LMN1_CAEEL - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LMN1_CAEEL
• UniProt AC: Q21443
• Protein Name: Lamin-1
• Gene Name: lmn-1
• Organism: Caenorhabditis elegans.
• Sequence Length: 566
• Subcellular Localization: Nucleus envelope . Nucleus inner membrane ; Lipid-anchor ; Nucleoplasmic side . Remains in the nuclear envelope until late anaphase in early embryos (PubMed:10982402). Depends on mel-28 for nuclear envelope localization after mitosis (PubMed:16950114
• Protein Description: Major component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane. Provides a framework for the nuclear envelope and probably also interacts with chromatin. Essential to maintain the shape and integrity of the nucleus, and for DNA replication. Involved in spatial organization of nuclear pore complexes. It is not a target for ced-3 during apoptosis, suggesting that lamin cleavage is not essential for apoptosis in C.elegans..
• Protein Sequence: MSSRKGTRSSRIVTLERSANSSLSNNGGGDDSFGSTLLETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQVDMTTYAKQINDEYQSKLQDQIEEMRAQFKNNLHQNKTAFEDAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRSELDTLKRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQEAPQNTSVHHVSFSSGGASAQRGVKRRRVVDVNGEDQDIDYLNRRSKLNKETVGPVGIDEVDEEGKWVRVANNSEEEQSIGGYKLVVKAGNKEASFQFSSRMKLAPHASATVWSADAGAVHHPPEVYVMKKQQWPIGDNPSARLEDSEGDTVSSITVEFSESSDPSDPADRCSIM

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
2	Acetylation	------MSSRKGTRS ------CCCCCCCCC	38.56	-
21	Phosphorylation	TLERSANSSLSNNGG EEEECCCCCCCCCCC	32.16	30078680
22	Phosphorylation	LERSANSSLSNNGGG EEECCCCCCCCCCCC	35.31	30078680
32	Phosphorylation	NNGGGDDSFGSTLLE CCCCCCCCHHHHHHH	35.93	30078680
281	Phosphorylation	KTAFEDAYKNKLNAA CHHHHHHHHHHHHHH	27.67	27067626
397	Phosphorylation	TQEAPQNTSVHHVSF CCCCCCCCEEEEEEE	27.21	21082442
398	Phosphorylation	QEAPQNTSVHHVSFS CCCCCCCEEEEEEEC	27.31	21082442
403	Phosphorylation	NTSVHHVSFSSGGAS CCEEEEEEECCCCCH	18.30	28854356
405	Phosphorylation	SVHHVSFSSGGASAQ EEEEEEECCCCCHHH	22.14	21082442
406	Phosphorylation	VHHVSFSSGGASAQR EEEEEECCCCCHHHC	38.96	21082442
410	Phosphorylation	SFSSGGASAQRGVKR EECCCCCHHHCCCCC	28.36	21082442
470	Phosphorylation	NNSEEEQSIGGYKLV CCCHHHHCCCCEEEE	26.87	30078680
486	Phosphorylation	KAGNKEASFQFSSRM EECCCEEEEEECCCC	22.22	19530675
490	Phosphorylation	KEASFQFSSRMKLAP CEEEEEECCCCCCCC	13.27	18806794
491	Phosphorylation	EASFQFSSRMKLAPH EEEEEECCCCCCCCC	37.37	19530675
563	Farnesylation	PSDPADRCSIM---- CCCHHHHCCCC----	3.13	-
563	Methylation	PSDPADRCSIM---- CCCHHHHCCCC----	3.13	-

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

Oops, there are no upstream regulatory protein records of LMN1_CAEEL !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LMN1_CAEEL !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of LMN1_CAEEL !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LMN1_CAEEL	lmn-1	physical	18692475

Drug and Disease Associations

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