GOGA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GOGA2_MOUSE
• UniProt AC: Q921M4
• Protein Name: Golgin subfamily A member 2
• Gene Name: Golga2
• Organism: Mus musculus (Mouse).
• Sequence Length: 999
• Subcellular Localization: Golgi apparatus, cis-Golgi network membrane ; Peripheral membrane protein . Cytoplasm, cytoskeleton, spindle pole . Peripheral membrane protein associated with cis-Golgi stacks (By similarity). Associates with the mitotic spindle during mitosis (By s
• Protein Description: Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane. Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis. Also plays a key role in spindle pole assembly and centrosome organization (By similarity). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (By similarity). Regulates the meiotic spindle pole assembly, probably via the same mechanism. [PubMed: 21552007 Also regulates the centrosome organization (By similarity Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (By similarity]
• Protein Sequence: MWPPRFPPPRPGMSEETRQSKLAAAKKKLREYQQKNSPGVPAGAKKKKKIKNGHSPERPTASDCQSPENVPTDHIAPAPPTAATDTMFLGVTPSPDADLTQSHDAGNCSNLMEETKTFSSTESLRQLSQQLNGLVSESTSYINGEGLTSSNMKELENRYQELAVALDSSYVTNKQLSSTIEELKQQNQDTLDQLEKEKKDYQQKLAKEQGSLREQLQVHIQTIGILVSEKAELQTALAHTQQAARQKAGESEDLASRLQSSRQRVGELERTLSTVSTQQKQADRYNKDLTKERDALKLELYKNSKSNEDLRQQNSELEEKLRVLVAEKAAAQLGVEELQKKLEMSELLLQQFSSQSSAAGGNEQLQHAMEERAQLETHVSQLMESLKQLQVERDQYAENLKGESAMWQQRVQQMAEQVHTLKEEKEHRERQVQELETSLAALRSQMEEPPPPEPPAGPSEAEEQLQGEVEQLHKELERLTGQLRAQVQDNESLSHLNREQEGRLLELEREAQRWSEQAEERKQILESMQSDRTTISRALSQNRELKEQLAELQNGFVRLTNENMEITSALQSEQHVKKELARKLGELQERLGELKETVELKSQEAQGLQEQRDQCLSHLQQYAAAYQQHLAAYEQLTSEKEAIHKQLLLQTQLMDQLQHEEVQGKMAAELARQELQEAQERLKATSQENQQLQAQLSLLVLPGEGDVDQEEEDEEVPQSSLAIPEDLDSREAMVAFFNAAIARAEEEQARLRVQLKEQKARCRSLSHLAAPVQSKLEKEAVVPRNVDDSASEESNQALHVAMEKLQSRFLEVMQEKVELKERVEELEHCCIQLSGETDTIGEYIALYQNQRAVLKARHLEKEEYISRLAQDKEEMKVKLLELQELVLRLVNERNEWQGKFLAVSQNPGDVLTPVPTGSQEFGAADQQDDLREVSLADDIEPAQGEAGVPAPHENPTAQQIMQLLREIQNPRERPGLGSNPCIPFFYRADENDEVKIMVV

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
9	Phosphorylation	WPPRFPPPRPGMSEE CCCCCCCCCCCCCHH	56.17	17242355
18	Methylation	PGMSEETRQSKLAAA CCCCHHHHHHHHHHH	41.89	-
30	Methylation	AAAKKKLREYQQKNS HHHHHHHHHHHHHCC	49.83	-
37	Phosphorylation	REYQQKNSPGVPAGA HHHHHHCCCCCCCCH	30.02	24899341
55	Phosphorylation	KKIKNGHSPERPTAS CCCCCCCCCCCCCCC	29.83	23684622
55 (in isoform 2)	Phosphorylation	-	29.83	22802335
60 (in isoform 2)	Phosphorylation	-	45.04	27717184
62 (in isoform 2)	Phosphorylation	-	41.20	27717184
66 (in isoform 2)	Phosphorylation	-	40.28	27717184
66	Phosphorylation	PTASDCQSPENVPTD CCCCCCCCCCCCCCC	40.28	-
72	Phosphorylation	QSPENVPTDHIAPAP CCCCCCCCCCCCCCC	35.61	22802335
81	Phosphorylation	HIAPAPPTAATDTMF CCCCCCCCCCCCCEE	28.06	22802335
84	Phosphorylation	PAPPTAATDTMFLGV CCCCCCCCCCEEECC	29.55	22802335
119	Phosphorylation	MEETKTFSSTESLRQ HHHHCCCCCHHHHHH	41.40	29472430
120	Phosphorylation	EETKTFSSTESLRQL HHHCCCCCHHHHHHH	31.81	23984901
121	Phosphorylation	ETKTFSSTESLRQLS HHCCCCCHHHHHHHH	28.53	23984901
123	Phosphorylation	KTFSSTESLRQLSQQ CCCCCHHHHHHHHHH	29.01	29472430
128	Phosphorylation	TESLRQLSQQLNGLV HHHHHHHHHHHHHHH	13.93	-
198	Acetylation	LDQLEKEKKDYQQKL HHHHHHHHHHHHHHH	63.11	-
199	Acetylation	DQLEKEKKDYQQKLA HHHHHHHHHHHHHHH	63.86	-
273	Phosphorylation	GELERTLSTVSTQQK HHHHHHHHHHHHHHH	26.59	30352176
274	Phosphorylation	ELERTLSTVSTQQKQ HHHHHHHHHHHHHHH	22.91	29472430
276	Phosphorylation	ERTLSTVSTQQKQAD HHHHHHHHHHHHHHH	22.16	30635358
285	Phosphorylation	QQKQADRYNKDLTKE HHHHHHHHCCHHHHH	27.41	18779572
306	Phosphorylation	ELYKNSKSNEDLRQQ HHHHCCCCHHHHHHH	45.32	27681418
315	Phosphorylation	EDLRQQNSELEEKLR HHHHHHHHHHHHHHH	38.94	29514104
396	Phosphorylation	LQVERDQYAENLKGE HHHHHHHHHHHHCCC	21.85	18779572
438	Phosphorylation	QVQELETSLAALRSQ HHHHHHHHHHHHHHC	13.46	25338131
480	Phosphorylation	HKELERLTGQLRAQV HHHHHHHHHHHHHHH	29.15	18779572
540	Phosphorylation	TTISRALSQNRELKE HHHHHHHHCCHHHHH	25.15	25338131
546	Ubiquitination	LSQNRELKEQLAELQ HHCCHHHHHHHHHHH	38.37	-
595	Acetylation	QERLGELKETVELKS HHHHHHHHHHHHHHH	47.22	23236377
595	Ubiquitination	QERLGELKETVELKS HHHHHHHHHHHHHHH	47.22	-
697	Phosphorylation	QQLQAQLSLLVLPGE HHHHHHHHHHCCCCC	13.94	-
764	Phosphorylation	EQKARCRSLSHLAAP HHHHHHHHHHHHHHC	37.54	25159016
766	Phosphorylation	KARCRSLSHLAAPVQ HHHHHHHHHHHHCHH	20.08	25159016
789	Phosphorylation	VPRNVDDSASEESNQ CCCCCCCCCCHHHHH	29.27	25619855
791	Phosphorylation	RNVDDSASEESNQAL CCCCCCCCHHHHHHH	45.94	25619855
794	Phosphorylation	DDSASEESNQALHVA CCCCCHHHHHHHHHH	30.14	25619855
804	Ubiquitination	ALHVAMEKLQSRFLE HHHHHHHHHHHHHHH	38.45	-
816	Ubiquitination	FLEVMQEKVELKERV HHHHHHHHHHHHHHH	24.90	-
861	Ubiquitination	LKARHLEKEEYISRL HHHHHHCHHHHHHHH	63.31	-
912	Phosphorylation	QNPGDVLTPVPTGSQ CCCCCCEEECCCCCC	23.30	30352176
918	Phosphorylation	LTPVPTGSQEFGAAD EEECCCCCCCCCCCC	29.08	25195567
934	Phosphorylation	QDDLREVSLADDIEP CCCHHHCCHHCCCCC	17.06	-
978	Phosphorylation	RERPGLGSNPCIPFF CCCCCCCCCCCCCEE	42.51	26239621
981	S-nitrosylation	PGLGSNPCIPFFYRA CCCCCCCCCCEEEEC	7.84	20925432
981	S-palmitoylation	PGLGSNPCIPFFYRA CCCCCCCCCCEEEEC	7.84	26165157
981	S-nitrosocysteine	PGLGSNPCIPFFYRA CCCCCCCCCCEEEEC	7.84	-

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

Oops, there are no upstream regulatory protein records of GOGA2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
37	S	Phosphorylation	A report however suggests that Golgi disassembly is independent of phosphorylation at Ser-37.	-
37	S	Phosphorylation	Phosphorylated at Ser-37 by CDK1 at the onset of mitosis, inhibiting the interaction with p115/USO1 and triggering Golgi disassembly.	-
37	S	Phosphorylation	Phosphorylated at Ser-37 in prophase as the Golgi complex starts to break down, and remains phosphorylated during further breakdown and partitioning of the Golgi fragments in metaphase and anaphase.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of GOGA2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of GOGA2_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND MASSSPECTROMETRY.
PubMed: 19367708

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.
PubMed: 17242355