GEMI6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GEMI6_HUMAN
• UniProt AC: Q8WXD5
• Protein Name: Gem-associated protein 6
• Gene Name: GEMIN6
• Organism: Homo sapiens (Human).
• Sequence Length: 167
• Subcellular Localization: Nucleus, nucleoplasm . Nucleus, gem . Cytoplasm . Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. 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: MSEWMKKGPLEWQDYIYKEVRVTASEKNEYKGWVLTTDPVSANIVLVNFLEDGSMSVTGIMGHAVQTVETMNEGDHRVREKLMHLFTSGDCKAYSPEDLEERKNSLKKWLEKNHIPITEQGDAPRTLCVAGVLTIDPPYGPENCSSSNEIILSRVQDLIEGHLTASQ

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
6	Ubiquitination	--MSEWMKKGPLEWQ --CCHHHHCCCCCHH	56.50	-
7	Ubiquitination	-MSEWMKKGPLEWQD -CCHHHHCCCCCHHH	50.05	29967540
18	Acetylation	EWQDYIYKEVRVTAS CHHHHEEEEEEECCC	39.93	26051181
27	Ubiquitination	VRVTASEKNEYKGWV EEECCCCCCCCCEEE	53.21	21906983
31	Ubiquitination	ASEKNEYKGWVLTTD CCCCCCCCEEEEECC	39.87	22817900
92	Ubiquitination	LFTSGDCKAYSPEDL HHHCCCCCCCCHHHH	55.91	32015554
94	Phosphorylation	TSGDCKAYSPEDLEE HCCCCCCCCHHHHHH	15.39	29978859
95	Phosphorylation	SGDCKAYSPEDLEER CCCCCCCCHHHHHHH	27.03	25159151
103	Ubiquitination	PEDLEERKNSLKKWL HHHHHHHHHHHHHHH	54.92	22817900
107	Ubiquitination	EERKNSLKKWLEKNH HHHHHHHHHHHHHCC	41.55	23000965
108	Ubiquitination	ERKNSLKKWLEKNHI HHHHHHHHHHHHCCC	63.40	23000965
112	Ubiquitination	SLKKWLEKNHIPITE HHHHHHHHCCCCCCC	52.21	23000965
164	Phosphorylation	DLIEGHLTASQ---- HHHHHCCCCCC----	20.70	22210691
166	Phosphorylation	IEGHLTASQ------ HHHCCCCCC------	31.05	25159151

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

Oops, there are no upstream regulatory protein records of GEMI6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GEMI6_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 GEMI6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMN_HUMAN	SMN1	physical	11748230
GEMI2_HUMAN	GEMIN2	physical	11748230
DDX20_HUMAN	DDX20	physical	11748230
GEMI4_HUMAN	GEMIN4	physical	11748230
GEMI8_HUMAN	GEMIN8	physical	28514442
STRAP_HUMAN	STRAP	physical	28514442
RU17_HUMAN	SNRNP70	physical	28514442
GEMI2_HUMAN	GEMIN2	physical	28514442
GEMI4_HUMAN	GEMIN4	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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.
PubMed: 18691976