TSYL2_HUMAN
ID TSYL2_HUMAN Reviewed; 693 AA.
AC Q9H2G4; O94799; Q96DG7; Q9BZW6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Testis-specific Y-encoded-like protein 2;
DE Short=TSPY-like protein 2;
DE AltName: Full=Cell division autoantigen 1;
DE AltName: Full=Cutaneous T-cell lymphoma-associated antigen se20-4;
DE Short=CTCL-associated antigen se20-4;
DE AltName: Full=Differentially-expressed nucleolar TGF-beta1 target protein;
DE AltName: Full=Nuclear protein of 79 kDa;
DE Short=NP79;
GN Name=TSPYL2; Synonyms=CDA1, DENTT, TSPX; ORFNames=HRIHFB2216;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-20
RP AND THR-340, MUTAGENESIS OF SER-20 AND THR-340, AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=11395479; DOI=10.1074/jbc.m007681200;
RA Chai Z., Sarcevic B., Mawson A., Toh B.-H.;
RT "SET-related cell division autoantigen-1 (CDA1) arrests cell growth.";
RL J. Biol. Chem. 276:33665-33674(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-693, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INDUCTION BY TGFB1.
RX PubMed=11318608; DOI=10.1006/geno.2001.6505;
RA Ozbun L.L., You L., Kiang S., Angdisen J., Martinez A., Jakowlew S.B.;
RT "Identification of Differentially expressed nucleolar TGF-beta1 target
RT (DENTT) in human lung cancer cells that is a new member of the
RT TSPY/SET/NAP-1 superfamily.";
RL Genomics 73:179-193(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-693.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [8]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12393179; DOI=10.1016/s0925-4439(02)00171-0;
RA Sun G., Yuen Chan S., Yuan Y., Wang Chan K., Qiu G., Sun K., Ping Leung M.;
RT "Isolation of differentially expressed genes in human heart tissues.";
RL Biochim. Biophys. Acta 1588:241-246(2002).
RN [9]
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 [10]
RP INDUCTION.
RX PubMed=15069065; DOI=10.1074/jbc.m402143200;
RA Ito T., Tsukumo S., Suzuki N., Motohashi H., Yamamoto M.,
RA Fujii-Kuriyama Y., Mimura J., Lin T.-M., Peterson R.E., Tohyama C.,
RA Nohara K.;
RT "A constitutively active arylhydrocarbon receptor induces growth inhibition
RT of jurkat T cells through changes in the expression of genes related to
RT apoptosis and cell cycle arrest.";
RL J. Biol. Chem. 279:25204-25210(2004).
RN [11]
RP INDUCTION.
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).
RN [12]
RP FUNCTION.
RX PubMed=17317670; DOI=10.1074/jbc.m609623200;
RA Tu Y., Wu W., Wu T., Cao Z., Wilkins R., Toh B.-H., Cooper M.E., Chai Z.;
RT "Antiproliferative autoantigen CDA1 transcriptionally up-regulates
RT p21(Waf1/Cip1) by activating p53 and MEK/ERK1/2 MAPK pathways.";
RL J. Biol. Chem. 282:11722-11731(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-163 AND LYS-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP VARIANT MET-262.
RX PubMed=26529358; DOI=10.1097/ypg.0000000000000114;
RA Vasli N., Ahmed I., Mittal K., Ohadi M., Mikhailov A., Rafiq M.A.,
RA Bhatti A., Carter M.T., Andrade D.M., Ayub M., Vincent J.B., John P.;
RT "Identification of a homozygous missense mutation in LRP2 and a hemizygous
RT missense mutation in TSPYL2 in a family with mild intellectual
RT disability.";
RL Psychiatr. Genet. 26:66-73(2016).
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:11395479, ECO:0000269|PubMed:17317670}.
CC -!- SUBUNIT: Interacts with histones. Interacts with CASK. Part of a
CC complex containing CASK, TBR1 and TSPYL2 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9H2G4; Q9ULW3: ABT1; NbExp=3; IntAct=EBI-947459, EBI-2602396;
CC Q9H2G4; Q6ZN18-2: AEBP2; NbExp=3; IntAct=EBI-947459, EBI-10255023;
CC Q9H2G4; Q96LK0: CEP19; NbExp=3; IntAct=EBI-947459, EBI-741885;
CC Q9H2G4; P68400: CSNK2A1; NbExp=4; IntAct=EBI-947459, EBI-347804;
CC Q9H2G4; U3KQK0: H2BC15; NbExp=3; IntAct=EBI-947459, EBI-12142839;
CC Q9H2G4; A0A024R4Z4: hCG_2042749; NbExp=3; IntAct=EBI-947459, EBI-14231181;
CC Q9H2G4; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-947459, EBI-7261162;
CC Q9H2G4; Q9C086: INO80B; NbExp=3; IntAct=EBI-947459, EBI-715611;
CC Q9H2G4; Q4FZB7: KMT5B; NbExp=3; IntAct=EBI-947459, EBI-1047962;
CC Q9H2G4; P25791-3: LMO2; NbExp=3; IntAct=EBI-947459, EBI-11959475;
CC Q9H2G4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-947459, EBI-739832;
CC Q9H2G4; Q96EZ8: MCRS1; NbExp=5; IntAct=EBI-947459, EBI-348259;
CC Q9H2G4; Q9UGY1: NOL12; NbExp=3; IntAct=EBI-947459, EBI-716098;
CC Q9H2G4; Q9NZM5: NOP53; NbExp=4; IntAct=EBI-947459, EBI-720156;
CC Q9H2G4; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-947459, EBI-2339674;
CC Q9H2G4; Q96T37-3: RBM15; NbExp=3; IntAct=EBI-947459, EBI-12041043;
CC Q9H2G4; Q2KHN1: RNF151; NbExp=3; IntAct=EBI-947459, EBI-12002474;
CC Q9H2G4; P62851: RPS25; NbExp=3; IntAct=EBI-947459, EBI-353054;
CC Q9H2G4; Q8TAD8: SNIP1; NbExp=3; IntAct=EBI-947459, EBI-749336;
CC Q9H2G4; Q96EY4: TMA16; NbExp=3; IntAct=EBI-947459, EBI-1045338;
CC Q9H2G4; P13805-3: TNNT1; NbExp=3; IntAct=EBI-947459, EBI-12151635;
CC Q9H2G4; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-947459, EBI-723389;
CC Q9H2G4; Q9HD64: XAGE1B; NbExp=3; IntAct=EBI-947459, EBI-2340004;
CC Q9H2G4; O43167: ZBTB24; NbExp=3; IntAct=EBI-947459, EBI-744471;
CC Q9H2G4; P10074: ZBTB48; NbExp=3; IntAct=EBI-947459, EBI-744864;
CC Q9H2G4; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-947459, EBI-2555749;
CC Q9H2G4; Q8ND82: ZNF280C; NbExp=3; IntAct=EBI-947459, EBI-8831272;
CC Q9H2G4; Q9HBT8: ZNF286A; NbExp=3; IntAct=EBI-947459, EBI-10754950;
CC Q9H2G4; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-947459, EBI-7233259;
CC Q9H2G4; Q96C55: ZNF524; NbExp=3; IntAct=EBI-947459, EBI-10283126;
CC Q9H2G4; Q8N1G0: ZNF687; NbExp=4; IntAct=EBI-947459, EBI-1210558;
CC Q9H2G4; Q96BV0: ZNF775; NbExp=3; IntAct=EBI-947459, EBI-7149881;
CC Q9H2G4; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-947459, EBI-5667516;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11318608,
CC ECO:0000269|PubMed:11395479}. Cytoplasm {ECO:0000250}. Note=Enriched in
CC transcriptionally active regions of chromatin in neurons.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC brain, testis and heart, and lowest levels in liver and pancreas.
CC {ECO:0000269|PubMed:11149944, ECO:0000269|PubMed:11318608,
CC ECO:0000269|PubMed:12393179, ECO:0000269|PubMed:15241014}.
CC -!- INDUCTION: Up-regulated in growth-arrested T-cells. Induced by TGFB1
CC and all-trans retinoic acid (ATRA) in lung cancer cells (at protein
CC level). {ECO:0000269|PubMed:11318608, ECO:0000269|PubMed:15069065,
CC ECO:0000269|PubMed:15823505}.
CC -!- PTM: Phosphorylation at Ser-20 and/or Thr-340 impairs function on cell
CC proliferation. {ECO:0000305|PubMed:11395479}.
CC -!- MISCELLANEOUS: Synaptic activity down-regulates TSPYL2 protein levels
CC by inducing rapid proteasomal degradation. {ECO:0000250}.
CC -!- MISCELLANEOUS: Subject to X inactivation.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG53596.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF273046; AAG34906.1; -; mRNA.
DR EMBL; AY040871; AAK72407.1; -; mRNA.
DR EMBL; AL713652; CAD28461.1; -; mRNA.
DR EMBL; BX322635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001566; AAH01566.1; -; mRNA.
DR EMBL; BC024270; AAH24270.1; -; mRNA.
DR EMBL; AF254794; AAG53596.1; ALT_INIT; mRNA.
DR EMBL; AB015345; BAA34802.1; -; mRNA.
DR CCDS; CCDS14350.1; -.
DR RefSeq; NP_071400.1; NM_022117.3.
DR AlphaFoldDB; Q9H2G4; -.
DR SMR; Q9H2G4; -.
DR BioGRID; 122034; 90.
DR IntAct; Q9H2G4; 59.
DR MINT; Q9H2G4; -.
DR STRING; 9606.ENSP00000364591; -.
DR iPTMnet; Q9H2G4; -.
DR PhosphoSitePlus; Q9H2G4; -.
DR BioMuta; TSPYL2; -.
DR DMDM; 74752604; -.
DR EPD; Q9H2G4; -.
DR jPOST; Q9H2G4; -.
DR MassIVE; Q9H2G4; -.
DR MaxQB; Q9H2G4; -.
DR PaxDb; Q9H2G4; -.
DR PeptideAtlas; Q9H2G4; -.
DR PRIDE; Q9H2G4; -.
DR ProteomicsDB; 80546; -.
DR Antibodypedia; 12456; 263 antibodies from 37 providers.
DR DNASU; 64061; -.
DR Ensembl; ENST00000375442.8; ENSP00000364591.4; ENSG00000184205.14.
DR GeneID; 64061; -.
DR KEGG; hsa:64061; -.
DR MANE-Select; ENST00000375442.8; ENSP00000364591.4; NM_022117.4; NP_071400.1.
DR UCSC; uc004drw.4; human.
DR CTD; 64061; -.
DR DisGeNET; 64061; -.
DR GeneCards; TSPYL2; -.
DR HGNC; HGNC:24358; TSPYL2.
DR HPA; ENSG00000184205; Tissue enhanced (ovary).
DR MIM; 300564; gene.
DR neXtProt; NX_Q9H2G4; -.
DR OpenTargets; ENSG00000184205; -.
DR PharmGKB; PA134930188; -.
DR VEuPathDB; HostDB:ENSG00000184205; -.
DR eggNOG; KOG1508; Eukaryota.
DR GeneTree; ENSGT00940000162496; -.
DR HOGENOM; CLU_025445_0_0_1; -.
DR InParanoid; Q9H2G4; -.
DR OMA; PNGWANP; -.
DR OrthoDB; 1191764at2759; -.
DR PhylomeDB; Q9H2G4; -.
DR TreeFam; TF313386; -.
DR PathwayCommons; Q9H2G4; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q9H2G4; -.
DR SIGNOR; Q9H2G4; -.
DR BioGRID-ORCS; 64061; 16 hits in 708 CRISPR screens.
DR ChiTaRS; TSPYL2; human.
DR GeneWiki; TSPYL2; -.
DR GenomeRNAi; 64061; -.
DR Pharos; Q9H2G4; Tbio.
DR PRO; PR:Q9H2G4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9H2G4; protein.
DR Bgee; ENSG00000184205; Expressed in adenohypophysis and 194 other tissues.
DR ExpressionAtlas; Q9H2G4; baseline and differential.
DR Genevisible; Q9H2G4; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0000182; F:rDNA binding; NAS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045786; P:negative regulation of cell cycle; NAS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0045859; P:regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; NAS: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 Cell cycle; Chromatin regulator; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..693
FT /note="Testis-specific Y-encoded-like protein 2"
FT /id="PRO_0000289100"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..125
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 474..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..693
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 495..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..601
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..674
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11395479"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:11395479"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQI8"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQI8"
FT MOD_RES 671
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:0007744|PubMed:28112733"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 262
FT /note="I -> M (found in patients with mild intellectual
FT disability; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:26529358"
FT /id="VAR_075536"
FT MUTAGEN 20
FT /note="S->A: Impairs effect on cell proliferation; when
FT associated with A-340."
FT /evidence="ECO:0000269|PubMed:11395479"
FT MUTAGEN 340
FT /note="T->A: Impairs effect on cell proliferation; when
FT associated with A-20."
FT /evidence="ECO:0000269|PubMed:11395479"
FT CONFLICT 442
FT /note="D -> N (in Ref. 6; AAG53596)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="D -> V (in Ref. 6; AAG53596)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="V -> G (in Ref. 7; BAA34802)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="K -> R (in Ref. 7; BAA34802)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 79435 MW; 726F3BDC10A36165 CRC64;
MDRPDEGPPA KTRRLSSSES PQRDPPPPPP PPPLLRLPLP PPQQRPRLQE ETEAAQVLAD
MRGVGLGPAL PPPPPYVILE EGGIRAYFTL GAECPGWDST IESGYGEAPP PTESLEALPT
PEASGGSLEI DFQVVQSSSF GGEGALETCS AVGWAPQRLV DPKSKEEAII IVEDEDEDER
ESMRSSRRRR RRRRRKQRKV KRESRERNAE RMESILQALE DIQLDLEAVN IKAGKAFLRL
KRKFIQMRRP FLERRDLIIQ HIPGFWVKAF LNHPRISILI NRRDEDIFRY LTNLQVQDLR
HISMGYKMKL YFQTNPYFTN MVIVKEFQRN RSGRLVSHST PIRWHRGQEP QARRHGNQDA
SHSFFSWFSN HSLPEADRIA EIIKNDLWVN PLRYYLRERG SRIKRKKQEM KKRKTRGRCE
VVIMEDAPDY YAVEDIFSEI SDIDETIHDI KISDFMETTD YFETTDNEIT DINENICDSE
NPDHNEVPNN ETTDNNESAD DHETTDNNES ADDNNENPED NNKNTDDNEE NPNNNENTYG
NNFFKGGFWG SHGNNQDSSD SDNEADEASD DEDNDGNEGD NEGSDDDGNE GDNEGSDDDD
RDIEYYEKVI EDFDKDQADY EDVIEIISDE SVEEEGIEEG IQQDEDIYEE GNYEEEGSED
VWEEGEDSDD SDLEDVLQVP NGWANPGKRG KTG
