GEMI8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GEMI8_HUMAN
• UniProt AC: Q9NWZ8
• Protein Name: Gem-associated protein 8
• Gene Name: GEMIN8
• Organism: Homo sapiens (Human).
• Sequence Length: 242
• Subcellular Localization: Nucleus, gem . Cytoplasm . Found 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: MAAVKASTSKATRPWYSHPVYARYWQHYHQAMAWMQSHHNAYRKAVESCFNLPWYLPSALLPQSSYDNEAAYPQSFYDHHVAWQDYPCSSSHFRRSGQHPRYSSRIQASTKEDQALSKEEEMETESDAEVECDLSNMEITEELRQYFAETERHREERRRQQQLDAERLDSYVNADHDLYCNTRRSVEAPTERPGERRQAEMKRLYGDSAAKIQAMEAAVQLSFDKHCDRKQPKYWPVIPLKF

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
5	Ubiquitination	---MAAVKASTSKAT ---CCCCCCCCCCCC	31.71	-
7	Phosphorylation	-MAAVKASTSKATRP -CCCCCCCCCCCCCC	27.74	30631047
10	Ubiquitination	AVKASTSKATRPWYS CCCCCCCCCCCCCCC	54.59	21890473
10	Ubiquitination	AVKASTSKATRPWYS CCCCCCCCCCCCCCC	54.59	21890473
77	Phosphorylation	AAYPQSFYDHHVAWQ CCCCHHHCCCCCCCC	21.44	-
109	Phosphorylation	YSSRIQASTKEDQAL HHHHHCCCCHHHHHC	24.52	30624053
110	Phosphorylation	SSRIQASTKEDQALS HHHHCCCCHHHHHCC	41.28	30624053
117	Phosphorylation	TKEDQALSKEEEMET CHHHHHCCHHHHCCC	40.82	22617229
124	Phosphorylation	SKEEEMETESDAEVE CHHHHCCCCCCCEEE	39.21	21082442
126	Phosphorylation	EEEMETESDAEVECD HHHCCCCCCCEEEEC	49.92	21082442
135	Phosphorylation	AEVECDLSNMEITEE CEEEECCCCCHHHHH	22.37	30576142
140	Phosphorylation	DLSNMEITEELRQYF CCCCCHHHHHHHHHH	15.31	27251275
170	Phosphorylation	LDAERLDSYVNADHD HCHHHHHHHHCCCCC	35.26	29978859
171	Phosphorylation	DAERLDSYVNADHDL CHHHHHHHHCCCCCC	9.44	29978859
179	Phosphorylation	VNADHDLYCNTRRSV HCCCCCCCCCCCCCC	6.96	28796482
182	Phosphorylation	DHDLYCNTRRSVEAP CCCCCCCCCCCCCCC	24.73	29978859
185	Phosphorylation	LYCNTRRSVEAPTER CCCCCCCCCCCCCCC	22.48	25159151
190	Phosphorylation	RRSVEAPTERPGERR CCCCCCCCCCCCHHH	52.23	25850435
234	Phosphorylation	CDRKQPKYWPVIPLK CCCCCCCCCCCCCCC	22.94	-

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

Oops, there are no upstream regulatory protein records of GEMI8_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GEMI8_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 GEMI8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
STRAP_HUMAN	STRAP	physical	28514442
GEMI7_HUMAN	GEMIN7	physical	28514442
RU17_HUMAN	SNRNP70	physical	28514442
CPNE7_HUMAN	CPNE7	physical	28514442
GEMI2_HUMAN	GEMIN2	physical	28514442
KLHL8_HUMAN	KLHL8	physical	28514442

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

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124 AND SER-126, ANDMASS SPECTROMETRY.
PubMed: 18669648

"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-185, AND MASSSPECTROMETRY.
PubMed: 18691976