SPDYA_MOUSE
ID SPDYA_MOUSE Reviewed; 310 AA.
AC Q5IBH7; B8JJC0; Q5IBH8; Q8C5T5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Speedy protein A;
DE AltName: Full=Protein expressed in male leptotene and zygotene spermatocytes 465;
DE Short=MLZ-465;
DE AltName: Full=Rapid inducer of G2/M progression in oocytes A;
DE Short=RINGO A;
DE Short=mSpy/Ringo A;
DE AltName: Full=Speedy-1;
DE Short=Spy1;
GN Name=Spdya {ECO:0000312|MGI:MGI:1918141};
GN Synonyms=Spdy1 {ECO:0000312|MGI:MGI:1918141};
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] {ECO:0000305, ECO:0000312|EMBL:AAW32477.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP CDK1 AND CDK2, TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF ASP-89;
RP MET-102; TYR-106; PHE-107 AND 133-GLU--ASP-135.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAW32477.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAW32477.1};
RX PubMed=15611625; DOI=10.4161/cc.4.1.1347;
RA Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.;
RT "Identification and comparative analysis of multiple mammalian Speedy/Ringo
RT proteins.";
RL Cell Cycle 4:155-165(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC36637.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36637.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC36637.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=11730327; DOI=10.1016/s0248-4900(01)01122-4;
RA Terret M.E., Ferby I., Nebreda A.R., Verlhac M.H.;
RT "RINGO efficiently triggers meiosis resumption in mouse oocytes and induces
RT cell cycle arrest in embryos.";
RL Biol. Cell 93:89-97(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND THR-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20339383; DOI=10.1038/jhg.2010.26;
RA Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T.,
RA Inagaki H., Taniguchi M., Toda T., Kurahashi H.;
RT "Screening of genes involved in chromosome segregation during meiosis I:
RT toward the identification of genes responsible for infertility in humans.";
RL J. Hum. Genet. 55:293-299(2010).
CC -!- FUNCTION: Regulates the G1/S phase transition of the cell cycle by
CC binding and activating CDK1 and CDK2 (PubMed:15611625). Contributes to
CC CDK2 activation without promoting CDK2 phosphorylation, by inducing a
CC conformation change of the CDK2 T-loop that obstructs the substrate-
CC binding cleft prior to kinase activation. Interferes with CDKN1B-
CC mediated inhibition of CDK2. Mediates cell survival during the DNA
CC damage process through activation of CDK2 (By similarity).
CC {ECO:0000250|UniProtKB:Q5MJ70, ECO:0000269|PubMed:15611625}.
CC -!- SUBUNIT: Interacts with CDK1, CDK2 and CDKN1B/KIP1 (PubMed:15611625).
CC Identified in a complex with CDK2 and CDKN1B/KIP1, where it interacts
CC primarily with CDK2 (By similarity). {ECO:0000250|UniProtKB:Q5MJ70,
CC ECO:0000269|PubMed:15611625}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20339383}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2 {ECO:0000269|PubMed:15611625}; Synonyms=A2
CC {ECO:0000269|PubMed:15611625};
CC IsoId=Q5IBH7-2; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:15611625}; Synonyms=A1
CC {ECO:0000269|PubMed:15611625};
CC IsoId=Q5IBH7-1; Sequence=VSP_052029, VSP_052030;
CC -!- TISSUE SPECIFICITY: Expressed at a high level in testis. Also expressed
CC in the adult ovary and in immature oocytes.
CC {ECO:0000269|PubMed:11730327, ECO:0000269|PubMed:15611625,
CC ECO:0000269|PubMed:20339383}.
CC -!- DOMAIN: The C-terminus is required for CDK2-activation, but not CDK2-
CC binding. {ECO:0000269|PubMed:15611625}.
CC -!- SIMILARITY: Belongs to the Speedy/Ringo family. {ECO:0000305}.
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DR EMBL; AY820306; AAW32476.1; -; mRNA.
DR EMBL; AY820307; AAW32477.1; -; mRNA.
DR EMBL; AK077138; BAC36637.1; -; mRNA.
DR EMBL; CT010429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50178.1; -. [Q5IBH7-2]
DR CCDS; CCDS50179.1; -. [Q5IBH7-1]
DR RefSeq; NP_001136103.1; NM_001142631.1. [Q5IBH7-1]
DR RefSeq; NP_083530.1; NM_029254.1. [Q5IBH7-2]
DR RefSeq; XP_006524970.1; XM_006524907.2. [Q5IBH7-2]
DR RefSeq; XP_006524971.1; XM_006524908.2. [Q5IBH7-2]
DR RefSeq; XP_011244904.1; XM_011246602.2. [Q5IBH7-2]
DR AlphaFoldDB; Q5IBH7; -.
DR SMR; Q5IBH7; -.
DR STRING; 10090.ENSMUSP00000118426; -.
DR iPTMnet; Q5IBH7; -.
DR PhosphoSitePlus; Q5IBH7; -.
DR SwissPalm; Q5IBH7; -.
DR PaxDb; Q5IBH7; -.
DR PRIDE; Q5IBH7; -.
DR ProteomicsDB; 257556; -. [Q5IBH7-2]
DR ProteomicsDB; 257557; -. [Q5IBH7-1]
DR Antibodypedia; 28865; 220 antibodies from 26 providers.
DR Ensembl; ENSMUST00000124001; ENSMUSP00000118426; ENSMUSG00000052525. [Q5IBH7-1]
DR Ensembl; ENSMUST00000144142; ENSMUSP00000118994; ENSMUSG00000052525. [Q5IBH7-2]
DR Ensembl; ENSMUST00000167641; ENSMUSP00000125912; ENSMUSG00000052525. [Q5IBH7-2]
DR GeneID; 70891; -.
DR KEGG; mmu:70891; -.
DR UCSC; uc008dmo.2; mouse. [Q5IBH7-2]
DR CTD; 245711; -.
DR MGI; MGI:1918141; Spdya.
DR VEuPathDB; HostDB:ENSMUSG00000052525; -.
DR eggNOG; KOG3938; Eukaryota.
DR GeneTree; ENSGT00940000154524; -.
DR HOGENOM; CLU_070353_1_2_1; -.
DR InParanoid; Q5IBH7; -.
DR OMA; VCQTPPT; -.
DR OrthoDB; 1480540at2759; -.
DR PhylomeDB; Q5IBH7; -.
DR TreeFam; TF329827; -.
DR BioGRID-ORCS; 70891; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Spdya; mouse.
DR PRO; PR:Q5IBH7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q5IBH7; protein.
DR Bgee; ENSMUSG00000052525; Expressed in spermatocyte and 82 other tissues.
DR ExpressionAtlas; Q5IBH7; baseline and differential.
DR Genevisible; Q5IBH7; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IEP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
DR InterPro; IPR020984; Speedy.
DR Pfam; PF11357; Spy1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Developmental protein; DNA damage;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..310
FT /note="Speedy protein A"
FT /id="PRO_0000234113"
FT REGION 67..199
FT /note="Speedy/Ringo box; Required for CDK-binding"
FT /evidence="ECO:0000269|PubMed:15611625"
FT REGION 241..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 281..283
FT /note="VAN -> GMA (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15611625,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052029"
FT VAR_SEQ 284..310
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15611625,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052030"
FT MUTAGEN 89
FT /note="D->A: Abolishes interaction with CDK2."
FT /evidence="ECO:0000269|PubMed:15611625"
FT MUTAGEN 102
FT /note="M->A: Abolishes interaction with CDK2."
FT /evidence="ECO:0000269|PubMed:15611625"
FT MUTAGEN 106
FT /note="Y->A: Abolishes interaction with CDK2."
FT /evidence="ECO:0000269|PubMed:15611625"
FT MUTAGEN 107
FT /note="F->A: Abolishes interaction with CDK2."
FT /evidence="ECO:0000269|PubMed:15611625"
FT MUTAGEN 133..135
FT /note="EED->AAA: No effect on CDK2-binding."
FT /evidence="ECO:0000269|PubMed:15611625"
FT CONFLICT 258
FT /note="D -> G (in Ref. 1; AAW32476/AAW32477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 36115 MW; 10F372690FF03826 CRC64;
MRHNQMYCET PPTVTIHVKS GSNRSHQTRK PISLKRPILK DSWEASENNA QNNKSKRPRG
PCLIIQRQEM TAFFKLFDDD LIQDFLWMDC CCKIADKYLL AMTFVYFKRA KFTINEHTRI
NFFIALYLAN TVEEDEEEAK YEIFPWALGK NWRKLFPNFL KLRDQLWDRI DYRAIVSRRC
CEEVMAIAPT HYIWQRERSV HHSGAVRNYN RDEVHLPRGP SATPVDCSLC GKKGRYVRLG
LSSSSSSSSD TGELMEKDSQ ELHSAFSVDT AGDPPHTYSQ VANDHQSNKE NETNFVKKNK
SVEWFAESEE
