CDY2_HUMAN
ID CDY2_HUMAN Reviewed; 541 AA.
AC Q9Y6F7; A8K868;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Testis-specific chromodomain protein Y 2;
DE EC=2.3.1.48;
GN Name=CDY2A; Synonyms=CDY2;
GN and
GN Name=CDY2B;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 282-541.
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: May have histone acetyltransferase activity. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis specific.
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DR EMBL; AF080598; AAD22733.1; -; mRNA.
DR EMBL; AK292233; BAF84922.1; -; mRNA.
DR EMBL; BC069087; AAH69087.1; -; mRNA.
DR CCDS; CCDS14789.1; -.
DR CCDS; CCDS35473.1; -.
DR RefSeq; NP_001001722.1; NM_001001722.1.
DR RefSeq; NP_004816.1; NM_004825.2.
DR PDB; 2FW2; X-ray; 2.20 A; A/B/C/D/E/F=282-541.
DR PDBsum; 2FW2; -.
DR AlphaFoldDB; Q9Y6F7; -.
DR SMR; Q9Y6F7; -.
DR BioGRID; 114819; 20.
DR BioGRID; 128481; 8.
DR IntAct; Q9Y6F7; 8.
DR MINT; Q9Y6F7; -.
DR iPTMnet; Q9Y6F7; -.
DR PhosphoSitePlus; Q9Y6F7; -.
DR BioMuta; CDY2A; -.
DR DMDM; 20138088; -.
DR EPD; Q9Y6F7; -.
DR jPOST; Q9Y6F7; -.
DR MassIVE; Q9Y6F7; -.
DR MaxQB; Q9Y6F7; -.
DR PaxDb; Q9Y6F7; -.
DR PeptideAtlas; Q9Y6F7; -.
DR PRIDE; Q9Y6F7; -.
DR ProteomicsDB; 86669; -.
DR ABCD; Q9Y6F7; 2 sequenced antibodies.
DR Antibodypedia; 21874; 67 antibodies from 9 providers.
DR Antibodypedia; 59758; 37 antibodies from 10 providers.
DR DNASU; 9426; -.
DR Ensembl; ENST00000250838.6; ENSP00000250838.4; ENSG00000182415.11.
DR Ensembl; ENST00000382867.4; ENSP00000372319.3; ENSG00000129873.8.
DR GeneID; 203611; -.
DR GeneID; 9426; -.
DR KEGG; hsa:203611; -.
DR KEGG; hsa:9426; -.
DR MANE-Select; ENST00000250838.6; ENSP00000250838.4; NM_004825.2; NP_004816.1.
DR MANE-Select; ENST00000382867.4; ENSP00000372319.3; NM_001001722.2; NP_001001722.1.
DR UCSC; uc004ftl.2; human.
DR CTD; 203611; -.
DR CTD; 9426; -.
DR DisGeNET; 203611; -.
DR DisGeNET; 9426; -.
DR GeneCards; CDY2A; -.
DR GeneCards; CDY2B; -.
DR GeneReviews; CDY2A; -.
DR HGNC; HGNC:1810; CDY2A.
DR HGNC; HGNC:23921; CDY2B.
DR HPA; ENSG00000129873; Not detected.
DR HPA; ENSG00000182415; Group enriched (epididymis, testis).
DR MalaCards; CDY2A; -.
DR MIM; 400018; gene.
DR neXtProt; NX_Q9Y6F7; -.
DR OpenTargets; ENSG00000129873; -.
DR PharmGKB; PA26355; -.
DR VEuPathDB; HostDB:ENSG00000129873; -.
DR VEuPathDB; HostDB:ENSG00000182415; -.
DR GeneTree; ENSGT00940000155106; -.
DR HOGENOM; CLU_009834_24_0_1; -.
DR InParanoid; Q9Y6F7; -.
DR OrthoDB; 1471901at2759; -.
DR PhylomeDB; Q9Y6F7; -.
DR TreeFam; TF313375; -.
DR PathwayCommons; Q9Y6F7; -.
DR SignaLink; Q9Y6F7; -.
DR BioGRID-ORCS; 203611; 7 hits in 582 CRISPR screens.
DR BioGRID-ORCS; 9426; 4 hits in 232 CRISPR screens.
DR EvolutionaryTrace; Q9Y6F7; -.
DR Pharos; Q9Y6F7; Tdark.
DR PRO; PR:Q9Y6F7; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; Q9Y6F7; protein.
DR Bgee; ENSG00000129873; Expressed in left testis and 1 other tissue.
DR Genevisible; Q9Y6F7; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
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; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..541
FT /note="Testis-specific chromodomain protein Y 2"
FT /id="PRO_0000080220"
FT DOMAIN 6..66
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 72..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:2FW2"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:2FW2"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 312..327
FT /evidence="ECO:0007829|PDB:2FW2"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 359..379
FT /evidence="ECO:0007829|PDB:2FW2"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:2FW2"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:2FW2"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 429..437
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 439..446
FT /evidence="ECO:0007829|PDB:2FW2"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:2FW2"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 472..483
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 488..521
FT /evidence="ECO:0007829|PDB:2FW2"
FT HELIX 524..535
FT /evidence="ECO:0007829|PDB:2FW2"
SQ SEQUENCE 541 AA; 60524 MW; 53F31A6603829E85 CRC64;
MASQEFEVEA IVDKRQDKNG NTQYLVRWKG YDKQDDTWEP EQHLMNCEKC VHDFNRRQTE
KQKKLTWTTT SRIFSNNARR RTSRSTKANY SKNSPKTPVT DKHHRSKNCK LFAASKNVRR
KAASTLSDTK NMEIINSTIE TLAPDSPFDH KKTVSGFQKL EKLDPIAADQ QDTVVFKVTE
GKLLRDPLSH PGAEQTGIQN KTQMHPLMSQ MSGSVTASMA TGSATRKGIV VLIDPLAANG
TTDMHTSVPR VKGGQRNITD DSRGQPFIKK MHFTIRLTES AITYRDIVVK KEDGFTQIVL
STRSTEKNAL NTEVIKEMVN ALNSAAADDS KLVLFSAAGS VFCCGLDFGY FVRHLRNDRN
TASLEMVDTI KNFVNTFIQF KKPIVVSVNG PAIGLGASIL PLCDLVWANE KAWFQTPYTT
FGQSPDGCSS ITFPKMMGKA SANEMLIAGR KLTAREACAK GLVSQVFLTG TFTQEVMIQI
KELASYNAIV LEECKALVRC NIKLELEQAN ERECEVLRKI WSSAQGIESM LKYVENKIDE
F
