dbPTM

GEMI2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GEMI2_HUMAN
UniProt AC	O14893
Protein Name	Gem-associated protein 2
Gene Name	GEMIN2
Organism	Homo sapiens (Human).
Sequence Length	280
Subcellular Localization	Nucleus, gem. Cytoplasm. Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs. Also found in the cytoplasm.
Protein Description	The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus..
Protein Sequence	MRRAELAGLKTMAWVPAESAVEELMPRLLPVEPCDLTEGFDPSVPPRTPQEYLRRVQIEAAQCPDVVVAQIDPKKLKRKQSVNISLSGCQPAPEGYSPTLQWQQQQVAQFSTVRQNVNKHRSHWKSQQLDSNVTMPKSEDEEGWKKFCLGEKLCADGAVGPATNESPGIDYVQIGFPPLLSIVSRMNQATVTSVLEYLSNWFGERDFTPELGRWLYALLACLEKPLLPEAHSLIRQLARRCSEVRLLVDSKDDERVPALNLLICLVSRYFDQRDLADEPS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	AELAGLKTMAWVPAE HHHCCCCEEEEEEHH	19.71	29255136
19	Phosphorylation	MAWVPAESAVEELMP EEEEEHHHHHHHHHH	39.46	24719451
34	Glutathionylation	RLLPVEPCDLTEGFD HHCCCCCCCCCCCCC	4.19	22555962
37	Phosphorylation	PVEPCDLTEGFDPSV CCCCCCCCCCCCCCC	22.32	22210691
43	Phosphorylation	LTEGFDPSVPPRTPQ CCCCCCCCCCCCCHH	49.45	22210691
48	Phosphorylation	DPSVPPRTPQEYLRR CCCCCCCCHHHHHHH	34.79	25159151
52	Phosphorylation	PPRTPQEYLRRVQIE CCCCHHHHHHHHHHH	10.56	29978859
54	Methylation	RTPQEYLRRVQIEAA CCHHHHHHHHHHHHH	35.50	115916985
63	Glutathionylation	VQIEAAQCPDVVVAQ HHHHHHHCCCEEEEE	2.39	22555962
74	Ubiquitination	VVAQIDPKKLKRKQS EEEECCHHHCCCCCC	67.97	29967540
75	Ubiquitination	VAQIDPKKLKRKQSV EEECCHHHCCCCCCE	65.71	-
81	Phosphorylation	KKLKRKQSVNISLSG HHCCCCCCEEEEECC	21.84	28450419
85	Phosphorylation	RKQSVNISLSGCQPA CCCCEEEEECCCCCC	15.98	28450419
87	Phosphorylation	QSVNISLSGCQPAPE CCEEEEECCCCCCCC	30.63	28450419
96	Phosphorylation	CQPAPEGYSPTLQWQ CCCCCCCCCCCHHHH	15.15	28450419
97	Phosphorylation	QPAPEGYSPTLQWQQ CCCCCCCCCCHHHHH	23.43	28450419
99	Phosphorylation	APEGYSPTLQWQQQQ CCCCCCCCHHHHHHH	26.16	28450419
125	Ubiquitination	NKHRSHWKSQQLDSN HHCHHHHHHHCCCCC	32.72	29967540
125	Methylation	NKHRSHWKSQQLDSN HHCHHHHHHHCCCCC	32.72	115981197
131	Phosphorylation	WKSQQLDSNVTMPKS HHHHCCCCCCCCCCC	41.62	20068231
145	Acetylation	SEDEEGWKKFCLGEK CCCCCHHHHHHHCCC	46.99	26051181
145	Ubiquitination	SEDEEGWKKFCLGEK CCCCCHHHHHHHCCC	46.99	-
146	Ubiquitination	EDEEGWKKFCLGEKL CCCCHHHHHHHCCCC	34.50	-
163	Phosphorylation	DGAVGPATNESPGID CCCCCCCCCCCCCCC	42.52	24732914
166	Phosphorylation	VGPATNESPGIDYVQ CCCCCCCCCCCCEEE	30.42	28348404
171	Phosphorylation	NESPGIDYVQIGFPP CCCCCCCEEEECCHH	7.73	28464451
197	Phosphorylation	TVTSVLEYLSNWFGE HHHHHHHHHHHHHCC	15.98	30257219
199	Phosphorylation	TSVLEYLSNWFGERD HHHHHHHHHHHCCCC	30.98	30257219
208	Phosphorylation	WFGERDFTPELGRWL HHCCCCCCHHHHHHH	21.83	30257219
280	Phosphorylation	RDLADEPS------- HHHCCCCC-------	51.29	23312004

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 GEMI2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GEMI2_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 GEMI2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAD50_HUMAN	RAD50	physical	20403813
RSMN_HUMAN	SNRPN	physical	18984161
GEMI5_HUMAN	GEMIN5	physical	23221635
DDX20_HUMAN	DDX20	physical	23221635
GEMI4_HUMAN	GEMIN4	physical	23221635
GEMI8_HUMAN	GEMIN8	physical	23221635
GEMI6_HUMAN	GEMIN6	physical	23221635
GEMI7_HUMAN	GEMIN7	physical	23221635
STRAP_HUMAN	STRAP	physical	23221635
SMN_HUMAN	SMN1	physical	23221635
STRN4_HUMAN	STRN4	physical	28514442
RU17_HUMAN	SNRNP70	physical	28514442
GEMI4_HUMAN	GEMIN4	physical	28514442
GEMI7_HUMAN	GEMIN7	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
SMD1_HUMAN	SNRPD1	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
NUFP1_HUMAN	NUFIP1	physical	26275778

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 GEMI2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-171, AND MASSSPECTROMETRY.	19413330 [Abstract]