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   09-APR-2025, entry version 138.
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_029836.4.
DR   AlphaFoldDB; Q7TQI8; -.
DR   SMR; Q7TQI8; -.
DR   BioGRID; 206838; 1.
DR   STRING; 10090.ENSMUSP00000046782; -.
DR   iPTMnet; Q7TQI8; -.
DR   PhosphoSitePlus; Q7TQI8; -.
DR   PaxDb; 10090-ENSMUSP00000046782; -.
DR   ProteomicsDB; 298003; -.
DR   Antibodypedia; 12456; 307 antibodies from 37 providers.
DR   DNASU; 52808; -.
DR   Ensembl; ENSMUST00000044509.7; ENSMUSP00000046782.7; ENSMUSG00000041096.14.
DR   GeneID; 52808; -.
DR   KEGG; mmu:52808; -.
DR   UCSC; uc009uqf.1; mouse.
DR   AGR; MGI:106244; -.
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; QDTSHSF; -.
DR   OrthoDB; 19419at2759; -.
DR   PhylomeDB; Q7TQI8; -.
DR   TreeFam; TF313386; -.
DR   BioGRID-ORCS; 52808; 1 hit in 78 CRISPR screens.
DR   PRO; PR:Q7TQI8; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q7TQI8; protein.
DR   Bgee; ENSMUSG00000041096; Expressed in retinal neural layer and 227 other cell types or tissues.
DR   ExpressionAtlas; Q7TQI8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0008156; P:negative regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   FunFam; 1.20.5.1500:FF:000006; Testis-specific Y-encoded-like protein 2; 1.
DR   FunFam; 3.30.1120.90:FF:000002; Testis-specific Y-encoded-like protein 2; 1.
DR   Gene3D; 1.20.5.1500; -; 1.
DR   Gene3D; 3.30.1120.90; Nucleosome assembly protein; 1.
DR   InterPro; IPR037231; NAP-like_sf.
DR   InterPro; IPR002164; NAP_family.
DR   PANTHER; PTHR11875; TESTIS-SPECIFIC Y-ENCODED PROTEIN; 1.
DR   Pfam; PF00956; NAP; 1.
DR   SUPFAM; SSF143113; NAP-like; 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        25..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..193
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..581
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..627
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..650
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
//