SPIN1_MOUSE
ID SPIN1_MOUSE Reviewed; 262 AA.
AC Q61142; Q3TLC3; Q3UT05; Q91VG8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Spindlin-1;
DE AltName: Full=30000 Mr metaphase complex;
DE AltName: Full=SSEC P;
DE AltName: Full=Spindlin1;
GN Name=Spin1; Synonyms=Spin;
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] (ISOFORM 2), SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Embryo;
RX PubMed=9053325; DOI=10.1242/dev.124.2.493;
RA Oh B., Hwang S.Y., Solter D., Knowles B.B.;
RT "Spindlin, a major maternal transcript expressed in the mouse during the
RT transition from oocyte to embryo.";
RL Development 124:493-503(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Embryo, Embryonic heart, Embryonic limb, and Thymus;
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 MRNA] (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 TISSUE SPECIFICITY (ISOFORM 1).
RX PubMed=18645677; DOI=10.1111/j.1745-7262.2008.00424.x;
RA Zhang K.M., Wang Y.F., Huo R., Bi Y., Lin M., Sha J.H., Zhou Z.M.;
RT "Characterization of Spindlin1 isoform2 in mouse testis.";
RL Asian J. Androl. 10:741-748(2008).
RN [5]
RP FUNCTION.
RX PubMed=18543248; DOI=10.1002/jcp.21515;
RA Zhang P., Cong B., Yuan H., Chen L., Lv Y., Bai C., Nan X., Shi S., Yue W.,
RA Pei X.;
RT "Overexpression of spindlin1 induces metaphase arrest and chromosomal
RT instability.";
RL J. Cell. Physiol. 217:400-408(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH HABP4 AND SERBP1.
RX PubMed=23894536; DOI=10.1371/journal.pone.0069764;
RA Chew T.G., Peaston A., Lim A.K., Lorthongpanich C., Knowles B.B.,
RA Solter D.;
RT "A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein
RT SERBP1 and is involved in mouse oocyte meiotic resumption.";
RL PLoS ONE 8:E69764-E69764(2013).
CC -!- FUNCTION: Chromatin reader that specifically recognizes and binds
CC histone H3 both trimethylated at 'Lys-4' and asymmetrically
CC dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator
CC of Wnt signaling pathway downstream of PRMT2. In case of cancer,
CC promotes cell cancer proliferation via activation of the Wnt signaling
CC pathway (By similarity). Overexpression induces metaphase arrest and
CC chromosomal instability (PubMed:18543248). Localizes to active rDNA
CC loci and promotes the expression of rRNA genes. May play a role in
CC cell-cycle regulation during the transition from gamete to embryo.
CC Involved in oocyte meiotic resumption, a process that takes place
CC before ovulation to resume meiosis of oocytes blocked in prophase I:
CC may act by regulating maternal transcripts to control meiotic
CC resumption (PubMed:23894536). {ECO:0000250|UniProtKB:Q9Y657,
CC ECO:0000269|PubMed:18543248, ECO:0000269|PubMed:23894536}.
CC -!- SUBUNIT: Homodimer; may form higher-order oligomers. Interacts with
CC TCF7L2/TCF4; the interaction is direct (By similarity). Interacts with
CC HABP4 and SERBP1 (PubMed:23894536). Interacts with C11orf84/SPINDOC (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y657,
CC ECO:0000269|PubMed:23894536}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9053325}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:9053325}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9Y657}. Note=Associates with the meiotic
CC spindle. {ECO:0000269|PubMed:9053325}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61142-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61142-2; Sequence=VSP_017942;
CC -!- TISSUE SPECIFICITY: Oocyte, egg, and very early embryo; not in the 8-,
CC and 16-cell stage of the embryo. Isoform 1: Present in testis. Isoform
CC 1 is more highly expressed in adult testes compared with newborn testes
CC (at protein level). {ECO:0000269|PubMed:9053325}.
CC -!- DEVELOPMENTAL STAGE: Gametogenesis. Synthesized from maternal
CC transcripts but not from the zygote genome.
CC {ECO:0000269|PubMed:9053325}.
CC -!- DOMAIN: The 3 tudor-like domains (also named Spin/Ssty repeats)
CC specifically recognize and bind methylated histones. H3K4me3 and
CC H3R8me2a are recognized by tudor-like domains 2 and 1, respectively.
CC {ECO:0000250|UniProtKB:Q9Y657}.
CC -!- PTM: Phosphorylated during oocyte meiotic maturation.
CC {ECO:0000269|PubMed:9053325}.
CC -!- PTM: Post-translationally modified during the first mitotic cell cycle.
CC -!- DISRUPTION PHENOTYPE: Early postnatal lethality. Ovarian
CC folliculogenesis and oocyte growth appear normal but fully grown
CC oocytes show defects in resuming meiosis.
CC {ECO:0000269|PubMed:23894536}.
CC -!- SIMILARITY: Belongs to the SPIN/STSY family. {ECO:0000305}.
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DR EMBL; U48972; AAA91233.1; -; mRNA.
DR EMBL; AK088127; BAC40162.1; -; mRNA.
DR EMBL; AK134259; BAE22069.1; -; mRNA.
DR EMBL; AK136251; BAE22897.1; -; mRNA.
DR EMBL; AK139899; BAE24175.1; -; mRNA.
DR EMBL; AK162171; BAE36769.1; -; mRNA.
DR EMBL; AK162195; BAE36784.1; -; mRNA.
DR EMBL; AK162258; BAE36820.1; -; mRNA.
DR EMBL; AK163263; BAE37266.1; -; mRNA.
DR EMBL; AK163293; BAE37280.1; -; mRNA.
DR EMBL; AK163382; BAE37327.1; -; mRNA.
DR EMBL; AK166528; BAE38832.1; -; mRNA.
DR EMBL; AK166580; BAE38869.1; -; mRNA.
DR EMBL; AK166677; BAE38937.1; -; mRNA.
DR EMBL; AK168544; BAE40420.1; -; mRNA.
DR EMBL; BC016517; AAH16517.1; -; mRNA.
DR CCDS; CCDS26510.1; -. [Q61142-1]
DR RefSeq; NP_001269957.1; NM_001283028.1. [Q61142-1]
DR RefSeq; NP_001269958.1; NM_001283029.1. [Q61142-1]
DR RefSeq; NP_001269959.1; NM_001283030.1.
DR RefSeq; NP_035592.1; NM_011462.3. [Q61142-2]
DR RefSeq; NP_666155.1; NM_146043.4. [Q61142-1]
DR RefSeq; XP_006516956.1; XM_006516893.3. [Q61142-1]
DR RefSeq; XP_006516957.1; XM_006516894.3. [Q61142-1]
DR RefSeq; XP_017170958.1; XM_017315469.1. [Q61142-1]
DR AlphaFoldDB; Q61142; -.
DR SMR; Q61142; -.
DR BioGRID; 203451; 4.
DR IntAct; Q61142; 1.
DR MINT; Q61142; -.
DR STRING; 10090.ENSMUSP00000093473; -.
DR iPTMnet; Q61142; -.
DR PhosphoSitePlus; Q61142; -.
DR REPRODUCTION-2DPAGE; Q61142; -.
DR EPD; Q61142; -.
DR MaxQB; Q61142; -.
DR PaxDb; Q61142; -.
DR PeptideAtlas; Q61142; -.
DR PRIDE; Q61142; -.
DR ProteomicsDB; 258591; -. [Q61142-1]
DR ProteomicsDB; 258592; -. [Q61142-2]
DR Antibodypedia; 6817; 209 antibodies from 30 providers.
DR DNASU; 20729; -.
DR Ensembl; ENSMUST00000095797; ENSMUSP00000093473; ENSMUSG00000021395. [Q61142-1]
DR GeneID; 20729; -.
DR KEGG; mmu:20729; -.
DR UCSC; uc007qly.2; mouse. [Q61142-1]
DR UCSC; uc007qmb.3; mouse. [Q61142-2]
DR CTD; 10927; -.
DR MGI; MGI:109242; Spin1.
DR VEuPathDB; HostDB:ENSMUSG00000021395; -.
DR eggNOG; ENOG502QRYD; Eukaryota.
DR GeneTree; ENSGT00950000182925; -.
DR HOGENOM; CLU_068595_0_0_1; -.
DR InParanoid; Q61142; -.
DR OMA; CMCEYRK; -.
DR OrthoDB; 1027563at2759; -.
DR PhylomeDB; Q61142; -.
DR TreeFam; TF332665; -.
DR BioGRID-ORCS; 20729; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Spin1; mouse.
DR PRO; PR:Q61142; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61142; protein.
DR Bgee; ENSMUSG00000021395; Expressed in primary oocyte and 263 other tissues.
DR Genevisible; Q61142; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007143; P:female meiotic nuclear division; IC:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009303; P:rRNA transcription; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.80.10.70; -; 1.
DR InterPro; IPR003671; SPIN/Ssty.
DR InterPro; IPR042567; SPIN/Ssty_sf.
DR InterPro; IPR029565; Spindlin-1.
DR PANTHER; PTHR10405; PTHR10405; 1.
DR PANTHER; PTHR10405:SF15; PTHR10405:SF15; 1.
DR Pfam; PF02513; Spin-Ssty; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Chromatin regulator;
KW Cytoplasm; Cytoskeleton; Developmental protein; DNA-binding;
KW Isopeptide bond; Meiosis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..262
FT /note="Spindlin-1"
FT /id="PRO_0000181368"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..116
FT /note="Tudor-like domain 1"
FT /evidence="ECO:0000250"
FT REGION 93..98
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT REGION 132..193
FT /note="Tudor-like domain 2"
FT /evidence="ECO:0000250"
FT REGION 142
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT REGION 213..262
FT /note="Tudor-like domain 3"
FT /evidence="ECO:0000250"
FT REGION 250..252
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT SITE 173
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT SITE 184
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 109
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT MOD_RES 124
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT VAR_SEQ 1..34
FT /note="MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHK -> MASASSPASCPR
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9053325"
FT /id="VSP_017942"
SQ SEQUENCE 262 AA; 29643 MW; 33005229982E110E CRC64;
MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRTSV GPSKPVSQPR RNIVGCRIQH
GWREGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL ELNKDERVSA LEVLPDRVAT
SRISDAHLAD TMIGKAVEHM FETEDGSKDE WRGMVLARAP VMNTWFYITY EKDPVLYMYQ
LLDDYKEGDL RIMPDSNDSP PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP
SVYFIKFDDD FHIYVYDLVK TS
