LMNB2_HUMAN - dbPTM
LMNB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMNB2_HUMAN
UniProt AC Q03252
Protein Name Lamin-B2
Gene Name LMNB2
Organism Homo sapiens (Human).
Sequence Length 620
Subcellular Localization Nucleus inner membrane
Lipid-anchor
Nucleoplasmic side.
Protein Description Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin..
Protein Sequence MSPPSPGRRREQRRPRAAATMATPLPGRAGGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLKISEKEEVTTREVSGIKALYESELADARRVLDETARERARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEELRSQHDEQVRLYKLELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEERLKLSPSPSSRVTVSRATSSSSGSLSATGRLGRSKRKRLEVEEPLGSGPSVLGTGTGGSGGFHLAQQASASGSVSIEEIDLEGKFVQLKNNSDKDQSLGNWRIKRQVLEGEEIAYKFTPKYILRAGQMVTVWAAGAGVAHSPPSTLVWKGQSSWGTGESFRTVLVNADGEEVAMRTVKKSSVMRENENGEEEEEEAEFGEEDLFHQQGDPRTTSRGCYVM
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
2Phosphorylation------MSPPSPGRR
------CCCCCCCCC
20.2329691806
3Phosphorylation-----MSPPSPGRRR
-----CCCCCCCCCH
24.8624719451
5Phosphorylation---MSPPSPGRRREQ
---CCCCCCCCCHHH
6.4529691806
14PhosphorylationGRRREQRRPRAAATM
CCCHHHCCCCHHHCC
28.0923911959
17PhosphorylationREQRRPRAAATMATP
HHHCCCCHHHCCCCC
25.9816964243
19PhosphorylationQRRPRAAATMATPLP
HCCCCHHHCCCCCCC
40.6525850435
20PhosphorylationRRPRAAATMATPLPG
CCCCHHHCCCCCCCC
33.7727251275
22PhosphorylationPRAAATMATPLPGRA
CCHHHCCCCCCCCCC
27.8822199227
23PhosphorylationRAAATMATPLPGRAG
CHHHCCCCCCCCCCC
45.0129255136
27AcetylationTMATPLPGRAGGPAT
CCCCCCCCCCCCCCC
43.45-
28MethylationMATPLPGRAGGPATP
CCCCCCCCCCCCCCC
62.60115481669
34PhosphorylationGRAGGPATPLSPTRL
CCCCCCCCCCCHHHH
27.8329255136
37PhosphorylationGGPATPLSPTRLSRL
CCCCCCCCHHHHHHH
3.7229255136
39PhosphorylationPATPLSPTRLSRLQE
CCCCCCHHHHHHHHH
25.3629255136
42PhosphorylationPLSPTRLSRLQEKEE
CCCHHHHHHHHHHHH
35.5426055452
47AcetylationRLSRLQEKEELRELN
HHHHHHHHHHHHHHH
5.6022631257
47UbiquitinationRLSRLQEKEELRELN
HHHHHHHHHHHHHHH
5.60-
56MethylationELRELNDRLAHYIDR
HHHHHHHHHHHHHHH
5.69115481679
57UbiquitinationLRELNDRLAHYIDRV
HHHHHHHHHHHHHHH
44.1221890473
59PhosphorylationELNDRLAHYIDRVRA
HHHHHHHHHHHHHHH
40.8221406692
60PhosphorylationLNDRLAHYIDRVRAL
HHHHHHHHHHHHHHH
68.8828152594
61AcetylationNDRLAHYIDRVRALE
HHHHHHHHHHHHHHH
53.00-
61UbiquitinationNDRLAHYIDRVRALE
HHHHHHHHHHHHHHH
53.0021890473
66PhosphorylationHYIDRVRALELENDR
HHHHHHHHHHCCCCE
29.9721406692
70PhosphorylationRVRALELENDRLLLK
HHHHHHCCCCEEEEE
30.0124719451
73MethylationALELENDRLLLKISE
HHHCCCCEEEEEEEC
35.5572659601
73UbiquitinationALELENDRLLLKISE
HHHCCCCEEEEEEEC
35.5521890473
77AcetylationENDRLLLKISEKEEV
CCCEEEEEEECCCCC
38.2925825284
77MalonylationENDRLLLKISEKEEV
CCCEEEEEEECCCCC
38.2926320211
77SumoylationENDRLLLKISEKEEV
CCCEEEEEEECCCCC
38.2928112733
77UbiquitinationENDRLLLKISEKEEV
CCCEEEEEEECCCCC
38.2921890473
79PhosphorylationDRLLLKISEKEEVTT
CEEEEEEECCCCCCH
35.7221406692
81AcetylationLLLKISEKEEVTTRE
EEEEEECCCCCCHHH
12.3619608861
81SumoylationLLLKISEKEEVTTRE
EEEEEECCCCCCHHH
12.3628112733
81UbiquitinationLLLKISEKEEVTTRE
EEEEEECCCCCCHHH
12.3633845483
85PhosphorylationISEKEEVTTREVSGI
EECCCCCCHHHCCHH
34.7621406692
86PhosphorylationSEKEEVTTREVSGIK
ECCCCCCHHHCCHHH
7.0521406692
90PhosphorylationEVTTREVSGIKALYE
CCCHHHCCHHHHHHH
30.5924719451
93AcetylationTREVSGIKALYESEL
HHHCCHHHHHHHHHH
48.5026051181
93UbiquitinationTREVSGIKALYESEL
HHHCCHHHHHHHHHH
48.5029967540
96PhosphorylationVSGIKALYESELADA
CCHHHHHHHHHHHHH
33.0928152594
98PhosphorylationGIKALYESELADARR
HHHHHHHHHHHHHHH
26.2228152594
103UbiquitinationYESELADARRVLDET
HHHHHHHHHHHHHHH
40.2221890473
113UbiquitinationVLDETARERARLQIE
HHHHHHHHHHHHHHH
57.9021890473
114PhosphorylationLDETARERARLQIEI
HHHHHHHHHHHHHHH
39.8719691289
123AcetylationRLQIEIGKLRAELDE
HHHHHHHHHHHHHHH
14.9725953088
123MalonylationRLQIEIGKLRAELDE
HHHHHHHHHHHHHHH
14.9726320211
123UbiquitinationRLQIEIGKLRAELDE
HHHHHHHHHHHHHHH
14.9723000965
130UbiquitinationKLRAELDEVNKSAKK
HHHHHHHHHHHHHHH
56.0621890473
133AcetylationAELDEVNKSAKKREG
HHHHHHHHHHHHHHC
56.3725953088
133MalonylationAELDEVNKSAKKREG
HHHHHHHHHHHHHHC
56.3726320211
133UbiquitinationAELDEVNKSAKKREG
HHHHHHHHHHHHHHC
56.3733845483
134PhosphorylationELDEVNKSAKKREGE
HHHHHHHHHHHHHCC
43.5719691289
136UbiquitinationDEVNKSAKKREGELT
HHHHHHHHHHHCCEE
6.6523503661
137UbiquitinationEVNKSAKKREGELTV
HHHHHHHHHHCCEEE
37.3423503661
143PhosphorylationKKREGELTVAQGRVK
HHHHCCEEEEECCCC
4.7928634120
148PhosphorylationELTVAQGRVKDLESL
CEEEEECCCCCHHHH
36.0420068231
150AcetylationTVAQGRVKDLESLFH
EEEECCCCCHHHHHC
45.0123749302
150UbiquitinationTVAQGRVKDLESLFH
EEEECCCCCHHHHHC
45.0123000965
154PhosphorylationGRVKDLESLFHRSEV
CCCCCHHHHHCHHHH
47.9528857561
155PhosphorylationRVKDLESLFHRSEVE
CCCCHHHHHCHHHHH
42.29-
159PhosphorylationLESLFHRSEVELAAA
HHHHHCHHHHHHHHH
38.3420068231
166UbiquitinationSEVELAAALSDKRGL
HHHHHHHHHHCCCCC
61.9821890473
168PhosphorylationVELAAALSDKRGLES
HHHHHHHHCCCCCHH
64.9130266825
170AcetylationLAAALSDKRGLESDV
HHHHHHCCCCCHHHH
11.3630589825
170UbiquitinationLAAALSDKRGLESDV
HHHHHHCCCCCHHHH
11.3622817900
171MethylationAAALSDKRGLESDVA
HHHHHCCCCCHHHHH
29.38115481719
175PhosphorylationSDKRGLESDVAELRA
HCCCCCHHHHHHHHH
34.1628857561
180UbiquitinationLESDVAELRAQLAKA
CHHHHHHHHHHHHHH
65.6721890473
186AcetylationELRAQLAKAEDGHAV
HHHHHHHHHCCCCHH
6.4922424773
186UbiquitinationELRAQLAKAEDGHAV
HHHHHHHHHCCCCHH
6.4923000965
195AcetylationEDGHAVAKKQLEKET
CCCCHHHHHHHHHHH
2.8330589819
195SumoylationEDGHAVAKKQLEKET
CCCCHHHHHHHHHHH
2.8328112733
195UbiquitinationEDGHAVAKKQLEKET
CCCCHHHHHHHHHHH
2.8323000965
196UbiquitinationDGHAVAKKQLEKETL
CCCHHHHHHHHHHHH
47.5723000965
200AcetylationVAKKQLEKETLMRVD
HHHHHHHHHHHHHCC
44.5823749302
200UbiquitinationVAKKQLEKETLMRVD
HHHHHHHHHHHHHCC
44.5821890473
211MethylationMRVDLENRCQSLQEE
HHCCHHHHHHHHHHH
42.73115481739
214PhosphorylationDLENRCQSLQEELDF
CHHHHHHHHHHHHHH
28.9628348404
223MalonylationQEELDFRKSVFEEEV
HHHHHHHHHHHHHHH
45.2426320211
223UbiquitinationQEELDFRKSVFEEEV
HHHHHHHHHHHHHHH
45.2429967540
224PhosphorylationEELDFRKSVFEEEVR
HHHHHHHHHHHHHHH
7.2527499020
226PhosphorylationLDFRKSVFEEEVRET
HHHHHHHHHHHHHHH
32.3719691289
235UbiquitinationEEVRETRRRHERRLV
HHHHHHHHHHHHHEE
30.3521890473
236SulfoxidationEVRETRRRHERRLVE
HHHHHHHHHHHHEEE
3.1821406390
246PhosphorylationRRLVEVDSSRQQEYD
HHEEEECCCHHHHHH
41.4319691289
247PhosphorylationRLVEVDSSRQQEYDF
HEEEECCCHHHHHHH
41.6519691289
252PhosphorylationDSSRQQEYDFKMAQA
CCCHHHHHHHHHHHH
31.8130108239
255AcetylationRQQEYDFKMAQALEE
HHHHHHHHHHHHHHH
39.8226051181
255SumoylationRQQEYDFKMAQALEE
HHHHHHHHHHHHHHH
39.8228112733
255UbiquitinationRQQEYDFKMAQALEE
HHHHHHHHHHHHHHH
39.8229967540
264MethylationAQALEELRSQHDEQV
HHHHHHHHHCCHHHH
12.17115481699
265PhosphorylationQALEELRSQHDEQVR
HHHHHHHHCCHHHHH
36.9827251275
265UbiquitinationQALEELRSQHDEQVR
HHHHHHHHCCHHHHH
36.9821890473
270UbiquitinationLRSQHDEQVRLYKLE
HHHCCHHHHHHEEEH
53.5021890473
272MethylationSQHDEQVRLYKLELE
HCCHHHHHHEEEHHH
31.03115481729
274PhosphorylationHDEQVRLYKLELEQT
CHHHHHHEEEHHHHH
48.1828152594
275AcetylationDEQVRLYKLELEQTY
HHHHHHEEEHHHHHH
63.0726051181
275UbiquitinationDEQVRLYKLELEQTY
HHHHHHEEEHHHHHH
63.0723000965
278UbiquitinationVRLYKLELEQTYQAK
HHHEEEHHHHHHHHH
54.0921890473
281PhosphorylationYKLELEQTYQAKLDS
EEEHHHHHHHHHHCH
27.5928152594
282PhosphorylationKLELEQTYQAKLDSA
EEHHHHHHHHHHCHH
13.0528152594
285AcetylationLEQTYQAKLDSAKLS
HHHHHHHHHCHHCCC
64.0623236377
285UbiquitinationLEQTYQAKLDSAKLS
HHHHHHHHHCHHCCC
64.0623000965
288UbiquitinationTYQAKLDSAKLSSDQ
HHHHHHCHHCCCCCC
53.2421890473
290AcetylationQAKLDSAKLSSDQND
HHHHCHHCCCCCCCH
14.6923749302
290UbiquitinationQAKLDSAKLSSDQND
HHHHCHHCCCCCCCH
14.6923000965
292PhosphorylationKLDSAKLSSDQNDKA
HHCHHCCCCCCCHHH
8.0628348404
293PhosphorylationLDSAKLSSDQNDKAA
HCHHCCCCCCCHHHH
29.7428348404
296PhosphorylationAKLSSDQNDKAASAA
HCCCCCCCHHHHHHH
27.4925850435
298AcetylationLSSDQNDKAASAARE
CCCCCCHHHHHHHHH
21.8023749302
298PhosphorylationLSSDQNDKAASAARE
CCCCCCHHHHHHHHH
21.8022817900
298UbiquitinationLSSDQNDKAASAARE
CCCCCCHHHHHHHHH
21.8033845483
299PhosphorylationSSDQNDKAASAAREE
CCCCCHHHHHHHHHH
20.8324961811
301PhosphorylationDQNDKAASAAREELK
CCCHHHHHHHHHHHH
3.1325159151
302PhosphorylationQNDKAASAAREELKE
CCHHHHHHHHHHHHH
23.18-
306UbiquitinationAASAAREELKEARMR
HHHHHHHHHHHHHHH
53.5321890473
308AcetylationSAAREELKEARMRLE
HHHHHHHHHHHHHHH
14.2625953088
308UbiquitinationSAAREELKEARMRLE
HHHHHHHHHHHHHHH
14.2633845483
316PhosphorylationEARMRLESLSYQLSG
HHHHHHHHHHHHHHH
43.2627273156
318PhosphorylationRMRLESLSYQLSGLQ
HHHHHHHHHHHHHHH
5.3130266825
319PhosphorylationMRLESLSYQLSGLQK
HHHHHHHHHHHHHHH
38.6725884760
322PhosphorylationESLSYQLSGLQKQAS
HHHHHHHHHHHHHHH
5.7928152594
326AcetylationYQLSGLQKQASAAED
HHHHHHHHHHHHHHH
52.0523236377
326UbiquitinationYQLSGLQKQASAAED
HHHHHHHHHHHHHHH
52.0523000965
329PhosphorylationSGLQKQASAAEDRIR
HHHHHHHHHHHHHHH
12.1423828894
331UbiquitinationLQKQASAAEDRIREL
HHHHHHHHHHHHHHH
47.12-
334MethylationQASAAEDRIRELEEA
HHHHHHHHHHHHHHH
52.69115481709
336UbiquitinationSAAEDRIRELEEAMA
HHHHHHHHHHHHHHC
60.64-
351UbiquitinationGERDKFRKMLDAKEQ
CCHHHHHHHHHHHHH
3.2124816145
354PhosphorylationDKFRKMLDAKEQEMT
HHHHHHHHHHHHHHH
11.1519664995
356UbiquitinationFRKMLDAKEQEMTEM
HHHHHHHHHHHHHHH
50.8532015554
373AcetylationVMQQQLAEYQELLDV
HHHHHHHHHHHHHHH
44.76-
373UbiquitinationVMQQQLAEYQELLDV
HHHHHHHHHHHHHHH
44.7621890473
374PhosphorylationMQQQLAEYQELLDVK
HHHHHHHHHHHHHHH
3.7819664995
383UbiquitinationELLDVKLALDMEINA
HHHHHHHHHHHHHHH
53.8121890473
385PhosphorylationLDVKLALDMEINAYR
HHHHHHHHHHHHHHH
23.0320363803
387PhosphorylationVKLALDMEINAYRKL
HHHHHHHHHHHHHHH
33.7620815410
389PhosphorylationLALDMEINAYRKLLE
HHHHHHHHHHHHHHH
34.8018669648
390PhosphorylationALDMEINAYRKLLEG
HHHHHHHHHHHHHHC
33.8720068231
393SumoylationMEINAYRKLLEGEEE
HHHHHHHHHHHCHHH
16.20-
393AcetylationMEINAYRKLLEGEEE
HHHHHHHHHHHCHHH
16.2022631249
393NeddylationMEINAYRKLLEGEEE
HHHHHHHHHHHCHHH
16.2032015554
393PhosphorylationMEINAYRKLLEGEEE
HHHHHHHHHHHCHHH
16.2021406692
393SumoylationMEINAYRKLLEGEEE
HHHHHHHHHHHCHHH
16.20-
393UbiquitinationMEINAYRKLLEGEEE
HHHHHHHHHHHCHHH
16.2032015554
395PhosphorylationINAYRKLLEGEEERL
HHHHHHHHHCHHHHH
13.5621406692
398PhosphorylationYRKLLEGEEERLKLS
HHHHHHCHHHHHCCC
28.2120164059
399PhosphorylationRKLLEGEEERLKLSP
HHHHHCHHHHHCCCC
27.5122115753
400PhosphorylationKLLEGEEERLKLSPS
HHHHCHHHHHCCCCC
24.9419664995
401MethylationLLEGEEERLKLSPSP
HHHCHHHHHCCCCCC
38.19-
401PhosphorylationLLEGEEERLKLSPSP
HHHCHHHHHCCCCCC
38.1920363803
402PhosphorylationLEGEEERLKLSPSPS
HHCHHHHHCCCCCCC
34.0623911959
403SumoylationEGEEERLKLSPSPSS
HCHHHHHCCCCCCCC
34.26-
403SumoylationEGEEERLKLSPSPSS
HCHHHHHCCCCCCCC
34.26-
403UbiquitinationEGEEERLKLSPSPSS
HCHHHHHCCCCCCCC
34.2623000965
404PhosphorylationGEEERLKLSPSPSSR
CHHHHHCCCCCCCCC
22.5420164059
405PhosphorylationEEERLKLSPSPSSRV
HHHHHCCCCCCCCCE
4.6329255136
406PhosphorylationEERLKLSPSPSSRVT
HHHHCCCCCCCCCEE
26.0219664995
407PhosphorylationERLKLSPSPSSRVTV
HHHCCCCCCCCCEEE
21.2629255136
408PhosphorylationRLKLSPSPSSRVTVS
HHCCCCCCCCCEEEE
21.3220068231
409PhosphorylationLKLSPSPSSRVTVSR
HCCCCCCCCCEEEEE
23.6429255136
410PhosphorylationKLSPSPSSRVTVSRA
CCCCCCCCCEEEEEE
29.6129255136
413PhosphorylationPSPSSRVTVSRATSS
CCCCCCEEEEEEECC
43.5330266825
415PhosphorylationPSSRVTVSRATSSSS
CCCCEEEEEEECCCC
61.6530266825
418PhosphorylationRVTVSRATSSSSGSL
CEEEEEEECCCCCCC
39.8630266825
419PhosphorylationVTVSRATSSSSGSLS
EEEEEEECCCCCCCC
10.9629255136
420PhosphorylationTVSRATSSSSGSLSA
EEEEEECCCCCCCCC
52.4929255136
421PhosphorylationVSRATSSSSGSLSAT
EEEEECCCCCCCCCC
13.7830266825
422PhosphorylationSRATSSSSGSLSATG
EEEECCCCCCCCCCC
44.5129255136
424PhosphorylationATSSSSGSLSATGRL
EECCCCCCCCCCCCC
28.6329255136
426PhosphorylationSSSSGSLSATGRLGR
CCCCCCCCCCCCCCC
41.0729255136
428PhosphorylationSSGSLSATGRLGRSK
CCCCCCCCCCCCCCC
19.3930266825
433MethylationSATGRLGRSKRKRLE
CCCCCCCCCCCCCEE
21.68-
472PhosphorylationAQQASASGSVSIEEI
CHHHCCCCCEEEEEE
56.2720068231
474UbiquitinationQASASGSVSIEEIDL
HHCCCCCEEEEEEEC
58.4521890473
477PhosphorylationASGSVSIEEIDLEGK
CCCCEEEEEEECCCC
48.6725850435
489SumoylationEGKFVQLKNNSDKDQ
CCCEEEECCCCCCCC
66.7528112733
489UbiquitinationEGKFVQLKNNSDKDQ
CCCEEEECCCCCCCC
66.7523000965
492PhosphorylationFVQLKNNSDKDQSLG
EEEECCCCCCCCCCC
43.7220068231
494AcetylationQLKNNSDKDQSLGNW
EECCCCCCCCCCCCC
12.5426051181
494MalonylationQLKNNSDKDQSLGNW
EECCCCCCCCCCCCC
12.5426320211
494UbiquitinationQLKNNSDKDQSLGNW
EECCCCCCCCCCCCC
12.5423000965
495PhosphorylationLKNNSDKDQSLGNWR
ECCCCCCCCCCCCCE
16.5820068231
496UbiquitinationKNNSDKDQSLGNWRI
CCCCCCCCCCCCCEE
33.4721890473
497PhosphorylationNNSDKDQSLGNWRIK
CCCCCCCCCCCCEEE
10.3425159151
498PhosphorylationNSDKDQSLGNWRIKR
CCCCCCCCCCCEEEE
18.0824719451
500AcetylationDKDQSLGNWRIKRQV
CCCCCCCCCEEEEEE
41.69-
500UbiquitinationDKDQSLGNWRIKRQV
CCCCCCCCCEEEEEE
41.6921890473
515PhosphorylationLEGEEIAYKFTPKYI
ECCCCCEEECCHHHH
18.3430266825
516AcetylationEGEEIAYKFTPKYIL
CCCCCEEECCHHHHC
12.4523236377
516UbiquitinationEGEEIAYKFTPKYIL
CCCCCEEECCHHHHC
12.4523000965
518PhosphorylationEEIAYKFTPKYILRA
CCCEEECCHHHHCCC
4.2530266825
520AcetylationIAYKFTPKYILRAGQ
CEEECCHHHHCCCCC
38.1325825284
520MalonylationIAYKFTPKYILRAGQ
CEEECCHHHHCCCCC
38.1326320211
520UbiquitinationIAYKFTPKYILRAGQ
CEEECCHHHHCCCCC
38.1323000965
521PhosphorylationAYKFTPKYILRAGQM
EEECCHHHHCCCCCE
28.8624719451
524PhosphorylationFTPKYILRAGQMVTV
CCHHHHCCCCCEEEE
37.4420068231
525PhosphorylationTPKYILRAGQMVTVW
CHHHHCCCCCEEEEE
30.9822199227
530PhosphorylationLRAGQMVTVWAAGAG
CCCCCEEEEEECCCC
19.5228102081
532PhosphorylationAGQMVTVWAAGAGVA
CCCEEEEEECCCCCC
36.4124719451
533PhosphorylationGQMVTVWAAGAGVAH
CCEEEEEECCCCCCC
22.9525627689
536PhosphorylationVTVWAAGAGVAHSPP
EEEEECCCCCCCCCC
31.3625627689
541PhosphorylationAGAGVAHSPPSTLVW
CCCCCCCCCCCEEEE
32.9522199227
544PhosphorylationGVAHSPPSTLVWKGQ
CCCCCCCCEEEEECC
2.1322199227
545PhosphorylationVAHSPPSTLVWKGQS
CCCCCCCEEEEECCC
4.8922199227
552PhosphorylationTLVWKGQSSWGTGES
EEEEECCCCCCCCCC
4.3930108239
553PhosphorylationLVWKGQSSWGTGESF
EEEECCCCCCCCCCE
5.7530108239
554SulfoxidationVWKGQSSWGTGESFR
EEECCCCCCCCCCEE
4.4521406390
556PhosphorylationKGQSSWGTGESFRTV
ECCCCCCCCCCEEEE
24.4830108239
559PhosphorylationSSWGTGESFRTVLVN
CCCCCCCCEEEEEEC
43.5630108239
561PhosphorylationWGTGESFRTVLVNAD
CCCCCCEEEEEECCC
28.8923898821
576PhosphorylationGEEVAMRTVKKSSVM
CCEEEHHHHHHHHHH
22.2428555341
581PhosphorylationMRTVKKSSVMRENEN
HHHHHHHHHHCCCCC
61.4623898821
617FarnesylationPRTTSRGCYVM----
CCCCCCCEECC----
-
617MethylationPRTTSRGCYVM----
CCCCCCCEECC----
-

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
37SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMNB2_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 LMNB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOX4_HUMANSOX4physical
25969425
MK01_HUMANMAPK1physical
26344197
MK03_HUMANMAPK3physical
26344197

Drug and Disease Associations
Kegg Disease
H00420 Familial partial lipodystrophy (FPL), including the following four diseases: Kobberling-type lipodys
OMIM Disease
608709Partial acquired lipodystrophy (APLD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LMNB2_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-27; LYS-61; LYS-373 ANDLYS-500, 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 THR-14 AND SER-17, 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 THR-14; SER-17; SER-401;SER-402 AND SER-406, 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 THR-14; SER-17; SER-385;SER-389; SER-399; SER-402; SER-404 AND SER-406, 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 THR-14; SER-17; SER-385 ANDSER-387, 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-17 AND THR-19, 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 THR-14; SER-17; SER-385 ANDSER-387, AND MASS SPECTROMETRY.

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