LSM6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LSM6_HUMAN
• UniProt AC: P62312
• Protein Name: U6 snRNA-associated Sm-like protein LSm6
• Gene Name: LSM6
• Organism: Homo sapiens (Human).
• Sequence Length: 80
• Subcellular Localization: Cytoplasm . Nucleus.
• Protein Description: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity)..
• Protein Sequence: MSLRKQTPSDFLKQIIGRPVVVKLNSGVDYRGVLACLDGYMNIALEQTEEYVNGQLKNKYGDAFIRGNNVLYISTQKRRM

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
5	Sumoylation	---MSLRKQTPSDFL ---CCCCCCCHHHHH	64.91	-
5	Neddylation	---MSLRKQTPSDFL ---CCCCCCCHHHHH	64.91	32015554
5	Ubiquitination	---MSLRKQTPSDFL ---CCCCCCCHHHHH	64.91	27667366
5	Sumoylation	---MSLRKQTPSDFL ---CCCCCCCHHHHH	64.91	-
7	Phosphorylation	-MSLRKQTPSDFLKQ -CCCCCCCHHHHHHH	28.00	20068231
9	Phosphorylation	SLRKQTPSDFLKQII CCCCCCHHHHHHHHH	44.36	20068231
13	Ubiquitination	QTPSDFLKQIIGRPV CCHHHHHHHHHCCCE	39.17	21890473
13	Ubiquitination	QTPSDFLKQIIGRPV CCHHHHHHHHHCCCE	39.17	21890473
13	Acetylation	QTPSDFLKQIIGRPV CCHHHHHHHHHCCCE	39.17	26051181
23	Acetylation	IGRPVVVKLNSGVDY HCCCEEEECCCCCCH	30.27	26051181
23	Ubiquitination	IGRPVVVKLNSGVDY HCCCEEEECCCCCCH	30.27	22817900
23	Ubiquitination	IGRPVVVKLNSGVDY HCCCEEEECCCCCCH	30.27	21890473
59	Ubiquitination	VNGQLKNKYGDAFIR HHCCCCCCCCCEEEC	49.36	19608861
59	Acetylation	VNGQLKNKYGDAFIR HHCCCCCCCCCEEEC	49.36	19608861
66	Methylation	KYGDAFIRGNNVLYI CCCCEEECCCCEEEE	35.02	115482381
72	Phosphorylation	IRGNNVLYISTQKRR ECCCCEEEEEECCCC	6.64	28152594
74	Phosphorylation	GNNVLYISTQKRRM- CCCEEEEEECCCCC-	15.95	28152594
75	Phosphorylation	NNVLYISTQKRRM-- CCEEEEEECCCCC--	28.66	28152594
77	Acetylation	VLYISTQKRRM---- EEEEEECCCCC----	41.90	25953088

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

Oops, there are no upstream regulatory protein records of LSM6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LSM6_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of LSM6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMD2_HUMAN	SNRPD2	physical	15231747
MCRS1_HUMAN	MCRS1	physical	15231747
DPOD2_HUMAN	POLD2	physical	15231747
A4_HUMAN	APP	physical	21832049
LSM8_HUMAN	LSM8	physical	22939629
LSM7_HUMAN	LSM7	physical	22939629
SNAG_HUMAN	NAPG	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22365833
RUXF_HUMAN	SNRPF	physical	22365833
LSM2_HUMAN	LSM2	physical	22365833
LSM5_HUMAN	LSM5	physical	22365833
LSM7_HUMAN	LSM7	physical	22365833
ICLN_HUMAN	CLNS1A	physical	22365833
LSM5_HUMAN	LSM5	physical	15231747
LSM7_HUMAN	LSM7	physical	15231747
LSM3_HUMAN	LSM3	physical	15231747
LSM1_HUMAN	LSM1	physical	15231747
LSM8_HUMAN	LSM8	physical	15231747
LSM5_HUMAN	LSM5	physical	25416956
LSM3_HUMAN	LSM3	physical	25416956
HERC4_HUMAN	HERC4	physical	26344197
LSM7_HUMAN	LSM7	physical	26344197
LSMD1_HUMAN	NAA38	physical	26344197
PATL1_HUMAN	PATL1	physical	28514442
LSM5_HUMAN	LSM5	physical	28514442
STPAP_HUMAN	TUT1	physical	28514442
AKA7A_HUMAN	AKAP7	physical	28514442
AKA7G_HUMAN	AKAP7	physical	28514442
LSM1_HUMAN	LSM1	physical	28514442
ICLN_HUMAN	CLNS1A	physical	28514442
PRPF3_HUMAN	PRPF3	physical	28514442
RIOK1_HUMAN	RIOK1	physical	28514442
SART3_HUMAN	SART3	physical	28514442
LSM2_HUMAN	LSM2	physical	28514442
LSM8_HUMAN	LSM8	physical	28514442
COPRS_HUMAN	COPRS	physical	28514442
MEPCE_HUMAN	MEPCE	physical	28514442
LSM4_HUMAN	LSM4	physical	28514442
WBP4_HUMAN	WBP4	physical	28514442
PRP4_HUMAN	PRPF4	physical	28514442
ANM5_HUMAN	PRMT5	physical	28514442
LSM7_HUMAN	LSM7	physical	28514442
ZN511_HUMAN	ZNF511	physical	28514442
LSM10_HUMAN	LSM10	physical	28514442
RUXE_HUMAN	SNRPE	physical	28514442
LSM3_HUMAN	LSM3	physical	28514442
SMD1_HUMAN	SNRPD1	physical	28514442
SMD2_HUMAN	SNRPD2	physical	28514442
MEP50_HUMAN	WDR77	physical	28514442
PRP31_HUMAN	PRPF31	physical	28514442
GEMI2_HUMAN	GEMIN2	physical	28514442

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"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-59, AND MASS SPECTROMETRY.
PubMed: 19608861