ZCPW2_HUMAN
ID ZCPW2_HUMAN Reviewed; 356 AA.
AC Q504Y3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Zinc finger CW-type PWWP domain protein 2;
GN Name=ZCWPW2;
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 [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 [2]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 21-78 IN COMPLEX WITH THE AMINO
RP TERMINUS OF HISTONE H3, FUNCTION, DOMAIN CW-TYPE ZINC FINGER, AND
RP MUTAGENESIS OF TRP-30; TRP-41 AND PHE-78.
RX PubMed=26933034; DOI=10.1074/jbc.m116.718973;
RA Liu Y., Tempel W., Zhang Q., Liang X., Loppnau P., Qin S., Min J.;
RT "Family-wide Characterization of Histone Binding Abilities of Human CW
RT Domain-containing Proteins.";
RL J. Biol. Chem. 291:9000-9013(2016).
CC -!- FUNCTION: Histone methylation reader which binds to non-methylated
CC (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and
CC trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034). The
CC order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0
CC (PubMed:26933034). {ECO:0000269|PubMed:26933034}.
CC -!- INTERACTION:
CC Q504Y3; O75031: HSF2BP; NbExp=3; IntAct=EBI-12274792, EBI-7116203;
CC Q504Y3; P40425: PBX2; NbExp=3; IntAct=EBI-12274792, EBI-348489;
CC -!- DOMAIN: The CW-TYPE zinc finger mediates its binding to trimethylated
CC histone H3K4me3. {ECO:0000269|PubMed:26933034}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC094696; AAH94696.1; -; mRNA.
DR CCDS; CCDS33723.1; -.
DR RefSeq; NP_001035522.1; NM_001040432.3.
DR RefSeq; NP_001311098.1; NM_001324169.1.
DR RefSeq; XP_016861244.1; XM_017005755.1.
DR PDB; 4O62; X-ray; 1.78 A; A/B/C=21-78.
DR PDB; 4Z0O; X-ray; 1.57 A; A=21-78.
DR PDB; 4Z0R; X-ray; 1.75 A; A/B/C=21-78.
DR PDBsum; 4O62; -.
DR PDBsum; 4Z0O; -.
DR PDBsum; 4Z0R; -.
DR AlphaFoldDB; Q504Y3; -.
DR SMR; Q504Y3; -.
DR BioGRID; 127425; 4.
DR IntAct; Q504Y3; 2.
DR STRING; 9606.ENSP00000373278; -.
DR BioMuta; ZCWPW2; -.
DR DMDM; 74740233; -.
DR PaxDb; Q504Y3; -.
DR PeptideAtlas; Q504Y3; -.
DR PRIDE; Q504Y3; -.
DR Antibodypedia; 27555; 28 antibodies from 11 providers.
DR DNASU; 152098; -.
DR Ensembl; ENST00000383768.7; ENSP00000373278.2; ENSG00000206559.8.
DR GeneID; 152098; -.
DR KEGG; hsa:152098; -.
DR MANE-Select; ENST00000383768.7; ENSP00000373278.2; NM_001040432.4; NP_001035522.1.
DR UCSC; uc003ceh.4; human.
DR CTD; 152098; -.
DR DisGeNET; 152098; -.
DR GeneCards; ZCWPW2; -.
DR HGNC; HGNC:23574; ZCWPW2.
DR HPA; ENSG00000206559; Tissue enhanced (testis).
DR neXtProt; NX_Q504Y3; -.
DR OpenTargets; ENSG00000206559; -.
DR PharmGKB; PA134888742; -.
DR VEuPathDB; HostDB:ENSG00000206559; -.
DR eggNOG; ENOG502QS46; Eukaryota.
DR GeneTree; ENSGT00560000077278; -.
DR HOGENOM; CLU_077983_1_0_1; -.
DR InParanoid; Q504Y3; -.
DR OMA; AFVGHYS; -.
DR OrthoDB; 1159953at2759; -.
DR PhylomeDB; Q504Y3; -.
DR TreeFam; TF318885; -.
DR PathwayCommons; Q504Y3; -.
DR SignaLink; Q504Y3; -.
DR BioGRID-ORCS; 152098; 21 hits in 1066 CRISPR screens.
DR ChiTaRS; ZCWPW2; human.
DR GenomeRNAi; 152098; -.
DR Pharos; Q504Y3; Tdark.
DR PRO; PR:Q504Y3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q504Y3; protein.
DR Bgee; ENSG00000206559; Expressed in sperm and 99 other tissues.
DR ExpressionAtlas; Q504Y3; baseline and differential.
DR Genevisible; Q504Y3; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR042778; ZCWPW1/ZCWPW2.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR15999; PTHR15999; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF07496; zf-CW; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..356
FT /note="Zinc finger CW-type PWWP domain protein 2"
FT /id="PRO_0000286348"
FT DOMAIN 98..162
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT ZN_FING 24..79
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 279..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT VARIANT 202
FT /note="L -> Q (in dbSNP:rs1563656)"
FT /id="VAR_051499"
FT MUTAGEN 30
FT /note="W->A,V,L,M,G,S,T,N,Q: Reduced histone H3K4me3
FT binding."
FT /evidence="ECO:0000269|PubMed:26933034"
FT MUTAGEN 30
FT /note="W->C,D,E,H,K,R: Significantly reduced histone
FT H3K4me3 binding."
FT /evidence="ECO:0000269|PubMed:26933034"
FT MUTAGEN 30
FT /note="W->L: Loss of histone H3K4me3 binding; when
FT associated with F-41."
FT /evidence="ECO:0000269|PubMed:26933034"
FT MUTAGEN 30
FT /note="W->M: Loss of histone H3K4me3 binding; when
FT associated with F-41."
FT /evidence="ECO:0000269|PubMed:26933034"
FT MUTAGEN 30
FT /note="W->P: Loss of histone H3K4me3 binding."
FT /evidence="ECO:0000269|PubMed:26933034"
FT MUTAGEN 41
FT /note="W->F: Significantly reduced histone H3K4me3 binding.
FT Loss of histone H3K4me3 binding; when associated with L-30
FT or M-30."
FT /evidence="ECO:0000269|PubMed:26933034"
FT MUTAGEN 78
FT /note="F->S,I,P,D,E,H,R,Q: Little effect on histone H3K4me3
FT binding."
FT /evidence="ECO:0000269|PubMed:26933034"
FT MUTAGEN 78
FT /note="Missing: Little effect on histone H3K4me3 binding."
FT /evidence="ECO:0000269|PubMed:26933034"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4Z0O"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4Z0O"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:4Z0O"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:4Z0O"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4Z0O"
SQ SEQUENCE 356 AA; 41376 MW; 90CB5558C9801B1F CRC64;
MDKEKLDVKI EYCNYAMDSS VENMYVNKVW VQCENENCLK WRLLSSEDSA KVDHDEPWYC
FMNTDSRYNN CSISEEDFPE ESQLHQCGFK IVYSQLPLGS LVLVKLQNWP SWPGILCPDR
FKGKYVTYDP DGNVEEYHIE FLGDPHSRSW IKATFVGHYS ITLKPEKCKN KKKWYKSALQ
EACLLYGYSH EQRLEMCCLS KLQDKSETHD KVAALVKKRK QTSKNNIEKK KPKFRKRKRK
AILKCSFENV YSDDALSKEN RVVCETEVLL KELEQMLQQA LQPTATPDES EEGHGEEINM
GEKLSKCSPE APAGSLFENH YEEDYLVIDG IKLKAGECIE DITNKFKEID ALMSEF
