LAMC_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LAMC_DROME
• UniProt AC: Q03427
• Protein Name: Lamin-C
• Gene Name: LamC
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 621
• Subcellular Localization: Nucleus . Nucleus lamina . Nuclear periphery (PubMed:7593280). In premeiotic nuclei of primary spermatocytes, localization to the nuclear lamina depends on type-B lamin Lam. In spermatocytes, temporarily depleted between anaphase I and telophase I, a
• 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 (By similarity). In spermatocytes, regulates cytokinesis during meiosis. [PubMed: 27402967]
• Protein Sequence: MSARRVTLNTRVSRASTSTPVGGASTSSRVGATSPTSPTRTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHTQELTETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAAYDKLLCGEERRLNIESPGRPTTDSGISSNGSHLTASASSRSGRVTPSGRRSATPGISGSSAVKRRRTVIDESEDRTLSEYSVNAAAKGDLEIIEADVEGRFIKLHNKGTEEINLTGWQLTRIAGDEELAFKFSRGSKVLGGASVTIWSVDAGTAHDPPNNLVMKKKWPVANSMRSVLANADKEDVASYDRVRANVSSHTSRHRSSGTPSTGFTLGSGAGSTGVRSLFSLLF

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
13	Phosphorylation	VTLNTRVSRASTSTP EEECHHCCCCCCCCC	20.88	28490779
16	Phosphorylation	NTRVSRASTSTPVGG CHHCCCCCCCCCCCC	23.06	28490779
17	Phosphorylation	TRVSRASTSTPVGGA HHCCCCCCCCCCCCC	35.32	28490779
18	Phosphorylation	RVSRASTSTPVGGAS HCCCCCCCCCCCCCC	28.37	28490779
19	Phosphorylation	VSRASTSTPVGGAST CCCCCCCCCCCCCCC	23.29	28490779
25	Phosphorylation	STPVGGASTSSRVGA CCCCCCCCCCCCCCC	31.90	25749252
27	Phosphorylation	PVGGASTSSRVGATS CCCCCCCCCCCCCCC	17.41	25749252
33	Phosphorylation	TSSRVGATSPTSPTR CCCCCCCCCCCCCCC	29.34	19429919
34	Phosphorylation	SSRVGATSPTSPTRT CCCCCCCCCCCCCCC	26.16	19429919
36	Phosphorylation	RVGATSPTSPTRTSR CCCCCCCCCCCCCCC	47.29	22668510
37	Phosphorylation	VGATSPTSPTRTSRQ CCCCCCCCCCCCCCH	27.88	19429919
39	Phosphorylation	ATSPTSPTRTSRQQE CCCCCCCCCCCCHHH	46.47	19429919
249	Phosphorylation	SEIDGRLSRQYEAKL HEECHHHHHHHHHHH	18.90	25749252
406	Phosphorylation	ERRLNIESPGRPTTD CCCCCCCCCCCCCCC	28.94	22817900
431	Phosphorylation	TASASSRSGRVTPSG EEECCCCCCCCCCCC	32.66	25749252
435	Phosphorylation	SSRSGRVTPSGRRSA CCCCCCCCCCCCCCC	15.46	22817900
437	Phosphorylation	RSGRVTPSGRRSATP CCCCCCCCCCCCCCC	35.25	25749252
441	Phosphorylation	VTPSGRRSATPGISG CCCCCCCCCCCCCCC	34.82	19429919
443	Phosphorylation	PSGRRSATPGISGSS CCCCCCCCCCCCCCH	24.24	19429919
447	Phosphorylation	RSATPGISGSSAVKR CCCCCCCCCCHHHHH	38.24	28490779
449	Phosphorylation	ATPGISGSSAVKRRR CCCCCCCCHHHHHCC	14.34	28490779
450	Phosphorylation	TPGISGSSAVKRRRT CCCCCCCHHHHHCCE	40.38	28490779
457	Phosphorylation	SAVKRRRTVIDESED HHHHHCCEEECCCCC	21.72	21082442
587	Phosphorylation	RVRANVSSHTSRHRS HHHHHCCCCCCCCCC	26.88	25749252
594	Phosphorylation	SHTSRHRSSGTPSTG CCCCCCCCCCCCCCC	27.31	28490779
595	Phosphorylation	HTSRHRSSGTPSTGF CCCCCCCCCCCCCCE	46.79	28490779
597	Phosphorylation	SRHRSSGTPSTGFTL CCCCCCCCCCCCEEC	18.93	28490779
599	Phosphorylation	HRSSGTPSTGFTLGS CCCCCCCCCCEECCC	40.79	28490779

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LAMC_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LAMC_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of LAMC_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TNG6_DROME	Tango6	physical	14605208
LAM0_DROME	Lam	physical	19855837
LAMC_DROME	LamC	physical	19855837

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-406; SER-441 ANDTHR-443, AND MASS SPECTROMETRY.
PubMed: 18327897