CDY1_HUMAN
ID CDY1_HUMAN Reviewed; 540 AA.
AC Q9Y6F8; A2RUK1; O14600;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Testis-specific chromodomain protein Y 1;
DE EC=2.3.1.48;
GN Name=CDY1; Synonyms=CDY1A;
GN and
GN Name=CDY1B;
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] (CDY1) (ISOFORM 2).
RX PubMed=9381176; DOI=10.1126/science.278.5338.675;
RA Lahn B.T., Page D.C.;
RT "Functional coherence of the human Y chromosome.";
RL Science 278:675-680(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (CDY1A) (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=10192397; DOI=10.1038/7771;
RA Lahn B.T., Page D.C.;
RT "Retroposition of autosomal mRNA yielded testis-specific gene family on
RT human Y chromosome.";
RL Nat. Genet. 21:429-433(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CDY1B) (ISOFORM 2).
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12072557; DOI=10.1073/pnas.082248899;
RA Lahn B.T., Tang Z.L., Zhou J., Barndt R.J., Parvinen M., Allis C.D.,
RA Page D.C.;
RT "Previously uncharacterized histone acetyltransferases implicated in
RT mammalian spermatogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8707-8712(2002).
RN [5]
RP INTERACTION WITH HISTONE H3K9ME3, AND SUBCELLULAR LOCATION.
RX PubMed=18450745; DOI=10.1074/jbc.m802655200;
RA Fischle W., Franz H., Jacobs S.A., Allis C.D., Khorasanizadeh S.;
RT "Specificity of the chromodomain Y chromosome family of chromodomains for
RT lysine-methylated ARK(S/T) motifs.";
RL J. Biol. Chem. 283:19626-19635(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 281-531.
RX PubMed=19507244; DOI=10.1002/prot.22472;
RA Wu H., Min J., Antoshenko T., Plotnikov A.N.;
RT "Crystal structures of human CDY proteins reveal a crotonase-like fold.";
RL Proteins 76:1054-1061(2009).
CC -!- FUNCTION: Has histone acetyltransferase activity, with a preference for
CC histone H4. {ECO:0000269|PubMed:12072557}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC -!- SUBUNIT: Interacts (via chromo domain) with histone H3K9me3.
CC {ECO:0000269|PubMed:18450745}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18450745}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6F8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6F8-2; Sequence=VSP_001079;
CC -!- TISSUE SPECIFICITY: Testis-specific. Detected in spermatids (at protein
CC level). {ECO:0000269|PubMed:12072557}.
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DR EMBL; AF000981; AAC52116.1; -; mRNA.
DR EMBL; AF080597; AAD22732.1; -; mRNA.
DR EMBL; BC132929; AAI32930.1; -; mRNA.
DR EMBL; BC132955; AAI32956.1; -; mRNA.
DR CCDS; CCDS14801.1; -. [Q9Y6F8-2]
DR CCDS; CCDS14802.1; -. [Q9Y6F8-1]
DR CCDS; CCDS35486.1; -. [Q9Y6F8-2]
DR CCDS; CCDS35487.1; -. [Q9Y6F8-1]
DR RefSeq; NP_001003894.1; NM_001003894.1. [Q9Y6F8-1]
DR RefSeq; NP_001003895.1; NM_001003895.1. [Q9Y6F8-2]
DR RefSeq; NP_004671.1; NM_004680.2. [Q9Y6F8-2]
DR RefSeq; NP_733841.1; NM_170723.1. [Q9Y6F8-1]
DR PDB; 2FBM; X-ray; 2.28 A; A/B/C=281-531.
DR PDB; 6V41; X-ray; 1.60 A; AAA=2-63.
DR PDBsum; 2FBM; -.
DR PDBsum; 6V41; -.
DR AlphaFoldDB; Q9Y6F8; -.
DR SMR; Q9Y6F8; -.
DR BioGRID; 114541; 4.
DR BioGRID; 128959; 1.
DR BindingDB; Q9Y6F8; -.
DR ChEMBL; CHEMBL3879864; -.
DR iPTMnet; Q9Y6F8; -.
DR PhosphoSitePlus; Q9Y6F8; -.
DR BioMuta; CDY1; -.
DR DMDM; 20138089; -.
DR jPOST; Q9Y6F8; -.
DR MassIVE; Q9Y6F8; -.
DR MaxQB; Q9Y6F8; -.
DR PaxDb; Q9Y6F8; -.
DR PeptideAtlas; Q9Y6F8; -.
DR PRIDE; Q9Y6F8; -.
DR ABCD; Q9Y6F8; 2 sequenced antibodies.
DR Antibodypedia; 21896; 45 antibodies from 15 providers.
DR Antibodypedia; 73015; 62 antibodies from 6 providers.
DR DNASU; 253175; -.
DR Ensembl; ENST00000306609.4; ENSP00000302968.4; ENSG00000172288.7. [Q9Y6F8-2]
DR Ensembl; ENST00000306882.4; ENSP00000303178.4; ENSG00000172352.5. [Q9Y6F8-2]
DR Ensembl; ENST00000361963.3; ENSP00000354799.2; ENSG00000172288.7. [Q9Y6F8-1]
DR Ensembl; ENST00000382407.1; ENSP00000371844.1; ENSG00000172352.5. [Q9Y6F8-1]
DR GeneID; 253175; -.
DR GeneID; 9085; -.
DR KEGG; hsa:253175; -.
DR KEGG; hsa:9085; -.
DR MANE-Select; ENST00000306609.5; ENSP00000302968.4; NM_004680.3; NP_004671.1. [Q9Y6F8-2]
DR MANE-Select; ENST00000382407.1; ENSP00000371844.1; NM_001003894.2; NP_001003894.1.
DR UCSC; uc004fvz.4; human. [Q9Y6F8-1]
DR CTD; 253175; -.
DR CTD; 9085; -.
DR DisGeNET; 253175; -.
DR DisGeNET; 9085; -.
DR GeneCards; CDY1; -.
DR GeneCards; CDY1B; -.
DR GeneReviews; CDY1; -.
DR HGNC; HGNC:1809; CDY1.
DR HGNC; HGNC:23920; CDY1B.
DR HPA; ENSG00000172288; Not detected.
DR HPA; ENSG00000172352; Tissue enriched (testis).
DR MalaCards; CDY1; -.
DR MIM; 400016; gene.
DR neXtProt; NX_Q9Y6F8; -.
DR OpenTargets; ENSG00000172352; -.
DR PharmGKB; PA26354; -.
DR VEuPathDB; HostDB:ENSG00000172288; -.
DR VEuPathDB; HostDB:ENSG00000172352; -.
DR GeneTree; ENSGT00940000155106; -.
DR HOGENOM; CLU_009834_24_0_1; -.
DR InParanoid; Q9Y6F8; -.
DR OrthoDB; 1471901at2759; -.
DR PhylomeDB; Q9Y6F8; -.
DR TreeFam; TF313375; -.
DR PathwayCommons; Q9Y6F8; -.
DR SignaLink; Q9Y6F8; -.
DR BioGRID-ORCS; 253175; 10 hits in 571 CRISPR screens.
DR BioGRID-ORCS; 9085; 7 hits in 237 CRISPR screens.
DR EvolutionaryTrace; Q9Y6F8; -.
DR GeneWiki; CDY1; -.
DR Pharos; Q9Y6F8; Tchem.
DR PRO; PR:Q9Y6F8; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; Q9Y6F8; protein.
DR Bgee; ENSG00000172288; Expressed in left testis and 1 other tissue.
DR Genevisible; Q9Y6F8; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00378; ECH_1; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..540
FT /note="Testis-specific chromodomain protein Y 1"
FT /id="PRO_0000080219"
FT DOMAIN 6..66
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 76..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 532..540
FT /note="YVENKIDEF -> IPLLGYKAAFPPRKTQNDQRWCP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9381176"
FT /id="VSP_001079"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:2FBM"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:2FBM"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 311..326
FT /evidence="ECO:0007829|PDB:2FBM"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 358..378
FT /evidence="ECO:0007829|PDB:2FBM"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:2FBM"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:2FBM"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 428..436
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:2FBM"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:2FBM"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 472..482
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 487..498
FT /evidence="ECO:0007829|PDB:2FBM"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 502..520
FT /evidence="ECO:0007829|PDB:2FBM"
FT HELIX 523..530
FT /evidence="ECO:0007829|PDB:2FBM"
SQ SEQUENCE 540 AA; 60473 MW; 5B7AEB789092A265 CRC64;
MASQEFEVEA IVDKRQDKNG NTQYLVRWKG YDKQDDTWEP EQHLMNCEKC VHDFNRRQTE
KQKKLTWTTT SRIFSNNARR RTSRSTKANY SKNSPKTPVT DKHHRSKNRK LFAASKNVRR
KAASILSDTK NMEIINSTIE TLAPDSPFDH KTVSGFQKLE KLDPIAADQQ DTVVFKVTEG
KLLRDPLSRP GAEQTGIQNK TQIHPLMSQM SGSVTASMAT GSATRKGIVV LIDPLAANGT
TDMHTSVPRV KGGQRNITDD SRDQPFIKKM HFTIRLTESA STYRDIVVKK EDGFTQIVLS
TRSTEKNALN TEVIKEIVNA LNSAAADDSK LVLFSAAGSV FCCGLDFGYF VKHLRNNRNT
ASLEMVDTIK NFVNTFIQFK KPIVVSVNGP AIGLGASILP LCDLVWANEK AWFQTPYTTF
GQSPDGCSSI TFPKMMGKAS ANEMLIAGRK LTAREACAKG LVSQVFLTGT FTQEVMIQIK
ELASYNPIVL EECKALVRCN IKLELEQANE RECEVLRKIW SSAQGIESML KYVENKIDEF
