LAP2B_MOUSE - dbPTM
LAP2B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAP2B_MOUSE
UniProt AC Q61029
Protein Name Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma
Gene Name Tmpo
Organism Mus musculus (Mouse).
Sequence Length 452
Subcellular Localization Nucleus inner membrane
Single-pass type II membrane protein. Chromosome. Tightly associated with the nuclear lamina..
Protein Description May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95 (By similarity)..
Protein Sequence MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLAAGANSKGPPDFSSDEEREPTPVLGSGASVGRGRGAVGRKATKKTDKPRLEDKDDLDVTELSNEELLDQLVRYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTVSSSAENTRQNGSNDSDRYSDNDEDSKIELKLEKREPLKGRAKTPVTLKQRRTEHNQSYSQAGVTETEWTSGSSTGGPLQALTRESTRGSRRTPRKRVETSQHFRIDGAVISESTPIAETIKASSNESLVANRLTGNFKHASSILPITEFSDITRRTPKKPLTRAEVGEKTEERRVDRDILKEMFPYEASTPTGISASCRRPIKGAAGRPLELSDFRMEESFSSKYVPKYAPLADVKSEKTKKRRSVPMWIKMLLFALVAVFLFLVYQAMETNQGNPFTNFLQDTKISN
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
17AcetylationVLTKDKLKSELVANN
CCCHHHHHHHHHHCC		47.8522826441
59PhosphorylationPLAAGANSKGPPDFS
CCCCCCCCCCCCCCC		38.15-
66PhosphorylationSKGPPDFSSDEEREP
CCCCCCCCCCCCCCC		44.2317242355
67PhosphorylationKGPPDFSSDEEREPT
CCCCCCCCCCCCCCC		49.3817242355
71MethylationDFSSDEEREPTPVLG
CCCCCCCCCCCCCCC		53.8216187287
74PhosphorylationSDEEREPTPVLGSGA
CCCCCCCCCCCCCCC		22.6710413518
79PhosphorylationEPTPVLGSGASVGRG
CCCCCCCCCCCCCCC		27.33-
82PhosphorylationPVLGSGASVGRGRGA
CCCCCCCCCCCCCCH		28.7321183079
85DimethylationGSGASVGRGRGAVGR
CCCCCCCCCCCHHCC		29.49-
85MethylationGSGASVGRGRGAVGR
CCCCCCCCCCCHHCC		29.4924129315
87DimethylationGASVGRGRGAVGRKA
CCCCCCCCCHHCCCC		28.65-
87MethylationGASVGRGRGAVGRKA
CCCCCCCCCHHCCCC		28.6524129315
92MethylationRGRGAVGRKATKKTD
CCCCHHCCCCCCCCC		20.8815231561
106AcetylationDKPRLEDKDDLDVTE
CCCCCCCCCCCCHHH		43.7123954790
153PhosphorylationLKLREQGTESRSSTP
HHHHHCCCCCCCCCC		30.4024719451
155PhosphorylationLREQGTESRSSTPLP
HHHCCCCCCCCCCCC		36.9821183079
157PhosphorylationEQGTESRSSTPLPTV
HCCCCCCCCCCCCCC		48.0923608596
157 (in isoform 2)Phosphorylation-48.0923608596
157 (in isoform 3)Phosphorylation-48.0919144319
157 (in isoform 4)Phosphorylation-48.0923608596
158PhosphorylationQGTESRSSTPLPTVS
CCCCCCCCCCCCCCC		32.6923608596
158 (in isoform 2)Phosphorylation-32.6923608596
158 (in isoform 3)Phosphorylation-32.6923608596
158 (in isoform 4)Phosphorylation-32.6923608596
159PhosphorylationGTESRSSTPLPTVSS
CCCCCCCCCCCCCCC		30.0510413518
159 (in isoform 2)Phosphorylation-30.0529899451
159 (in isoform 3)Phosphorylation-30.0529899451
159 (in isoform 4)Phosphorylation-30.0529899451
163PhosphorylationRSSTPLPTVSSSAEN
CCCCCCCCCCCCCCC		40.4823608596
163 (in isoform 2)Phosphorylation-40.4823608596
163 (in isoform 3)Phosphorylation-40.4823608596
163 (in isoform 4)Phosphorylation-40.4823608596
165PhosphorylationSTPLPTVSSSAENTR
CCCCCCCCCCCCCCC		22.5121183079
165 (in isoform 2)Phosphorylation-22.5125338131
165 (in isoform 3)Phosphorylation-22.5125338131
165 (in isoform 4)Phosphorylation-22.5125338131
166PhosphorylationTPLPTVSSSAENTRQ
CCCCCCCCCCCCCCC		29.2725338131
166 (in isoform 2)Phosphorylation-29.2725338131
166 (in isoform 3)Phosphorylation-29.2725338131
166 (in isoform 4)Phosphorylation-29.2725338131
167PhosphorylationPLPTVSSSAENTRQN
CCCCCCCCCCCCCCC		31.9023608596
167 (in isoform 2)Phosphorylation-31.9023608596
167 (in isoform 3)Phosphorylation-31.9023608596
167 (in isoform 4)Phosphorylation-31.9023608596
171PhosphorylationVSSSAENTRQNGSND
CCCCCCCCCCCCCCC		25.7423608596
171 (in isoform 2)Phosphorylation-25.7423608596
171 (in isoform 3)Phosphorylation-25.7423608596
171 (in isoform 4)Phosphorylation-25.7423608596
176PhosphorylationENTRQNGSNDSDRYS
CCCCCCCCCCCCCCC		45.0425521595
176 (in isoform 2)Phosphorylation-45.0425521595
176 (in isoform 3)Phosphorylation-45.0425521595
176 (in isoform 4)Phosphorylation-45.0425521595
179PhosphorylationRQNGSNDSDRYSDND
CCCCCCCCCCCCCCC		28.3925521595
179 (in isoform 2)Phosphorylation-28.3925521595
179 (in isoform 3)Phosphorylation-28.3925521595
179 (in isoform 4)Phosphorylation-28.3925521595
182PhosphorylationGSNDSDRYSDNDEDS
CCCCCCCCCCCCCCC		25.9325521595
182 (in isoform 2)Phosphorylation-25.9325521595
182 (in isoform 3)Phosphorylation-25.9325521595
182 (in isoform 4)Phosphorylation-25.9325521595
183PhosphorylationSNDSDRYSDNDEDSK
CCCCCCCCCCCCCCC		30.7225521595
183 (in isoform 2)Phosphorylation-30.7225521595
183 (in isoform 3)Phosphorylation-30.7225521595
183 (in isoform 4)Phosphorylation-30.7225521595
189PhosphorylationYSDNDEDSKIELKLE
CCCCCCCCCEEEEEE		33.2227742792
189 (in isoform 2)Phosphorylation-33.2227742792
189 (in isoform 3)Phosphorylation-33.2227742792
189 (in isoform 4)Phosphorylation-33.2227742792
206AcetylationEPLKGRAKTPVTLKQ
CCCCCCCCCCCCHHH		52.5923806337
206MalonylationEPLKGRAKTPVTLKQ
CCCCCCCCCCCCHHH		52.5926320211
207PhosphorylationPLKGRAKTPVTLKQR
CCCCCCCCCCCHHHH		23.2326824392
207 (in isoform 2)Phosphorylation-23.2328725479
207 (in isoform 3)Phosphorylation-23.2328725479
207 (in isoform 4)Phosphorylation-23.2328725479
210PhosphorylationGRAKTPVTLKQRRTE
CCCCCCCCHHHHHHH		29.4628833060
210 (in isoform 2)Phosphorylation-29.4628833060
210 (in isoform 3)Phosphorylation-29.4628833060
210 (in isoform 4)Phosphorylation-29.4628833060
212AcetylationAKTPVTLKQRRTEHN
CCCCCCHHHHHHHCC		32.1823806337
212MalonylationAKTPVTLKQRRTEHN
CCCCCCHHHHHHHCC		32.1826320211
212UbiquitinationAKTPVTLKQRRTEHN
CCCCCCHHHHHHHCC		32.18-
216PhosphorylationVTLKQRRTEHNQSYS
CCHHHHHHHCCCCHH		43.7325266776
216 (in isoform 4)Phosphorylation-43.7329899451
221PhosphorylationRRTEHNQSYSQAGVT
HHHHCCCCHHHCCCC		31.8825266776
223PhosphorylationTEHNQSYSQAGVTET
HHCCCCHHHCCCCEE		20.85-
223 (in isoform 3)Phosphorylation-20.8528066266
224 (in isoform 3)Phosphorylation-33.6228066266
228PhosphorylationSYSQAGVTETEWTSG
CHHHCCCCEEEEECC		35.95-
233 (in isoform 2)Phosphorylation-19.5825177544
234 (in isoform 2)Phosphorylation-37.4425177544
235 (in isoform 3)Phosphorylation-20.4522942356
237 (in isoform 3)Phosphorylation-34.3022942356
238 (in isoform 3)Phosphorylation-48.1026824392
239 (in isoform 2)Phosphorylation-37.3525619855
241 (in isoform 4)Phosphorylation-23.7325159016
242 (in isoform 2)Phosphorylation-5.4221082442
243 (in isoform 3)Phosphorylation-37.1429472430
244 (in isoform 4)Phosphorylation-20.7026239621
245 (in isoform 2)Phosphorylation-2.7525619855
245 (in isoform 4)Phosphorylation-2.7522942356
247 (in isoform 3)Phosphorylation-36.4028833060
247 (in isoform 4)Phosphorylation-36.4027600695
248 (in isoform 2)Phosphorylation-51.7526824392
248 (in isoform 3)Phosphorylation-51.7525521595
249PhosphorylationLQALTRESTRGSRRT
HHHHHHCCCCCCCCC		21.80-
250 (in isoform 4)Phosphorylation-34.0125159016
251 (in isoform 3)Phosphorylation-50.8226824392
252 (in isoform 4)Phosphorylation-26.1225159016
253PhosphorylationTRESTRGSRRTPRKR
HHCCCCCCCCCCCCC		18.46-
258 (in isoform 3)Phosphorylation-38.5126824392
262 (in isoform 2)Phosphorylation-46.9325266776
263PhosphorylationTPRKRVETSQHFRID
CCCCCEECCCCEEEC		30.7225266776
264PhosphorylationPRKRVETSQHFRIDG
CCCCEECCCCEEECC		14.2525266776
265 (in isoform 3)Phosphorylation-47.3525177544
266 (in isoform 3)Phosphorylation-17.4526824392
268 (in isoform 4)Phosphorylation-24.7826239621
271 (in isoform 3)Phosphorylation-21.2625619855
274 (in isoform 3)Phosphorylation-3.6121082442
275PhosphorylationRIDGAVISESTPIAE
EECCEEECCCCCHHH		20.9226824392
275 (in isoform 4)Phosphorylation-20.9226824392
277PhosphorylationDGAVISESTPIAETI
CCEEECCCCCHHHHH		32.4722942356
277 (in isoform 3)Phosphorylation-32.4725619855
277 (in isoform 4)Phosphorylation-32.4728833060
278PhosphorylationGAVISESTPIAETIK
CEEECCCCCHHHHHH		18.0526824392
278 (in isoform 2)Phosphorylation-18.0525159016
278 (in isoform 4)Phosphorylation-18.0528833060
280 (in isoform 3)Phosphorylation-5.6826824392
280 (in isoform 4)Phosphorylation-5.6828576409
281 (in isoform 2)Phosphorylation-14.7526239621
282 (in isoform 2)Phosphorylation-52.3522942356
283PhosphorylationESTPIAETIKASSNE
CCCCHHHHHHHCCCH		20.8229472430
284 (in isoform 2)Phosphorylation-2.3627600695
284 (in isoform 4)Phosphorylation-2.3625159016
285UbiquitinationTPIAETIKASSNESL
CCHHHHHHHCCCHHH		50.03-
287PhosphorylationIAETIKASSNESLVA
HHHHHHHCCCHHHHH		28.7928833060
287 (in isoform 2)Phosphorylation-28.7925159016
288PhosphorylationAETIKASSNESLVAN
HHHHHHCCCHHHHHH		49.8525521595
289 (in isoform 2)Phosphorylation-40.1425159016
291PhosphorylationIKASSNESLVANRLT
HHHCCCHHHHHHHHC		32.1826824392
292 (in isoform 4)Phosphorylation-3.2625266776
294 (in isoform 3)Phosphorylation-10.7525266776
298PhosphorylationSLVANRLTGNFKHAS
HHHHHHHCCCCCCHH		27.1726824392
302AcetylationNRLTGNFKHASSILP
HHHCCCCCCHHHCCC		42.1123806337
302UbiquitinationNRLTGNFKHASSILP
HHHCCCCCCHHHCCC		42.11-
305PhosphorylationTGNFKHASSILPITE
CCCCCCHHHCCCEEE		20.0325177544
305 (in isoform 2)Phosphorylation-20.0326239621
306PhosphorylationGNFKHASSILPITEF
CCCCCHHHCCCEEEH		29.0026824392
310 (in isoform 3)Phosphorylation-5.3025159016
311PhosphorylationASSILPITEFSDITR
HHHCCCEEEHHHCCC		29.1025619855
312 (in isoform 2)Phosphorylation-43.8226824392
313 (in isoform 3)Phosphorylation-6.2726239621
314PhosphorylationILPITEFSDITRRTP
CCCEEEHHHCCCCCC		23.1321082442
314 (in isoform 2)Phosphorylation-23.1328833060
314 (in isoform 3)Phosphorylation-23.1322942356
315 (in isoform 2)Phosphorylation-52.1528833060
316 (in isoform 3)Phosphorylation-2.9027600695
317PhosphorylationITEFSDITRRTPKKP
EEEHHHCCCCCCCCC		21.0625619855
317 (in isoform 2)Phosphorylation-21.0628576409
319CitrullinationEFSDITRRTPKKPLT
EHHHCCCCCCCCCCC		46.89-
319CitrullinationEFSDITRRTPKKPLT
EHHHCCCCCCCCCCC		46.8924463520
319 (in isoform 3)Phosphorylation-46.8925159016
320PhosphorylationFSDITRRTPKKPLTR
HHHCCCCCCCCCCCH		35.8526824392
321 (in isoform 2)Phosphorylation-40.6425159016
321 (in isoform 3)Phosphorylation-40.6425159016
329 (in isoform 2)Phosphorylation-48.0025266776
333AcetylationTRAEVGEKTEERRVD
CHHHCCCCHHHHHCC		56.1422826441
333UbiquitinationTRAEVGEKTEERRVD
CHHHCCCCHHHHHCC		56.14-
334PhosphorylationRAEVGEKTEERRVDR
HHHCCCCHHHHHCCH		38.4825266776
337 (in isoform 3)Phosphorylation-37.3826239621
344 (in isoform 3)Phosphorylation-4.5026824392
345UbiquitinationRVDRDILKEMFPYEA
HCCHHHHHHHCCCCC		47.68-
346 (in isoform 3)Phosphorylation-42.4828833060
347 (in isoform 3)Phosphorylation-3.8128833060
349 (in isoform 3)Phosphorylation-25.4128576409
350PhosphorylationILKEMFPYEASTPTG
HHHHHCCCCCCCCCC		16.9225159016
353PhosphorylationEMFPYEASTPTGISA
HHCCCCCCCCCCCCH		23.9926239621
353 (in isoform 3)Phosphorylation-23.9925159016
354PhosphorylationMFPYEASTPTGISAS
HCCCCCCCCCCCCHH		31.7322942356
356PhosphorylationPYEASTPTGISASCR
CCCCCCCCCCCHHHC		47.4327600695
359PhosphorylationASTPTGISASCRRPI
CCCCCCCCHHHCCCC		18.5725159016
361PhosphorylationTPTGISASCRRPIKG
CCCCCCHHHCCCCCC		11.0228725479
361 (in isoform 3)Phosphorylation-11.0225266776
362GlutathionylationPTGISASCRRPIKGA
CCCCCHHHCCCCCCC		4.2324333276
377PhosphorylationAGRPLELSDFRMEES
CCCCCCHHHHCCCHH		25.9026239621
384PhosphorylationSDFRMEESFSSKYVP
HHHCCCHHHCCCCCC		19.6826824392
386PhosphorylationFRMEESFSSKYVPKY
HCCCHHHCCCCCCCC		34.8928833060
387PhosphorylationRMEESFSSKYVPKYA
CCCHHHCCCCCCCCC		26.4528833060
388AcetylationMEESFSSKYVPKYAP
CCHHHCCCCCCCCCC		49.4123806337
388UbiquitinationMEESFSSKYVPKYAP
CCHHHCCCCCCCCCC		49.41-
389PhosphorylationEESFSSKYVPKYAPL
CHHHCCCCCCCCCCH		24.7528576409
392UbiquitinationFSSKYVPKYAPLADV
HCCCCCCCCCCHHHC		43.96-
393PhosphorylationSSKYVPKYAPLADVK
CCCCCCCCCCHHHCC		13.8425159016
400UbiquitinationYAPLADVKSEKTKKR
CCCHHHCCCHHHCCC		54.14-
401PhosphorylationAPLADVKSEKTKKRR
CCHHHCCCHHHCCCC		44.1425266776
403UbiquitinationLADVKSEKTKKRRSV
HHHCCCHHHCCCCCH		73.13-
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
179SPhosphorylationKinasePRKCAP20444
GPS
179SPhosphorylationKinasePKC-FAMILY-GPS
179SPhosphorylationKinasePKC-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAP2B_MOUSE !!
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 LAP2B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LAP2B_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAP2B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND THR-207,AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; SER-155;SER-183 AND THR-207, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND THR-74,AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.
"Identification of phosphorylation sites in native lamina-associatedpolypeptide 2 beta.";
Dreger M., Otto H., Neubauer G., Mann M., Hucho F.;
Biochemistry 38:9426-9434(1999).
Cited for: PROTEIN SEQUENCE OF 61-85 AND 173-194 (ISOFORM BETA), PHOSPHORYLATIONAT THR-74; THR-159; SER-176 AND SER-179, AND MASS SPECTROMETRY.

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