SPAG5
entrez
10615
canonical
uniprot
Q96R06
canonical
ensembl
ENSG00000076382
resolver
ensp
ENSP00000323300
resolver
enst
ENST00000321765
resolver
genesymbol
SPAG5
resolver
hgnc
HGNC:13452
resolver
uniprot
O95213
resolver
uniprot
Q9BWE8
resolver
uniprot
Q9NT17
resolver
uniprot
Q9UFE6
resolver
uniprot_entry
SPAG5_HUMAN
resolver
uniprot_sec
O95213
resolver
uniprot_sec
Q9BWE8
resolver
uniprot_sec
Q9NT17
resolver
uniprot_sec
Q9UFE6
resolver
amino_acid_sequence
MWRVKKLSLSLSPSPQTGKPSMRTPLRELTLQPGALTNSGKRSPACSSLTPSLCKLGLQEGSNNSSPVDFVNNKRTDLSSEHFSHSSKWLETCQHESDEQPLDPIPQISSTPKTSEEAVDPLGNYMVKTIVLVPSPLGQQQDMIFEARLDTMAETNSISLNGPLRTDDLVREEVAPCMGDRFSEVAAVSEKPIFQESPSHLLEESPPNPCSEQLHCSKESLSSRTEAVREDLVPSESNAFLPSSVLWLSPSTALAADFRVNHVDPEEEIVEHGAMEEREMRFPTHPKESETEDQALVSSVEDILSTCLTPNLVEMESQEAPGPAVEDVGRILGSDTESWMSPLAWLEKGVNTSVMLENLRQSLSLPSMLRDAAIGTTPFSTCSVGTWFTPSAPQEKSTNTSQTGLVGTKHSTSETEQLLCGRPPDLTALSRHDLEDNLLSSLVILEVLSRQLRDWKSQLAVPHPETQDSSTQTDTSHSGITNKLQHLKESHEMGQALQQARNVMQSWVLISKELISLLHLSLLHLEEDKTTVSQESRRAETLVCCCFDLLKKLRAKLQSLKAEREEARHREEMALRGKDAAEIVLEAFCAHASQRISQLEQDLASMREFRGLLKDAQTQLVGLHAKQEELVQQTVSLTSTLQQDWRSMQLDYTTWTALLSRSRQLTEKLTVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQDLAMKDELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKEKTEQETLLLSTACPPTQEHPLPNDRTFLGSILTAVADEEPESTPVPLLGSDKSAFTRVASMVSLQPAETPGMEESLAEMSIMTTELQSLCSLLQESKEEAIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGELISLREEVTHLTRSLRRAETETKVLQEALAGQLDSNCQPMATNWIQEKVWLSQEVDKLRVMFLEMKNEKEKLMIKFQSHRNILEENLRRSDKELEKLDDIVQHIYKTLLSIPEVVRGCKELQGLLEFLS
uniprot
proteins
function
FUNCTION: Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase (PubMed:11724960, PubMed:12356910, PubMed:27462074). Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:17664331, PubMed:27462074). In complex with SKAP, promotes stable microtubule-kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle, but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes (PubMed:18361916, PubMed:21402792). Involved in centriole duplication. Required for CDK5RAP2, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). In non-mitotic cells, upon stress induction, inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs), thereby preventing mTORC1 hyperactivation-induced apoptosis (PubMed:23953116). May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU (PubMed:18055457). {ECO:0000269|PubMed:12356910, ECO:0000269|PubMed:17664331, ECO:0000269|PubMed:18055457, ECO:0000269|PubMed:18361916, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:23953116, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:27462074, ECO:0000305|PubMed:11724960}.
uniprot
proteins
mass_dalton
134422
uniprot
proteins
mutagenesis
MUTAGEN 111; /note="T->A: Decreased phosphorylation by GSK3-beta. Partial loss of spindle association; when associated with A-937, A974 and A-978."; /evidence="ECO:0000269|PubMed:18055457"; MUTAGEN 937; /note="T->A: Decreased phosphorylation by GSK3-beta. Partial loss of spindle association; when associated with A-111, A974 and A-978."; /evidence="ECO:0000269|PubMed:18055457"; MUTAGEN 974; /note="S->A: Decreased phosphorylation by GSK3-beta; when associated with A-978. Partial loss of spindle association; when associated with A-111, A937 and A-978."; /evidence="ECO:0000269|PubMed:18055457"; MUTAGEN 978; /note="T->A: Decreased phosphorylation by GSK3-beta; when associated with A-97A. Partial loss of spindle association; when associated with A-111, A-937 and A-974."; /evidence="ECO:0000269|PubMed:18055457
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by AURKA. {ECO:0000269|PubMed:18055457, ECO:0000269|PubMed:18361916}.
uniprot
proteins
pubmed
11549262
uniprot
proteins
pubmed
11724960
uniprot
proteins
pubmed
12356910
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17664331
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18055457
uniprot
proteins
pubmed
18361916
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19197158
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21402792
uniprot
proteins
pubmed
22965910
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23953116
uniprot
proteins
pubmed
24424245
uniprot
proteins
pubmed
26297806
uniprot
proteins
pubmed
27462074
uniprot
proteins
sequence_length
1193
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27462074}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27462074}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:27462074}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:27462074}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:27462074}. Midbody. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic granule. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:26297806}. Note=Colocalizes with PCM1 at centriolar satellites throughout the cell cycle (PubMed:26297806). In a punctate pattern in interphase cells. During mitosis, detected at spindle poles during prophase, throughout the spindle in metaphase and anaphase, and at midzone microtubules in anaphase and telophase (PubMed:27462074). Efficient targeting to the mitotic spindle may depend upon phosphorylation by GSK3B. Detected on kinetochores of chromosomes that have congressed. The astrin (SPAG5)-kinastrin (SKAP) complex localizes to the microtubule plus ends (By similarity). In non-mitotic non-stressed cells, shows a microtubuli pattern. In arsenite-stressed cells, accumulates in stress granules. {ECO:0000250, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:27462074}.
uniprot
proteins