TSYL2_MACFA
ID TSYL2_MACFA Reviewed; 695 AA.
AC Q9BE64; Q4R4M4; Q95K93;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Testis-specific Y-encoded-like protein 2;
DE Short=TSPY-like protein 2;
DE AltName: Full=Differentially-expressed nucleolar TGF-beta1 target protein;
GN Name=TSPYL2; Synonyms=DENTT; ORFNames=QflA-11354, QflA-13812, QmoA-12404;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Frontal cortex, and Medulla oblongata;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Frontal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15823505; DOI=10.1016/j.bbaexp.2005.02.010;
RA Ozbun L.L., Martinez A., Jakowlew S.B.;
RT "Differentially expressed nucleolar TGF-beta1 target (DENTT) shows tissue-
RT specific nuclear and cytoplasmic localization and increases TGF-beta1-
RT responsive transcription in primates.";
RL Biochim. Biophys. Acta 1728:163-180(2005).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with histones. Interacts with CASK. Part of a
CC complex containing CASK, TBR1 and TSPYL2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15823505}. Cytoplasm
CC {ECO:0000269|PubMed:15823505}. Note=Enriched in transcriptionally
CC active regions of chromatin in neurons. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BE64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BE64-2; Sequence=VSP_025896;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testis, adrenal gland, cerebral cortex, ovary, skeletal muscle and
CC spleen. Present in testis, adrenal gland, cerebral cortex and ovary (at
CC protein level). {ECO:0000269|PubMed:15823505}.
CC -!- INDUCTION: By TGFB1 and all-trans retinoic acid in lung cells (at
CC protein level). {ECO:0000269|PubMed:15823505}.
CC -!- PTM: Phosphorylation at Ser-20 and/or Thr-340 impairs function on cell
CC proliferation. {ECO:0000250}.
CC -!- MISCELLANEOUS: Synaptic activity down-regulates TSPYL2 protein levels
CC by inducing rapid proteasomal degradation. {ECO:0000250}.
CC -!- MISCELLANEOUS: Subject to X inactivation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; AB056806; BAB39330.1; -; mRNA.
DR EMBL; AB063061; BAB60783.1; -; mRNA.
DR EMBL; AB169870; BAE01951.1; -; mRNA.
DR RefSeq; NP_001270585.1; NM_001283656.1.
DR AlphaFoldDB; Q9BE64; -.
DR SMR; Q9BE64; -.
DR STRING; 9541.XP_005593684.1; -.
DR GeneID; 101866575; -.
DR CTD; 64061; -.
DR eggNOG; KOG1508; Eukaryota.
DR OrthoDB; 1191764at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
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 Alternative splicing; Cell cycle; Chromatin regulator; Cytoplasm;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..695
FT /note="Testis-specific Y-encoded-like protein 2"
FT /id="PRO_0000289101"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..202
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..514
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..600
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..676
FT /note="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 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQI8"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQI8"
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 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G4"
FT VAR_SEQ 179..376
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025896"
FT CONFLICT 268
FT /note="K -> E (in Ref. 2; BAE01951)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="P -> S (in Ref. 2; BAE01951)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="E -> G (in Ref. 2; BAE01951)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="L -> P (in Ref. 1; BAB60783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 79653 MW; 56CC1ADAE3A4D19E CRC64;
MDRPDEGPPA KTRRLSSSES PQRDPPPPPP PPPLLRLPLP PPQQRPRLQE ETEAAQVLAD
MRGVGLGPAL PPPPPYVILE EGGVRAYFTL GAECPGWDST IESGYGEAPP PTESLEALPT
PEVSGGSLEI DFEVVQPSSF GGEGALETCS AVGWGPQRLI DPKSKEEAII IVEDEDEDEQ
ESMRSSRRRR RRRRRKQRKV KRESRQRNAE RMESILQALE DIQLDLEAVN IKAGKAFLRL
KRKFIQMRRP FLERRDLIIQ HIPGFWVKAF LNHPRIPILI NRRDEDIFRY LTNLQVQDLR
HISMGYKMKL YFQTNPYFTN MVIVKEFQRN RSGRLVSHST PIRWHRGQEP QARRHGNQDA
SHSFFSWFSN HSLPEADRIA EIIKNDLWVN PLRYYLRERG SRIKRKKQEM KKRKTRGRCE
VVIMEDAPDY YAVEDIFSEI SDIDETIHDI KISDFMETTD YFETTDNEIT DINENICDSE
SPDHDEVRNE TTDNNESADD NETTDNNESA DDNNENPEDN NKNADDNKEN PDNNKHTYGN
NFFNGGFWGS HGNNQDSSDS DNEADEASDD EDNDGNEGDN EGSDDDGNEG DNEGSDDDDR
DIEYYEKVIE DPFDRDQDDY EDVIEIISDE SVEEEEGIVE GIEQDEDVYQ EEGNYEGEGN
EDVWEEGEDS DDSDLEDVLQ VPNGWANPGK RGKTG
