LSM12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LSM12_HUMAN
• UniProt AC: Q3MHD2
• Protein Name: Protein LSM12 homolog
• Gene Name: LSM12
• Organism: Homo sapiens (Human).
• Sequence Length: 195
• Protein Sequence: MAAPPGEYFSVGSQVSCRTCQEQRLQGEVVAFDYQSKMLALKCPSSSGKPNHADILLINLQYVSEVEIINDRTETPPPLASLNVSKLASKARTEKEEKLSQAYAISAGVSLEGQQLFQTIHKTIKDCKWQEKNIVVMEEVVITPPYQVENCKGKEGSALSHVRKIVEKHFRDVESQKILQRSQAQQPQKEAALSS

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	------MAAPPGEYF ------CCCCCCCCE	28.77	22814378
8	Phosphorylation	MAAPPGEYFSVGSQV CCCCCCCCEECCCEE	13.68	26552605
8	Nitration	MAAPPGEYFSVGSQV CCCCCCCCEECCCEE	13.68	-
10	Phosphorylation	APPGEYFSVGSQVSC CCCCCCEECCCEEEC	25.35	26552605
13	Phosphorylation	GEYFSVGSQVSCRTC CCCEECCCEEECCCC	25.83	26552605
16	Phosphorylation	FSVGSQVSCRTCQEQ EECCCEEECCCCHHH	7.11	25850435
34	Phosphorylation	GEVVAFDYQSKMLAL CEEEEEECCCCEEEE	14.29	28152594
36	Phosphorylation	VVAFDYQSKMLALKC EEEEECCCCEEEEEC	17.50	28152594
73	Phosphorylation	VEIINDRTETPPPLA EEEECCCCCCCCCCH	47.26	30266825
75	Phosphorylation	IINDRTETPPPLASL EECCCCCCCCCCHHC	40.25	29255136
78 (in isoform 2)	Phosphorylation	-	41.59	21406692
81	Phosphorylation	ETPPPLASLNVSKLA CCCCCCHHCCHHHHH	28.32	23927012
85	Phosphorylation	PLASLNVSKLASKAR CCHHCCHHHHHHHHC	22.37	23927012
86	Ubiquitination	LASLNVSKLASKART CHHCCHHHHHHHHCH	43.73	27667366
86 (in isoform 1)	Ubiquitination	-	43.73	21890473
86	Acetylation	LASLNVSKLASKART CHHCCHHHHHHHHCH	43.73	25953088
89	Phosphorylation	LNVSKLASKARTEKE CCHHHHHHHHCHHHH	36.97	26074081
89 (in isoform 2)	Ubiquitination	-	36.97	21890473
90	Ubiquitination	NVSKLASKARTEKEE CHHHHHHHHCHHHHH	35.96	22817900
93	Phosphorylation	KLASKARTEKEEKLS HHHHHHCHHHHHHHH	57.16	26074081
103	Phosphorylation	EEKLSQAYAISAGVS HHHHHHHHHHHCCCC	9.24	-
119	Ubiquitination	EGQQLFQTIHKTIKD CHHHHHHHHHHHHHH	20.09	33845483
154	Ubiquitination	QVENCKGKEGSALSH CCCCCCCCCCCHHHH	44.38	29967540
154	Sumoylation	QVENCKGKEGSALSH CCCCCCCCCCCHHHH	44.38	-
154	Acetylation	QVENCKGKEGSALSH CCCCCCCCCCCHHHH	44.38	26051181
154	Sumoylation	QVENCKGKEGSALSH CCCCCCCCCCCHHHH	44.38	-
157 (in isoform 2)	Ubiquitination	-	27.42	-
157	Phosphorylation	NCKGKEGSALSHVRK CCCCCCCCHHHHHHH	27.42	25159151
160	Phosphorylation	GKEGSALSHVRKIVE CCCCCHHHHHHHHHH	21.47	25159151
168	Ubiquitination	HVRKIVEKHFRDVES HHHHHHHHHCCCHHH	36.83	19608861
168	Acetylation	HVRKIVEKHFRDVES HHHHHHHHHCCCHHH	36.83	19608861
177	Ubiquitination	FRDVESQKILQRSQA CCCHHHHHHHHHHHC	55.45	32015554
177	Acetylation	FRDVESQKILQRSQA CCCHHHHHHHHHHHC	55.45	25953088
182	Phosphorylation	SQKILQRSQAQQPQK HHHHHHHHHCCCHHH	19.53	27282143
189 (in isoform 1)	Ubiquitination	-	56.88	21890473
189	Ubiquitination	SQAQQPQKEAALSS- HHCCCHHHHHHHCC-	56.88	22817900
192 (in isoform 2)	Ubiquitination	-	14.74	21890473
194	Phosphorylation	PQKEAALSS------ HHHHHHHCC------	29.31	23911959
195	Phosphorylation	QKEAALSS------- HHHHHHCC-------	45.12	22617229
209	Ubiquitination	--------------------- ---------------------		33845483

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

Oops, there are no upstream regulatory protein records of LSM12_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LSM12_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 LSM12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCBP1_HUMAN	PCBP1	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.

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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-75 AND SER-195, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-168, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-75 AND SER-195, AND MASS SPECTROMETRY.
PubMed: 19413330

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND MASSSPECTROMETRY.
PubMed: 19690332