Golga2
entrez
64528
canonical
uniprot
Q62839
canonical
ensembl
ENSRNOG00000011884
resolver
ensp
ENSRNOP00000074890
resolver
ensp
ENSRNOP00000078482
resolver
ensp
ENSRNOP00000079188
resolver
ensp
ENSRNOP00000080186
resolver
ensp
ENSRNOP00000087352
resolver
ensp
ENSRNOP00000108836
resolver
enst
ENSRNOT00000091171
resolver
enst
ENSRNOT00000095262
resolver
enst
ENSRNOT00000100279
resolver
genesymbol
Golga2
resolver
uniprot
A0A0G2K977
resolver
uniprot
A0A8I6A5P6
resolver
uniprot
A0A8I6G694
resolver
uniprot
F1LSS0
resolver
uniprot_entry
A0A0G2K977_RAT
resolver
uniprot_entry
A0A8I6A5P6_RAT
resolver
uniprot_entry
A0A8I6G694_RAT
resolver
uniprot_entry
GOGA2_RAT
resolver
uniprot_sec
F1LSS0
resolver
amino_acid_sequence
MWPPRFPPPRPGMSEETRQSKLAAAKKKLREYQQKNSPGVPAGAKKKKKIKNGHSPERTSASDCQSAENVPTDHTAPAPPSTAAATMFLGVVPSPDADLIQSHDAGNCSNLMEETKTFSSTESLRQLSQQLNGLVSESTSYINGEGLTSSNMKELESRYQELAVALDSSYVTNKQLSSTIEELKQQNQDTLDQLEKEKKDYQQKLAKEQGALREQLQVHIQTIGILVSEKAELQTALAHTQQAARQKAGESEDLASRLQSSRQRVGELERTLSTVSTQQKQADRYNKDLTKERDALKLELYKNGKSNEDLRQQNSELEEKLRVLVAEKAAAQLGAEELQKKLEMSELLLQQFSSQSEASGSNEQLQQAMEERAQLESHVGQLMESLKQLQVERDQYAENLKGESAMWQQRVQQMAEQVHALKEEKEQRESQVQELEASLAELRSQMEEPPPPEPPTGPSEAEERLQGEVEQLQKELEGLTGQLRAQVQDNESLSHLNREQEGRLLELEREAQHWSEQAEERKQILESMQSDRTTISRALSQNRELKEQLAELQNGFVRLTNENMEITSALQSEQHVKKELARKLGELQERLGELKETVELKSQEAQGLQEQRDQCLSHLQQYAAAYQQHLTAYEQLTSEKEALHKQLLLQTQLMDQLQHEEVQGKMAAEMARQELQEAQERLKASSQENQQLQAQLSLLVLPGEDMDQEEQDEEVPQPSLTIPEDLVSREAMVAFCNAAIARAEEEQARLRVQLREQKARCRSLAHLAAPVQSKLEKEAVVPRDMGDSVSEESNQALHVAMEKLQNRFLEVMQEKVELKERVEELEHCCIQLSGETDTIGEYIALYQNQRAVLKARHLEKEEYISRLAQDKEEMKVKLLELQELVLRLVNERNEWQGKFLAVSQNPADVPAPVPTGSQEFGAADQQGDLREVSLADDTEPAQGEAGVPAPQENPTAQQIMQLLREIQNPQERPGLGSNPCIPFFYRADENDEVKIMVI
uniprot
proteins
function
FUNCTION: 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 (PubMed:20197635, PubMed:9150144). Required for normal protein transport from the endoplasmic reticulum to the Golgi apparatus and the cell membrane (By similarity). 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 (PubMed:10679020, PubMed:11035033, PubMed:18167358). 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 (PubMed:9753325). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). 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 (By similarity). Also regulates the centrosome organization (By similarity). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (By similarity). {ECO:0000250|UniProtKB:Q08379, ECO:0000250|UniProtKB:Q921M4, ECO:0000269|PubMed:10679020, ECO:0000269|PubMed:11035033, ECO:0000269|PubMed:18167358, ECO:0000269|PubMed:26165940, ECO:0000269|PubMed:9150144, ECO:0000269|PubMed:9753325, ECO:0000303|PubMed:20197635}.
uniprot
proteins
mass_dalton
112872
uniprot
proteins
mutagenesis
MUTAGEN 37; /note="S->A: Constitutive interaction with p115/USO1; under mitotic as well as interphase conditions."; /evidence="ECO:0000269|PubMed:9753325"; MUTAGEN 37; /note="S->D: Phosphomimetic mutant that strongly reduces interaction with p115/USO1."; /evidence="ECO:0000269|PubMed:9753325"; MUTAGEN 55; /note="S->A: Does not affect interaction with p115/USO1."; /evidence="ECO:0000269|PubMed:9753325"; MUTAGEN 94; /note="S->A: Does not affect interaction with p115/USO1."; /evidence="ECO:0000269|PubMed:9753325"; MUTAGEN 988; /note="D->A: Does not affect with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 989; /note="E->A: Does not affect with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 990; /note="N->A: Strongly impairs interaction with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 991; /note="D->A: Strongly impairs interaction with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 992; /note="E->A: Does not affect with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 993; /note="V->A: Does not affect with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 994; /note="K->A: Does not affect with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 995; /note="I->A: Strongly impairs interaction with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 996; /note="M->A: Strongly impairs interaction with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 997; /note="V->A: Impairs interaction with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863"; MUTAGEN 998; /note="I->A: Impairs interaction with GORASP1/GRASP65."; /evidence="ECO:0000269|PubMed:9628863
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-37 by CDK1 at the onset of mitosis, inhibiting the interaction with p115/USO1 and triggering Golgi disassembly (PubMed:9150144, PubMed:9753325). A report however suggests that Golgi disassembly is independent of phosphorylation at Ser-37 (PubMed:20699666). 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. In telophase, GM130 is dephosphorylated by PP2A as the Golgi fragments start to reassemble (PubMed:10769027). {ECO:0000269|PubMed:10769027, ECO:0000269|PubMed:20699666, ECO:0000269|PubMed:9150144, ECO:0000269|PubMed:9753325}.; PTM: Cleaved by caspases at the onset of apoptosis. {ECO:0000250|UniProtKB:Q08379}.; PTM: Methylation by PRMT5 is required for Golgi ribbon formation. {ECO:0000250|UniProtKB:Q08379}.
uniprot
proteins
protein_family
GOLGA2 family
uniprot
proteins
pubmed
10679020
uniprot
proteins
pubmed
10744704
uniprot
proteins
pubmed
10769027
uniprot
proteins
pubmed
11035033
uniprot
proteins
pubmed
11739401
uniprot
proteins
pubmed
14742712
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
18167358
uniprot
proteins
pubmed
20197635
uniprot
proteins
pubmed
20699666
uniprot
proteins
pubmed
25787021
uniprot
proteins
pubmed
26165940
uniprot
proteins
pubmed
8557739
uniprot
proteins
pubmed
9150144
uniprot
proteins
pubmed
9346242
uniprot
proteins
pubmed
9628863
uniprot
proteins
pubmed
9753325
uniprot
proteins
sequence_length
998
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:10769027, ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:20699666, ECO:0000269|PubMed:8557739, ECO:0000269|PubMed:9150144}; Peripheral membrane protein {ECO:0000269|PubMed:10769027, ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:8557739, ECO:0000269|PubMed:9150144}; Cytoplasmic side {ECO:0000269|PubMed:8557739}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q08379}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q08379}; Cytoplasmic side {ECO:0000250|UniProtKB:Q08379}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q08379}. Note=Associates with the mitotic spindle during mitosis. {ECO:0000250|UniProtKB:Q08379}.
uniprot
proteins