SPAG5_MOUSE
ID SPAG5_MOUSE Reviewed; 1165 AA.
AC Q7TME2; B1AQC8; Q8CH61;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Sperm-associated antigen 5;
DE AltName: Full=Mastrin;
DE AltName: Full=Mitotic spindle-associated protein p126;
DE Short=MAP126;
GN Name=Spag5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ, and NIH Swiss; TISSUE=Testis;
RX PubMed=12893248; DOI=10.1016/s0006-291x(03)01220-8;
RA Chang M.-S., Chen C.-Y., Huang C.-J., Fan C.-C., Chu J.-M., Yang Y.-C.;
RT "Expression and promoter analysis of mouse mastrin gene.";
RL Biochem. Biophys. Res. Commun. 307:491-497(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Osteoblast;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Essential component of the mitotic spindle required for
CC normal chromosome segregation and progression into anaphase. Required
CC for chromosome alignment, normal timing of sister chromatid
CC segregation, and maintenance of spindle pole architecture. In complex
CC with SKAP, promotes stable microtubule-kinetochore attachments. May
CC contribute to the regulation of separase activity. May regulate AURKA
CC localization to mitotic spindle, but not to centrosomes and CCNB1
CC localization to both mitotic spindle and centrosomes. Involved in
CC centriole duplication. Required for CDK5RAP22, CEP152, WDR62 and CEP63
CC centrosomal localization and promotes the centrosomal localization of
CC CDK2. In non-mitotic cells, upon stress induction, inhibits mammalian
CC target of rapamycin complex 1 (mTORC1) association and recruits the
CC mTORC1 component RPTOR to stress granules (SGs), thereby preventing
CC mTORC1 hyperactivation-induced apoptosis. May enhance GSK3B-mediated
CC phosphorylation of other substrates, such as MAPT/TAU (By similarity).
CC {ECO:0000250|UniProtKB:Q96R06}.
CC -!- SUBUNIT: Homodimer, with a globular head domain and a long stalk.
CC Homooligomer; the globular head domains associate, resulting in aster-
CC like structures. Binds to microtubules in the mitotic spindle.
CC Interacts with DCLRE1B/Apollo. Part of an astrin (SPAG5)-kinastrin
CC (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2.
CC Interacts with KNSTRN. Interacts with RPTOR; this interaction competes
CC with RPTOR binding to MTOR, resulting in decreased mTORC1 formation.
CC Interacts with G3BP1. The complex formed with G3BP1 AND RPTOR is
CC increased by oxidative stress. Interacts with OSBPL8, PCM1 and
CC CDK5RAP2. Interacts (via C-terminus) with NUMA1 (via C-terminus); this
CC interaction promotes the recruitment of SPAG5 to the microtubules at
CC spindle poles in a dynein-dynactin-dependent manner. Interacts with
CC DYNLL1 (By similarity). {ECO:0000250|UniProtKB:Q96R06}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96R06}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96R06}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96R06}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96R06}.
CC Midbody {ECO:0000250|UniProtKB:Q96R06}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q96R06}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q96R06}. Note=Colocalizes with PCM1 at
CC centriolar satellites throughout the cell cycle (By similarity). In a
CC punctate pattern in interphase cells. During mitosis, detected at
CC spindle poles during prophase, throughout the spindle in metaphase and
CC anaphase, and at midzone microtubules in anaphase and telophase.
CC Efficient targeting to the mitotic spindle may depend upon
CC phosphorylation by GSK3B. Detected on kinetochores of chromosomes that
CC have congressed. The astrin (SPAG5)-kinastrin (SKAP) complex localizes
CC to the microtubule plus ends (By similarity). In non-mitotic non-
CC stressed cells, shows a microtubuli pattern. During oxidative stress,
CC accumulates in stress granules (By similarity).
CC {ECO:0000250|UniProtKB:Q96R06}.
CC -!- TISSUE SPECIFICITY: Detected in testis, but not in the other tissues
CC tested. {ECO:0000269|PubMed:12893248}.
CC -!- INDUCTION: Expression is cell cycle-regulated, with an increase from
CC prophase to cytokinesis and return to basal levels at the next G1
CC phase. {ECO:0000250}.
CC -!- PTM: Phosphorylated by AURKA. {ECO:0000250}.
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DR EMBL; AF420307; AAO15441.1; -; mRNA.
DR EMBL; AY226907; AAP46103.1; -; Genomic_DNA.
DR EMBL; AL591070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052672; AAH52672.1; -; mRNA.
DR CCDS; CCDS25098.1; -.
DR RefSeq; NP_059103.1; NM_017407.2.
DR AlphaFoldDB; Q7TME2; -.
DR SMR; Q7TME2; -.
DR BioGRID; 207577; 27.
DR IntAct; Q7TME2; 11.
DR STRING; 10090.ENSMUSP00000045286; -.
DR iPTMnet; Q7TME2; -.
DR PhosphoSitePlus; Q7TME2; -.
DR EPD; Q7TME2; -.
DR MaxQB; Q7TME2; -.
DR PaxDb; Q7TME2; -.
DR PeptideAtlas; Q7TME2; -.
DR PRIDE; Q7TME2; -.
DR ProteomicsDB; 261559; -.
DR DNASU; 54141; -.
DR Ensembl; ENSMUST00000045026; ENSMUSP00000045286; ENSMUSG00000002055.
DR GeneID; 54141; -.
DR KEGG; mmu:54141; -.
DR UCSC; uc007kiv.2; mouse.
DR CTD; 10615; -.
DR MGI; MGI:1927470; Spag5.
DR VEuPathDB; HostDB:ENSMUSG00000002055; -.
DR eggNOG; ENOG502RW0Y; Eukaryota.
DR GeneTree; ENSGT00400000022377; -.
DR HOGENOM; CLU_007803_0_0_1; -.
DR InParanoid; Q7TME2; -.
DR OMA; LEDCKGQ; -.
DR OrthoDB; 257437at2759; -.
DR PhylomeDB; Q7TME2; -.
DR TreeFam; TF336280; -.
DR BioGRID-ORCS; 54141; 11 hits in 74 CRISPR screens.
DR ChiTaRS; Spag5; mouse.
DR PRO; PR:Q7TME2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7TME2; protein.
DR Bgee; ENSMUSG00000002055; Expressed in epithelium of lens and 203 other tissues.
DR Genevisible; Q7TME2; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0051294; P:establishment of spindle orientation; IMP:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0032388; P:positive regulation of intracellular transport; ISS:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; ISS:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:MGI.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0090235; P:regulation of metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
DR InterPro; IPR028728; Astrin.
DR PANTHER; PTHR15347; PTHR15347; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Kinetochore; Microtubule; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1165
FT /note="Sperm-associated antigen 5"
FT /id="PRO_0000072094"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..821
FT /note="Interaction with KNSTRN"
FT /evidence="ECO:0000250"
FT REGION 875..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 509..856
FT /evidence="ECO:0000255"
FT COILED 937..1146
FT /evidence="ECO:0000255"
FT COMPBIAS 875..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96R06"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96R06"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96R06"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96R06"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96R06"
FT MOD_RES 946
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q96R06"
FT CONFLICT 48
FT /note="A -> S (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="P -> S (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="L -> P (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> N (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="S -> P (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="S -> G (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
FT CONFLICT 663..665
FT /note="KEV -> TGM (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="F -> S (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
FT CONFLICT 888..889
FT /note="SN -> PS (in Ref. 1; AAO15441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1165 AA; 129993 MW; 0885C71A3AB7A96A CRC64;
MWRVKTLNLG LSPSPQKGKP AMSTPLRELK LQPEALADSG KGPSMISALT PYLCRLELKE
RCNNSSPVDF INTENNFLSE QFSHPSTHIE ACQRESDPTP ESNSLFHTLE EAIETVDDFV
VDPRDDSIVE SMVLLPFSLG QQQDLMLQAH LDTTAERTKS SLNESLGLED LVGKEVAPCV
EDSLTEIVAI RPEQPTFQDP PLGPSDTEDA PVDLVPSENV LNFSLARLSP SAVLAQDFSV
DHVDPGEETV ENRVLQEMET SFPTFPEEAE LGDQAPAANA EAVSPLYLTS SLVEMGPREA
PGPTVEDASR IPGLESETWM SPLAWLEKGV NTSVMLQNLR QSLSFSSVLQ DAAVGNTPLA
TCSVGTSFTP PAPLEVGTKD STSETERLLL GCRPPDLATL SRHDLEENLL NSLVLLEVLS
HQLQAWKSQL TVPHREARDS STQTDSSPCG VTKTPKHLQD SKEIRQALLQ ARNVMQSWGL
VSGDLLSLLH LSLTHVQEGR VTVSQESQRS KTLVSSCSRV LKKLKAKLQS LKTECEEARH
SKEMALKGKA AAEAVLEAFR AHASQRISQL EQGLTSMQEF RGLLQEAQTQ LIGLHTEQKE
LAQQTVSLSS ALQQDWTSVQ LNYGIWAALL SWSRELTKKL TAKSRQALQE RDAAIEEKKQ
VVKEVEQVSA HLEDCKGQIE QLKLENSRLT ADLSAQLQIL TSTESQLKEV RSQHSRCVQD
LAVKDELLCQ LTQSNKEQAT QWQKEEMELK HIQAELLQQQ AVLAKEVQDL RETVEFIDEE
SQVAHRELGQ IESQLKVTLE LLRERSLQCE TLRDTVDSLR AELASTEAKH EKQALEKTHQ
HSQELRLLAE QLQSLTLFLQ AKLKENKAES EIILPSTGSA PAQEHPLSND SSISEQTPTA
AVDEVPEPAP VPLLGSVKSA FTRVASMASF QPTETPDLEK SLAEMSTVLQ ELKSLCSLLQ
ESKEEATGVL QREICELHSR LQAQEEEHQE ALKAKEADME KLNQALCLLR KNEKELLEVI
QKQNEKILGQ IDKSGQLINL REEVTQLTQS LRRAETETKV LQEALEGQLD PSCQLMATNW
IQEKVFLSQE VSKLRVMFLE MKTEKEQLMD KYLSHRHILE ENLRRSDTEL KKLDDTIQHV
YETLLSIPET MKSCKELQGL LEFLS
