ID ZFY_HUMAN Reviewed; 801 AA.
AC P08048; B4DVF7; Q14021; Q15558; Q1RME9; Q24JR0; Q96TF3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 27-MAR-2024, entry version 221.
DE RecName: Full=Zinc finger Y-chromosomal protein;
GN Name=ZFY;
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] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=2511751;
RA Lau Y.-F.C., Chan K.;
RT "The putative testis-determining factor and related genes are expressed as
RT discrete-sized transcripts in adult gonadal and somatic tissues.";
RL Am. J. Hum. Genet. 45:942-952(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2308929; DOI=10.1073/pnas.87.5.1681;
RA Palmer M.S., Berta P., Sinclair A.H., Pym B., Goodfellow P.N.;
RT "Comparison of human ZFY and ZFX transcripts.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1681-1685(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10779541; DOI=10.1093/oxfordjournals.molbev.a026359;
RA Erlandsson R., Wilson J.F., Paabo S.;
RT "Sex chromosomal transposable element accumulation and male-driven
RT substitutional evolution in humans.";
RL Mol. Biol. Evol. 17:804-812(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [7]
RP NUCLEOTIDE SEQUENCE OF 408-801.
RX PubMed=3690661; DOI=10.1016/0092-8674(87)90595-2;
RA Page D.C., Mosher R., Simpson E.M., Fisher E.M.C., Mardon G., Pollack J.,
RA McGillivray B., de la Chapelle A., Brown L.G.;
RT "The sex-determining region of the human Y chromosome encodes a finger
RT protein.";
RL Cell 51:1091-1104(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 423-801.
RX PubMed=2041734; DOI=10.1093/nar/19.10.2579;
RA North M., Sargent C., O'Brien J., Taylor K., Wolfe J., Affara N.A.,
RA Ferguson-Smith M.A.;
RT "Comparison of ZFY and ZFX gene structure and analysis of alternative 3'
RT untranslated regions of ZFY.";
RL Nucleic Acids Res. 19:2579-2586(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 397-446.
RX PubMed=2498838; DOI=10.1093/nar/17.8.2987;
RA Affara N.A., Chambers D., O'Brien J., Habeebu S.S.M., Kalaitsidaki M.,
RA Bishop C.E., Ferguson-Smith M.A.;
RT "Evidence for distinguishable transcripts of the putative testis
RT determining gene (ZFY) and mapping of homologous cDNA sequences to
RT chromosomes X,Y and 9.";
RL Nucleic Acids Res. 17:2987-2999(1989).
RN [10]
RP FUNCTION, AND DOMAIN DNA-BINDING.
RX PubMed=20028140; DOI=10.1021/bi9018626;
RA Grants J., Flanagan E., Yee A., Romaniuk P.J.;
RT "Characterization of the DNA binding activity of the ZFY zinc finger
RT domain.";
RL Biochemistry 49:679-686(2010).
RN [11]
RP STRUCTURE BY NMR OF ZINC-FINGERS.
RX PubMed=1849423; DOI=10.1021/bi00228a004;
RA Kochoyan M., Havel T.F., Nguyen D.Z., Dahl C.E., Keutmann H.T., Weiss M.A.;
RT "Alternating zinc fingers in the human male associated protein ZFY: 2D NMR
RT structure of an even finger and implications for 'jumping-linker' DNA
RT recognition.";
RL Biochemistry 30:3371-3386(1991).
RN [12]
RP STRUCTURE BY NMR OF ZINC-FINGERS.
RX PubMed=1854720; DOI=10.1021/bi00243a005;
RA Kochoyan M., Keutmann H.T., Weiss M.A.;
RT "Alternating zinc fingers in the human male associated protein ZFY:
RT refinement of the NMR structure of an even finger by selective deuterium
RT labeling and implications for DNA recognition.";
RL Biochemistry 30:7063-7072(1991).
RN [13]
RP STRUCTURE BY NMR OF 572-598.
RX PubMed=15557258; DOI=10.1110/ps.04866404;
RA Lachenmann M.J., Ladbury J.E., Qian X., Huang K., Singh R., Weiss M.A.;
RT "Solvation and the hidden thermodynamics of a zinc finger probed by
RT nonstandard repair of a protein crevice.";
RL Protein Sci. 13:3115-3126(2004).
CC -!- FUNCTION: Probable transcriptional activator. Binds to the consensus
CC sequence 5'-AGGCCY-3'. {ECO:0000269|PubMed:20028140}.
CC -!- INTERACTION:
CC P08048; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-12239601, EBI-9679045;
CC P08048; Q9H8E8: KAT14; NbExp=3; IntAct=EBI-12239601, EBI-750907;
CC P08048; Q969R5: L3MBTL2; NbExp=6; IntAct=EBI-12239601, EBI-739909;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P08048-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08048-2; Sequence=VSP_042774, VSP_042775;
CC Name=3;
CC IsoId=P08048-3; Sequence=VSP_042824, VSP_042825, VSP_042826;
CC -!- DOMAIN: The binding of ZFY to DNA is mediated by the interaction of the
CC GGCC core base pairs with zinc fingers 12 and 13.
CC {ECO:0000269|PubMed:20028140}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. ZFX/ZFY subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the testis determining factor
CC (TDF). {ECO:0000305}.
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DR EMBL; L10393; AAA72344.1; -; mRNA.
DR EMBL; M30607; AAA61310.1; -; mRNA.
DR EMBL; AF114156; AAF21973.1; -; Genomic_DNA.
DR EMBL; AK301061; BAG62669.1; -; mRNA.
DR EMBL; AC006157; AAD15612.1; -; Genomic_DNA.
DR EMBL; BC114526; AAI14527.1; -; mRNA.
DR EMBL; BC114960; AAI14961.1; -; mRNA.
DR EMBL; X15470; CAA33498.1; -; Genomic_DNA.
DR CCDS; CCDS14774.1; -. [P08048-1]
DR CCDS; CCDS48200.1; -. [P08048-2]
DR CCDS; CCDS48201.1; -. [P08048-3]
DR PIR; A33630; A33630.
DR RefSeq; NP_001138747.1; NM_001145275.1. [P08048-3]
DR RefSeq; NP_001138748.1; NM_001145276.1. [P08048-2]
DR RefSeq; NP_003402.2; NM_003411.3. [P08048-1]
DR RefSeq; XP_005262627.1; XM_005262570.2.
DR RefSeq; XP_016885564.1; XM_017030075.1. [P08048-1]
DR RefSeq; XP_016885566.1; XM_017030077.1.
DR PDB; 1KLR; NMR; -; A=570-598.
DR PDB; 1KLS; NMR; -; A=570-598.
DR PDB; 1XRZ; NMR; -; A=570-598.
DR PDB; 5ZNF; NMR; -; A=570-598.
DR PDB; 7ZNF; NMR; -; A=570-598.
DR PDBsum; 1KLR; -.
DR PDBsum; 1KLS; -.
DR PDBsum; 1XRZ; -.
DR PDBsum; 5ZNF; -.
DR PDBsum; 7ZNF; -.
DR AlphaFoldDB; P08048; -.
DR SMR; P08048; -.
DR BioGRID; 113376; 14.
DR IntAct; P08048; 8.
DR STRING; 9606.ENSP00000155093; -.
DR DrugBank; DB02884; 3-Cyclohexyl-L-alanine.
DR DrugBank; DB05483; Picolinic acid.
DR GlyGen; P08048; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P08048; -.
DR PhosphoSitePlus; P08048; -.
DR BioMuta; ZFY; -.
DR DMDM; 51338719; -.
DR jPOST; P08048; -.
DR MassIVE; P08048; -.
DR MaxQB; P08048; -.
DR PeptideAtlas; P08048; -.
DR ProteomicsDB; 52062; -. [P08048-1]
DR ProteomicsDB; 52063; -. [P08048-2]
DR ProteomicsDB; 52064; -. [P08048-3]
DR Pumba; P08048; -.
DR Antibodypedia; 21843; 110 antibodies from 17 providers.
DR DNASU; 7544; -.
DR Ensembl; ENST00000155093.8; ENSP00000155093.3; ENSG00000067646.12. [P08048-1]
DR Ensembl; ENST00000383052.5; ENSP00000372525.1; ENSG00000067646.12. [P08048-1]
DR Ensembl; ENST00000449237.4; ENSP00000393908.1; ENSG00000067646.12. [P08048-3]
DR Ensembl; ENST00000625061.3; ENSP00000485605.1; ENSG00000067646.12. [P08048-2]
DR GeneID; 7544; -.
DR KEGG; hsa:7544; -.
DR MANE-Select; ENST00000155093.8; ENSP00000155093.3; NM_003411.4; NP_003402.2.
DR UCSC; uc004fqj.4; human. [P08048-1]
DR AGR; HGNC:12870; -.
DR CTD; 7544; -.
DR DisGeNET; 7544; -.
DR GeneCards; ZFY; -.
DR HGNC; HGNC:12870; ZFY.
DR HPA; ENSG00000067646; Low tissue specificity.
DR MIM; 490000; gene.
DR neXtProt; NX_P08048; -.
DR OpenTargets; ENSG00000067646; -.
DR PharmGKB; PA37459; -.
DR VEuPathDB; HostDB:ENSG00000067646; -.
DR GeneTree; ENSGT00940000158684; -.
DR InParanoid; P08048; -.
DR OrthoDB; 4630845at2759; -.
DR PhylomeDB; P08048; -.
DR TreeFam; TF335557; -.
DR PathwayCommons; P08048; -.
DR SignaLink; P08048; -.
DR SIGNOR; P08048; -.
DR BioGRID-ORCS; 7544; 9 hits in 790 CRISPR screens.
DR ChiTaRS; ZFY; human.
DR EvolutionaryTrace; P08048; -.
DR GeneWiki; ZFY; -.
DR GenomeRNAi; 7544; -.
DR Pharos; P08048; Tdark.
DR PRO; PR:P08048; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; P08048; Protein.
DR Bgee; ENSG00000067646; Expressed in sperm and 160 other cell types or tissues.
DR ExpressionAtlas; P08048; baseline and differential.
DR Genevisible; P08048; HS.
DR GO; GO:0000785; C:chromatin; ISS:ARUK-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:ARUK-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR InterPro; IPR006794; Transcrp_activ_Zfx/Zfy-dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24381:SF393; CHROMATIN-LINKED ADAPTOR FOR MSL PROTEINS, ISOFORM B-RELATED; 1.
DR PANTHER; PTHR24381; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR Pfam; PF13909; zf-H2C2_5; 1.
DR Pfam; PF04704; Zfx_Zfy_act; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..801
FT /note="Zinc finger Y-chromosomal protein"
FT /id="PRO_0000047261"
FT ZN_FING 421..443
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..474
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..506
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..538
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..566
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 572..595
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 601..623
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 629..652
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 658..680
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 686..709
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 715..737
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 743..766
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 772..795
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17012"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042824"
FT VAR_SEQ 21
FT /note="G -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042774"
FT VAR_SEQ 22..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042775"
FT VAR_SEQ 310
FT /note="N -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042825"
FT VAR_SEQ 311..361
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042826"
FT CONFLICT 333
FT /note="A -> R (in Ref. 1; AAA72344)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..407
FT /note="RRPDSRQYQT -> ALILLSFPFL (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="R -> S (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="H -> Y (in Ref. 2; AAA61310)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="Missing (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="T -> R (in Ref. 8)"
FT /evidence="ECO:0000305"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:1KLR"
FT STRAND 580..583
FT /evidence="ECO:0007829|PDB:1XRZ"
FT HELIX 585..594
FT /evidence="ECO:0007829|PDB:1KLR"
SQ SEQUENCE 801 AA; 90505 MW; 956B9B3DA16648FA CRC64;
MDEDEFELQP QEPNSFFDGI GADATHMDGD QIVVEIQEAV FVSNIVDSDI TVHNFVPDDP
DSVVIQDVVE DVVIEEDVQC SDILEEADVS ENVIIPEQVL DSDVTEEVSL PHCTVPDDVL
ASDITSTSMS MPEHVLTSES MHVCDIGHVE HMVHDSVVEA EIITDPLTSD IVSEEVLVAD
CAPEAVIDAS GISVDQQDND KASCEDYLMI SLDDAGKIEH DGSTGVTIDA ESEMDPCKVD
STCPEVIKVY IFKADPGEDD LGGTVDIVES EPENDHGVEL LDQNSSIRVP REKMVYMTVN
DSQQEDEDLN VAEIADEVYM EVIVGEEDAA VAAAAAAVHE QQIDEDEMKT FVPIAWAAAY
GNNSDGIENR NGTASALLHI DESAGLGRLA KQKPKKKRRP DSRQYQTAII IGPDGHPLTV
YPCMICGKKF KSRGFLKRHM KNHPEHLAKK KYHCTDCDYT TNKKISLHNH LESHKLTSKA
EKAIECDECG KHFSHAGALF THKMVHKEKG ANKMHKCKFC EYETAEQGLL NRHLLAVHSK
NFPHICVECG KGFRHPSELR KHMRIHTGEK PYQCQYCEYR SADSSNLKTH IKTKHSKEMP
FKCDICLLTF SDTKEVQQHT LVHQESKTHQ CLHCDHKSSN SSDLKRHVIS VHTKDYPHKC
EMCEKGFHRP SELKKHVAVH KGKKMHQCRH CDFKIADPFV LSRHILSVHT KDLPFRCKRC
RKGFRQQNEL KKHMKTHSGR KVYQCEYCEY STTDASGFKR HVISIHTKDY PHRCEYCKKG
FRRPSEKNQH IMRHHKEVGL P
//
