dbPTM

LSM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LSM2_HUMAN
UniProt AC	Q9Y333
Protein Name	U6 snRNA-associated Sm-like protein LSm2
Gene Name	LSM2
Organism	Homo sapiens (Human).
Sequence Length	95
Subcellular Localization	Nucleus .
Protein Description	Binds specifically to the 3'-terminal U-tract of U6 snRNA. May be involved in pre-mRNA splicing..
Protein Sequence	MLFYSFFKSLVGKDVVVELKNDLSICGTLHSVDQYLNIKLTDISVTDPEKYPHMLSVKNCFIRGSVVRYVQLPADEVDTQLLQDAARKEALQQKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MLFYSFFKSLV ----CCCHHHHHHHH	10.70	25839225
5	Phosphorylation	---MLFYSFFKSLVG ---CCCHHHHHHHHC	19.51	29083192
8	Ubiquitination	MLFYSFFKSLVGKDV CCCHHHHHHHHCCHH	40.65	-
9	Phosphorylation	LFYSFFKSLVGKDVV CCHHHHHHHHCCHHE	24.11	29083192
35	Phosphorylation	TLHSVDQYLNIKLTD CCCCHHHHHCEEEEE	9.39	22817900
41	Phosphorylation	QYLNIKLTDISVTDP HHHCEEEEEEECCCH	26.70	20068231
44	Phosphorylation	NIKLTDISVTDPEKY CEEEEEEECCCHHHC	23.05	21253578
46	Phosphorylation	KLTDISVTDPEKYPH EEEEEECCCHHHCCC	38.76	-
50	Acetylation	ISVTDPEKYPHMLSV EECCCHHHCCCEEEE	70.26	26051181
50	Ubiquitination	ISVTDPEKYPHMLSV EECCCHHHCCCEEEE	70.26	29967540
51	Phosphorylation	SVTDPEKYPHMLSVK ECCCHHHCCCEEEEE	9.19	20068231
56	Phosphorylation	EKYPHMLSVKNCFIR HHCCCEEEEECCEEC	24.38	24719451
65	Phosphorylation	KNCFIRGSVVRYVQL ECCEECCCEEEEEEC	13.95	23403867
69	Phosphorylation	IRGSVVRYVQLPADE ECCCEEEEEECCHHH	4.86	27642862
79	Phosphorylation	LPADEVDTQLLQDAA CCHHHHHHHHHHHHH	26.71	17525332
88	Ubiquitination	LLQDAARKEALQQKQ HHHHHHHHHHHHHCC	42.48	33845483
88	2-Hydroxyisobutyrylation	LLQDAARKEALQQKQ HHHHHHHHHHHHHCC	42.48	-
94	Ubiquitination	RKEALQQKQ------ HHHHHHHCC------	45.04	24816145

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
Oops, there are no upstream regulatory protein records of LSM2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LSM2_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 LSM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LSM8_HUMAN	LSM8	physical	15231747
LSM3_HUMAN	LSM3	physical	15231747
LSM7_HUMAN	LSM7	physical	15231747
LSM8_HUMAN	LSM8	physical	14667819
LSM3_HUMAN	LSM3	physical	14667819
LSM7_HUMAN	LSM7	physical	14667819
GBP2_HUMAN	GBP2	physical	16169070
ZBT16_HUMAN	ZBTB16	physical	16169070
ERG28_HUMAN	C14orf1	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
LSM3_HUMAN	LSM3	physical	16169070
LSM3_HUMAN	LSM3	physical	22939629
LSM8_HUMAN	LSM8	physical	22939629
LSM7_HUMAN	LSM7	physical	22939629
LSM4_HUMAN	LSM4	physical	22939629
LSM5_HUMAN	LSM5	physical	22939629
LSM6_HUMAN	LSM6	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
PRP16_HUMAN	DHX38	physical	22939629
RBM8A_HUMAN	RBM8A	physical	22939629
TRI56_HUMAN	TRIM56	physical	22939629
PYRD1_HUMAN	PYROXD1	physical	22939629
RSMB_HUMAN	SNRPB	physical	22365833
SMD2_HUMAN	SNRPD2	physical	22365833
SF3B2_HUMAN	SF3B2	physical	22365833
LSM3_HUMAN	LSM3	physical	22365833
LSM6_HUMAN	LSM6	physical	22365833
LSM7_HUMAN	LSM7	physical	22365833
LSM8_HUMAN	LSM8	physical	22365833
PRCC_HUMAN	PRCC	physical	22365833
ICLN_HUMAN	CLNS1A	physical	22365833
RUXE_HUMAN	SNRPE	physical	15231747
ZN408_HUMAN	ZNF408	physical	15231747
DNJA1_HUMAN	DNAJA1	physical	15231747
SMD2_HUMAN	SNRPD2	physical	15231747
EXOSX_HUMAN	EXOSC10	physical	15231747
LSM1_HUMAN	LSM1	physical	15231747
RAB1B_HUMAN	RAB1B	physical	22863883
RINI_HUMAN	RNH1	physical	22863883
LNX1_HUMAN	LNX1	physical	25416956
LSM1_HUMAN	LSM1	physical	26344197
LSM3_HUMAN	LSM3	physical	26344197
LSM6_HUMAN	LSM6	physical	26344197
LSM7_HUMAN	LSM7	physical	26344197
LSMD1_HUMAN	NAA38	physical	26344197

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.

Regulatory Network of LSM2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND MASSSPECTROMETRY.	15592455 [Abstract]