ANKL2_HUMAN - dbPTM
ANKL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANKL2_HUMAN
UniProt AC Q86XL3
Protein Name Ankyrin repeat and LEM domain-containing protein 2
Gene Name ANKLE2
Organism Homo sapiens (Human).
Sequence Length 938
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type III membrane protein .
Protein Description Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of BAF/BANF1 during mitotic exit. Coordinates the control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex. Involved in brain development. [PubMed: 25259927]
Protein Sequence MLWPRLAAAEWAALAWELLGASVLLIAVRWLVRRLGPRPGGLGRSGTPVPPPSAAAAPASGEMTMDALLARLKLLNPDDLREEIVKAGLKCGPITSTTRFIFEKKLAQALLEQGGRLSSFYHHEAGVTALSQDPQRILKPAEGNPTDQAGFSEDRDFGYSVGLNPPEEEAVTSKTCSVPPSDTDTYRAGATASKEPPLYYGVCPVYEDVPARNERIYVYENKKEALQAVKMIKGSRFKAFSTREDAEKFARGICDYFPSPSKTSLPLSPVKTAPLFSNDRLKDGLCLSESETVNKERANSYKNPRTQDLTAKLRKAVEKGEEDTFSDLIWSNPRYLIGSGDNPTIVQEGCRYNVMHVAAKENQASICQLTLDVLENPDFMRLMYPDDDEAMLQKRIRYVVDLYLNTPDKMGYDTPLHFACKFGNADVVNVLSSHHLIVKNSRNKYDKTPEDVICERSKNKSVELKERIREYLKGHYYVPLLRAEETSSPVIGELWSPDQTAEASHVSRYGGSPRDPVLTLRAFAGPLSPAKAEDFRKLWKTPPREKAGFLHHVKKSDPERGFERVGRELAHELGYPWVEYWEFLGCFVDLSSQEGLQRLEEYLTQQEIGKKAQQETGEREASCRDKATTSGSNSISVRAFLDEDDMSLEEIKNRQNAARNNSPPTVGAFGHTRCSAFPLEQEADLIEAAEPGGPHSSRNGLCHPLNHSRTLAGKRPKAPRGEEAHLPPVSDLTVEFDKLNLQNIGRSVSKTPDESTKTKDQILTSRINAVERDLLEPSPADQLGNGHRRTESEMSARIAKMSLSPSSPRHEDQLEVTREPARRLFLFGEEPSKLDQDVLAALECADVDPHQFPAVHRWKSAVLCYSPSDRQSWPSPAVKGRFKSQLPDLSGPHSYSPGRNSVAGSNPAKPGLGSPGRYSPVHGSQLRRMARLAELAAL
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
11UbiquitinationPRLAAAEWAALAWEL
HHHHHHHHHHHHHHH
5.1027667366
28UbiquitinationASVLLIAVRWLVRRL
HHHHHHHHHHHHHHH
3.4124816145
45PhosphorylationRPGGLGRSGTPVPPP
CCCCCCCCCCCCCCC
45.2630278072
47PhosphorylationGGLGRSGTPVPPPSA
CCCCCCCCCCCCCCC
23.5121712546
53PhosphorylationGTPVPPPSAAAAPAS
CCCCCCCCCCCCCCC
35.9922199227
60PhosphorylationSAAAAPASGEMTMDA
CCCCCCCCCCCCHHH
33.9463732289
64PhosphorylationAPASGEMTMDALLAR
CCCCCCCCHHHHHHH
13.9526657352
73UbiquitinationDALLARLKLLNPDDL
HHHHHHHHHCCHHHH
45.4333845483
86UbiquitinationDLREEIVKAGLKCGP
HHHHHHHHCCCCCCC
42.2632015554
90UbiquitinationEIVKAGLKCGPITST
HHHHCCCCCCCCCCC
35.9132015554
97PhosphorylationKCGPITSTTRFIFEK
CCCCCCCCHHHHHHH
17.2246163677
105MalonylationTRFIFEKKLAQALLE
HHHHHHHHHHHHHHH
41.6926320211
105UbiquitinationTRFIFEKKLAQALLE
HHHHHHHHHHHHHHH
41.6929967540
118PhosphorylationLEQGGRLSSFYHHEA
HHCCCCCHHHEECCC
19.6223401153
119PhosphorylationEQGGRLSSFYHHEAG
HCCCCCHHHEECCCC
34.1228796482
121PhosphorylationGGRLSSFYHHEAGVT
CCCCHHHEECCCCCE
12.2928796482
128PhosphorylationYHHEAGVTALSQDPQ
EECCCCCEECCCCHH
22.4423312004
131PhosphorylationEAGVTALSQDPQRIL
CCCCEECCCCHHHHC
30.0323312004
139UbiquitinationQDPQRILKPAEGNPT
CCHHHHCCCCCCCCC
39.5529967540
146PhosphorylationKPAEGNPTDQAGFSE
CCCCCCCCCCCCCCC
44.7528796482
152PhosphorylationPTDQAGFSEDRDFGY
CCCCCCCCCCCCCCC
37.3628796482
159PhosphorylationSEDRDFGYSVGLNPP
CCCCCCCCCCCCCCC
10.5228796482
160PhosphorylationEDRDFGYSVGLNPPE
CCCCCCCCCCCCCCH
15.3028796482
186UbiquitinationPPSDTDTYRAGATAS
CCCCCCCCCCCCCCC
10.9824816145
191PhosphorylationDTYRAGATASKEPPL
CCCCCCCCCCCCCCC
30.4621945579
193PhosphorylationYRAGATASKEPPLYY
CCCCCCCCCCCCCEE
32.9521945579
194UbiquitinationRAGATASKEPPLYYG
CCCCCCCCCCCCEEE
72.3129967540
199PhosphorylationASKEPPLYYGVCPVY
CCCCCCCEEEECCCC
12.1621945579
200PhosphorylationSKEPPLYYGVCPVYE
CCCCCCEEEECCCCC
15.6821945579
206PhosphorylationYYGVCPVYEDVPARN
EEEECCCCCCCCCCC
7.4921945579
215UbiquitinationDVPARNERIYVYENK
CCCCCCCEEEEECCH
29.1424816145
217PhosphorylationPARNERIYVYENKKE
CCCCCEEEEECCHHH
11.8228796482
219PhosphorylationRNERIYVYENKKEAL
CCCEEEEECCHHHHH
9.2328796482
222UbiquitinationRIYVYENKKEALQAV
EEEEECCHHHHHHHH
39.8029967540
223UbiquitinationIYVYENKKEALQAVK
EEEECCHHHHHHHHH
60.8629967540
235PhosphorylationAVKMIKGSRFKAFST
HHHHHHCCCCCCCCC
29.5520068231
238MethylationMIKGSRFKAFSTRED
HHHCCCCCCCCCHHH
47.62-
238UbiquitinationMIKGSRFKAFSTRED
HHHCCCCCCCCCHHH
47.6229967540
242PhosphorylationSRFKAFSTREDAEKF
CCCCCCCCHHHHHHH
31.4620068231
248UbiquitinationSTREDAEKFARGICD
CCHHHHHHHHHCHHH
46.1524816145
256PhosphorylationFARGICDYFPSPSKT
HHHCHHHHCCCCCCC
16.9930266825
259PhosphorylationGICDYFPSPSKTSLP
CHHHHCCCCCCCCCC
31.7219664994
261PhosphorylationCDYFPSPSKTSLPLS
HHHCCCCCCCCCCCC
53.5630266825
262UbiquitinationDYFPSPSKTSLPLSP
HHCCCCCCCCCCCCC
45.5829967540
263PhosphorylationYFPSPSKTSLPLSPV
HCCCCCCCCCCCCCC
39.5730266825
264PhosphorylationFPSPSKTSLPLSPVK
CCCCCCCCCCCCCCC
31.5530266825
268PhosphorylationSKTSLPLSPVKTAPL
CCCCCCCCCCCCCCC
26.2125159151
271UbiquitinationSLPLSPVKTAPLFSN
CCCCCCCCCCCCCCC
42.2129967540
272PhosphorylationLPLSPVKTAPLFSND
CCCCCCCCCCCCCCC
33.4723927012
277PhosphorylationVKTAPLFSNDRLKDG
CCCCCCCCCCCCCCC
45.5721815630
282UbiquitinationLFSNDRLKDGLCLSE
CCCCCCCCCCCCCCC
51.1229967540
295UbiquitinationSESETVNKERANSYK
CCCHHCCHHHHHHCC
44.2129967540
300PhosphorylationVNKERANSYKNPRTQ
CCHHHHHHCCCCHHH
36.1828857561
301PhosphorylationNKERANSYKNPRTQD
CHHHHHHCCCCHHHH
18.0029978859
302AcetylationKERANSYKNPRTQDL
HHHHHHCCCCHHHHH
61.36-
302UbiquitinationKERANSYKNPRTQDL
HHHHHHCCCCHHHHH
61.3629967540
306PhosphorylationNSYKNPRTQDLTAKL
HHCCCCHHHHHHHHH
27.9129978859
312UbiquitinationRTQDLTAKLRKAVEK
HHHHHHHHHHHHHHC
43.5229967540
319UbiquitinationKLRKAVEKGEEDTFS
HHHHHHHCCCCCCHH
66.0929967540
320UbiquitinationLRKAVEKGEEDTFSD
HHHHHHCCCCCCHHH
29.9824816145
332UbiquitinationFSDLIWSNPRYLIGS
HHHHHCCCCCEEECC
15.2922817900
339PhosphorylationNPRYLIGSGDNPTIV
CCCEEECCCCCCHHH
35.6625159151
363UbiquitinationHVAAKENQASICQLT
EHHHHCCCCCEEHHH
37.2624816145
384PhosphorylationPDFMRLMYPDDDEAM
CCCHHHCCCCCHHHH
14.2224043423
394UbiquitinationDDEAMLQKRIRYVVD
CHHHHHHHHHHHHHH
45.9222817900
394 (in isoform 1)Ubiquitination-45.9221906983
394 (in isoform 2)Ubiquitination-45.9221906983
398PhosphorylationMLQKRIRYVVDLYLN
HHHHHHHHHHHHHHC
11.4918452278
403PhosphorylationIRYVVDLYLNTPDKM
HHHHHHHHHCCCCCC
8.0820068231
403UbiquitinationIRYVVDLYLNTPDKM
HHHHHHHHHCCCCCC
8.0824816145
406PhosphorylationVVDLYLNTPDKMGYD
HHHHHHCCCCCCCCC
30.2120068231
439UbiquitinationSSHHLIVKNSRNKYD
HHCEEEEECCCCCCC
42.0629967540
447UbiquitinationNSRNKYDKTPEDVIC
CCCCCCCCCHHHCCC
63.9929967540
448PhosphorylationSRNKYDKTPEDVICE
CCCCCCCCHHHCCCH
29.0721815630
458UbiquitinationDVICERSKNKSVELK
HCCCHHHCCCCHHHH
74.7029967540
460UbiquitinationICERSKNKSVELKER
CCHHHCCCCHHHHHH
60.6629967540
465UbiquitinationKNKSVELKERIREYL
CCCCHHHHHHHHHHH
31.2924816145
472UbiquitinationKERIREYLKGHYYVP
HHHHHHHHCCCCEEE
4.6124816145
473UbiquitinationERIREYLKGHYYVPL
HHHHHHHCCCCEEEE
42.6229967540
476PhosphorylationREYLKGHYYVPLLRA
HHHHCCCCEEEEEEC
18.1528796482
477PhosphorylationEYLKGHYYVPLLRAE
HHHCCCCEEEEEECC
7.0128796482
486PhosphorylationPLLRAEETSSPVIGE
EEEECCCCCCCCCCC
26.4725159151
487PhosphorylationLLRAEETSSPVIGEL
EEECCCCCCCCCCCC
35.6023927012
488PhosphorylationLRAEETSSPVIGELW
EECCCCCCCCCCCCC
30.5223927012
496PhosphorylationPVIGELWSPDQTAEA
CCCCCCCCCCCCCCH
31.0923927012
500PhosphorylationELWSPDQTAEASHVS
CCCCCCCCCCHHHHH
33.5722199227
504PhosphorylationPDQTAEASHVSRYGG
CCCCCCHHHHHHCCC
18.8723927012
507PhosphorylationTAEASHVSRYGGSPR
CCCHHHHHHCCCCCC
17.8622199227
509PhosphorylationEASHVSRYGGSPRDP
CHHHHHHCCCCCCCC
20.5230266825
512PhosphorylationHVSRYGGSPRDPVLT
HHHHCCCCCCCCCCH
16.6430266825
519PhosphorylationSPRDPVLTLRAFAGP
CCCCCCCHHHHHCCC
17.9030266825
528PhosphorylationRAFAGPLSPAKAEDF
HHHCCCCCHHHHHHH
26.4123401153
531UbiquitinationAGPLSPAKAEDFRKL
CCCCCHHHHHHHHHH
56.5529967540
540UbiquitinationEDFRKLWKTPPREKA
HHHHHHCCCCHHHHC
62.6829967540
541PhosphorylationDFRKLWKTPPREKAG
HHHHHCCCCHHHHCC
27.2621949786
546UbiquitinationWKTPPREKAGFLHHV
CCCCHHHHCCCCHHC
55.9029967540
554UbiquitinationAGFLHHVKKSDPERG
CCCCHHCCCCCHHCC
42.0529967540
555AcetylationGFLHHVKKSDPERGF
CCCHHCCCCCHHCCH
60.0320167786
556PhosphorylationFLHHVKKSDPERGFE
CCHHCCCCCHHCCHH
53.3228555341
590UbiquitinationFLGCFVDLSSQEGLQ
HHCCCCCCCCHHHHH
4.4524816145
610UbiquitinationLTQQEIGKKAQQETG
HHHHHHHHHHHHHHC
51.07-
624MethylationGEREASCRDKATTSG
CCCCHHHHHCCCCCC
46.07-
626UbiquitinationREASCRDKATTSGSN
CCHHHHHCCCCCCCC
28.4229967540
629PhosphorylationSCRDKATTSGSNSIS
HHHHCCCCCCCCCEE
35.6325627689
630PhosphorylationCRDKATTSGSNSISV
HHHCCCCCCCCCEEE
35.5525159151
632PhosphorylationDKATTSGSNSISVRA
HCCCCCCCCCEEEEE
27.4625159151
634PhosphorylationATTSGSNSISVRAFL
CCCCCCCCEEEEEEE
20.2425159151
646SulfoxidationAFLDEDDMSLEEIKN
EEECCCCCCHHHHHH
8.3421406390
647PhosphorylationFLDEDDMSLEEIKNR
EECCCCCCHHHHHHH
39.3622199227
652UbiquitinationDMSLEEIKNRQNAAR
CCCHHHHHHHHHHHH
49.7324816145
662PhosphorylationQNAARNNSPPTVGAF
HHHHHCCCCCCHHHC
35.4929255136
665PhosphorylationARNNSPPTVGAFGHT
HHCCCCCCHHHCCCC
34.6530266825
672PhosphorylationTVGAFGHTRCSAFPL
CHHHCCCCCCCCCCH
33.4823927012
675PhosphorylationAFGHTRCSAFPLEQE
HCCCCCCCCCCHHHH
29.6526074081
695UbiquitinationAAEPGGPHSSRNGLC
HCCCCCCCCCCCCCC
41.5024816145
708PhosphorylationLCHPLNHSRTLAGKR
CCCCCCCCCCCCCCC
26.3628555341
730PhosphorylationEAHLPPVSDLTVEFD
CCCCCCCCCEEEEEE
32.4546163655
733PhosphorylationLPPVSDLTVEFDKLN
CCCCCCEEEEEEHHC
23.9946163667
738UbiquitinationDLTVEFDKLNLQNIG
CEEEEEEHHCHHHHC
44.5924816145
747PhosphorylationNLQNIGRSVSKTPDE
CHHHHCCCCCCCCCC
26.0629514088
749PhosphorylationQNIGRSVSKTPDEST
HHHCCCCCCCCCCCC
31.8729514088
751PhosphorylationIGRSVSKTPDESTKT
HCCCCCCCCCCCCCC
28.5928985074
757UbiquitinationKTPDESTKTKDQILT
CCCCCCCCCHHHHHH
63.9624816145
758PhosphorylationTPDESTKTKDQILTS
CCCCCCCCHHHHHHH
39.6846163673
759UbiquitinationPDESTKTKDQILTSR
CCCCCCCHHHHHHHH
49.5529967540
764PhosphorylationKTKDQILTSRINAVE
CCHHHHHHHHHHHHH
20.0024719451
778PhosphorylationERDLLEPSPADQLGN
HHHHCCCCHHHHCCC
24.2825159151
790PhosphorylationLGNGHRRTESEMSAR
CCCCCCCCHHHHHHH
43.7629449344
792PhosphorylationNGHRRTESEMSARIA
CCCCCCHHHHHHHHH
37.6829449344
800UbiquitinationEMSARIAKMSLSPSS
HHHHHHHHHCCCCCC
27.0124816145
802PhosphorylationSARIAKMSLSPSSPR
HHHHHHHCCCCCCCC
25.6225159151
804PhosphorylationRIAKMSLSPSSPRHE
HHHHHCCCCCCCCCH
18.5425159151
806PhosphorylationAKMSLSPSSPRHEDQ
HHHCCCCCCCCCHHH
49.9925159151
807PhosphorylationKMSLSPSSPRHEDQL
HHCCCCCCCCCHHHH
29.3625159151
817PhosphorylationHEDQLEVTREPARRL
CHHHHHHCCHHHHHH
21.6827174698
832PhosphorylationFLFGEEPSKLDQDVL
HHHCCCCCCCCHHHH
49.4850565243
833UbiquitinationLFGEEPSKLDQDVLA
HHCCCCCCCCHHHHH
67.7929967540
847UbiquitinationAALECADVDPHQFPA
HHHHHCCCCHHHCCH
7.0224816145
859UbiquitinationFPAVHRWKSAVLCYS
CCHHHCCCCEEEEEC
28.6129967540
860PhosphorylationPAVHRWKSAVLCYSP
CHHHCCCCEEEEECC
19.3622199227
865PhosphorylationWKSAVLCYSPSDRQS
CCCEEEEECCCCCCC
21.3222199227
866PhosphorylationKSAVLCYSPSDRQSW
CCEEEEECCCCCCCC
19.5525159151
868PhosphorylationAVLCYSPSDRQSWPS
EEEEECCCCCCCCCC
39.2121712546
872PhosphorylationYSPSDRQSWPSPAVK
ECCCCCCCCCCHHHC
41.6822199227
875PhosphorylationSDRQSWPSPAVKGRF
CCCCCCCCHHHCCCH
21.1625159151
883MethylationPAVKGRFKSQLPDLS
HHHCCCHHHCCCCCC
35.61-
883UbiquitinationPAVKGRFKSQLPDLS
HHHCCCHHHCCCCCC
35.6129967540
884PhosphorylationAVKGRFKSQLPDLSG
HHCCCHHHCCCCCCC
33.9529396449
890PhosphorylationKSQLPDLSGPHSYSP
HHCCCCCCCCCCCCC
58.6220068231
894PhosphorylationPDLSGPHSYSPGRNS
CCCCCCCCCCCCCCC
30.3625159151
895PhosphorylationDLSGPHSYSPGRNSV
CCCCCCCCCCCCCCC
18.8222199227
896PhosphorylationLSGPHSYSPGRNSVA
CCCCCCCCCCCCCCC
24.7225159151
901PhosphorylationSYSPGRNSVAGSNPA
CCCCCCCCCCCCCCC
16.3923663014
905PhosphorylationGRNSVAGSNPAKPGL
CCCCCCCCCCCCCCC
29.8723663014
909UbiquitinationVAGSNPAKPGLGSPG
CCCCCCCCCCCCCCC
40.6624816145
914PhosphorylationPAKPGLGSPGRYSPV
CCCCCCCCCCCCCCC
29.2625159151
918PhosphorylationGLGSPGRYSPVHGSQ
CCCCCCCCCCCCHHH
24.2021712546
919PhosphorylationLGSPGRYSPVHGSQL
CCCCCCCCCCCHHHH
21.0525159151
924PhosphorylationRYSPVHGSQLRRMAR
CCCCCCHHHHHHHHH
15.9123401153
927MethylationPVHGSQLRRMARLAE
CCCHHHHHHHHHHHH
20.77-

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
528SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANKL2_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 ANKL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAA_HUMANPPP2R1Aphysical
27173435

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 ANKL2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-259; SER-268; SER-487;SER-488; SER-496; SER-512; SER-528; SER-662; SER-896; SER-914 ANDSER-919, AND MASS SPECTROMETRY.
"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-896, 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-259 AND SER-528, ANDMASS SPECTROMETRY.
"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-662, AND MASSSPECTROMETRY.

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