PUM1_HUMAN - dbPTM
PUM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUM1_HUMAN
UniProt AC Q14671
Protein Name Pumilio homolog 1 {ECO:0000305}
Gene Name PUM1 {ECO:0000312|HGNC:HGNC:14957}
Organism Homo sapiens (Human).
Sequence Length 1186
Subcellular Localization Cytoplasm . Cytoplasm, P-body . Cytoplasmic granule . Recruited to cytoplasmic stress granules upon viral infection.
Protein Description Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE). [PubMed: 21572425]
Protein Sequence MSVACVLKRKAVLWQDSFSPHLKHHPQEPANPNMPVVLTSGTGSQAQPQPAANQALAAGTHSSPVPGSIGVAGRSQDDAMVDYFFQRQHGEQLGGGGSGGGGYNNSKHRWPTGDNIHAEHQVRSMDELNHDFQALALEGRAMGEQLLPGKKFWETDESSKDGPKGIFLGDQWRDSAWGTSDHSVSQPIMVQRRPGQSFHVNSEVNSVLSPRSESGGLGVSMVEYVLSSSPGDSCLRKGGFGPRDADSDENDKGEKKNKGTFDGDKLGDLKEEGDVMDKTNGLPVQNGIDADVKDFSRTPGNCQNSANEVDLLGPNQNGSEGLAQLTSTNGAKPVEDFSNMESQSVPLDPMEHVGMEPLQFDYSGTQVPVDSAAATVGLFDYNSQQQLFQRPNALAVQQLTAAQQQQYALAAAHQPHIGLAPAAFVPNPYIISAAPPGTDPYTAGLAAAATLGPAVVPHQYYGVTPWGVYPASLFQQQAAAAAAATNSANQQTTPQAQQGQQQVLRGGASQRPLTPNQNQQGQQTDPLVAAAAVNSALAFGQGLAAGMPGYPVLAPAAYYDQTGALVVNAGARNGLGAPVRLVAPAPVIISSSAAQAAVAAAAASANGAAGGLAGTTNGPFRPLGTQQPQPQPQQQPNNNLASSSFYGNNSLNSNSQSSSLFSQGSAQPANTSLGFGSSSSLGATLGSALGGFGTAVANSNTGSGSRRDSLTGSSDLYKRTSSSLTPIGHSFYNGLSFSSSPGPVGMPLPSQGPGHSQTPPPSLSSHGSSSSLNLGGLTNGSGRYISAAPGAEAKYRSASSASSLFSPSSTLFSSSRLRYGMSDVMPSGRSRLLEDFRNNRYPNLQLREIAGHIMEFSQDQHGSRFIQLKLERATPAERQLVFNEILQAAYQLMVDVFGNYVIQKFFEFGSLEQKLALAERIRGHVLSLALQMYGCRVIQKALEFIPSDQQNEMVRELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFALSTHPYGCRVIQRILEHCLPDQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVAEIRGNVLVLSQHKFASNVVEKCVTHASRTERAVLIDEVCTMNDGPHSALYTMMKDQYANYVVQKMIDVAEPGQRKIVMHKIRPHIATLRKYTYGKHILAKLEKYYMKNGVDLGPICGPPNGII
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------MSVACVLKR
------CCHHHHEEC
29.7122814378
2Phosphorylation------MSVACVLKR
------CCHHHHEEC
29.7130631047
8MethylationMSVACVLKRKAVLWQ
CCHHHHEECCEEEEC
31.30115975911
17PhosphorylationKAVLWQDSFSPHLKH
CEEEECCCCCHHHCC
16.7218669648
19PhosphorylationVLWQDSFSPHLKHHP
EEECCCCCHHHCCCC
18.5025159151
19 (in isoform 3)Phosphorylation-18.5024719451
39PhosphorylationPNMPVVLTSGTGSQA
CCCCEEEECCCCCCC
17.3218691976
44PhosphorylationVLTSGTGSQAQPQPA
EEECCCCCCCCCCHH
23.3720068231
60PhosphorylationNQALAAGTHSSPVPG
HHHHHCCCCCCCCCC
17.5429632367
60 (in isoform 3)Phosphorylation-17.5427251275
62PhosphorylationALAAGTHSSPVPGSI
HHHCCCCCCCCCCCE
35.8529632367
63PhosphorylationLAAGTHSSPVPGSIG
HHCCCCCCCCCCCEE
23.4729632367
68PhosphorylationHSSPVPGSIGVAGRS
CCCCCCCCEEECCCC
15.3129632367
75PhosphorylationSIGVAGRSQDDAMVD
CEEECCCCCCHHHHH
36.7221712546
75 (in isoform 3)Phosphorylation-36.7227251275
83PhosphorylationQDDAMVDYFFQRQHG
CCHHHHHHHHHHHCC
8.5528796482
98PhosphorylationEQLGGGGSGGGGYNN
CCCCCCCCCCCCCCC
37.2225159151
98 (in isoform 3)Phosphorylation-37.2224719451
103PhosphorylationGGSGGGGYNNSKHRW
CCCCCCCCCCCCCCC
17.9120068231
106PhosphorylationGGGGYNNSKHRWPTG
CCCCCCCCCCCCCCC
26.6323401153
106 (in isoform 3)Phosphorylation-26.6327251275
107UbiquitinationGGGYNNSKHRWPTGD
CCCCCCCCCCCCCCC
39.0329967540
112PhosphorylationNSKHRWPTGDNIHAE
CCCCCCCCCCCCCHH
50.6527273156
112 (in isoform 3)Phosphorylation-50.6524719451
124PhosphorylationHAEHQVRSMDELNHD
CHHHHCCCHHHCCHH
31.5629255136
124 (in isoform 3)Phosphorylation-31.5627251275
125SulfoxidationAEHQVRSMDELNHDF
HHHHCCCHHHCCHHH
3.0421406390
143UbiquitinationALEGRAMGEQLLPGK
HHCCHHHHHCCCCCC
20.65-
150AcetylationGEQLLPGKKFWETDE
HHCCCCCCCEECCCC
42.7425953088
150UbiquitinationGEQLLPGKKFWETDE
HHCCCCCCCEECCCC
42.7429967540
151UbiquitinationEQLLPGKKFWETDES
HCCCCCCCEECCCCC
62.7229967540
158PhosphorylationKFWETDESSKDGPKG
CEECCCCCCCCCCCC
45.5629507054
159PhosphorylationFWETDESSKDGPKGI
EECCCCCCCCCCCCE
32.4923917254
160UbiquitinationWETDESSKDGPKGIF
ECCCCCCCCCCCCEE
75.8029967540
164UbiquitinationESSKDGPKGIFLGDQ
CCCCCCCCCEEECCH
70.89-
175PhosphorylationLGDQWRDSAWGTSDH
ECCHHHCCCCCCCCC
19.8324719451
180PhosphorylationRDSAWGTSDHSVSQP
HCCCCCCCCCCCCCC
29.4128555341
183PhosphorylationAWGTSDHSVSQPIMV
CCCCCCCCCCCCEEE
28.5828555341
185PhosphorylationGTSDHSVSQPIMVQR
CCCCCCCCCCEEEEE
33.0028348404
185 (in isoform 3)Phosphorylation-33.0027251275
187 (in isoform 4)Phosphorylation-14.7728102081
197PhosphorylationVQRRPGQSFHVNSEV
EEECCCCCEECCCHH
24.2023927012
197 (in isoform 3)Phosphorylation-24.2027251275
202PhosphorylationGQSFHVNSEVNSVLS
CCCEECCCHHCCCCC
41.6623927012
206PhosphorylationHVNSEVNSVLSPRSE
ECCCHHCCCCCCCCC
29.6129255136
206 (in isoform 3)Phosphorylation-29.6127251275
209PhosphorylationSEVNSVLSPRSESGG
CHHCCCCCCCCCCCC
18.9929255136
209 (in isoform 3)Phosphorylation-18.9924719451
210UbiquitinationEVNSVLSPRSESGGL
HHCCCCCCCCCCCCC
39.39-
212PhosphorylationNSVLSPRSESGGLGV
CCCCCCCCCCCCCCE
39.2323663014
214PhosphorylationVLSPRSESGGLGVSM
CCCCCCCCCCCCEEE
39.1323663014
214 (in isoform 3)Phosphorylation-39.1327251275
220PhosphorylationESGGLGVSMVEYVLS
CCCCCCEEEEEHHHH
18.4723663014
224PhosphorylationLGVSMVEYVLSSSPG
CCEEEEEHHHHCCCC
8.6928450419
227PhosphorylationSMVEYVLSSSPGDSC
EEEEHHHHCCCCCCH
20.8030278072
228PhosphorylationMVEYVLSSSPGDSCL
EEEHHHHCCCCCCHH
36.0730278072
229PhosphorylationVEYVLSSSPGDSCLR
EEHHHHCCCCCCHHH
29.5330278072
229 (in isoform 3)Phosphorylation-29.5324719451
233PhosphorylationLSSSPGDSCLRKGGF
HHCCCCCCHHHCCCC
22.4422617229
234GlutathionylationSSSPGDSCLRKGGFG
HCCCCCCHHHCCCCC
5.1822555962
237AcetylationPGDSCLRKGGFGPRD
CCCCHHHCCCCCCCC
50.8926051181
237UbiquitinationPGDSCLRKGGFGPRD
CCCCHHHCCCCCCCC
50.8929967540
243MethylationRKGGFGPRDADSDEN
HCCCCCCCCCCCCCC
52.72115489651
247PhosphorylationFGPRDADSDENDKGE
CCCCCCCCCCCCCCC
48.8525849741
260PhosphorylationGEKKNKGTFDGDKLG
CCCCCCCCCCCCCCC
21.8424719451
260 (in isoform 3)Phosphorylation-21.8424719451
265UbiquitinationKGTFDGDKLGDLKEE
CCCCCCCCCCCCCCC
60.9622817900
270UbiquitinationGDKLGDLKEEGDVMD
CCCCCCCCCCCCCCC
59.4621906983
270 (in isoform 1)Ubiquitination-59.4621890473
270 (in isoform 2)Ubiquitination-59.4621890473
276SulfoxidationLKEEGDVMDKTNGLP
CCCCCCCCCCCCCCC
5.3521406390
279PhosphorylationEGDVMDKTNGLPVQN
CCCCCCCCCCCCCCC
30.1928555341
298PhosphorylationDVKDFSRTPGNCQNS
CHHHHCCCCCCCCCC
34.0625850435
305PhosphorylationTPGNCQNSANEVDLL
CCCCCCCCCCCCCCC
13.4425850435
514PhosphorylationGASQRPLTPNQNQQG
CCCCCCCCCCCCCCC
23.9121552520
580MethylationNGLGAPVRLVAPAPV
CCCCCCCEEEECCCE
23.5381452721
659UbiquitinationNSNSQSSSLFSQGSA
CCCCCCCCCCCCCCC
38.3921890473
672PhosphorylationSAQPANTSLGFGSSS
CCCCCCCCCCCCCCC
26.7126657352
677PhosphorylationNTSLGFGSSSSLGAT
CCCCCCCCCCHHHHH
25.4526074081
678PhosphorylationTSLGFGSSSSLGATL
CCCCCCCCCHHHHHH
25.0726074081
679PhosphorylationSLGFGSSSSLGATLG
CCCCCCCCHHHHHHH
31.1426074081
680PhosphorylationLGFGSSSSLGATLGS
CCCCCCCHHHHHHHH
32.5426074081
687PhosphorylationSLGATLGSALGGFGT
HHHHHHHHHHCCCCE
24.3526074081
694PhosphorylationSALGGFGTAVANSNT
HHHCCCCEEECCCCC
18.7226074081
699PhosphorylationFGTAVANSNTGSGSR
CCEEECCCCCCCCCC
26.4926074081
701PhosphorylationTAVANSNTGSGSRRD
EEECCCCCCCCCCCC
32.3326074081
703PhosphorylationVANSNTGSGSRRDSL
ECCCCCCCCCCCCCC
31.4026074081
705PhosphorylationNSNTGSGSRRDSLTG
CCCCCCCCCCCCCCC
26.3226074081
709PhosphorylationGSGSRRDSLTGSSDL
CCCCCCCCCCCCHHH
26.4829255136
709 (in isoform 3)Phosphorylation-26.4824719451
711PhosphorylationGSRRDSLTGSSDLYK
CCCCCCCCCCHHHHH
38.6829255136
713PhosphorylationRRDSLTGSSDLYKRT
CCCCCCCCHHHHHHC
18.5529255136
714PhosphorylationRDSLTGSSDLYKRTS
CCCCCCCHHHHHHCC
32.7420164059
717PhosphorylationLTGSSDLYKRTSSSL
CCCCHHHHHHCCCCC
11.9223927012
7182-HydroxyisobutyrylationTGSSDLYKRTSSSLT
CCCHHHHHHCCCCCC
57.40-
718UbiquitinationTGSSDLYKRTSSSLT
CCCHHHHHHCCCCCC
57.4022817900
718 (in isoform 1)Ubiquitination-57.4021890473
719 (in isoform 2)Ubiquitination-26.7021890473
719UbiquitinationGSSDLYKRTSSSLTP
CCHHHHHHCCCCCCC
26.7021890473
735AcetylationGHSFYNGLSFSSSPG
CCCCCCCCCCCCCCC
4.10-
735UbiquitinationGHSFYNGLSFSSSPG
CCCCCCCCCCCCCCC
4.1021890473
736PhosphorylationHSFYNGLSFSSSPGP
CCCCCCCCCCCCCCC
25.2022798277
738PhosphorylationFYNGLSFSSSPGPVG
CCCCCCCCCCCCCCC
26.9126074081
739PhosphorylationYNGLSFSSSPGPVGM
CCCCCCCCCCCCCCC
38.2426074081
740PhosphorylationNGLSFSSSPGPVGMP
CCCCCCCCCCCCCCC
32.4526074081
750PhosphorylationPVGMPLPSQGPGHSQ
CCCCCCCCCCCCCCC
56.2926074081
756PhosphorylationPSQGPGHSQTPPPSL
CCCCCCCCCCCCCCC
41.4826074081
758PhosphorylationQGPGHSQTPPPSLSS
CCCCCCCCCCCCCCC
40.5526074081
762PhosphorylationHSQTPPPSLSSHGSS
CCCCCCCCCCCCCCC
46.8126074081
764PhosphorylationQTPPPSLSSHGSSSS
CCCCCCCCCCCCCCC
25.3226074081
765PhosphorylationTPPPSLSSHGSSSSL
CCCCCCCCCCCCCCC
36.8426074081
768PhosphorylationPSLSSHGSSSSLNLG
CCCCCCCCCCCCCCC
22.9426074081
769PhosphorylationSLSSHGSSSSLNLGG
CCCCCCCCCCCCCCC
28.6526074081
770PhosphorylationLSSHGSSSSLNLGGL
CCCCCCCCCCCCCCC
40.3126074081
771PhosphorylationSSHGSSSSLNLGGLT
CCCCCCCCCCCCCCC
24.1926074081
784PhosphorylationLTNGSGRYISAAPGA
CCCCCCCEEECCCCC
11.6228152594
786PhosphorylationNGSGRYISAAPGAEA
CCCCCEEECCCCCCE
14.9428442448
794AcetylationAAPGAEAKYRSASSA
CCCCCCEECCCCCCC
32.4723236377
794UbiquitinationAAPGAEAKYRSASSA
CCCCCCEECCCCCCC
32.4727667366
794 (in isoform 1)Ubiquitination-32.4721890473
795PhosphorylationAPGAEAKYRSASSAS
CCCCCEECCCCCCCH
19.4929396449
795 (in isoform 2)Ubiquitination-19.4921890473
795UbiquitinationAPGAEAKYRSASSAS
CCCCCEECCCCCCCH
19.4921890473
796MethylationPGAEAKYRSASSASS
CCCCEECCCCCCCHH
25.6624129315
797PhosphorylationGAEAKYRSASSASSL
CCCEECCCCCCCHHH
29.4320044836
797 (in isoform 3)Phosphorylation-29.4324719451
799PhosphorylationEAKYRSASSASSLFS
CEECCCCCCCHHHCC
27.9021712546
800PhosphorylationAKYRSASSASSLFSP
EECCCCCCCHHHCCC
31.7021712546
800 (in isoform 3)Phosphorylation-31.7027251275
802PhosphorylationYRSASSASSLFSPSS
CCCCCCCHHHCCCCH
29.5330183078
803PhosphorylationRSASSASSLFSPSST
CCCCCCHHHCCCCHH
32.9021712546
806PhosphorylationSSASSLFSPSSTLFS
CCCHHHCCCCHHHCC
29.2123401153
806 (in isoform 3)Phosphorylation-29.2124719451
808PhosphorylationASSLFSPSSTLFSSS
CHHHCCCCHHHCCCC
34.4522617229
809PhosphorylationSSLFSPSSTLFSSSR
HHHCCCCHHHCCCCC
32.3030183078
809 (in isoform 3)Phosphorylation-32.3024719451
810UbiquitinationSLFSPSSTLFSSSRL
HHCCCCHHHCCCCCH
35.84-
810PhosphorylationSLFSPSSTLFSSSRL
HHCCCCHHHCCCCCH
35.8421712546
813PhosphorylationSPSSTLFSSSRLRYG
CCCHHHCCCCCHHCC
30.4328450419
814PhosphorylationPSSTLFSSSRLRYGM
CCHHHCCCCCHHCCC
16.4920044836
815PhosphorylationSSTLFSSSRLRYGMS
CHHHCCCCCHHCCCC
33.8529396449
818MethylationLFSSSRLRYGMSDVM
HCCCCCHHCCCCCCC
25.5058856365
822PhosphorylationSRLRYGMSDVMPSGR
CCHHCCCCCCCCCCH
23.7721572425
855UbiquitinationEIAGHIMEFSQDQHG
HHHHHHHHHCCCCCC
41.36-
869UbiquitinationGSRFIQLKLERATPA
CCCEEEEHHHCCCHH
31.74-
881UbiquitinationTPAERQLVFNEILQA
CHHHHHHHHHHHHHH
3.51-
904UbiquitinationFGNYVIQKFFEFGSL
HHHHHHHHHHHCCCH
40.68-
907UbiquitinationYVIQKFFEFGSLEQK
HHHHHHHHCCCHHHH
52.83-
914UbiquitinationEFGSLEQKLALAERI
HCCCHHHHHHHHHHH
26.7622817900
914 (in isoform 1)Ubiquitination-26.7621890473
915 (in isoform 2)Ubiquitination-4.7621890473
917UbiquitinationSLEQKLALAERIRGH
CHHHHHHHHHHHHHH
8.03-
940UbiquitinationYGCRVIQKALEFIPS
HHHHHHHHHHHHCCH
43.7622817900
941 (in isoform 2)Ubiquitination-8.9221890473
963AcetylationELDGHVLKCVKDQNG
HHCCEEEEEEECCCC
35.5725953088
963UbiquitinationELDGHVLKCVKDQNG
HHCCEEEEEEECCCC
35.5733845483
965UbiquitinationDGHVLKCVKDQNGNH
CCEEEEEEECCCCCC
7.9727667366
966UbiquitinationGHVLKCVKDQNGNHV
CEEEEEEECCCCCCH
64.1729967540
968UbiquitinationVLKCVKDQNGNHVVQ
EEEEEECCCCCCHHH
54.7529967540
976UbiquitinationNGNHVVQKCIECVQP
CCCCHHHHHHHHHCC
26.10-
1017UbiquitinationIQRILEHCLPDQTLP
HHHHHHHHCCCCCHH
4.27-
1025UbiquitinationLPDQTLPILEELHQH
CCCCCHHHHHHHHHH
9.46-
1058AcetylationEHGRPEDKSKIVAEI
HCCCCCCHHHHEEEE
52.5718603697
1068UbiquitinationIVAEIRGNVLVLSQH
HEEEEECCEEEEECC
17.69-
1073PhosphorylationRGNVLVLSQHKFASN
ECCEEEEECCHHHHC
23.8227251275
1075 (in isoform 3)Phosphorylation-24.6727251275
1076AcetylationVLVLSQHKFASNVVE
EEEEECCHHHHCHHH
34.6826051181
1076UbiquitinationVLVLSQHKFASNVVE
EEEEECCHHHHCHHH
34.68-
1084UbiquitinationFASNVVEKCVTHASR
HHHCHHHHHHHHHCC
23.5421906983
1084 (in isoform 1)Ubiquitination-23.5421890473
1086UbiquitinationSNVVEKCVTHASRTE
HCHHHHHHHHHCCCC
6.9622817900
1087 (in isoform 2)Ubiquitination-22.6121890473
1102GlutathionylationAVLIDEVCTMNDGPH
EEEEEEEECCCCCCC
2.5522555962
1104AcetylationLIDEVCTMNDGPHSA
EEEEEECCCCCCCHH
3.49-
1104UbiquitinationLIDEVCTMNDGPHSA
EEEEEECCCCCCCHH
3.49-
1107UbiquitinationEVCTMNDGPHSALYT
EEECCCCCCCHHHHH
19.47-
1113PhosphorylationDGPHSALYTMMKDQY
CCCCHHHHHHHHHHH
7.7220090780
1120PhosphorylationYTMMKDQYANYVVQK
HHHHHHHHHHHHHHH
13.6225884760
1123PhosphorylationMKDQYANYVVQKMID
HHHHHHHHHHHHHHH
8.2025884760
1127UbiquitinationYANYVVQKMIDVAEP
HHHHHHHHHHHCCCC
26.6422817900
1127 (in isoform 1)Ubiquitination-26.6421890473
1129UbiquitinationNYVVQKMIDVAEPGQ
HHHHHHHHHCCCCCC
5.0622817900
1130 (in isoform 2)Ubiquitination-30.0321890473
1150PhosphorylationKIRPHIATLRKYTYG
ECHHHHHHHHHHHHH
26.8830576142
1152 (in isoform 3)Phosphorylation-26.1127251275
1153UbiquitinationPHIATLRKYTYGKHI
HHHHHHHHHHHHHHH
45.0927667366
1154PhosphorylationHIATLRKYTYGKHIL
HHHHHHHHHHHHHHH
9.9618083107
1155UbiquitinationIATLRKYTYGKHILA
HHHHHHHHHHHHHHH
28.9127667366
1158AcetylationLRKYTYGKHILAKLE
HHHHHHHHHHHHHHH
19.6325953088
1158UbiquitinationLRKYTYGKHILAKLE
HHHHHHHHHHHHHHH
19.6329967540
1160UbiquitinationKYTYGKHILAKLEKY
HHHHHHHHHHHHHHH
4.5729967540
1163AcetylationYGKHILAKLEKYYMK
HHHHHHHHHHHHHHH
54.4523236377
1163UbiquitinationYGKHILAKLEKYYMK
HHHHHHHHHHHHHHH
54.4529967540
1165UbiquitinationKHILAKLEKYYMKNG
HHHHHHHHHHHHHHC
38.0029967540
1166UbiquitinationHILAKLEKYYMKNGV
HHHHHHHHHHHHHCC
52.71-
1168PhosphorylationLAKLEKYYMKNGVDL
HHHHHHHHHHHCCCC
16.8118083107

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 PUM1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
714SPhosphorylation

20818387
714SPhosphorylation

20818387

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 PUM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PUR6_HUMANPAICSphysical
22939629
VP26A_HUMANVPS26Aphysical
22939629
SPS1_HUMANSEPHS1physical
22939629
SPS1_HUMANSEPHS1physical
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
There are no disease associations of PTM sites.
Regulatory Network of PUM1_HUMAN

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Related Literatures of Post-Translational Modification
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-75; SER-209; SER-709 ANDSER-806, 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 SER-19; SER-75; SER-209 ANDSER-709, 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-709, AND MASSSPECTROMETRY.
"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-714, 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-209, AND MASSSPECTROMETRY.

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