GOLGA2
entrez
2801
canonical
uniprot
Q08379
canonical
ensembl
ENSG00000167110
resolver
ensp
ENSP00000416097
resolver
ensp
ENSP00000478799
resolver
ensp
ENSP00000481685
resolver
ensp
ENSP00000508841
resolver
ensp
ENSP00000510145
resolver
ensp
ENSP00000510790
resolver
ensp
ENSP00000634696
resolver
enst
ENST00000611957
resolver
enst
ENST00000686291
resolver
enst
ENST00000687179
resolver
enst
ENST00000693185
resolver
genesymbol
GOLGA2
resolver
hgnc
HGNC:4425
resolver
uniprot
A0A0C4DGS5
resolver
uniprot
A0A8I5KNZ1
resolver
uniprot
A0A8I5KZ68
resolver
uniprot
A0A8I5QJQ7
resolver
uniprot
A0A8J9BZL8
resolver
uniprot
Q6GRM9
resolver
uniprot
Q9BRB0
resolver
uniprot
Q9NYF9
resolver
uniprot_entry
A0A8I5KNZ1_HUMAN
resolver
uniprot_entry
A0A8I5KZ68_HUMAN
resolver
uniprot_entry
A0A8I5QJQ7_HUMAN
resolver
uniprot_entry
A0A8J9BZL8_HUMAN
resolver
uniprot_entry
GOGA2_HUMAN
resolver
uniprot_sec
A0A0C4DGS5
resolver
uniprot_sec
Q6GRM9
resolver
uniprot_sec
Q9BRB0
resolver
uniprot_sec
Q9NYF9
resolver
amino_acid_sequence
MWPQPRLPPRPAMSEETRQSKLAAAKKKLREYQQRNSPGVPTGAKKKKKIKNGSNPETTTSGGCHSPEDTPKDNAATLQPSDDTVLPGGVPSPGASLTSMAASQNHDADNVPNLMDETKTFSSTESLRQLSQQLNGLVCESATCVNGEGPASSANLKDLESRYQQLAVALDSSYVTNKQLNITIEKLKQQNQEITDQLEEEKKECHQKQGALREQLQVHIQTIGILVSEKAELQTALAHTQHAARQKEGESEDLASRLQYSRRRVGELERALSAVSTQQKKADRYNKELTKERDALRLELYKNTQSNEDLKQEKSELEEKLRVLVTEKAGMQLNLEELQKKLEMTELLLQQFSSRCEAPDANQQLQQAMEERAQLEAHLGQVMESVRQLQMERDKYAENLKGESAMWRQRMQQMSEQVHTLREEKECSMSRVQELETSLAELRNQMAEPPPPEPPAGPSEVEQQLQAEAEHLRKELEGLAGQLQAQVQDNEGLSRLNREQEERLLELERAAELWGEQAEARRQILETMQNDRTTISRALSQNRELKEQLAELQSGFVKLTNENMEITSALQSEQHVKRELGKKLGELQEKLSELKETVELKSQEAQSLQQQRDQYLGHLQQYVAAYQQLTSEKEVLHNQLLLQTQLVDQLQQQEAQGKAVAEMARQELQETQERLEAATQQNQQLRAQLSLMAHPGEGDGLDREEEEDEEEEEEEAVAVPQPMPSIPEDLESREAMVAFFNSAVASAEEEQARLRGQLKEQRVRCRRLAHLLASAQKEPEAAAPAPGTGGDSVCGETHRALQGAMEKLQSRFMELMQEKADLKERVEELEHRCIQLSGETDTIGEYIALYQSQRAVLKERHREKEEYISRLAQDKEEMKVKLLELQELVLRLVGDRNEWHGRFLAAAQNPADEPTSGAPAPQELGAANQQGDLCEVSLAGSVEPAQGEAREGSPRDNPTAQQIMQLLREMQNPRERPGLGSNPCIPFFYRADENDEVKITVI
uniprot
proteins
disease_involvement
DISEASE: Developmental delay with hypotonia, myopathy, and brain abnormalities (DEDHMB) [MIM:620240]: An autosomal recessive neurodevelopmental disorder characterized by global developmental delay and muscle weakness apparent in infancy, microcephaly, seizures, central hypotonia, and skeletal muscle myopathy. Brain imaging shows cerebral atrophy, thinning of the corpus callosum, and delayed myelination. {ECO:0000269|PubMed:26742501, ECO:0000269|PubMed:30237576, ECO:0000269|PubMed:34424553}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (Probable) (PubMed:16489344). 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. 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 (By similarity). 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 (PubMed:19242490, PubMed:26165940). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (PubMed:18045989, PubMed:19109421). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (PubMed:16489344, PubMed:17314401). {ECO:0000250|UniProtKB:Q62839, ECO:0000250|UniProtKB:Q921M4, ECO:0000269|PubMed:16489344, ECO:0000269|PubMed:17314401, ECO:0000269|PubMed:18045989, ECO:0000269|PubMed:19109421, ECO:0000269|PubMed:19242490, ECO:0000269|PubMed:26165940, ECO:0000305|PubMed:26363069}.
uniprot
proteins
mass_dalton
113086
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="R->K: Impaired methylation; when associated with R-30 and R-35."; /evidence="ECO:0000269|PubMed:20421892"; MUTAGEN 26..49; /note="KKKLREYQQRNSPGVPTGAKKKKK->AAALAEYQQANSPGVPTGAAAAAA: Abolishes interaction with importin-alpha."; /evidence="ECO:0000269|PubMed:26165940"; MUTAGEN 30; /note="R->K: Impaired methylation; when associated with R-18 and R-35."; /evidence="ECO:0000269|PubMed:20421892"; MUTAGEN 35; /note="R->K: Impaired methylation; when associated with R-18 and R-35."; /evidence="ECO:0000269|PubMed:20421892"; MUTAGEN 37; /note="S->D: Phosphomimetic mutant. Does not affect interaction with importin-alpha."; /evidence="ECO:0000269|PubMed:26165940"; MUTAGEN 987; /note="F->A: Abolishes interaction with GORASP1. Abolishes membrane clustering."; /evidence="ECO:0000269|PubMed:26363069"; MUTAGEN 1002; /note="I->R: Abolishes interaction with GORASP1. Abolishes membrane clustering."; /evidence="ECO:0000269|PubMed:26363069
uniprot
proteins
post_translational_modification
PTM: Cleaved by caspases at the onset of apoptosis. {ECO:0000269|PubMed:15003503}.; PTM: Methylation by PRMT5 is required for Golgi ribbon formation. While dimethylation at Arg-30 and Arg-35 are confirmed in vivo, it is unclear whether Arg-18 is methylated in vivo. {ECO:0000269|PubMed:20421892}.; PTM: Phosphorylated at Ser-37 by CDK1 at the onset of mitosis, inhibiting the interaction with p115/USO1 and triggering Golgi disassembly (PubMed:20421892, PubMed:26165940). 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 (By similarity). {ECO:0000250|UniProtKB:Q62839, ECO:0000269|PubMed:20421892, ECO:0000269|PubMed:26165940}.
uniprot
proteins
protein_family
GOLGA2 family
uniprot
proteins
pubmed
11306556
uniprot
proteins
pubmed
11781572
uniprot
proteins
pubmed
15003503
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16489344
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17314401
uniprot
proteins
pubmed
18045989
uniprot
proteins
pubmed
18323775
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19109421
uniprot
proteins
pubmed
19242490
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20421892
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26165940
uniprot
proteins
pubmed
26363069
uniprot
proteins
pubmed
26742501
uniprot
proteins
pubmed
30237576
uniprot
proteins
pubmed
34424553
uniprot
proteins
pubmed
8315394
uniprot
proteins
sequence_length
1002
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:11781572, ECO:0000305|PubMed:8315394}; Peripheral membrane protein {ECO:0000269|PubMed:11781572}; Cytoplasmic side {ECO:0000269|PubMed:11781572}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:11781572}; Peripheral membrane protein {ECO:0000269|PubMed:11781572}; Cytoplasmic side {ECO:0000269|PubMed:11781572}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26165940}. Note=Associates with the mitotic spindle during mitosis (PubMed:26165940). {ECO:0000250|UniProtKB:Q62839, ECO:0000269|PubMed:26165940}.
uniprot
proteins