F120A_HUMAN - dbPTM
F120A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F120A_HUMAN
UniProt AC Q9NZB2
Protein Name Constitutive coactivator of PPAR-gamma-like protein 1
Gene Name FAM120A
Organism Homo sapiens (Human).
Sequence Length 1118
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Translocates to plasma membrane upon ultraviolet exposure.
Protein Description May participate in mRNA transport in the cytoplasm (By similarity). Critical component of the oxidative stress-induced survival signaling. Activates src family kinases and acts as a scaffolding protein enabling src family kinases to phosphorylate and activate PI3-kinase. Binds RNA and promotes the secretion of IGF-II. May play a pivotal role in the progression of scirrhous-type gastric cancer by supporting cancer cell survival in environments with various oxidative stresses..
Protein Sequence MGVQGFQDYIEKHCPSAVVPVELQKLARGSLVGGGRQRPPQTPLRLLVDADNCLHRLYGGFYTDWVSGGQWNHMLGYLAALAKACFGGNIELFVFFNGALEKARLHEWVKRQGNERQTAQQIVSHVQNKGTPPPKVWFLPPVCMAHCIRLALIRFHVKVAQSIEDHHQEVIGFCRENGFHGLVAYDSDYALCNIPYYFSAHALKLSRNGKSLTTSQYLMHEVAKQLDLNPNRFPIFAALLGNHILPDEDLASFHWSLLGPEHPLASLKVRAHQLVLPPCDVVIKAVADYVRNIQDTSDLDAIAKDVFQHSQSRTDDKVIRFKRAIGYYSATSKPMSFHPPHYLAARPGPFGMPGMVPPHVPPQMLNIPQTSLQAKPVAPQVPSPGGAPGQGPYPYSLSEPAPLTLDTSGKNLTEQNSYSNIPHEGKHTPLYERSSPINPAQSGSPNHVDSAYFPGSSTSSSSDNDEGSGGATNHISGNKIGWEKTGSHSEPQARGDPGDQTKAEGSSTASSGSQLAEGKGSQMGTVQPIPCLLSMPTRNHMDITTPPLPPVAPEVLRVAEHRHKKGLMYPYIFHVLTKGEIKIAVSIEDEANKDLPPAALLYRPVRQYVYGVLFSLAESRKKTERLAFRKNRLPPEFSPVIIKEWAAYKGKSPQTPELVEALAFREWTCPNLKRLWLGKAVEDKNRRMRAFLACMRSDTPAMLNPANVPTHLMVLCCVLRYMVQWPGARILRRQELDAFLAQALSPKLYEPDQLQELKIENLDPRGIQLSALFMSGVDMALFANDACGQPIPWEHCCPWMYFDGKLFQSKLLKASREKTPLIDLCDGQADQAAKVEKMRQSVLEGLSFSRQSHTLPFPPPPALPFYPASAYPRHFGPVPPSQGRGRGFAGVCGFGGPYGETVATGPYRAFRVAAASGHCGAFSGSDSSRTSKSQGGVQPIPSQGGKLEIAGTVVGHWAGSRRGRGGRGPFPLQVVSVGGPARGRPRGVISTPVIRTFGRGGRYYGRGYKNQAAIQGRPPYAASAEEVAKELKSKSGESKSSAMSSDGSLAENGVMAEEKPAPQMNGSTGDARAPSHSESALNNDSKTCNTNPHLNALSTDSACRREAALEAAVLNKEE
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
9PhosphorylationGVQGFQDYIEKHCPS
CCCHHHHHHHHHCCC
10.53-
12AcetylationGFQDYIEKHCPSAVV
HHHHHHHHHCCCCEE
40.7321466224
12UbiquitinationGFQDYIEKHCPSAVV
HHHHHHHHHCCCCEE
40.7329967540
12 (in isoform 6)Ubiquitination-40.73-
14S-nitrosylationQDYIEKHCPSAVVPV
HHHHHHHCCCCEEEH
4.162212679
25UbiquitinationVVPVELQKLARGSLV
EEEHHHHHHHCCCCC
57.6533845483
25 (in isoform 6)Ubiquitination-57.65-
30PhosphorylationLQKLARGSLVGGGRQ
HHHHHCCCCCCCCCC
17.8326699800
42PhosphorylationGRQRPPQTPLRLLVD
CCCCCCCCCHHHEEC
30.02-
110UbiquitinationARLHEWVKRQGNERQ
HHHHHHHHHCCCCHH
39.8229967540
110 (in isoform 6)Ubiquitination-39.82-
118PhosphorylationRQGNERQTAQQIVSH
HCCCCHHHHHHHHHH
32.4321406692
124PhosphorylationQTAQQIVSHVQNKGT
HHHHHHHHHHHHCCC
21.4121406692
129UbiquitinationIVSHVQNKGTPPPKV
HHHHHHHCCCCCCCC
47.2529967540
131PhosphorylationSHVQNKGTPPPKVWF
HHHHHCCCCCCCCCC
33.9424719451
210UbiquitinationLKLSRNGKSLTTSQY
HHHCCCCCCCCHHHH
45.93-
210 (in isoform 6)Ubiquitination-45.93-
211PhosphorylationKLSRNGKSLTTSQYL
HHCCCCCCCCHHHHH
32.1422210691
284AcetylationPPCDVVIKAVADYVR
CCHHHHHHHHHHHHH
25.7926051181
289PhosphorylationVIKAVADYVRNIQDT
HHHHHHHHHHHCCCC
7.5025690035
297PhosphorylationVRNIQDTSDLDAIAK
HHHCCCCCCHHHHHH
44.45-
304UbiquitinationSDLDAIAKDVFQHSQ
CCHHHHHHHHHHHHC
48.5922817900
304 (in isoform 1)Ubiquitination-48.5921890473
304 (in isoform 2)Ubiquitination-48.5921890473
304 (in isoform 4)Ubiquitination-48.5921890473
304 (in isoform 5)Ubiquitination-48.5921890473
304 (in isoform 6)Ubiquitination-48.5921890473
327PhosphorylationRFKRAIGYYSATSKP
HHHHHHCCCCCCCCC
6.53-
328PhosphorylationFKRAIGYYSATSKPM
HHHHHCCCCCCCCCC
6.14-
336PhosphorylationSATSKPMSFHPPHYL
CCCCCCCCCCCCCCC
29.0023312004
342PhosphorylationMSFHPPHYLAARPGP
CCCCCCCCCCCCCCC
12.10-
370PhosphorylationQMLNIPQTSLQAKPV
HHHCCCCCCCCCCCC
26.5024043423
371PhosphorylationMLNIPQTSLQAKPVA
HHCCCCCCCCCCCCC
17.1524043423
382PhosphorylationKPVAPQVPSPGGAPG
CCCCCCCCCCCCCCC
29.5632142685
383PhosphorylationPVAPQVPSPGGAPGQ
CCCCCCCCCCCCCCC
37.0028355574
393PhosphorylationGAPGQGPYPYSLSEP
CCCCCCCCCCCCCCC
22.9428102081
395PhosphorylationPGQGPYPYSLSEPAP
CCCCCCCCCCCCCCC
19.1925159151
396PhosphorylationGQGPYPYSLSEPAPL
CCCCCCCCCCCCCCC
22.4026657352
398PhosphorylationGPYPYSLSEPAPLTL
CCCCCCCCCCCCCEE
35.2829978859
404PhosphorylationLSEPAPLTLDTSGKN
CCCCCCCEECCCCCC
22.8729978859
407PhosphorylationPAPLTLDTSGKNLTE
CCCCEECCCCCCCCC
42.3520639409
408PhosphorylationAPLTLDTSGKNLTEQ
CCCEECCCCCCCCCC
47.6520639409
413PhosphorylationDTSGKNLTEQNSYSN
CCCCCCCCCCCCCCC
44.9421945579
417PhosphorylationKNLTEQNSYSNIPHE
CCCCCCCCCCCCCCC
29.6321945579
417 (in isoform 6)Phosphorylation-29.6327642862
418PhosphorylationNLTEQNSYSNIPHEG
CCCCCCCCCCCCCCC
17.1821945579
418 (in isoform 6)Phosphorylation-17.1827642862
419PhosphorylationLTEQNSYSNIPHEGK
CCCCCCCCCCCCCCC
28.2721945579
419 (in isoform 6)Phosphorylation-28.2727642862
425UbiquitinationYSNIPHEGKHTPLYE
CCCCCCCCCCCCCCC
24.8229967540
426UbiquitinationSNIPHEGKHTPLYER
CCCCCCCCCCCCCCC
41.1229967540
426 (in isoform 6)Malonylation-41.1230639696
428PhosphorylationIPHEGKHTPLYERSS
CCCCCCCCCCCCCCC
20.6222167270
428 (in isoform 6)Phosphorylation-20.6227642862
431PhosphorylationEGKHTPLYERSSPIN
CCCCCCCCCCCCCCC
15.5327273156
431 (in isoform 6)Phosphorylation-15.5327642862
434PhosphorylationHTPLYERSSPINPAQ
CCCCCCCCCCCCHHH
28.6423927012
435PhosphorylationTPLYERSSPINPAQS
CCCCCCCCCCCHHHC
35.7030278072
442PhosphorylationSPINPAQSGSPNHVD
CCCCHHHCCCCCCCC
43.2630278072
444PhosphorylationINPAQSGSPNHVDSA
CCHHHCCCCCCCCCC
27.9823927012
450PhosphorylationGSPNHVDSAYFPGSS
CCCCCCCCCCCCCCC
24.6323927012
452PhosphorylationPNHVDSAYFPGSSTS
CCCCCCCCCCCCCCC
17.7923663014
456PhosphorylationDSAYFPGSSTSSSSD
CCCCCCCCCCCCCCC
30.5823927012
457PhosphorylationSAYFPGSSTSSSSDN
CCCCCCCCCCCCCCC
37.9223927012
458PhosphorylationAYFPGSSTSSSSDND
CCCCCCCCCCCCCCC
34.0323663014
459PhosphorylationYFPGSSTSSSSDNDE
CCCCCCCCCCCCCCC
30.1225159151
460PhosphorylationFPGSSTSSSSDNDEG
CCCCCCCCCCCCCCC
33.6725159151
461PhosphorylationPGSSTSSSSDNDEGS
CCCCCCCCCCCCCCC
41.2923927012
462PhosphorylationGSSTSSSSDNDEGSG
CCCCCCCCCCCCCCC
42.2425159151
468PhosphorylationSSDNDEGSGGATNHI
CCCCCCCCCCCCCCC
31.8223663014
472PhosphorylationDEGSGGATNHISGNK
CCCCCCCCCCCCCCC
30.5123663014
476PhosphorylationGGATNHISGNKIGWE
CCCCCCCCCCCCCCE
28.8523663014
478 (in isoform 6)Phosphorylation-26.4425159151
483UbiquitinationSGNKIGWEKTGSHSE
CCCCCCCEECCCCCC
35.2129967540
484UbiquitinationGNKIGWEKTGSHSEP
CCCCCCEECCCCCCC
52.2429967540
485PhosphorylationNKIGWEKTGSHSEPQ
CCCCCEECCCCCCCC
32.1926699800
487PhosphorylationIGWEKTGSHSEPQAR
CCCEECCCCCCCCCC
29.1325849741
489PhosphorylationWEKTGSHSEPQARGD
CEECCCCCCCCCCCC
53.3128985074
501PhosphorylationRGDPGDQTKAEGSST
CCCCCCCCCCCCCCC
36.6423312004
501UbiquitinationRGDPGDQTKAEGSST
CCCCCCCCCCCCCCC
36.6421963094
502AcetylationGDPGDQTKAEGSSTA
CCCCCCCCCCCCCCC
38.5226051181
502UbiquitinationGDPGDQTKAEGSSTA
CCCCCCCCCCCCCCC
38.5221906983
502 (in isoform 1)Ubiquitination-38.5221890473
502 (in isoform 2)Ubiquitination-38.5221890473
502 (in isoform 4)Ubiquitination-38.5221890473
502 (in isoform 5)Ubiquitination-38.5221890473
504 (in isoform 6)Phosphorylation-62.2524275569
506PhosphorylationDQTKAEGSSTASSGS
CCCCCCCCCCCCCCC
18.9329255136
507PhosphorylationQTKAEGSSTASSGSQ
CCCCCCCCCCCCCCC
38.5629255136
508PhosphorylationTKAEGSSTASSGSQL
CCCCCCCCCCCCCCC
32.0529255136
510PhosphorylationAEGSSTASSGSQLAE
CCCCCCCCCCCCCCC
35.0129255136
511PhosphorylationEGSSTASSGSQLAEG
CCCCCCCCCCCCCCC
39.7429255136
513PhosphorylationSSTASSGSQLAEGKG
CCCCCCCCCCCCCCC
24.7829255136
521PhosphorylationQLAEGKGSQMGTVQP
CCCCCCCCCCCCCCC
22.0822210691
525PhosphorylationGKGSQMGTVQPIPCL
CCCCCCCCCCCCCEE
15.6028348404
529UbiquitinationQMGTVQPIPCLLSMP
CCCCCCCCCEEECCC
1.7921963094
530UbiquitinationMGTVQPIPCLLSMPT
CCCCCCCCEEECCCC
14.9121963094
530 (in isoform 6)Ubiquitination-14.9121890473
534PhosphorylationQPIPCLLSMPTRNHM
CCCCEEECCCCCCCC
15.1227251275
537PhosphorylationPCLLSMPTRNHMDIT
CEEECCCCCCCCCCC
35.1522210691
545PhosphorylationRNHMDITTPPLPPVA
CCCCCCCCCCCCCCC
24.2022210691
619PhosphorylationVLFSLAESRKKTERL
HHHHHHHHHHHHHHH
43.7429083192
638PhosphorylationNRLPPEFSPVIIKEW
CCCCCCCCHHHHHHH
19.3227050516
650UbiquitinationKEWAAYKGKSPQTPE
HHHHHHCCCCCCCHH
24.0129967540
651UbiquitinationEWAAYKGKSPQTPEL
HHHHHCCCCCCCHHH
55.6129967540
652PhosphorylationWAAYKGKSPQTPELV
HHHHCCCCCCCHHHH
30.7925850435
655PhosphorylationYKGKSPQTPELVEAL
HCCCCCCCHHHHHHH
23.3229255136
673AcetylationEWTCPNLKRLWLGKA
CCCCCCCHHHHCCHH
52.6825953088
673UbiquitinationEWTCPNLKRLWLGKA
CCCCCCCHHHHCCHH
52.68-
678UbiquitinationNLKRLWLGKAVEDKN
CCHHHHCCHHHHCHH
12.3229967540
679UbiquitinationLKRLWLGKAVEDKNR
CHHHHCCHHHHCHHH
47.2729967540
701 (in isoform 6)Ubiquitination-19.72-
721PhosphorylationVLCCVLRYMVQWPGA
HHHHHHHHHHHCCCH
9.47-
745PhosphorylationAFLAQALSPKLYEPD
HHHHHHHCCCCCCHH
24.0124719451
757UbiquitinationEPDQLQELKIENLDP
CHHHHHHHCCCCCCC
4.3433845483
758UbiquitinationPDQLQELKIENLDPR
HHHHHHHCCCCCCCC
47.4221906983
758 (in isoform 1)Ubiquitination-47.4221890473
758 (in isoform 4)Ubiquitination-47.4221890473
777 (in isoform 6)Phosphorylation-3.4027642862
786 (in isoform 6)Ubiquitination-10.1121890473
810AcetylationDGKLFQSKLLKASRE
CCHHHHHHHHHHHHC
47.2425953088
810UbiquitinationDGKLFQSKLLKASRE
CCHHHHHHHHHHHHC
47.24-
817UbiquitinationKLLKASREKTPLIDL
HHHHHHHCCCCCHHC
59.8032015554
818UbiquitinationLLKASREKTPLIDLC
HHHHHHCCCCCHHCC
55.0933845483
833UbiquitinationDGQADQAAKVEKMRQ
CCCHHHHHHHHHHHH
15.7029967540
834AcetylationGQADQAAKVEKMRQS
CCHHHHHHHHHHHHH
54.6826051181
834UbiquitinationGQADQAAKVEKMRQS
CCHHHHHHHHHHHHH
54.6829967540
838 (in isoform 6)Ubiquitination-2.74-
841PhosphorylationKVEKMRQSVLEGLSF
HHHHHHHHHHHHHCC
20.5020068231
845UbiquitinationMRQSVLEGLSFSRQS
HHHHHHHHHCCCCCC
23.5924816145
846UbiquitinationRQSVLEGLSFSRQSH
HHHHHHHHCCCCCCC
3.2224816145
846 (in isoform 6)Ubiquitination-3.22-
847PhosphorylationQSVLEGLSFSRQSHT
HHHHHHHCCCCCCCC
31.8420068231
849PhosphorylationVLEGLSFSRQSHTLP
HHHHHCCCCCCCCCC
26.4920068231
852PhosphorylationGLSFSRQSHTLPFPP
HHCCCCCCCCCCCCC
19.82-
854PhosphorylationSFSRQSHTLPFPPPP
CCCCCCCCCCCCCCC
41.18-
873MethylationYPASAYPRHFGPVPP
CCCCCCCCCCCCCCC
25.7024129315
884DimethylationPVPPSQGRGRGFAGV
CCCCCCCCCCCCCCC
24.81-
884MethylationPVPPSQGRGRGFAGV
CCCCCCCCCCCCCCC
24.8124129315
886DimethylationPPSQGRGRGFAGVCG
CCCCCCCCCCCCCCC
35.38-
886MethylationPPSQGRGRGFAGVCG
CCCCCCCCCCCCCCC
35.3824129315
916PhosphorylationAFRVAAASGHCGAFS
HHHHHHCCCCCCCCC
25.0923312004
923PhosphorylationSGHCGAFSGSDSSRT
CCCCCCCCCCCCCCC
36.5325850435
925PhosphorylationHCGAFSGSDSSRTSK
CCCCCCCCCCCCCCC
32.8725850435
927PhosphorylationGAFSGSDSSRTSKSQ
CCCCCCCCCCCCCCC
24.3430576142
928PhosphorylationAFSGSDSSRTSKSQG
CCCCCCCCCCCCCCC
44.5630576142
930PhosphorylationSGSDSSRTSKSQGGV
CCCCCCCCCCCCCCC
42.3226434776
931PhosphorylationGSDSSRTSKSQGGVQ
CCCCCCCCCCCCCCC
29.2426434776
931UbiquitinationGSDSSRTSKSQGGVQ
CCCCCCCCCCCCCCC
29.2427667366
932AcetylationSDSSRTSKSQGGVQP
CCCCCCCCCCCCCCC
46.30-
932UbiquitinationSDSSRTSKSQGGVQP
CCCCCCCCCCCCCCC
46.3027667366
932 (in isoform 1)Ubiquitination-46.3021890473
933PhosphorylationDSSRTSKSQGGVQPI
CCCCCCCCCCCCCCC
33.5526055452
942PhosphorylationGGVQPIPSQGGKLEI
CCCCCCCCCCCEEEE
42.02-
952PhosphorylationGKLEIAGTVVGHWAG
CEEEEECEEEECCCC
11.73-
959UbiquitinationTVVGHWAGSRRGRGG
EEEECCCCCCCCCCC
19.2527667366
960PhosphorylationVVGHWAGSRRGRGGR
EEECCCCCCCCCCCC
15.8528857561
960UbiquitinationVVGHWAGSRRGRGGR
EEECCCCCCCCCCCC
15.8527667366
960 (in isoform 6)Ubiquitination-15.8521890473
964MethylationWAGSRRGRGGRGPFP
CCCCCCCCCCCCCCC
42.45-
967MethylationSRRGRGGRGPFPLQV
CCCCCCCCCCCCEEE
53.05-
976PhosphorylationPFPLQVVSVGGPARG
CCCEEEEEECCCCCC
19.0528857561
981MethylationVVSVGGPARGRPRGV
EEEECCCCCCCCCCC
29.8115782174
982DimethylationVSVGGPARGRPRGVI
EEECCCCCCCCCCCC
44.80-
982MethylationVSVGGPARGRPRGVI
EEECCCCCCCCCCCC
44.8024129315
984MethylationVGGPARGRPRGVIST
ECCCCCCCCCCCCCC
16.52-
986MethylationGPARGRPRGVISTPV
CCCCCCCCCCCCCHH
51.1224129315
990PhosphorylationGRPRGVISTPVIRTF
CCCCCCCCCHHHCCC
25.0129978859
991PhosphorylationRPRGVISTPVIRTFG
CCCCCCCCHHHCCCC
15.5116964243
995MethylationVISTPVIRTFGRGGR
CCCCHHHCCCCCCCC
25.00-
996PhosphorylationISTPVIRTFGRGGRY
CCCHHHCCCCCCCCC
21.2221406692
999MethylationPVIRTFGRGGRYYGR
HHHCCCCCCCCCCCC
39.95-
1002MethylationRTFGRGGRYYGRGYK
CCCCCCCCCCCCCCC
25.07-
1003PhosphorylationTFGRGGRYYGRGYKN
CCCCCCCCCCCCCCC
17.34-
1004PhosphorylationFGRGGRYYGRGYKNQ
CCCCCCCCCCCCCCC
10.05-
1006DimethylationRGGRYYGRGYKNQAA
CCCCCCCCCCCCCHH
29.19-
1006MethylationRGGRYYGRGYKNQAA
CCCCCCCCCCCCCHH
29.19-
1020PhosphorylationAIQGRPPYAASAEEV
HHCCCCCCCCCHHHH
19.9229255136
1023PhosphorylationGRPPYAASAEEVAKE
CCCCCCCCHHHHHHH
28.2123401153
1029AcetylationASAEEVAKELKSKSG
CCHHHHHHHHHHCCC
69.6126051181
1033PhosphorylationEVAKELKSKSGESKS
HHHHHHHHCCCCCHH
44.68-
1035PhosphorylationAKELKSKSGESKSSA
HHHHHHCCCCCHHHC
55.6825954137
1038PhosphorylationLKSKSGESKSSAMSS
HHHCCCCCHHHCCCC
41.17-
1040PhosphorylationSKSGESKSSAMSSDG
HCCCCCHHHCCCCCC
32.3923927012
1041PhosphorylationKSGESKSSAMSSDGS
CCCCCHHHCCCCCCC
31.5623927012
1044PhosphorylationESKSSAMSSDGSLAE
CCHHHCCCCCCCHHH
25.6223401153
1045PhosphorylationSKSSAMSSDGSLAEN
CHHHCCCCCCCHHHC
32.6723927012
1048PhosphorylationSAMSSDGSLAENGVM
HCCCCCCCHHHCCCC
29.4223927012
1067PhosphorylationPAPQMNGSTGDARAP
CCCCCCCCCCCCCCC
24.9825159151
1068PhosphorylationAPQMNGSTGDARAPS
CCCCCCCCCCCCCCC
40.2423927012
1075PhosphorylationTGDARAPSHSESALN
CCCCCCCCCCHHHHC
38.3629255136
1077PhosphorylationDARAPSHSESALNND
CCCCCCCCHHHHCCC
37.2726657352
1079PhosphorylationRAPSHSESALNNDSK
CCCCCCHHHHCCCCC
40.8625627689
1085UbiquitinationESALNNDSKTCNTNP
HHHHCCCCCCCCCCC
31.8029967540
1086UbiquitinationSALNNDSKTCNTNPH
HHHCCCCCCCCCCCC
61.0229967540
1098PhosphorylationNPHLNALSTDSACRR
CCCHHHCCCCHHHHH
27.9728348404
1099PhosphorylationPHLNALSTDSACRRE
CCHHHCCCCHHHHHH
34.5228348404
1101PhosphorylationLNALSTDSACRREAA
HHHCCCCHHHHHHHH
29.3828857561
1115UbiquitinationALEAAVLNKEE----
HHHHHHHCCCC----
42.9924816145
1116UbiquitinationLEAAVLNKEE-----
HHHHHHCCCC-----
60.0924816145
1143Ubiquitination--------------------------------
--------------------------------
24816145
1144Ubiquitination---------------------------------
---------------------------------
24816145

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 F120A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
982RMethylation

24129315

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 F120A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of F120A_HUMAN !!

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 F120A_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-982, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-1044; SER-1045 ANDSER-1048, AND MASS SPECTROMETRY.
"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-383, 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-1023, 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-30, AND MASSSPECTROMETRY.
"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-383, 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 THR-991, 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-393 AND TYR-395, ANDMASS SPECTROMETRY.

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