LSM3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LSM3_HUMAN
• UniProt AC: P62310
• Protein Name: U6 snRNA-associated Sm-like protein LSm3
• Gene Name: LSM3
• Organism: Homo sapiens (Human).
• Sequence Length: 102
• Subcellular Localization: Nucleus .
• Protein Description: Binds specifically to the 3'-terminal U-tract of U6 snRNA..
• Protein Sequence: MADDVDQQQTTNTVEEPLDLIRLSLDERIYVKMRNDRELRGRLHAYDQHLNMILGDVEETVTTIEIDEETYEEIYKSTKRNIPMLFVRGDGVVLVAPPLRVG

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	------MADDVDQQQ ------CCCCCCCHH	23.01	22814378
10	Phosphorylation	DDVDQQQTTNTVEEP CCCCCHHHCCCCCCC	20.06	19664995
11	Phosphorylation	DVDQQQTTNTVEEPL CCCCHHHCCCCCCCH	25.26	30377224
13	Phosphorylation	DQQQTTNTVEEPLDL CCHHHCCCCCCCHHH	27.48	30377224
24	Phosphorylation	PLDLIRLSLDERIYV CHHHHHHCCCCCEEE	24.75	21815630
28	Methylation	IRLSLDERIYVKMRN HHHCCCCCEEEEECC	25.79	115482369
32	Ubiquitination	LDERIYVKMRNDREL CCCCEEEEECCCHHH	18.38	-
71	Phosphorylation	IEIDEETYEEIYKST EEECHHHHHHHHHHC	18.16	-

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

Oops, there are no upstream regulatory protein records of LSM3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LSM3_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 LSM3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RUXE_HUMAN	SNRPE	physical	15231747
SMD3_HUMAN	SNRPD3	physical	15231747
LSM7_HUMAN	LSM7	physical	15231747
XRN2_HUMAN	XRN2	physical	15231747
LSM10_HUMAN	LSM10	physical	15231747
LSM2_HUMAN	LSM2	physical	16189514
LSM10_HUMAN	LSM10	physical	16189514
GDF9_HUMAN	GDF9	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
UT14A_HUMAN	UTP14A	physical	16169070
LSM2_HUMAN	LSM2	physical	16169070
LSM6_HUMAN	LSM6	physical	22939629
LSM7_HUMAN	LSM7	physical	22939629
LSM4_HUMAN	LSM4	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22365833
SMD3_HUMAN	SNRPD3	physical	22365833
RUXG_HUMAN	SNRPG	physical	22365833
SF3B2_HUMAN	SF3B2	physical	22365833
YBOX1_HUMAN	YBX1	physical	22365833
LSM2_HUMAN	LSM2	physical	22365833
LSM7_HUMAN	LSM7	physical	22365833
LSM8_HUMAN	LSM8	physical	22365833
WDR83_HUMAN	WDR83	physical	22365833
THOC5_HUMAN	THOC5	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
ICLN_HUMAN	CLNS1A	physical	22365833
LSM10_HUMAN	LSM10	physical	19060904
LSM8_HUMAN	LSM8	physical	21988832
LSM2_HUMAN	LSM2	physical	15231747
LSM8_HUMAN	LSM8	physical	15231747
XPC_HUMAN	XPC	physical	15231747
CEP95_HUMAN	CEP95	physical	15231747
LSM1_HUMAN	LSM1	physical	15231747
LSM5_HUMAN	LSM5	physical	15231747
LSM6_HUMAN	LSM6	physical	15231747
LSM2_HUMAN	LSM2	physical	25416956
LSM1_HUMAN	LSM1	physical	26344197
LSM6_HUMAN	LSM6	physical	26344197
LSM7_HUMAN	LSM7	physical	26344197
LSMD1_HUMAN	NAA38	physical	26344197
LSM2_HUMAN	LSM2	physical	21516116

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

"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, AND MASS SPECTROMETRY.
PubMed: 19413330