHHHCCCHHHCCCCC
49.36-
900PhosphorylationAGFMRILSGPFVQKW
HHHHHHHCCCHHHCC
41.8920068231
906UbiquitinationLSGPFVQKWNGKMLN
HCCCHHHCCCCEECC
37.01-
910UbiquitinationFVQKWNGKMLNIHPS
HHHCCCCEECCCCHH
36.6821890473
910 (in isoform 1)Ubiquitination-36.6821890473
921PhosphorylationIHPSLLPSFKGSNAH
CCHHHCCCCCCCCHH
39.2924719451
977UbiquitinationATLSERVKLAEHKIF
EEHHHHHHHHHCCHH
48.47-
982AcetylationRVKLAEHKIFPAALQ
HHHHHHCCHHHHHHH
37.23156527
1008UbiquitinationNGKICWVKEE-----
CCCEEEEECC-----
31.46-

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 PUR2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUR2_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 PUR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PUR6_HUMANPAICSphysical
22939629
SPS1_HUMANSEPHS1physical
22939629
SYWC_HUMANWARSphysical
22939629
PAXI_HUMANPXNphysical
21988832
IMA1_HUMANKPNA2physical
21988832
SYCC_HUMANCARSphysical
22863883
HIRP3_HUMANHIRIP3physical
22863883
HSP74_HUMANHSPA4physical
22863883
RANB3_HUMANRANBP3physical
22863883
RL24_HUMANRPL24physical
22863883
SET_HUMANSETphysical
22863883
SF01_HUMANSF1physical
22863883
SPT5H_HUMANSUPT5Hphysical
22863883
SWP70_HUMANSWAP70physical
22863883
RO60_HUMANTROVE2physical
22863883
XPO7_HUMANXPO7physical
22863883
ZYX_HUMANZYXphysical
22863883
PUR8_HUMANADSLphysical
26344197
AK1C2_HUMANAKR1C2physical
26344197
ARFP1_HUMANARFIP1physical
26344197
IF4H_HUMANEIF4Hphysical
26344197
HIP1R_HUMANHIP1Rphysical
26344197
ROA1_HUMANHNRNPA1physical
26344197
PUR4_HUMANPFASphysical
26344197
DHPR_HUMANQDPRphysical
26344197
RAVR1_HUMANRAVER1physical
26344197
SPS1_HUMANSEPHS1physical
26344197
STAT6_HUMANSTAT6physical
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
DB00642Pemetrexed
Regulatory Network of PUR2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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, 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-350, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-348, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-348, AND MASSSPECTROMETRY.

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