GORASP2
entrez
26003
canonical
uniprot
Q9H8Y8
canonical
ensembl
ENSG00000115806
resolver
ensp
ENSP00000234160
resolver
genesymbol
GORASP2
resolver
genesymbol_syn
GOLPH6
resolver
hgnc
HGNC:17500
resolver
uniprot
B4DKT0
resolver
uniprot
Q53TE3
resolver
uniprot
Q96I74
resolver
uniprot
Q96K84
resolver
uniprot
Q9H946
resolver
uniprot
Q9UFW4
resolver
uniprot_entry
GORS2_HUMAN
resolver
uniprot_sec
B4DKT0
resolver
uniprot_sec
Q53TE3
resolver
uniprot_sec
Q96I74
resolver
uniprot_sec
Q96K84
resolver
uniprot_sec
Q9H946
resolver
uniprot_sec
Q9UFW4
resolver
amino_acid_sequence
MGSSQSVEIPGGGTEGYHVLRVQENSPGHRAGLEPFFDFIVSINGSRLNKDNDTLKDLLKANVEKPVKMLIYSSKTLELRETSVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGADTVMNESEDLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPTRPFEEGKKISLPGQMAGTPITPLKDGFTEVQLSSVNPPSLSPPGTTGIEQSLTGLSISSTPPAVSSVLSTGVPTVPLLPPQVNQSLTSVPPMNPATTLPGLMPLPAGLPNLPNLNLNLPAPHIMPGVGLPELVNPGLPPLPSMPPRNLPGIAPLPLPSEFLPSFPLVPESSSAASSGELLSSLPPTSNAPSDPATTTAKADAASSLTVDVTPPTAKAPTTVEDRVGDSTPVSEKPVSAAVDANASESP
uniprot
proteins
function
FUNCTION: Key structural protein of the Golgi apparatus (PubMed:33301566). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (PubMed:33301566). Acting in concert with GORASP1/GRASP65, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (PubMed:33301566). However, other studies suggest that GORASP2 plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis (PubMed:10487747, PubMed:21515684, PubMed:22523075). May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA (PubMed:11101516). Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936, PubMed:27062250, PubMed:28067262). {ECO:0000250|UniProtKB:Q99JX3, ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:11101516, ECO:0000269|PubMed:21515684, ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:22523075, ECO:0000269|PubMed:27062250, ECO:0000269|PubMed:28067262}.
uniprot
proteins
mass_dalton
47145
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Abolishes myristoylation. Loss of its ability to mediate unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane. No effect on ER stress-induced relocalization from Golgi to ER."; /evidence="ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:27062250"; MUTAGEN 59; /note="L->A: Abolishes organelle clustering; when associated with S-100."; /evidence="ECO:0000269|PubMed:21515684"; MUTAGEN 100; /note="I->S: Abolishes organelle clustering; when associated with A-59."; /evidence="ECO:0000269|PubMed:21515684"; MUTAGEN 148; /note="D->N: Enhances homodimerization. Loss of ER stress-induced relocalization from Golgi to ER."; /evidence="ECO:0000269|PubMed:27062250"; MUTAGEN 189; /note="S->D: Phosphomimetic mutation that decreases the ability to promote organelle clustering."; /evidence="ECO:0000269|PubMed:22523075"; MUTAGEN 222; /note="T->A: Abolishes mitotic phosphorylation; when associated with A-225."; /evidence="ECO:0000269|PubMed:11408587"; MUTAGEN 225; /note="T->A: Abolishes mitotic phosphorylation; when associated with A-222."; /evidence="ECO:0000269|PubMed:11408587"; MUTAGEN 441; /note="S->A: Loss of phosphorylation and its ability to mediate unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane. Inhibits ER stress-mediated disruption of homodimerization. Loss of ER stress-induced relocalization from Golgi to ER."; /evidence="ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:27062250"; MUTAGEN 441; /note="S->D: Phosphomimetic mutant. No loss of its ability to mediate unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane. Disrupts homodimerization. No loss of ER stress-induced relocalization from Golgi to ER."; /evidence="ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:27062250"; MUTAGEN 449; /note="S->A: Loss of phosphorylation. Does not inhibit ER stress-mediated disruption of homodimerization."; /evidence="ECO:0000269|PubMed:27062250"; MUTAGEN 449; /note="S->D: Phosphomimetic mutant. No disruption of homodimerization."; /evidence="ECO:0000269|PubMed:27062250"; MUTAGEN 451; /note="S->A: Loss of phosphorylation. Does not inhibit ER stress-mediated disruption of homodimerization."; /evidence="ECO:0000269|PubMed:27062250"; MUTAGEN 451; /note="S->D: Phosphomimetic mutant. Partial disruption of homodimerization."; /evidence="ECO:0000269|PubMed:27062250
uniprot
proteins
post_translational_modification
PTM: Myristoylated (PubMed:11101516). Myristoylation is essential for the Golgi targeting (By similarity). {ECO:0000250|UniProtKB:Q9R064, ECO:0000269|PubMed:11101516}.; PTM: Palmitoylated. {ECO:0000269|PubMed:11101516}.; PTM: Phosphorylated in mitotic cells (PubMed:11408587). ER stress-induced phosphorylation at Ser-441 induces monomerization and subsequent relocalization from Golgi to ER which is essential for mediating unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane (PubMed:21884936, PubMed:27062250). {ECO:0000269|PubMed:11408587, ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:27062250}.
uniprot
proteins
protein_family
GORASP family
uniprot
proteins
pubmed
10487747
uniprot
proteins
pubmed
11101516
uniprot
proteins
pubmed
11408587
uniprot
proteins
pubmed
11739401
uniprot
proteins
pubmed
11739402
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17607000
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19361449
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21515684
uniprot
proteins
pubmed
21884936
uniprot
proteins
pubmed
22523075
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25255805
uniprot
proteins
pubmed
25807930
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27062250
uniprot
proteins
pubmed
28067262
uniprot
proteins
pubmed
33301566
uniprot
proteins
sequence_length
452
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:11101516, ECO:0000269|PubMed:27062250}; Lipid-anchor {ECO:0000269|PubMed:11101516}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27062250}. Golgi apparatus {ECO:0000269|PubMed:28067262}. Note=Detected in the intermediate Golgi, membrane-associated (By similarity). ER stress triggers its relocalization from Golgi to ER membrane (PubMed:27062250, PubMed:28067262). {ECO:0000250|UniProtKB:Q9R064, ECO:0000269|PubMed:27062250, ECO:0000269|PubMed:28067262}.
uniprot
proteins