dbPTM

LMNB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LMNB1_HUMAN
UniProt AC	P20700
Protein Name	Lamin-B1
Gene Name	LMNB1
Organism	Homo sapiens (Human).
Sequence Length	586
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	MATATPVPPRMGSRAGGPTTPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEAAGVVVEEELFHQQGTPRASNRSCAIM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATATPVPP ------CCCCCCCCC	13.12	22223895
3	Phosphorylation	-----MATATPVPPR -----CCCCCCCCCC	29.75	30108239
5	Phosphorylation	---MATATPVPPRMG ---CCCCCCCCCCCC	22.06	23401153
10	Methylation	TATPVPPRMGSRAGG CCCCCCCCCCCCCCC	35.70	115481603
13	Phosphorylation	PVPPRMGSRAGGPTT CCCCCCCCCCCCCCC	15.04	23403867
14	Methylation	VPPRMGSRAGGPTTP CCCCCCCCCCCCCCC	31.36	24129315
19	Phosphorylation	GSRAGGPTTPLSPTR CCCCCCCCCCCCHHH	44.30	29255136
20	Phosphorylation	SRAGGPTTPLSPTRL CCCCCCCCCCCHHHH	25.93	29255136
23	Phosphorylation	GGPTTPLSPTRLSRL CCCCCCCCHHHHHHH	25.98	19664994
25	Phosphorylation	PTTPLSPTRLSRLQE CCCCCCHHHHHHHHH	40.65	29255136
28	O-linked_Glycosylation	PLSPTRLSRLQEKEE CCCHHHHHHHHHHHH	27.88	28510447
28	Phosphorylation	PLSPTRLSRLQEKEE CCCHHHHHHHHHHHH	27.88	26055452
33	Acetylation	RLSRLQEKEELRELN HHHHHHHHHHHHHHH	43.45	23749302
33	Ubiquitination	RLSRLQEKEELRELN HHHHHHHHHHHHHHH	43.45	19608861
42	Methylation	ELRELNDRLAVYIDK HHHHHHHHHHHHHHH	24.39	115481619
46	Phosphorylation	LNDRLAVYIDKVRSL HHHHHHHHHHHHHCC	9.59	-
49	Acetylation	RLAVYIDKVRSLETE HHHHHHHHHHCCCCC	29.95	23749302
49	Ubiquitination	RLAVYIDKVRSLETE HHHHHHHHHHCCCCC	29.95	21890473
52	Phosphorylation	VYIDKVRSLETENSA HHHHHHHCCCCCCCC	33.28	28450419
55	Phosphorylation	DKVRSLETENSALQL HHHHCCCCCCCCEEE	45.84	22817901
58	Phosphorylation	RSLETENSALQLQVT HCCCCCCCCEEEEEE	24.91	28450419
76	Phosphorylation	EVRGRELTGLKALYE HHCCCCCHHHHHHHH	35.40	24247654
79	Acetylation	GRELTGLKALYETEL CCCCHHHHHHHHHHH	37.38	25953088
79	Ubiquitination	GRELTGLKALYETEL CCCCHHHHHHHHHHH	37.38	21890473
82	Nitration	LTGLKALYETELADA CHHHHHHHHHHHHHH	26.18	-
82	Phosphorylation	LTGLKALYETELADA CHHHHHHHHHHHHHH	26.18	28152594
84	Phosphorylation	GLKALYETELADARR HHHHHHHHHHHHHHH	23.81	24719451
102	Sumoylation	DTARERAKLQIELGK HHHHHHHHHHHHHCC	47.33	-
102	Acetylation	DTARERAKLQIELGK HHHHHHHHHHHHHCC	47.33	25953088
102	Malonylation	DTARERAKLQIELGK HHHHHHHHHHHHHCC	47.33	26320211
102	Sumoylation	DTARERAKLQIELGK HHHHHHHHHHHHHCC	47.33	28112733
102	Ubiquitination	DTARERAKLQIELGK HHHHHHHHHHHHHCC	47.33	21906983
109	Acetylation	KLQIELGKCKAEHDQ HHHHHHCCCHHHHHH	45.23	25953088
109	Ubiquitination	KLQIELGKCKAEHDQ HHHHHHCCCHHHHHH	45.23	-
111	Acetylation	QIELGKCKAEHDQLL HHHHCCCHHHHHHHH	61.36	23236377
111	Ubiquitination	QIELGKCKAEHDQLL HHHHCCCHHHHHHHH	61.36	-
121	Nitration	HDQLLLNYAKKESDL HHHHHHHHHHHHHHC	21.55	-
123	Acetylation	QLLLNYAKKESDLNG HHHHHHHHHHHHCCC	46.87	19608861
123	Succinylation	QLLLNYAKKESDLNG HHHHHHHHHHHHCCC	46.87	23954790
123	Sumoylation	QLLLNYAKKESDLNG HHHHHHHHHHHHCCC	46.87	28112733
123	Ubiquitination	QLLLNYAKKESDLNG HHHHHHHHHHHHCCC	46.87	21890473
124	Acetylation	LLLNYAKKESDLNGA HHHHHHHHHHHCCCC	55.04	26051181
124	Ubiquitination	LLLNYAKKESDLNGA HHHHHHHHHHHCCCC	55.04	-
126	Phosphorylation	LNYAKKESDLNGAQI HHHHHHHHHCCCCHH	57.17	23401153
134	Acetylation	DLNGAQIKLREYEAA HCCCCHHHHHHHHHH	29.43	25953088
134	Ubiquitination	DLNGAQIKLREYEAA HCCCCHHHHHHHHHH	29.43	21890473
138	Phosphorylation	AQIKLREYEAALNSK CHHHHHHHHHHHCCH	12.39	28152594
144	Phosphorylation	EYEAALNSKDAALAT HHHHHHCCHHHHHHH	32.53	27251275
145	Sumoylation	YEAALNSKDAALATA HHHHHCCHHHHHHHH	50.76	28112733
145	Ubiquitination	YEAALNSKDAALATA HHHHHCCHHHHHHHH	50.76	21890473
156	Acetylation	LATALGDKKSLEGDL HHHHHCCHHHHCCCH	42.33	25953088
156	Ubiquitination	LATALGDKKSLEGDL HHHHHCCHHHHCCCH	42.33	-
157	Acetylation	ATALGDKKSLEGDLE HHHHCCHHHHCCCHH	66.08	19608861
157	Sumoylation	ATALGDKKSLEGDLE HHHHCCHHHHCCCHH	66.08	28112733
157	Ubiquitination	ATALGDKKSLEGDLE HHHHCCHHHHCCCHH	66.08	21890473
158	Phosphorylation	TALGDKKSLEGDLED HHHCCHHHHCCCHHH	37.08	28355574
167	Ubiquitination	EGDLEDLKDQIAQLE CCCHHHHHHHHHHHH	60.97	-
176	Phosphorylation	QIAQLEASLAAAKKQ HHHHHHHHHHHHHHH	14.79	28555341
181	Acetylation	EASLAAAKKQLADET HHHHHHHHHHHCCCH	36.00	19608861
181	Succinylation	EASLAAAKKQLADET HHHHHHHHHHHCCCH	36.00	23954790
181	Sumoylation	EASLAAAKKQLADET HHHHHHHHHHHCCCH	36.00	28112733
181	Ubiquitination	EASLAAAKKQLADET HHHHHHHHHHHCCCH	36.00	19608861
182	Acetylation	ASLAAAKKQLADETL HHHHHHHHHHCCCHH	45.90	26051181
182	Ubiquitination	ASLAAAKKQLADETL HHHHHHHHHHCCCHH	45.90	21890473
188	Phosphorylation	KKQLADETLLKVDLE HHHHCCCHHHHCCHH	37.63	29496963
191	Acetylation	LADETLLKVDLENRC HCCCHHHHCCHHHHH	36.49	26051181
197	Methylation	LKVDLENRCQSLTED HHCCHHHHHHHHHHC	15.52	115481651
198	Glutathionylation	KVDLENRCQSLTEDL HCCHHHHHHHHHHCH	4.93	22555962
200	Phosphorylation	DLENRCQSLTEDLEF CHHHHHHHHHHCHHH	40.67	23401153
202	Phosphorylation	ENRCQSLTEDLEFRK HHHHHHHHHCHHHHH	32.47	23403867
209	Acetylation	TEDLEFRKSMYEEEI HHCHHHHHHHHHHHH	44.91	25825284
209	Ubiquitination	TEDLEFRKSMYEEEI HHCHHHHHHHHHHHH	44.91	21906983
210	Phosphorylation	EDLEFRKSMYEEEIN HCHHHHHHHHHHHHH	23.49	23401153
211	Sulfoxidation	DLEFRKSMYEEEINE CHHHHHHHHHHHHHH	5.68	21406390
212	Phosphorylation	LEFRKSMYEEEINET HHHHHHHHHHHHHHH	27.55	28796482
219	Phosphorylation	YEEEINETRRKHETR HHHHHHHHHHHHCEE	31.14	27251275
222	Ubiquitination	EINETRRKHETRLVE HHHHHHHHHCEEEEE	42.37	-
232	Phosphorylation	TRLVEVDSGRQIEYE EEEEEECCCCCEEHH	40.84	23401153
238	Phosphorylation	DSGRQIEYEYKLAQA CCCCCEEHHHHHHHH	26.62	-
241	Sumoylation	RQIEYEYKLAQALHE CCEEHHHHHHHHHHH	25.96	-
241	Acetylation	RQIEYEYKLAQALHE CCEEHHHHHHHHHHH	25.96	26822725
241	Sumoylation	RQIEYEYKLAQALHE CCEEHHHHHHHHHHH	25.96	28112733
241	Ubiquitination	RQIEYEYKLAQALHE CCEEHHHHHHHHHHH	25.96	21890473
249	Sulfoxidation	LAQALHEMREQHDAQ HHHHHHHHHHHHHHH	3.88	21406390
250	Methylation	AQALHEMREQHDAQV HHHHHHHHHHHHHHH	37.12	115481627
260	Phosphorylation	HDAQVRLYKEELEQT HHHHHHHHHHHHHHH	13.04	27642862
261	Sumoylation	DAQVRLYKEELEQTY HHHHHHHHHHHHHHH	49.67	-
261	Acetylation	DAQVRLYKEELEQTY HHHHHHHHHHHHHHH	49.67	25953088
261	Sumoylation	DAQVRLYKEELEQTY HHHHHHHHHHHHHHH	49.67	28112733
261	Ubiquitination	DAQVRLYKEELEQTY HHHHHHHHHHHHHHH	49.67	21890473
267	Phosphorylation	YKEELEQTYHAKLEN HHHHHHHHHHHHHHH	14.11	28152594
268	Phosphorylation	KEELEQTYHAKLENA HHHHHHHHHHHHHHH	10.24	28152594
271	Acetylation	LEQTYHAKLENARLS HHHHHHHHHHHHHHC	42.92	19608861
271	Sumoylation	LEQTYHAKLENARLS HHHHHHHHHHHHHHC	42.92	28112733
271	Ubiquitination	LEQTYHAKLENARLS HHHHHHHHHHHHHHC	42.92	21890473
278	Phosphorylation	KLENARLSSEMNTST HHHHHHHCHHCCHHH	20.78	30266825
279	Phosphorylation	LENARLSSEMNTSTV HHHHHHCHHCCHHHH	45.52	30266825
281	Sulfoxidation	NARLSSEMNTSTVNS HHHHCHHCCHHHHHH	7.77	21406390
283	Phosphorylation	RLSSEMNTSTVNSAR HHCHHCCHHHHHHHH	25.19	30266825
284	Phosphorylation	LSSEMNTSTVNSARE HCHHCCHHHHHHHHH	25.92	23401153
285	Phosphorylation	SSEMNTSTVNSAREE CHHCCHHHHHHHHHH	22.97	30266825
288	Phosphorylation	MNTSTVNSAREELME CCHHHHHHHHHHHHH	25.11	30266825
297	Methylation	REELMESRMRIESLS HHHHHHHHHHHHHHH	12.70	115481611
299	Methylation	ELMESRMRIESLSSQ HHHHHHHHHHHHHHH	28.54	115481643
302	Phosphorylation	ESRMRIESLSSQLSN HHHHHHHHHHHHHHH	31.05	30266825
304	Phosphorylation	RMRIESLSSQLSNLQ HHHHHHHHHHHHHHH	25.89	30266825
305	Phosphorylation	MRIESLSSQLSNLQK HHHHHHHHHHHHHHH	40.20	30266825
308	Phosphorylation	ESLSSQLSNLQKESR HHHHHHHHHHHHHHH	28.05	26074081
312	Acetylation	SQLSNLQKESRACLE HHHHHHHHHHHHHHH	61.90	25953088
312	Malonylation	SQLSNLQKESRACLE HHHHHHHHHHHHHHH	61.90	26320211
312	Sumoylation	SQLSNLQKESRACLE HHHHHHHHHHHHHHH	61.90	28112733
312	Ubiquitination	SQLSNLQKESRACLE HHHHHHHHHHHHHHH	61.90	21890473
330	Acetylation	ELEDLLAKEKDNSRR HHHHHHHHCCCCHHC	66.33	25953088
330	Sumoylation	ELEDLLAKEKDNSRR HHHHHHHHCCCCHHC	66.33	28112733
330	Ubiquitination	ELEDLLAKEKDNSRR HHHHHHHHCCCCHHC	66.33	21906983
340	Phosphorylation	DNSRRMLTDKEREMA CCHHCCCCHHHHHHH	35.36	21406692
342	Acetylation	SRRMLTDKEREMAEI HHCCCCHHHHHHHHH	54.13	25953088
342	Ubiquitination	SRRMLTDKEREMAEI HHCCCCHHHHHHHHH	54.13	-
353	Sulfoxidation	MAEIRDQMQQQLNDY HHHHHHHHHHHHCCH	4.56	28465586
360	Phosphorylation	MQQQLNDYEQLLDVK HHHHHCCHHHHHHHH	12.42	28796482
375	Phosphorylation	LALDMEISAYRKLLE HHHHCHHHHHHHHHC	13.12	30266825
377	Phosphorylation	LDMEISAYRKLLEGE HHCHHHHHHHHHCCH	11.07	23403867
379	Sumoylation	MEISAYRKLLEGEEE CHHHHHHHHHCCHHH	44.76	-
379	Acetylation	MEISAYRKLLEGEEE CHHHHHHHHHCCHHH	44.76	22631273
379	Sumoylation	MEISAYRKLLEGEEE CHHHHHHHHHCCHHH	44.76	-
379	Ubiquitination	MEISAYRKLLEGEEE CHHHHHHHHHCCHHH	44.76	21906983
387	Methylation	LLEGEEERLKLSPSP HHCCHHHHHCCCCCC	40.16	-
389	Sumoylation	EGEEERLKLSPSPSS CCHHHHHCCCCCCCC	53.81	-
389	Acetylation	EGEEERLKLSPSPSS CCHHHHHCCCCCCCC	53.81	25953088
389	Sumoylation	EGEEERLKLSPSPSS CCHHHHHCCCCCCCC	53.81	-
389	Ubiquitination	EGEEERLKLSPSPSS CCHHHHHCCCCCCCC	53.81	21890473
391	Phosphorylation	EEERLKLSPSPSSRV HHHHHCCCCCCCCCE	23.03	29255136
393	Phosphorylation	ERLKLSPSPSSRVTV HHHCCCCCCCCCEEE	33.76	29255136
395	Phosphorylation	LKLSPSPSSRVTVSR HCCCCCCCCCEEEEC	34.80	29255136
396	Phosphorylation	KLSPSPSSRVTVSRA CCCCCCCCCEEEECC	33.87	29255136
399	Phosphorylation	PSPSSRVTVSRASSS CCCCCCEEEECCCCC	16.20	30266825
401	O-linked_Glycosylation	PSSRVTVSRASSSRS CCCCEEEECCCCCCC	16.86	28510447
401	Phosphorylation	PSSRVTVSRASSSRS CCCCEEEECCCCCCC	16.86	23401153
404	Phosphorylation	RVTVSRASSSRSVRT CEEEECCCCCCCCCC	27.95	23927012
405	Phosphorylation	VTVSRASSSRSVRTT EEEECCCCCCCCCCC	28.87	30266825
406	Phosphorylation	TVSRASSSRSVRTTR EEECCCCCCCCCCCC	26.53	30266825
408	Phosphorylation	SRASSSRSVRTTRGK ECCCCCCCCCCCCCC	20.21	27273156
411	Phosphorylation	SSSRSVRTTRGKRKR CCCCCCCCCCCCCEE	20.77	26074081
412	Phosphorylation	SSRSVRTTRGKRKRV CCCCCCCCCCCCEEC	27.19	26074081
413	Methylation	SRSVRTTRGKRKRVD CCCCCCCCCCCEECC	48.28	-
457	Ubiquitination	DGKFIRLKNTSEQDQ CCCEEEEECCCCCCC	48.62	-
460	Phosphorylation	FIRLKNTSEQDQPMG EEEEECCCCCCCCCC	42.53	-
474	Acetylation	GGWEMIRKIGDTSVS CCHHHHHHHCCCEEE	39.87	26051181
474	Malonylation	GGWEMIRKIGDTSVS CCHHHHHHHCCCEEE	39.87	26320211
474	Ubiquitination	GGWEMIRKIGDTSVS CCHHHHHHHCCCEEE	39.87	-
478	Phosphorylation	MIRKIGDTSVSYKYT HHHHHCCCEEEEEEE	26.30	23186163
479	Phosphorylation	IRKIGDTSVSYKYTS HHHHCCCEEEEEEEE	17.51	21815630
481	Phosphorylation	KIGDTSVSYKYTSRY HHCCCEEEEEEEEEE	18.70	30108239
482	Nitration	IGDTSVSYKYTSRYV HCCCEEEEEEEEEEE	13.08	-
483	Acetylation	GDTSVSYKYTSRYVL CCCEEEEEEEEEEEE	34.25	19608861
483	Ubiquitination	GDTSVSYKYTSRYVL CCCEEEEEEEEEEEE	34.25	21890473
484	Phosphorylation	DTSVSYKYTSRYVLK CCEEEEEEEEEEEEE	11.17	23882029
506	Phosphorylation	WAANAGVTASPPTDL EEECCCCCCCCCCEE	22.09	28348404
508	Phosphorylation	ANAGVTASPPTDLIW ECCCCCCCCCCEEEE	23.26	28348404
528	Acetylation	WGTGEDVKVILKNSQ CCCCCCEEEEEECCC	35.56	25953088
528	Ubiquitination	WGTGEDVKVILKNSQ CCCCCCEEEEEECCC	35.56	21890473
532	Acetylation	EDVKVILKNSQGEEV CCEEEEEECCCCCCH	43.35	25825284
532	Malonylation	EDVKVILKNSQGEEV CCEEEEEECCCCCCH	43.35	26320211
532	Sumoylation	EDVKVILKNSQGEEV CCEEEEEECCCCCCH	43.35	28112733
532	Ubiquitination	EDVKVILKNSQGEEV CCEEEEEECCCCCCH	43.35	21890473
534	Phosphorylation	VKVILKNSQGEEVAQ EEEEEECCCCCCHHH	37.67	25159151
543	Phosphorylation	GEEVAQRSTVFKTTI CCCHHHHCEEEEECC	19.49	28450419
544	Phosphorylation	EEVAQRSTVFKTTIP CCHHHHCEEEEECCC	31.95	28450419
547	Acetylation	AQRSTVFKTTIPEEE HHHCEEEEECCCHHH	40.18	26051181
547	Sumoylation	AQRSTVFKTTIPEEE HHHCEEEEECCCHHH	40.18	28112733
547	Ubiquitination	AQRSTVFKTTIPEEE HHHCEEEEECCCHHH	40.18	2190698
548	Phosphorylation	QRSTVFKTTIPEEEE HHCEEEEECCCHHHH	20.63	25849741
549	Phosphorylation	RSTVFKTTIPEEEEE HCEEEEECCCHHHHH	34.82	25849741
575	Phosphorylation	ELFHQQGTPRASNRS HHHHCCCCCCCCCCC	12.79	25159151
579	Phosphorylation	QQGTPRASNRSCAIM CCCCCCCCCCCCCCC	33.77	19007248
583	Farnesylation	PRASNRSCAIM---- CCCCCCCCCCC----	2.41	2684976
583	Farnesylation	PRASNRSCAIM---- CCCCCCCCCCC----	2.41	2684976
583	Methylation	PRASNRSCAIM---- CCCCCCCCCCC----	2.41	10679189

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
23	S	Phosphorylation	Kinase	CDK1	P06493	PSP
23	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
23	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
393	S	Phosphorylation	Kinase	CDK1	P06493	PSP
393	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
393	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
395	S	Phosphorylation	Kinase	KPCB	P05771	PhosphoELM
395	S	Phosphorylation	Kinase	PRKCB	P05771-2	GPS
396	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
396	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
405	S	Phosphorylation	Kinase	KPCB	P05771	PhosphoELM
405	S	Phosphorylation	Kinase	PRKCB	P05771-2	GPS
406	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
406	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LMNB1_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 LMNB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KPCA_HUMAN	PRKCA	physical	12135703
NDEL1_HUMAN	NDEL1	physical	19198602
AIRE_HUMAN	AIRE	physical	20085707
PO2F1_HUMAN	POU2F1	physical	21897860
PCGF2_HUMAN	PCGF2	physical	19727227
LMNA_HUMAN	LMNA	physical	19727227
EGF_HUMAN	EGF	physical	19727227
NICA_HUMAN	NCSTN	physical	22939629
MAGT1_HUMAN	MAGT1	physical	22939629
URB2_HUMAN	URB2	physical	15265697
AACT_HUMAN	SERPINA3	physical	21988832
MBIP1_HUMAN	MBIP	physical	21988832
ZZEF1_HUMAN	ZZEF1	physical	22863883
IMA3_HUMAN	KPNA4	physical	26344197
RFA1_HUMAN	RPA1	physical	26344197
RFA3_HUMAN	RPA3	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
SRSF6_HUMAN	SRSF6	physical	26344197
PIAS2_HUMAN	PIAS2	physical	21516116
MLP3B_HUMAN	MAP1LC3B	physical	26524528
LMNA_HUMAN	LMNA	physical	26524528
LMNB2_HUMAN	LMNB2	physical	26524528

Drug and Disease Associations

Kegg Disease
OMIM Disease
169500	Leukodystrophy, demyelinating, autosomal dominant, adult-onset (ADLD)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LMNB1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-5; THR-20 AND SER-23, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-157; LYS-271 AND LYS-483,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-20; SER-23; SER-375 ANDTHR-575, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-5; THR-20 AND SER-23, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-20; SER-23 AND THR-575,AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-20 AND SER-23, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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-23, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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-13, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-278; SER-279;SER-284; SER-391 AND SER-579, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND SER-391,AND MASS SPECTROMETRY.	16565220 [Abstract]
"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 THR-20 AND SER-23, AND MASSSPECTROMETRY.	16964243 [Abstract]
"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-19; SER-23; SER-28;SER-200; SER-404 AND THR-575, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-393, ANDMASS SPECTROMETRY.	16083285 [Abstract]
Prenylation
Reference	PubMed
"Human lamin B contains a farnesylated cysteine residue."; Farnsworth C.C., Wolda S.L., Gelb M.H., Glomset J.A.; J. Biol. Chem. 264:20422-20429(1989). Cited for: ISOPRENYLATION AT CYS-583.	2684976 [Abstract]