TSYL2_MOUSE
ID TSYL2_MOUSE Reviewed; 677 AA.
AC Q7TQI8; Q6WRI3; Q9CU22;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Testis-specific Y-encoded-like protein 2;
DE Short=TSPY-like protein 2;
DE AltName: Full=CASK-interacting nucleosome assembly protein;
DE AltName: Full=Differentially-expressed nucleolar TGF-beta1 target protein;
GN Name=Tspyl2; Synonyms=Cinap, Dentt, DXBwg1396e, Tspx;
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], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12619135; DOI=10.1002/dvdy.10257;
RA Ozbun L.L., Martinez A., Angdisen J., Umphress S., Kang Y., Wang M.,
RA You M., Jakowlew S.B.;
RT "Differentially expressed nucleolar TGF-beta1 target (DENTT) in mouse
RT development.";
RL Dev. Dyn. 226:491-511(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH CASK AND HISTONES, AND IDENTIFICATION IN COMPLEX WITH CASK AND TBR1.
RC STRAIN=C57BL/6J;
RX PubMed=15066269; DOI=10.1016/s0896-6273(04)00139-4;
RA Wang G.-S., Hong C.-J., Yen T.-Y., Huang H.-Y., Ou Y., Huang T.-N.,
RA Jung W.-G., Kuo T.-Y., Sheng M., Wang T.-F., Hsueh Y.-P.;
RT "Transcriptional modification by a CASK-interacting nucleosome assembly
RT protein.";
RL Neuron 42:113-128(2004).
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 1-400.
RC STRAIN=C57BL/6J; TISSUE=Fetal eye;
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 [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=12112471; DOI=10.1002/dvdy.10096;
RA Martinez A., Ozbun L.L., Angdisen J., Jakowlew S.B.;
RT "Expression of differentially expressed nucleolar transforming growth
RT factor-beta1 target (DENTT) in adult mouse tissues.";
RL Dev. Dyn. 224:186-199(2002).
RN [7]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15241014; DOI=10.1023/b:chro.0000034134.91243.1c;
RA Delbridge M.L., Longepied G., Depetris D., Mattei M.-G., Disteche C.M.,
RA Marshall Graves J.A., Mitchell M.J.;
RT "TSPY, the candidate gonadoblastoma gene on the human Y chromosome, has a
RT widely expressed homologue on the X -- implications for Y chromosome
RT evolution.";
RL Chromosome Res. 12:345-356(2004).
RN [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16374801; DOI=10.1002/cne.20825;
RA Lin C.-W., Huang T.-N., Wang G.-S., Kuo T.-Y., Yen T.-Y., Hsueh Y.-P.;
RT "Neural activity- and development-dependent expression and distribution of
RT CASK interacting nucleosome assembly protein in mouse brain.";
RL J. Comp. Neurol. 494:606-619(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648; SER-652 AND SER-655, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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: Part of the CASK/TBR1/TSPYL2 transcriptional complex which
CC modulates gene expression in response to neuronal synaptic activity,
CC probably by facilitating nucleosome assembly. May inhibit cell
CC proliferation by inducing p53-dependent CDKN1A expression.
CC {ECO:0000269|PubMed:15066269}.
CC -!- SUBUNIT: Interacts with histones. Interacts with CASK. Part of a
CC complex containing CASK, TBR1 and TSPYL2.
CC {ECO:0000269|PubMed:15066269}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Enriched in
CC transcriptionally active regions of chromatin in neurons.
CC -!- TISSUE SPECIFICITY: Present at high levels in the pituitary gland and
CC at moderate levels in adrenal gland, brain, testis and ovary. In brain,
CC expressed both in mature neurons and progenitor cells (at protein
CC level). {ECO:0000269|PubMed:12112471, ECO:0000269|PubMed:15241014,
CC ECO:0000269|PubMed:16374801}.
CC -!- DEVELOPMENTAL STAGE: Present widely throughout embryogenesis. Present
CC in developing brain from 10.5 dpc to P7 (at protein level).
CC {ECO:0000269|PubMed:12619135, ECO:0000269|PubMed:16374801}.
CC -!- INDUCTION: By TGFB1 or serum in pituitary cell lines (at protein
CC level). {ECO:0000269|PubMed:12112471}.
CC -!- PTM: Phosphorylation at Thr-333 impairs function on cell proliferation.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Synaptic activity down-regulates TSPYL2 protein levels
CC by inducing rapid proteasomal degradation.
CC -!- MISCELLANEOUS: Subject to X inactivation.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; BK000279; DAA00247.1; -; mRNA.
DR EMBL; AY273809; AAQ17208.1; -; mRNA.
DR EMBL; AL731727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054393; AAH54393.1; -; mRNA.
DR EMBL; AK018700; BAB31351.1; -; mRNA.
DR CCDS; CCDS30474.1; -.
DR RefSeq; NP_084112.1; NM_029836.3.
DR AlphaFoldDB; Q7TQI8; -.
DR SMR; Q7TQI8; -.
DR STRING; 10090.ENSMUSP00000046782; -.
DR iPTMnet; Q7TQI8; -.
DR PhosphoSitePlus; Q7TQI8; -.
DR EPD; Q7TQI8; -.
DR MaxQB; Q7TQI8; -.
DR PaxDb; Q7TQI8; -.
DR PRIDE; Q7TQI8; -.
DR ProteomicsDB; 298003; -.
DR Antibodypedia; 12456; 263 antibodies from 37 providers.
DR DNASU; 52808; -.
DR Ensembl; ENSMUST00000044509; ENSMUSP00000046782; ENSMUSG00000041096.
DR GeneID; 52808; -.
DR KEGG; mmu:52808; -.
DR UCSC; uc009uqf.1; mouse.
DR CTD; 64061; -.
DR MGI; MGI:106244; Tspyl2.
DR VEuPathDB; HostDB:ENSMUSG00000041096; -.
DR eggNOG; KOG1508; Eukaryota.
DR GeneTree; ENSGT00940000162496; -.
DR HOGENOM; CLU_025445_0_0_1; -.
DR InParanoid; Q7TQI8; -.
DR OMA; PNGWANP; -.
DR OrthoDB; 1191764at2759; -.
DR PhylomeDB; Q7TQI8; -.
DR TreeFam; TF313386; -.
DR BioGRID-ORCS; 52808; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q7TQI8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q7TQI8; protein.
DR Bgee; ENSMUSG00000041096; Expressed in retinal neural layer and 224 other tissues.
DR ExpressionAtlas; Q7TQI8; baseline and differential.
DR Genevisible; Q7TQI8; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0045859; P:regulation of protein kinase activity; ISO:MGI.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromatin regulator; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..677
FT /note="Testis-specific Y-encoded-like protein 2"
FT /id="PRO_0000289102"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..46
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..634
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT CROSSLNK 158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT CONFLICT 12
FT /note="T -> G (in Ref. 5; BAB31351)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="P -> A (in Ref. 5; BAB31351)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="G -> R (in Ref. 5; BAB31351)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="S -> N (in Ref. 2; AAQ17208)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="S -> N (in Ref. 2; AAQ17208)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="T -> I (in Ref. 2; AAQ17208)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="R -> G (in Ref. 2; AAQ17208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 77671 MW; A7897CEC90F7B403 CRC64;
MDRPDEGPPA KTPRLSSSEP RQRDLPPPPP PPLQRLPLPP PQQRPRPQEE TEAAQVLADM
RGVGPTLPPP LPYVILEEGG IRAYFTLSAE SPGWDHAMES GFGEAPSTGI METLPSSEIS
GGSLAIDFQV AEPSSLGEKA LETCSLGGWG PQMLVGPKRK EEAIIIVEDE DEDDKESVRR
RQRRRRRRRK QRKAKESRER SAQRMESILQ ALESIQMDLE AVNIKAGKAF LRLKRKFIQM
RRPFLERRDL IIQHIPGFWV KAFLNHPRIS ILINQRDRDI FRYLTNLQVQ DLRHISMGYK
MKLYFQTNPY FTNMVIVKEF QRNRSGRLVS HSTPIRWHRG QEPQAYNRRS HDTRESFFNW
FSNHSLPEAD RIAEIIKNDL WVNPVRYYMR RGGYRSSRKK QHGKERAKNQ YEMVIMEDAH
DHYAIEDILS DISEIDEITD NETIHDIKIS DFMETTDYFE TTDNEVTDAN ENLCDSENPD
HSEGYNTKIT DNKGSVAANP DDNSDDPEEK NTYDSEDSNS EKADGDNTTL RDNQQVTNIQ
DSSDSDNGDE GSDDEDDDGN EGDNEGSDDD DDDNEGSDDD DRDIRYYKNG PEVFDKALDN
RTNQNDYEEE VELISEDSVE EEEETSEEAS QLSEDSYEDE RIYGEERSEV NSEDSDIQEV
LPVPKAWASL GKKGKIG
