WAPL_HUMAN - dbPTM
WAPL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WAPL_HUMAN
UniProt AC Q7Z5K2
Protein Name Wings apart-like protein homolog
Gene Name WAPL {ECO:0000312|HGNC:HGNC:23293}
Organism Homo sapiens (Human).
Sequence Length 1190
Subcellular Localization Isoform 2: Nucleus.
Nucleus. Chromosome. Cytoplasm. Associates with chromatin through the cohesin complex during interphase. Released in the cytoplasm from nuclear envelope breakdown until anaphase, it reaccumulates in nucleus at telophase.
Protein Description Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair..
Protein Sequence MTSRFGKTYSRKGGNGSSKFDEVFSNKRTTLSTKWGETTFMAKLGQKRPNFKPDIQEIPKKPKVEEESTGDPFGFDSDDESLPVSSKNLAQVKCSSYSESSEAAQLEEVTSVLEANSKISHVVVEDTVVSDKCFPLEDTLLGKEKSTNRIVEDDASISSCNKLITSDKVENFHEEHEKNSHHIHKNADDSTKKPNAETTVASEIKETNDTWNSQFGKRPESPSEISPIKGSVRTGLFEWDNDFEDIRSEDCILSLDSDPLLEMKDDDFKNRLENLNEAIEEDIVQSVLRPTNCRTYCRANKTKSSQGASNFDKLMDGTSQALAKANSESSKDGLNQAKKGGVSCGTSFRGTVGRTRDYTVLHPSCLSVCNVTIQDTMERSMDEFTASTPADLGEAGRLRKKADIATSKTTTRFRPSNTKSKKDVKLEFFGFEDHETGGDEGGSGSSNYKIKYFGFDDLSESEDDEDDDCQVERKTSKKRTKTAPSPSLQPPPESNDNSQDSQSGTNNAENLDFTEDLPGVPESVKKPINKQGDKSKENTRKIFSGPKRSPTKAVYNARHWNHPDSEELPGPPVVKPQSVTVRLSSKEPNQKDDGVFKAPAPPSKVIKTVTIPTQPYQDIVTALKCRREDKELYTVVQHVKHFNDVVEFGENQEFTDDIEYLLSGLKSTQPLNTRCLSVISLATKCAMPSFRMHLRAHGMVAMVFKTLDDSQHHQNLSLCTAALMYILSRDRLNMDLDRASLDLMIRLLELEQDASSAKLLNEKDMNKIKEKIRRLCETVHNKHLDLENITTGHLAMETLLSLTSKRAGDWFKEELRLLGGLDHIVDKVKECVDHLSRDEDEEKLVASLWGAERCLRVLESVTVHNPENQSYLIAYKDSQLIVSSAKALQHCEELIQQYNRAEDSICLADSKPLPHQNVTNHVGKAVEDCMRAIIGVLLNLTNDNEWGSTKTGEQDGLIGTALNCVLQVPKYLPQEQRFDIRVLGLGLLINLVEYSARNRHCLVNMETSCSFDSSICSGEGDDSLRIGGQVHAVQALVQLFLERERAAQLAESKTDELIKDAPTTQHDKSGEWQETSGEIQWVSTEKTDGTEEKHKKEEEDEELDLNKALQHAGKHMEDCIVASYTALLLGCLCQESPINVTTVREYLPEGDFSIMTEMLKKFLSFMNLTCAVGTTGQKSISRVIEYLEHC
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
7Acetylation-MTSRFGKTYSRKGG
-CCCCCCCCCCCCCC
41.3926051181
8PhosphorylationMTSRFGKTYSRKGGN
CCCCCCCCCCCCCCC
27.4026074081
8 (in isoform 2)Phosphorylation-27.4024043423
8 (in isoform 3)Phosphorylation-27.4024043423
9PhosphorylationTSRFGKTYSRKGGNG
CCCCCCCCCCCCCCC
15.2326074081
10PhosphorylationSRFGKTYSRKGGNGS
CCCCCCCCCCCCCCC
32.5226074081
12AcetylationFGKTYSRKGGNGSSK
CCCCCCCCCCCCCCC
66.297934579
12 (in isoform 2)Phosphorylation-66.2924043423
12 (in isoform 3)Phosphorylation-66.2924043423
17PhosphorylationSRKGGNGSSKFDEVF
CCCCCCCCCCHHHHH
34.0626074081
18PhosphorylationRKGGNGSSKFDEVFS
CCCCCCCCCHHHHHC
38.4526074081
19AcetylationKGGNGSSKFDEVFSN
CCCCCCCCHHHHHCC
59.547934589
27AcetylationFDEVFSNKRTTLSTK
HHHHHCCCCEEECCC
50.347934599
27UbiquitinationFDEVFSNKRTTLSTK
HHHHHCCCCEEECCC
50.34-
34AcetylationKRTTLSTKWGETTFM
CCEEECCCCCHHHHH
50.2325953088
38PhosphorylationLSTKWGETTFMAKLG
ECCCCCHHHHHHHCC
22.7728555341
52AcetylationGQKRPNFKPDIQEIP
CCCCCCCCCCHHHCC
48.7121339330
68PhosphorylationKPKVEEESTGDPFGF
CCCCCCCCCCCCCCC
40.7523927012
69PhosphorylationPKVEEESTGDPFGFD
CCCCCCCCCCCCCCC
49.2130266825
77PhosphorylationGDPFGFDSDDESLPV
CCCCCCCCCCCCCCC
44.7029255136
81PhosphorylationGFDSDDESLPVSSKN
CCCCCCCCCCCCCCC
44.9930266825
85PhosphorylationDDESLPVSSKNLAQV
CCCCCCCCCCCEEEE
33.3923927012
86PhosphorylationDESLPVSSKNLAQVK
CCCCCCCCCCEEEEE
26.2923927012
93UbiquitinationSKNLAQVKCSSYSES
CCCEEEEECCCCCCC
19.13-
95PhosphorylationNLAQVKCSSYSESSE
CEEEEECCCCCCCCH
26.9629116813
96PhosphorylationLAQVKCSSYSESSEA
EEEEECCCCCCCCHH
41.9926074081
97PhosphorylationAQVKCSSYSESSEAA
EEEECCCCCCCCHHH
10.5226074081
98PhosphorylationQVKCSSYSESSEAAQ
EEECCCCCCCCHHHH
32.7126074081
100PhosphorylationKCSSYSESSEAAQLE
ECCCCCCCCHHHHHH
27.7726074081
101PhosphorylationCSSYSESSEAAQLEE
CCCCCCCCHHHHHHH
27.4826074081
120PhosphorylationLEANSKISHVVVEDT
HHHCCCCCEEEEECC
17.6119664995
127PhosphorylationSHVVVEDTVVSDKCF
CEEEEECCEEECCEE
14.8625849741
130PhosphorylationVVEDTVVSDKCFPLE
EEECCEEECCEEEHH
27.3225849741
132AcetylationEDTVVSDKCFPLEDT
ECCEEECCEEEHHHH
30.2126051181
143AcetylationLEDTLLGKEKSTNRI
HHHHHCCCCCCCCCC
63.0426051181
146PhosphorylationTLLGKEKSTNRIVED
HHCCCCCCCCCCCCC
31.8229759185
147PhosphorylationLLGKEKSTNRIVEDD
HCCCCCCCCCCCCCC
39.3129759185
156PhosphorylationRIVEDDASISSCNKL
CCCCCCCCHHHHCCC
29.9623401153
158PhosphorylationVEDDASISSCNKLIT
CCCCCCHHHHCCCCC
26.7525159151
159PhosphorylationEDDASISSCNKLITS
CCCCCHHHHCCCCCC
21.7520164059
162 (in isoform 3)Phosphorylation-45.6621406692
162AcetylationASISSCNKLITSDKV
CCHHHHCCCCCCHHH
45.6625953088
165PhosphorylationSSCNKLITSDKVENF
HHHCCCCCCHHHHHH
41.1128555341
166 (in isoform 3)Phosphorylation-28.5721406692
166PhosphorylationSCNKLITSDKVENFH
HHCCCCCCHHHHHHH
28.5728555341
168AcetylationNKLITSDKVENFHEE
CCCCCCHHHHHHHHH
51.7419608861
180PhosphorylationHEEHEKNSHHIHKNA
HHHHHHCCCCCCCCC
27.7524719451
190PhosphorylationIHKNADDSTKKPNAE
CCCCCCCCCCCCCCC
42.5526055452
191PhosphorylationHKNADDSTKKPNAET
CCCCCCCCCCCCCCC
50.5121712546
199PhosphorylationKKPNAETTVASEIKE
CCCCCCCHHHHHHHH
12.9428555341
202PhosphorylationNAETTVASEIKETND
CCCCHHHHHHHHHCC
35.2025159151
205UbiquitinationTTVASEIKETNDTWN
CHHHHHHHHHCCHHH
55.20-
207PhosphorylationVASEIKETNDTWNSQ
HHHHHHHHCCHHHHC
33.1326074081
210PhosphorylationEIKETNDTWNSQFGK
HHHHHCCHHHHCCCC
28.7226074081
213PhosphorylationETNDTWNSQFGKRPE
HHCCHHHHCCCCCCC
20.6022115753
221PhosphorylationQFGKRPESPSEISPI
CCCCCCCCHHHCCCC
36.0929255136
223PhosphorylationGKRPESPSEISPIKG
CCCCCCHHHCCCCCC
57.7622167270
226PhosphorylationPESPSEISPIKGSVR
CCCHHHCCCCCCCCC
19.2729255136
231PhosphorylationEISPIKGSVRTGLFE
HCCCCCCCCCCCCCC
11.9223927012
234PhosphorylationPIKGSVRTGLFEWDN
CCCCCCCCCCCCCCC
35.7626074081
254PhosphorylationRSEDCILSLDSDPLL
CCCCEEEECCCCCCH
15.3723663014
257PhosphorylationDCILSLDSDPLLEMK
CEEEECCCCCCHHCC
46.5523663014
286PhosphorylationIEEDIVQSVLRPTNC
HHHHHHHHHHCCCCH
16.5422067460
291PhosphorylationVQSVLRPTNCRTYCR
HHHHHCCCCHHHHHH
40.2822067460
293GlutathionylationSVLRPTNCRTYCRAN
HHHCCCCHHHHHHCC
3.6522555962
302PhosphorylationTYCRANKTKSSQGAS
HHHHCCCCCCCCCCC
35.6524719451
303UbiquitinationYCRANKTKSSQGASN
HHHCCCCCCCCCCCC
50.12-
304PhosphorylationCRANKTKSSQGASNF
HHCCCCCCCCCCCCH
32.88-
305PhosphorylationRANKTKSSQGASNFD
HCCCCCCCCCCCCHH
33.9028985074
306 (in isoform 3)Phosphorylation-59.5721406692
308 (in isoform 3)Phosphorylation-8.1521406692
309PhosphorylationTKSSQGASNFDKLMD
CCCCCCCCCHHHHHC
44.8730387612
311 (in isoform 3)Phosphorylation-8.9721406692
313UbiquitinationQGASNFDKLMDGTSQ
CCCCCHHHHHCHHHH
41.39-
313AcetylationQGASNFDKLMDGTSQ
CCCCCHHHHHCHHHH
41.3925953088
315SulfoxidationASNFDKLMDGTSQAL
CCCHHHHHCHHHHHH
5.7121406390
318PhosphorylationFDKLMDGTSQALAKA
HHHHHCHHHHHHHHH
17.2522468782
319PhosphorylationDKLMDGTSQALAKAN
HHHHCHHHHHHHHHC
20.9823403867
327PhosphorylationQALAKANSESSKDGL
HHHHHHCCCCCHHHH
43.6522468782
329PhosphorylationLAKANSESSKDGLNQ
HHHHCCCCCHHHHHH
42.3723403867
330PhosphorylationAKANSESSKDGLNQA
HHHCCCCCHHHHHHH
30.6223403867
343PhosphorylationQAKKGGVSCGTSFRG
HHHHCCCCCCCCCCC
15.3128450419
346PhosphorylationKGGVSCGTSFRGTVG
HCCCCCCCCCCCCCC
29.0828450419
347PhosphorylationGGVSCGTSFRGTVGR
CCCCCCCCCCCCCCC
9.7623401153
351PhosphorylationCGTSFRGTVGRTRDY
CCCCCCCCCCCCCCE
18.6126074081
355PhosphorylationFRGTVGRTRDYTVLH
CCCCCCCCCCEEEEC
23.20-
359PhosphorylationVGRTRDYTVLHPSCL
CCCCCCEEEECHHHH
22.38-
380PhosphorylationIQDTMERSMDEFTAS
HHHHHHHHHHHHHCC
19.7830266825
385PhosphorylationERSMDEFTASTPADL
HHHHHHHHCCCCHHH
20.0430266825
387PhosphorylationSMDEFTASTPADLGE
HHHHHHCCCCHHHHH
31.6930266825
388PhosphorylationMDEFTASTPADLGEA
HHHHHCCCCHHHHHH
21.7430266825
408UbiquitinationKADIATSKTTTRFRP
HHCCCCCCCCCCCCC
45.60-
420PhosphorylationFRPSNTKSKKDVKLE
CCCCCCCCCCCEEEE
42.7922067460
436PhosphorylationFGFEDHETGGDEGGS
EEECCCCCCCCCCCC
42.9429523821
443PhosphorylationTGGDEGGSGSSNYKI
CCCCCCCCCCCCCEE
46.4925159151
445PhosphorylationGDEGGSGSSNYKIKY
CCCCCCCCCCCEEEE
19.6722199227
446PhosphorylationDEGGSGSSNYKIKYF
CCCCCCCCCCEEEEE
47.9422199227
448PhosphorylationGGSGSSNYKIKYFGF
CCCCCCCCEEEEEEE
18.9522199227
452PhosphorylationSSNYKIKYFGFDDLS
CCCCEEEEEEECCCC
16.6526503892
459PhosphorylationYFGFDDLSESEDDED
EEEECCCCCCCCCCC
46.1823927012
461PhosphorylationGFDDLSESEDDEDDD
EECCCCCCCCCCCCC
42.8423927012
482PhosphorylationTSKKRTKTAPSPSLQ
HCCCCCCCCCCCCCC
43.0928985074
485PhosphorylationKRTKTAPSPSLQPPP
CCCCCCCCCCCCCCC
25.3425137130
487PhosphorylationTKTAPSPSLQPPPES
CCCCCCCCCCCCCCC
43.9330576142
494PhosphorylationSLQPPPESNDNSQDS
CCCCCCCCCCCCCCC
56.0827251275
498PhosphorylationPPESNDNSQDSQSGT
CCCCCCCCCCCCCCC
37.9227251275
501PhosphorylationSNDNSQDSQSGTNNA
CCCCCCCCCCCCCCH
20.7127251275
503PhosphorylationDNSQDSQSGTNNAEN
CCCCCCCCCCCCHHH
52.0825137130
505PhosphorylationSQDSQSGTNNAENLD
CCCCCCCCCCHHHCC
30.4625137130
514PhosphorylationNAENLDFTEDLPGVP
CHHHCCCCCCCCCCC
28.4020873877
523PhosphorylationDLPGVPESVKKPINK
CCCCCCHHHCCCCCC
32.9220873877
541MethylationKSKENTRKIFSGPKR
CCCCCCCHHHCCCCC
46.17116253061
544PhosphorylationENTRKIFSGPKRSPT
CCCCHHHCCCCCCCC
58.6223403867
544 (in isoform 3)Phosphorylation-58.6221406692
546 (in isoform 3)Phosphorylation-27.9121406692
549PhosphorylationIFSGPKRSPTKAVYN
HHCCCCCCCCHHHHC
42.9425159151
551PhosphorylationSGPKRSPTKAVYNAR
CCCCCCCCHHHHCCC
32.6523403867
555PhosphorylationRSPTKAVYNARHWNH
CCCCHHHHCCCCCCC
14.1524719451
580PhosphorylationVVKPQSVTVRLSSKE
CCCCCEEEEEECCCC
12.7324719451
597UbiquitinationQKDDGVFKAPAPPSK
CCCCCCEECCCCCCC
51.56-
603PhosphorylationFKAPAPPSKVIKTVT
EECCCCCCCEEEEEE
38.2029743597
604AcetylationKAPAPPSKVIKTVTI
ECCCCCCCEEEEEEE
54.4719608861
604UbiquitinationKAPAPPSKVIKTVTI
ECCCCCCCEEEEEEE
54.47-
608PhosphorylationPPSKVIKTVTIPTQP
CCCCEEEEEEECCCC
16.2620068231
610PhosphorylationSKVIKTVTIPTQPYQ
CCEEEEEEECCCCHH
26.8620068231
613PhosphorylationIKTVTIPTQPYQDIV
EEEEEECCCCHHHHH
38.0220068231
616PhosphorylationVTIPTQPYQDIVTAL
EEECCCCHHHHHHHH
14.7028796482
621PhosphorylationQPYQDIVTALKCRRE
CCHHHHHHHHHCCCC
26.9720068231
624UbiquitinationQDIVTALKCRREDKE
HHHHHHHHCCCCCHH
24.19-
629 (in isoform 3)Phosphorylation-48.1721406692
630AcetylationLKCRREDKELYTVVQ
HHCCCCCHHHHHHHH
44.8826051181
633PhosphorylationRREDKELYTVVQHVK
CCCCHHHHHHHHHHH
9.8928796482
634PhosphorylationREDKELYTVVQHVKH
CCCHHHHHHHHHHHH
27.1628796482
680PhosphorylationTRCLSVISLATKCAM
HHHHHHHHHHHHCCC
15.1429083192
683PhosphorylationLSVISLATKCAMPSF
HHHHHHHHHCCCCHH
31.7629083192
701 (in isoform 3)Phosphorylation-4.5927642862
718 (in isoform 3)Phosphorylation-3.2027642862
734SulfoxidationLSRDRLNMDLDRASL
HHHHCCCCCCCHHHH
6.8321406390
740PhosphorylationNMDLDRASLDLMIRL
CCCCCHHHHHHHHHH
24.2621955146
744SulfoxidationDRASLDLMIRLLELE
CHHHHHHHHHHHHHH
1.3521406390
758AcetylationEQDASSAKLLNEKDM
HCCHHHHHHCCHHHH
56.2925953088
763AcetylationSAKLLNEKDMNKIKE
HHHHCCHHHHHHHHH
62.2923749302
763UbiquitinationSAKLLNEKDMNKIKE
HHHHCCHHHHHHHHH
62.29-
790PhosphorylationHLDLENITTGHLAME
CCCCCCCCHHHHHHH
38.0026552605
791PhosphorylationLDLENITTGHLAMET
CCCCCCCHHHHHHHH
20.8526552605
798PhosphorylationTGHLAMETLLSLTSK
HHHHHHHHHHHHHHH
21.6626552605
801PhosphorylationLAMETLLSLTSKRAG
HHHHHHHHHHHHHCC
32.4926552605
803PhosphorylationMETLLSLTSKRAGDW
HHHHHHHHHHHCCHH
28.9126552605
804PhosphorylationETLLSLTSKRAGDWF
HHHHHHHHHHCCHHH
25.9926552605
812UbiquitinationKRAGDWFKEELRLLG
HHCCHHHHHHHHHCC
46.13-
827UbiquitinationGLDHIVDKVKECVDH
CHHHHHHHHHHHHHH
44.29-
829UbiquitinationDHIVDKVKECVDHLS
HHHHHHHHHHHHHHC
51.65-
843UbiquitinationSRDEDEEKLVASLWG
CCCCCHHHHHHHHHH
46.33-
848 (in isoform 3)Ubiquitination-3.36-
886UbiquitinationQLIVSSAKALQHCEE
HHHHCHHHHHHHHHH
52.13-
904PhosphorylationQYNRAEDSICLADSK
HHHHCCCCEEECCCC
13.5030266825
910PhosphorylationDSICLADSKPLPHQN
CCEEECCCCCCCCCC
30.4824732914
911UbiquitinationSICLADSKPLPHQNV
CEEECCCCCCCCCCC
51.63-
911AcetylationSICLADSKPLPHQNV
CEEECCCCCCCCCCC
51.6326051181
919PhosphorylationPLPHQNVTNHVGKAV
CCCCCCCCHHHHHHH
27.4424732914
964GlutathionylationLIGTALNCVLQVPKY
CHHHHHHHHHHCCCC
3.1722555962
1017PhosphorylationSFDSSICSGEGDDSL
ECCCHHCCCCCCCCE
37.9028985074
1059UbiquitinationSKTDELIKDAPTTQH
HCCHHHHHCCCCCCC
61.53-
1059AcetylationSKTDELIKDAPTTQH
HCCHHHHHCCCCCCC
61.5326051181
1063PhosphorylationELIKDAPTTQHDKSG
HHHHCCCCCCCCCCC
40.5923663014
1064PhosphorylationLIKDAPTTQHDKSGE
HHHCCCCCCCCCCCC
23.8923663014
1069PhosphorylationPTTQHDKSGEWQETS
CCCCCCCCCCCEECC
48.2625159151
1075PhosphorylationKSGEWQETSGEIQWV
CCCCCEECCCEEEEE
27.2525159151
1076PhosphorylationSGEWQETSGEIQWVS
CCCCEECCCEEEEEE
33.4125159151
1107UbiquitinationDEELDLNKALQHAGK
HHHCHHHHHHHHHHH
58.74-
1146PhosphorylationNVTTVREYLPEGDFS
CEEEHHHHCCCCCHH
19.5920068231
1153PhosphorylationYLPEGDFSIMTEMLK
HCCCCCHHHHHHHHH
19.0520068231
1156PhosphorylationEGDFSIMTEMLKKFL
CCCHHHHHHHHHHHH
19.3020068231
1164PhosphorylationEMLKKFLSFMNLTCA
HHHHHHHHHCCCCCC
26.1120860994
1169PhosphorylationFLSFMNLTCAVGTTG
HHHHCCCCCCCCCCC
8.0725219547
1174PhosphorylationNLTCAVGTTGQKSIS
CCCCCCCCCCCHHHH
22.5825219547
1175PhosphorylationLTCAVGTTGQKSISR
CCCCCCCCCCHHHHH
31.5225219547
1178UbiquitinationAVGTTGQKSISRVIE
CCCCCCCHHHHHHHH
51.61-
1263 (in isoform 3)Ubiquitination--

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 WAPL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WAPL_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 WAPL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDS5A_HUMANPDS5Aphysical
20360068
RAD21_HUMANRAD21physical
20360068
STAG2_HUMANSTAG2physical
20360068
STAG1_HUMANSTAG1physical
20360068
SMC1A_HUMANSMC1Aphysical
20360068
SMC3_HUMANSMC3physical
20360068
PDS5B_HUMANPDS5Bphysical
20360068
WAPL_HUMANWAPALphysical
20360068
PDS5A_HUMANPDS5Aphysical
17113138
PDS5B_HUMANPDS5Bphysical
17113138
SMC3_HUMANSMC3physical
17113138
STAG2_HUMANSTAG2physical
17113138
SMC1A_HUMANSMC1Aphysical
17113138
RAD21_HUMANRAD21physical
17113138
STAG1_HUMANSTAG1physical
17113138
RAD21_HUMANRAD21physical
26496610
RL10_HUMANRPL10physical
26496610
TTC3_HUMANTTC3physical
26496610
SMC1A_HUMANSMC1Aphysical
26496610
SMC3_HUMANSMC3physical
26496610
STAG1_HUMANSTAG1physical
26496610
STAG2_HUMANSTAG2physical
26496610
PDS5B_HUMANPDS5Bphysical
26496610
ATG2A_HUMANATG2Aphysical
26496610
PDS5A_HUMANPDS5Aphysical
26496610
E41LB_HUMANEPB41L4Bphysical
26496610
REN3A_HUMANUPF3Aphysical
26496610
ZSWM9_HUMANC19orf68physical
26496610
UBP37_HUMANUSP37physical
26299517

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 WAPL_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-168, 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-77; SER-221; SER-226 ANDSER-380, 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-77 AND SER-221, 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 SER-77 AND SER-221, 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-221; SER-226; SER-459AND SER-461, 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-77; SER-221; SER-223;SER-226; SER-380; SER-459; SER-461 AND SER-904, 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-77; SER-221 AND SER-226,AND MASS SPECTROMETRY.
"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-226, AND MASSSPECTROMETRY.

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