dbPTM

LBR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LBR_HUMAN
UniProt AC	Q14739
Protein Name	Lamin-B receptor
Gene Name	LBR
Organism	Homo sapiens (Human).
Sequence Length	615
Subcellular Localization	Nucleus inner membrane Multi-pass membrane protein.
Protein Description	Anchors the lamina and the heterochromatin to the inner nuclear membrane..
Protein Sequence	MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIKPLTSFRQRKGGSTSSSPSRRRGSRSRSRSRSPGRPPKSARRSASASHQADIKEARREVEVKLTPLILKPFGNSISRYNGEPEHIERNDAPHKNTQEKFSLSQESSYIATQYSLRPRREEVKLKEIDSKEEKYVAKELAVRTFEVTPIRAKDLEFGGVPGVFLIMFGLPVFLFLLLLMCKQKDPSLLNFPPPLPALYELWETRVFGVYLLWFLIQVLFYLLPIGKVVEGTPLIDGRRLKYRLNGFYAFILTSAVIGTSLFQGVEFHYVYSHFLQFALAATVFCVVLSVYLYMRSLKAPRNDLSPASSGNAVYDFFIGRELNPRIGTFDLKYFCELRPGLIGWVVINLVMLLAEMKIQDRAVPSLAMILVNSFQLLYVVDALWNEEALLTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPNEVSWPMASLIIVLKLCGYVIFRGANSQKNAFRKNPSDPKLAHLKTIHTSTGKNLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYIIYFTMLLVHREARDEYHCKKKYGVAWEKYCQRVPYRIFPYIY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Ubiquitination	---MPSRKFADGEVV ---CCCCCCCCCCEE	49.60	24816145
13	Methylation	FADGEVVRGRWPGSS CCCCCEECCCCCCCC	33.85	115481893
20	Phosphorylation	RGRWPGSSLYYEVEI CCCCCCCCCEEEEEE	26.72	-
22	Phosphorylation	RWPGSSLYYEVEILS CCCCCCCEEEEEEEE	10.26	-
23	Phosphorylation	WPGSSLYYEVEILSH CCCCCCEEEEEEEEC	20.84	-
29	Phosphorylation	YYEVEILSHDSTSQL EEEEEEEECCCCCCE	30.80	28122231
32	Phosphorylation	VEILSHDSTSQLYTV EEEEECCCCCCEEEE	25.24	28122231
33	Phosphorylation	EILSHDSTSQLYTVK EEEECCCCCCEEEEE	26.92	28122231
33	O-linked_Glycosylation	EILSHDSTSQLYTVK EEEECCCCCCEEEEE	26.92	28510447
34	Phosphorylation	ILSHDSTSQLYTVKY EEECCCCCCEEEEEE	23.34	28122231
34	O-linked_Glycosylation	ILSHDSTSQLYTVKY EEECCCCCCEEEEEE	23.34	28510447
37	Phosphorylation	HDSTSQLYTVKYKDG CCCCCCEEEEEECCC	11.23	28122231
38	Phosphorylation	DSTSQLYTVKYKDGT CCCCCEEEEEECCCC	21.08	28122231
42	2-Hydroxyisobutyrylation	QLYTVKYKDGTELEL CEEEEEECCCCEEEE	43.92	-
42	Ubiquitination	QLYTVKYKDGTELEL CEEEEEECCCCEEEE	43.92	33845483
42	Acetylation	QLYTVKYKDGTELEL CEEEEEECCCCEEEE	43.92	26051181
50	Ubiquitination	DGTELELKENDIKPL CCCEEEEECCCCCCC	45.13	32015554
50	Acetylation	DGTELELKENDIKPL CCCEEEEECCCCCCC	45.13	26051181
55	Acetylation	ELKENDIKPLTSFRQ EEECCCCCCCCCCCC	36.52	19608861
55	Malonylation	ELKENDIKPLTSFRQ EEECCCCCCCCCCCC	36.52	26320211
55	Ubiquitination	ELKENDIKPLTSFRQ EEECCCCCCCCCCCC	36.52	19608861
58	Phosphorylation	ENDIKPLTSFRQRKG CCCCCCCCCCCCCCC	34.05	23401153
59	Phosphorylation	NDIKPLTSFRQRKGG CCCCCCCCCCCCCCC	26.56	30266825
67	Phosphorylation	FRQRKGGSTSSSPSR CCCCCCCCCCCCCCC	33.51	28176443
68	Phosphorylation	RQRKGGSTSSSPSRR CCCCCCCCCCCCCCC	35.58	20363803
69	Phosphorylation	QRKGGSTSSSPSRRR CCCCCCCCCCCCCCC	30.43	20363803
70	Phosphorylation	RKGGSTSSSPSRRRG CCCCCCCCCCCCCCC	46.48	30278072
71	Phosphorylation	KGGSTSSSPSRRRGS CCCCCCCCCCCCCCC	27.02	30278072
73	Phosphorylation	GSTSSSPSRRRGSRS CCCCCCCCCCCCCCC	40.13	28176443
78	Phosphorylation	SPSRRRGSRSRSRSR CCCCCCCCCCCCCCC	25.85	20068231
80	Phosphorylation	SRRRGSRSRSRSRSP CCCCCCCCCCCCCCC	35.98	20068231
82	Phosphorylation	RRGSRSRSRSRSPGR CCCCCCCCCCCCCCC	35.54	30576142
84	Phosphorylation	GSRSRSRSRSPGRPP CCCCCCCCCCCCCCC	38.05	22167270
86	Phosphorylation	RSRSRSRSPGRPPKS CCCCCCCCCCCCCHH	32.71	30266825
93	Phosphorylation	SPGRPPKSARRSASA CCCCCCHHHHHHCCH	32.55	30576142
97	Phosphorylation	PPKSARRSASASHQA CCHHHHHHCCHHHHH	22.48	22167270
99	Phosphorylation	KSARRSASASHQADI HHHHHHCCHHHHHHH	31.39	22167270
101	Phosphorylation	ARRSASASHQADIKE HHHHCCHHHHHHHHH	17.40	23927012
107	Acetylation	ASHQADIKEARREVE HHHHHHHHHHHHHCC	45.96	7672315
107	Ubiquitination	ASHQADIKEARREVE HHHHHHHHHHHHHCC	45.96	23000965
107	2-Hydroxyisobutyrylation	ASHQADIKEARREVE HHHHHHHHHHHHHCC	45.96	-
116	Ubiquitination	ARREVEVKLTPLILK HHHHCCEEEEEEEEC	32.89	22817900
118	Phosphorylation	REVEVKLTPLILKPF HHCCEEEEEEEECCC	15.44	30266825
123	Ubiquitination	KLTPLILKPFGNSIS EEEEEEECCCCCCHH	31.16	23000965
123	Methylation	KLTPLILKPFGNSIS EEEEEEECCCCCCHH	31.16	70991
123	Acetylation	KLTPLILKPFGNSIS EEEEEEECCCCCCHH	31.16	23236377
128	Phosphorylation	ILKPFGNSISRYNGE EECCCCCCHHHCCCC	23.48	30266825
130	Phosphorylation	KPFGNSISRYNGEPE CCCCCCHHHCCCCHH	28.65	30266825
132	Phosphorylation	FGNSISRYNGEPEHI CCCCHHHCCCCHHHH	22.26	26074081
147	Ubiquitination	ERNDAPHKNTQEKFS CCCCCCCCCHHHCCC	61.71	29967540
154	Phosphorylation	KNTQEKFSLSQESSY CCHHHCCCCCHHHHH	37.87	30576142
156	Phosphorylation	TQEKFSLSQESSYIA HHHCCCCCHHHHHHH	30.61	30108239
159	Phosphorylation	KFSLSQESSYIATQY CCCCCHHHHHHHHHC	22.32	28152594
160	Phosphorylation	FSLSQESSYIATQYS CCCCHHHHHHHHHCC	21.58	28152594
161	Phosphorylation	SLSQESSYIATQYSL CCCHHHHHHHHHCCC	12.12	28152594
164	Phosphorylation	QESSYIATQYSLRPR HHHHHHHHHCCCCCC	20.62	28152594
166	Phosphorylation	SSYIATQYSLRPRRE HHHHHHHCCCCCCCH	12.81	28152594
167	Phosphorylation	SYIATQYSLRPRREE HHHHHHCCCCCCCHH	14.21	28152594
176	Ubiquitination	RPRREEVKLKEIDSK CCCCHHCCHHCCCCH	58.06	-
178	Ubiquitination	RREEVKLKEIDSKEE CCHHCCHHCCCCHHH	47.08	27667366
182	Phosphorylation	VKLKEIDSKEEKYVA CCHHCCCCHHHHHHH	47.86	30108239
183	Acetylation	KLKEIDSKEEKYVAK CHHCCCCHHHHHHHH	67.17	23749302
183	Ubiquitination	KLKEIDSKEEKYVAK CHHCCCCHHHHHHHH	67.17	33845483
186	Ubiquitination	EIDSKEEKYVAKELA CCCCHHHHHHHHHHH	46.23	23000965
187	Phosphorylation	IDSKEEKYVAKELAV CCCHHHHHHHHHHHH	14.66	-
190	Acetylation	KEEKYVAKELAVRTF HHHHHHHHHHHHCEE	43.12	19608861
190	Ubiquitination	KEEKYVAKELAVRTF HHHHHHHHHHHHCEE	43.12	23000965
190	2-Hydroxyisobutyrylation	KEEKYVAKELAVRTF HHHHHHHHHHHHCEE	43.12	-
196	Phosphorylation	AKELAVRTFEVTPIR HHHHHHCEEEECEEE	19.97	30266825
200	Phosphorylation	AVRTFEVTPIRAKDL HHCEEEECEEEHHHC	13.05	30266825
284	Phosphorylation	IGKVVEGTPLIDGRR CCCCCCCCCCCCCCE	11.04	-
357	Phosphorylation	KAPRNDLSPASSGNA CCCCCCCCCCCCCCC	22.68	21712546
360	Phosphorylation	RNDLSPASSGNAVYD CCCCCCCCCCCCCEE	42.01	21712546
361	Phosphorylation	NDLSPASSGNAVYDF CCCCCCCCCCCCEEE	37.87	21712546
366	Phosphorylation	ASSGNAVYDFFIGRE CCCCCCCEEEEECCC	12.48	27642862
380	Phosphorylation	ELNPRIGTFDLKYFC CCCCCCCEECHHHHH	16.17	-
385	Phosphorylation	IGTFDLKYFCELRPG CCEECHHHHHHCCCH	22.28	-
466	Ubiquitination	GDLVWVPFIYSFQAF CCEEEHHHEEEEEEE	6.24	24816145
498	Phosphorylation	IVLKLCGYVIFRGAN HHHHHHCHHHHCCCC	6.86	30108239
508	Ubiquitination	FRGANSQKNAFRKNP HCCCCHHHCCCCCCC	50.49	24816145
516	Phosphorylation	NAFRKNPSDPKLAHL CCCCCCCCCHHHHHC	75.77	29214152
519	Ubiquitination	RKNPSDPKLAHLKTI CCCCCCHHHHHCEEE	64.40	29967540
524	Ubiquitination	DPKLAHLKTIHTSTG CHHHHHCEEEECCCC	35.25	32015554
525	Phosphorylation	PKLAHLKTIHTSTGK HHHHHCEEEECCCCC	25.09	27080861
528	Phosphorylation	AHLKTIHTSTGKNLL HHCEEEECCCCCCEE	24.92	27080861
530	Phosphorylation	LKTIHTSTGKNLLVS CEEEECCCCCCEEEE	54.02	27080861
532	Ubiquitination	TIHTSTGKNLLVSGW EEECCCCCCEEEECE	44.50	-
559	Ubiquitination	LIMALAWSLPCGFNH HHHHHHHHCCCCCHH	19.47	23000965
593	Acetylation	RDEYHCKKKYGVAWE HHHHHHHCHHCCCHH	57.53	25953088
593	Ubiquitination	RDEYHCKKKYGVAWE HHHHHHHCHHCCCHH	57.53	29967540
594	Ubiquitination	DEYHCKKKYGVAWEK HHHHHHCHHCCCHHH	32.50	19608861
594	Malonylation	DEYHCKKKYGVAWEK HHHHHHCHHCCCHHH	32.50	26320211
594	Acetylation	DEYHCKKKYGVAWEK HHHHHHCHHCCCHHH	32.50	19608861
594	2-Hydroxyisobutyrylation	DEYHCKKKYGVAWEK HHHHHHCHHCCCHHH	32.50	-
601	Ubiquitination	KYGVAWEKYCQRVPY HHCCCHHHHHHCCCC	40.39	23000965
601	Methylation	KYGVAWEKYCQRVPY HHCCCHHHHHHCCCC	40.39	19608861
601	Malonylation	KYGVAWEKYCQRVPY HHCCCHHHHHHCCCC	40.39	26320211
601	Acetylation	KYGVAWEKYCQRVPY HHCCCHHHHHHCCCC	40.39	19608861

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
71	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
86	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBX3_HUMAN	CBX3	physical	8663349
CBX5_HUMAN	CBX5	physical	8663349
MECP2_HUMAN	MECP2	physical	19331822
CBX5_HUMAN	CBX5	physical	15882967
H31_HUMAN	HIST1H3A	physical	22052904
MD2BP_HUMAN	MAD2L1BP	physical	28514442
ZN579_HUMAN	ZNF579	physical	28514442
CHTOP_HUMAN	CHTOP	physical	28514442
PSMD3_HUMAN	PSMD3	physical	28031328

Drug and Disease Associations

Kegg Disease
H00234	Pelger-Huet anomaly
H00447	HEM skeletal dysplasia; Greenberg dysplasia
H01133	Reynolds syndrome
OMIM Disease
169400	Pelger-Huet anomaly (PHA)
215140	Greenberg dysplasia (GRBGD)
613471	Reynolds syndrome (REYNS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LBR_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-55; LYS-190; LYS-594 ANDLYS-601, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Temporal control of nuclear envelope assembly by phosphorylation oflamin B receptor."; Tseng L.C., Chen R.H.; Mol. Biol. Cell 22:3306-3317(2011). Cited for: PHOSPHORYLATION AT SER-71 AND SER-86 BY CDK1.	21795390 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.	17924679 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118, AND MASSSPECTROMETRY.	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-118, AND MASSSPECTROMETRY.	18669648 [Abstract]