SPAG5_HUMAN
ID SPAG5_HUMAN Reviewed; 1193 AA.
AC Q96R06; O95213; Q9BWE8; Q9NT17; Q9UFE6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sperm-associated antigen 5;
DE AltName: Full=Astrin;
DE AltName: Full=Deepest;
DE AltName: Full=Mitotic spindle-associated protein p126;
DE Short=MAP126;
GN Name=SPAG5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11724960; DOI=10.1073/pnas.261371298;
RA Mack G.J., Compton D.A.;
RT "Analysis of mitotic microtubule-associated proteins using mass
RT spectrometry identifies astrin, a spindle-associated protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14434-14439(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11549262; DOI=10.1006/bbrc.2001.5554;
RA Chang M.-S., Huang C.-J., Chen M.-L., Chen S.-T., Fan C.-C., Chu J.-M.,
RA Lin W.-C., Yang Y.-C.;
RT "Cloning and characterization of hMAP126, a new member of mitotic spindle-
RT associated proteins.";
RL Biochem. Biophys. Res. Commun. 287:116-121(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RA Schnabel J., Weber K., Hatzfeld M.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-1193.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT STRUCTURE.
RX PubMed=12356910; DOI=10.1242/jcs.00088;
RA Gruber J., Harborth J., Schnabel J., Weber K., Hatzfeld M.;
RT "The mitotic-spindle-associated protein astrin is essential for progression
RT through mitosis.";
RL J. Cell Sci. 115:4053-4059(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17664331; DOI=10.1083/jcb.200701163;
RA Thein K.H., Kleylein-Sohn J., Nigg E.A., Gruneberg U.;
RT "Astrin is required for the maintenance of sister chromatid cohesion and
RT centrosome integrity.";
RL J. Cell Biol. 178:345-354(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP FUNCTION, INTERACTION WITH TUBULINS, SUBCELLULAR LOCATION, INDUCTION, AND
RP PHOSPHORYLATION BY AURKA.
RX PubMed=18361916; DOI=10.1016/j.bbrc.2008.03.072;
RA Du J., Jablonski S., Yen T.J., Hannon G.J.;
RT "Astrin regulates Aurora-A localization.";
RL Biochem. Biophys. Res. Commun. 370:213-219(2008).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT THR-111; THR-937; SER-974 AND THR-978,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-111; THR-937; SER-974 AND
RP THR-978.
RX PubMed=18055457; DOI=10.1074/jbc.m706794200;
RA Cheng T.S., Hsiao Y.L., Lin C.C., Yu C.T., Hsu C.M., Chang M.S., Lee C.I.,
RA Huang C.Y., Howng S.L., Hong Y.R.;
RT "Glycogen synthase kinase 3beta interacts with and phosphorylates the
RT spindle-associated protein astrin.";
RL J. Biol. Chem. 283:2454-2464(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-135 AND SER-341, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP INTERACTION WITH DCLRE1B.
RX PubMed=19197158; DOI=10.4161/cc.8.4.7791;
RA Liu L., Akhter S., Bae J.B., Mukhopadhyay S.S., Richie C.T., Liu X.,
RA Legerski R.;
RT "SNM1B/Apollo interacts with astrin and is required for the prophase cell
RT cycle checkpoint.";
RL Cell Cycle 8:628-638(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-66; SER-135; SER-334;
RP THR-336; SER-341 AND SER-362, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH KNSTRN;
RP PLK1; DYNLL1 AND SGO2, AND INTERACTION WITH KNSTRN.
RX PubMed=21402792; DOI=10.1083/jcb.201008023;
RA Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.;
RT "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and
RT facilitates chromosome alignment.";
RL J. Cell Biol. 192:959-968(2011).
RN [19]
RP INTERACTION WITH DYNLL1.
RX PubMed=22965910; DOI=10.1083/jcb.201202112;
RA Dunsch A.K., Hammond D., Lloyd J., Schermelleh L., Gruneberg U., Barr F.A.;
RT "Dynein light chain 1 and a spindle-associated adaptor promote dynein
RT asymmetry and spindle orientation.";
RL J. Cell Biol. 198:1039-1054(2012).
RN [20]
RP FUNCTION, INTERACTION WITH G3BP1 AND RPTOR, AND SUBCELLULAR LOCATION.
RX PubMed=23953116; DOI=10.1016/j.cell.2013.07.031;
RA Thedieck K., Holzwarth B., Prentzell M.T., Boehlke C., Klasener K., Ruf S.,
RA Sonntag A.G., Maerz L., Grellscheid S.N., Kremmer E., Nitschke R.,
RA Kuehn E.W., Jonker J.W., Groen A.K., Reth M., Hall M.N., Baumeister R.;
RT "Inhibition of mTORC1 by astrin and stress granules prevents apoptosis in
RT cancer cells.";
RL Cell 154:859-874(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-159 AND SER-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP INTERACTION WITH OSBPL8.
RX PubMed=24424245; DOI=10.1016/j.yexcr.2014.01.002;
RA Zhong W., Zhou Y., Li J., Mysore R., Luo W., Li S., Chang M.S.,
RA Olkkonen V.M., Yan D.;
RT "OSBP-related protein 8 (ORP8) interacts with Homo sapiens sperm associated
RT antigen 5 (SPAG5) and mediates oxysterol interference of HepG2 cell
RT cycle.";
RL Exp. Cell Res. 322:227-235(2014).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDK5RAP2 AND PCM1.
RX PubMed=26297806; DOI=10.7554/elife.07519;
RA Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L.,
RA Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N.,
RA Walsh C.A., Reiter J.F.;
RT "Centriolar satellites assemble centrosomal microcephaly proteins to
RT recruit CDK2 and promote centriole duplication.";
RL Elife 4:0-0(2015).
RN [24]
RP FUNCTION, INTERACTION NUMA1, AND SUBCELLULAR LOCATION.
RX PubMed=27462074; DOI=10.1074/jbc.m116.724831;
RA Chu X., Chen X., Wan Q., Zheng Z., Du Q.;
RT "Nuclear mitotic apparatus (NuMA) interacts with and regulates astrin at
RT the mitotic spindle.";
RL J. Biol. Chem. 291:20055-20067(2016).
CC -!- FUNCTION: Essential component of the mitotic spindle required for
CC normal chromosome segregation and progression into anaphase
CC (PubMed:11724960, PubMed:12356910, PubMed:27462074). Required for
CC chromosome alignment, normal timing of sister chromatid segregation,
CC and maintenance of spindle pole architecture (PubMed:17664331,
CC PubMed:27462074). In complex with SKAP, promotes stable microtubule-
CC kinetochore attachments. May contribute to the regulation of separase
CC activity. May regulate AURKA localization to mitotic spindle, but not
CC to centrosomes and CCNB1 localization to both mitotic spindle and
CC centrosomes (PubMed:18361916, PubMed:21402792). Involved in centriole
CC duplication. Required for CDK5RAP2, CEP152, WDR62 and CEP63 centrosomal
CC localization and promotes the centrosomal localization of CDK2
CC (PubMed:26297806). In non-mitotic cells, upon stress induction,
CC inhibits mammalian target of rapamycin complex 1 (mTORC1) association
CC and recruits the mTORC1 component RPTOR to stress granules (SGs),
CC thereby preventing mTORC1 hyperactivation-induced apoptosis
CC (PubMed:23953116). May enhance GSK3B-mediated phosphorylation of other
CC substrates, such as MAPT/TAU (PubMed:18055457).
CC {ECO:0000269|PubMed:12356910, ECO:0000269|PubMed:17664331,
CC ECO:0000269|PubMed:18055457, ECO:0000269|PubMed:18361916,
CC ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:23953116,
CC ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:27462074,
CC ECO:0000305|PubMed:11724960}.
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 (PubMed:27462074). Interacts with DCLRE1B/Apollo. Part of an astrin
CC (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1
CC and SGO2. Interacts with KNSTRN. Interacts with RPTOR; this interaction
CC competes with RPTOR binding to MTOR, resulting in decreased mTORC1
CC formation. Interacts with G3BP1. The complex formed with G3BP1 AND
CC RPTOR is increased by oxidative stress. Interacts with OSBPL8, PCM1 and
CC CDK5RAP2 (PubMed:24424245, PubMed:26297806). Interacts (via C-terminus)
CC with NUMA1 (via C-terminus); this interaction promotes the recruitment
CC of SPAG5 to the microtubules at spindle poles in a dynein-dynactin-
CC dependent manner (PubMed:27462074). Interacts with DYNLL1
CC (PubMed:22965910). {ECO:0000269|PubMed:11724960,
CC ECO:0000269|PubMed:12356910, ECO:0000269|PubMed:18361916,
CC ECO:0000269|PubMed:19197158, ECO:0000269|PubMed:21402792,
CC ECO:0000269|PubMed:22965910, ECO:0000269|PubMed:23953116,
CC ECO:0000269|PubMed:24424245, ECO:0000269|PubMed:26297806,
CC ECO:0000269|PubMed:27462074}.
CC -!- INTERACTION:
CC Q96R06; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-413317, EBI-10187270;
CC Q96R06; O14965: AURKA; NbExp=3; IntAct=EBI-413317, EBI-448680;
CC Q96R06; A0AVN2: BARD1; NbExp=3; IntAct=EBI-413317, EBI-9977322;
CC Q96R06; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-413317, EBI-8643161;
CC Q96R06; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-413317, EBI-10175300;
CC Q96R06; Q86Y33: CDC20B; NbExp=3; IntAct=EBI-413317, EBI-10260504;
CC Q96R06; Q96SN8: CDK5RAP2; NbExp=3; IntAct=EBI-413317, EBI-308374;
CC Q96R06; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-413317, EBI-1003700;
CC Q96R06; Q9P209: CEP72; NbExp=2; IntAct=EBI-413317, EBI-739498;
CC Q96R06; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-413317, EBI-743375;
CC Q96R06; Q7Z460: CLASP1; NbExp=3; IntAct=EBI-413317, EBI-913476;
CC Q96R06; O43602: DCX; NbExp=3; IntAct=EBI-413317, EBI-8646694;
CC Q96R06; O60573: EIF4E2; NbExp=3; IntAct=EBI-413317, EBI-398610;
CC Q96R06; Q9NVF7: FBXO28; NbExp=3; IntAct=EBI-413317, EBI-740282;
CC Q96R06; P55040: GEM; NbExp=3; IntAct=EBI-413317, EBI-744104;
CC Q96R06; Q0D2H9: GOLGA8DP; NbExp=3; IntAct=EBI-413317, EBI-10181276;
CC Q96R06; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-413317, EBI-10181260;
CC Q96R06; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-413317, EBI-2514791;
CC Q96R06; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-413317, EBI-11955401;
CC Q96R06; Q7Z3B3: KANSL1; NbExp=3; IntAct=EBI-413317, EBI-740244;
CC Q96R06; P12035: KRT3; NbExp=3; IntAct=EBI-413317, EBI-2430095;
CC Q96R06; O95678: KRT75; NbExp=3; IntAct=EBI-413317, EBI-2949715;
CC Q96R06; Q8TCE9: LGALS14; NbExp=6; IntAct=EBI-413317, EBI-10274069;
CC Q96R06; Q96FE5: LINGO1; NbExp=3; IntAct=EBI-413317, EBI-719955;
CC Q96R06; O76041: NEBL; NbExp=3; IntAct=EBI-413317, EBI-2880203;
CC Q96R06; Q9Y5N6: ORC6; NbExp=4; IntAct=EBI-413317, EBI-374840;
CC Q96R06; Q9BZF1: OSBPL8; NbExp=6; IntAct=EBI-413317, EBI-2684038;
CC Q96R06; Q15154: PCM1; NbExp=2; IntAct=EBI-413317, EBI-741421;
CC Q96R06; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-413317, EBI-2568609;
CC Q96R06; Q16512: PKN1; NbExp=3; IntAct=EBI-413317, EBI-602382;
CC Q96R06; O00444: PLK4; NbExp=3; IntAct=EBI-413317, EBI-746202;
CC Q96R06; P62875: POLR2L; NbExp=3; IntAct=EBI-413317, EBI-359527;
CC Q96R06; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-413317, EBI-11956563;
CC Q96R06; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-413317, EBI-740773;
CC Q96R06; Q8N122: RPTOR; NbExp=9; IntAct=EBI-413317, EBI-1567928;
CC Q96R06; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-413317, EBI-747035;
CC Q96R06; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-413317, EBI-455078;
CC Q96R06; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-413317, EBI-10244848;
CC Q96R06; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-413317, EBI-9053916;
CC Q96R06; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-413317, EBI-6447954;
CC Q96R06; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-413317, EBI-740767;
CC Q96R06; G3V1X1: ZFC3H1; NbExp=3; IntAct=EBI-413317, EBI-6448783;
CC Q96R06; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-413317, EBI-2682299;
CC Q96R06; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-413317, EBI-10172590;
CC Q96R06; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-413317, EBI-16429014;
CC Q96R06; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-413317, EBI-25475920;
CC Q96R06; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-413317, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27462074}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27462074}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:27462074}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:27462074}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:27462074}. Midbody.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
CC Cytoplasmic granule. Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriolar satellite {ECO:0000269|PubMed:26297806}.
CC Note=Colocalizes with PCM1 at centriolar satellites throughout the cell
CC cycle (PubMed:26297806). In a punctate pattern in interphase cells.
CC During mitosis, detected at spindle poles during prophase, throughout
CC the spindle in metaphase and anaphase, and at midzone microtubules in
CC anaphase and telophase (PubMed:27462074). Efficient targeting to the
CC mitotic spindle may depend upon phosphorylation by GSK3B. Detected on
CC kinetochores of chromosomes that have congressed. The astrin (SPAG5)-
CC kinastrin (SKAP) complex localizes to the microtubule plus ends (By
CC similarity). In non-mitotic non-stressed cells, shows a microtubuli
CC pattern. In arsenite-stressed cells, accumulates in stress granules.
CC {ECO:0000250, ECO:0000269|PubMed:26297806,
CC ECO:0000269|PubMed:27462074}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Detected at low levels
CC in placenta, liver, pancreas, thymus and colon.
CC {ECO:0000269|PubMed:11549262}.
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:0000269|PubMed:18361916}.
CC -!- PTM: Phosphorylated by AURKA. {ECO:0000269|PubMed:18055457,
CC ECO:0000269|PubMed:18361916}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD02813.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL06396.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF399910; AAK91712.1; -; mRNA.
DR EMBL; AF345347; AAL06396.2; ALT_FRAME; mRNA.
DR EMBL; AF063308; AAD02813.1; ALT_FRAME; mRNA.
DR EMBL; BC000322; AAH00322.1; -; mRNA.
DR EMBL; AL122116; CAB59275.1; -; mRNA.
DR EMBL; AL137585; CAB70827.1; -; mRNA.
DR CCDS; CCDS32594.1; -.
DR PIR; JC7765; JC7765.
DR PIR; T34542; T34542.
DR PIR; T46296; T46296.
DR RefSeq; NP_006452.3; NM_006461.3.
DR AlphaFoldDB; Q96R06; -.
DR SMR; Q96R06; -.
DR BioGRID; 115861; 178.
DR CORUM; Q96R06; -.
DR DIP; DIP-30998N; -.
DR IntAct; Q96R06; 122.
DR MINT; Q96R06; -.
DR STRING; 9606.ENSP00000323300; -.
DR GlyGen; Q96R06; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96R06; -.
DR PhosphoSitePlus; Q96R06; -.
DR BioMuta; SPAG5; -.
DR DMDM; 47117278; -.
DR EPD; Q96R06; -.
DR jPOST; Q96R06; -.
DR MassIVE; Q96R06; -.
DR MaxQB; Q96R06; -.
DR PaxDb; Q96R06; -.
DR PeptideAtlas; Q96R06; -.
DR PRIDE; Q96R06; -.
DR ProteomicsDB; 77922; -.
DR Antibodypedia; 14156; 247 antibodies from 33 providers.
DR DNASU; 10615; -.
DR Ensembl; ENST00000321765.10; ENSP00000323300.5; ENSG00000076382.17.
DR GeneID; 10615; -.
DR KEGG; hsa:10615; -.
DR MANE-Select; ENST00000321765.10; ENSP00000323300.5; NM_006461.4; NP_006452.3.
DR UCSC; uc002hbq.4; human.
DR CTD; 10615; -.
DR DisGeNET; 10615; -.
DR GeneCards; SPAG5; -.
DR HGNC; HGNC:13452; SPAG5.
DR HPA; ENSG00000076382; Tissue enhanced (bone marrow, kidney, testis).
DR MIM; 615562; gene.
DR neXtProt; NX_Q96R06; -.
DR OpenTargets; ENSG00000076382; -.
DR PharmGKB; PA134868542; -.
DR VEuPathDB; HostDB:ENSG00000076382; -.
DR eggNOG; ENOG502RW0Y; Eukaryota.
DR GeneTree; ENSGT00400000022377; -.
DR HOGENOM; CLU_007803_0_0_1; -.
DR InParanoid; Q96R06; -.
DR OMA; LEDCKGQ; -.
DR OrthoDB; 257437at2759; -.
DR PhylomeDB; Q96R06; -.
DR TreeFam; TF336280; -.
DR PathwayCommons; Q96R06; -.
DR SignaLink; Q96R06; -.
DR SIGNOR; Q96R06; -.
DR BioGRID-ORCS; 10615; 136 hits in 1083 CRISPR screens.
DR ChiTaRS; SPAG5; human.
DR GeneWiki; Sperm_associated_antigen_5; -.
DR GenomeRNAi; 10615; -.
DR Pharos; Q96R06; Tbio.
DR PRO; PR:Q96R06; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96R06; protein.
DR Bgee; ENSG00000076382; Expressed in left testis and 128 other tissues.
DR ExpressionAtlas; Q96R06; baseline and differential.
DR Genevisible; Q96R06; HS.
DR GO; GO:0034451; C:centriolar satellite; IMP:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0051294; P:establishment of spindle orientation; IEA:Ensembl.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0032388; P:positive regulation of intracellular transport; IMP:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0090235; P:regulation of metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IMP: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..1193
FT /note="Sperm-associated antigen 5"
FT /id="PRO_0000072093"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..850
FT /note="Interaction with KNSTRN"
FT /evidence="ECO:0000269|PubMed:21402792"
FT COILED 545..608
FT /evidence="ECO:0000255"
FT COILED 759..868
FT /evidence="ECO:0000255"
FT COILED 979..1174
FT /evidence="ECO:0000255"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TME2"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TME2"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 111
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:18055457"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 937
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:18055457"
FT MOD_RES 974
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:18055457"
FT MOD_RES 978
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:18055457"
FT MUTAGEN 111
FT /note="T->A: Decreased phosphorylation by GSK3-beta.
FT Partial loss of spindle association; when associated with
FT A-937, A974 and A-978."
FT /evidence="ECO:0000269|PubMed:18055457"
FT MUTAGEN 937
FT /note="T->A: Decreased phosphorylation by GSK3-beta.
FT Partial loss of spindle association; when associated with
FT A-111, A974 and A-978."
FT /evidence="ECO:0000269|PubMed:18055457"
FT MUTAGEN 974
FT /note="S->A: Decreased phosphorylation by GSK3-beta; when
FT associated with A-978. Partial loss of spindle association;
FT when associated with A-111, A937 and A-978."
FT /evidence="ECO:0000269|PubMed:18055457"
FT MUTAGEN 978
FT /note="T->A: Decreased phosphorylation by GSK3-beta; when
FT associated with A-97A. Partial loss of spindle association;
FT when associated with A-111, A-937 and A-974."
FT /evidence="ECO:0000269|PubMed:18055457"
FT CONFLICT 38
FT /note="N -> T (in Ref. 1; AAK91712, 2; AAL06396 and 3;
FT AAD02813)"
FT /evidence="ECO:0000305"
FT CONFLICT 445..447
FT /note="LEV -> VEF (in Ref. 1; AAK91712, 2; AAL06396 and 3;
FT AAD02813)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="S -> N (in Ref. 1; AAK91712, 2; AAL06396 and 3;
FT AAD02813)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="S -> I (in Ref. 1; AAK91712, 2; AAL06396 and 3;
FT AAD02813)"
FT /evidence="ECO:0000305"
FT CONFLICT 771..772
FT /note="WQ -> CV (in Ref. 1; AAK91712, 2; AAL06396 and 3;
FT AAD02813)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="Missing (in Ref. 2; AAL06396 and 3; AAD02813)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1193 AA; 134422 MW; A846DB3FE624519C CRC64;
MWRVKKLSLS LSPSPQTGKP SMRTPLRELT LQPGALTNSG KRSPACSSLT PSLCKLGLQE
GSNNSSPVDF VNNKRTDLSS EHFSHSSKWL ETCQHESDEQ PLDPIPQISS TPKTSEEAVD
PLGNYMVKTI VLVPSPLGQQ QDMIFEARLD TMAETNSISL NGPLRTDDLV REEVAPCMGD
RFSEVAAVSE KPIFQESPSH LLEESPPNPC SEQLHCSKES LSSRTEAVRE DLVPSESNAF
LPSSVLWLSP STALAADFRV NHVDPEEEIV EHGAMEEREM RFPTHPKESE TEDQALVSSV
EDILSTCLTP NLVEMESQEA PGPAVEDVGR ILGSDTESWM SPLAWLEKGV NTSVMLENLR
QSLSLPSMLR DAAIGTTPFS TCSVGTWFTP SAPQEKSTNT SQTGLVGTKH STSETEQLLC
GRPPDLTALS RHDLEDNLLS SLVILEVLSR QLRDWKSQLA VPHPETQDSS TQTDTSHSGI
TNKLQHLKES HEMGQALQQA RNVMQSWVLI SKELISLLHL SLLHLEEDKT TVSQESRRAE
TLVCCCFDLL KKLRAKLQSL KAEREEARHR EEMALRGKDA AEIVLEAFCA HASQRISQLE
QDLASMREFR GLLKDAQTQL VGLHAKQEEL VQQTVSLTST LQQDWRSMQL DYTTWTALLS
RSRQLTEKLT VKSQQALQER DVAIEEKQEV SRVLEQVSAQ LEECKGQTEQ LELENSRLAT
DLRAQLQILA NMDSQLKELQ SQHTHCAQDL AMKDELLCQL TQSNEEQAAQ WQKEEMALKH
MQAELQQQQA VLAKEVRDLK ETLEFADQEN QVAHLELGQV ECQLKTTLEV LRERSLQCEN
LKDTVENLTA KLASTIADNQ EQDLEKTRQY SQKLGLLTEQ LQSLTLFLQT KLKEKTEQET
LLLSTACPPT QEHPLPNDRT FLGSILTAVA DEEPESTPVP LLGSDKSAFT RVASMVSLQP
AETPGMEESL AEMSIMTTEL QSLCSLLQES KEEAIRTLQR KICELQARLQ AQEEQHQEVQ
KAKEADIEKL NQALCLRYKN EKELQEVIQQ QNEKILEQID KSGELISLRE EVTHLTRSLR
RAETETKVLQ EALAGQLDSN CQPMATNWIQ EKVWLSQEVD KLRVMFLEMK NEKEKLMIKF
QSHRNILEEN LRRSDKELEK LDDIVQHIYK TLLSIPEVVR GCKELQGLLE FLS
