ZN541_HUMAN
ID ZN541_HUMAN Reviewed; 1346 AA.
AC Q9H0D2; Q8NDK8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Zinc finger protein 541;
GN Name=ZNF541;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 411-1346 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 545-1346 (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 546-1346 (ISOFORM 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 [4]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-712.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [5]
RP IDENTIFICATION IN HISTONE DEACETYLASE COMPLEX, AND INTERACTION WITH
RP DNTTIP1; HDAC1 AND HDAC2.
RX PubMed=21573134; DOI=10.1371/journal.pgen.1002065;
RA Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L.,
RA Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.;
RT "Nuclear cGMP-dependent kinase regulates gene expression via activity-
RT dependent recruitment of a conserved histone deacetylase complex.";
RL PLoS Genet. 7:E1002065-E1002065(2011).
CC -!- FUNCTION: Component of some chromatin remodeling multiprotein complex
CC that plays a role during spermatogenesis.
CC {ECO:0000250|UniProtKB:Q0GGX2}.
CC -!- SUBUNIT: Interacts with DNTTIP1 (PubMed:21573134). Identified in a
CC complex with KCDT19, HDAC1 and HSPA2 (By similarity). Component of a
CC histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2
CC (PubMed:21573134). {ECO:0000250|UniProtKB:Q0GGX2,
CC ECO:0000269|PubMed:21573134}.
CC -!- INTERACTION:
CC Q9H0D2; Q96IF1: AJUBA; NbExp=3; IntAct=EBI-3957075, EBI-949782;
CC Q9H0D2; Q15654: TRIP6; NbExp=3; IntAct=EBI-3957075, EBI-742327;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q0GGX2,
CC ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-
CC ProRule:PRU00624}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=3;
CC IsoId=Q9H0D2-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0D2-2; Sequence=VSP_016024;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI01051.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI01052.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI01053.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI01054.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB66780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD38720.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC010331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136846; CAB66780.1; ALT_INIT; mRNA.
DR EMBL; AL833862; CAD38720.2; ALT_FRAME; mRNA.
DR EMBL; BC101050; AAI01051.1; ALT_INIT; mRNA.
DR EMBL; BC101051; AAI01052.1; ALT_INIT; mRNA.
DR EMBL; BC101052; AAI01053.1; ALT_INIT; mRNA.
DR EMBL; BC101053; AAI01054.1; ALT_INIT; mRNA.
DR CCDS; CCDS46133.2; -. [Q9H0D2-3]
DR RefSeq; NP_001264004.1; NM_001277075.1. [Q9H0D2-3]
DR RefSeq; XP_005259368.1; XM_005259311.4. [Q9H0D2-3]
DR AlphaFoldDB; Q9H0D2; -.
DR SMR; Q9H0D2; -.
DR BioGRID; 123949; 2.
DR CORUM; Q9H0D2; -.
DR IntAct; Q9H0D2; 4.
DR STRING; 9606.ENSP00000375770; -.
DR iPTMnet; Q9H0D2; -.
DR PhosphoSitePlus; Q9H0D2; -.
DR BioMuta; ZNF541; -.
DR DMDM; 221222508; -.
DR MassIVE; Q9H0D2; -.
DR PaxDb; Q9H0D2; -.
DR PeptideAtlas; Q9H0D2; -.
DR PRIDE; Q9H0D2; -.
DR ProteomicsDB; 80255; -. [Q9H0D2-3]
DR ProteomicsDB; 80256; -. [Q9H0D2-2]
DR ProteomicsDB; 80257; -. [Q9H0D2-3]
DR Antibodypedia; 18215; 127 antibodies from 26 providers.
DR DNASU; 84215; -.
DR Ensembl; ENST00000391901.8; ENSP00000375770.3; ENSG00000118156.13. [Q9H0D2-3]
DR GeneID; 84215; -.
DR KEGG; hsa:84215; -.
DR MANE-Select; ENST00000391901.8; ENSP00000375770.3; NM_001277075.3; NP_001264004.1.
DR UCSC; uc002phg.5; human. [Q9H0D2-3]
DR CTD; 84215; -.
DR DisGeNET; 84215; -.
DR GeneCards; ZNF541; -.
DR HGNC; HGNC:25294; ZNF541.
DR HPA; ENSG00000118156; Tissue enriched (testis).
DR neXtProt; NX_Q9H0D2; -.
DR OpenTargets; ENSG00000118156; -.
DR PharmGKB; PA134941115; -.
DR VEuPathDB; HostDB:ENSG00000118156; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG4167; Eukaryota.
DR GeneTree; ENSGT00940000160330; -.
DR HOGENOM; CLU_006052_0_0_1; -.
DR InParanoid; Q9H0D2; -.
DR OMA; SHHPTPE; -.
DR OrthoDB; 165439at2759; -.
DR TreeFam; TF106431; -.
DR PathwayCommons; Q9H0D2; -.
DR SignaLink; Q9H0D2; -.
DR BioGRID-ORCS; 84215; 22 hits in 1092 CRISPR screens.
DR ChiTaRS; ZNF541; human.
DR GenomeRNAi; 84215; -.
DR Pharos; Q9H0D2; Tdark.
DR PRO; PR:Q9H0D2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H0D2; protein.
DR Bgee; ENSG00000118156; Expressed in left testis and 101 other tissues.
DR ExpressionAtlas; Q9H0D2; baseline and differential.
DR Genevisible; Q9H0D2; HS.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Spermatogenesis; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1346
FT /note="Zinc finger protein 541"
FT /id="PRO_0000197136"
FT DOMAIN 1053..1145
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 1160..1211
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 140..162
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 168..190
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 196..220
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 838..860
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1289..1311
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 932..1189
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_016024"
FT VARIANT 486
FT /note="P -> S (in dbSNP:rs3810320)"
FT /id="VAR_054220"
FT VARIANT 712
FT /note="S -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035717"
FT VARIANT 791
FT /note="K -> E (in dbSNP:rs34984302)"
FT /id="VAR_054221"
FT VARIANT 795
FT /note="T -> S (in dbSNP:rs3826835)"
FT /id="VAR_054222"
FT CONFLICT 473
FT /note="P -> A (in Ref. 2; CAD38720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1346 AA; 145587 MW; C9FEB46072EED963 CRC64;
MDQYSLGDEG ALPSEMHLPS FSESQGLNCS DTLNRDLGPN TRGFLYAGLS GLDPDPSLPT
PDMSSEVLED NLDTLSLYSG KDSDSVKLLE EYADSESQAS LQDLGLGVLK AKEADEGGRA
TSGSARKGKR QHSSPQNPLL DCSLCGKVFS SASSLSKHYL THSQERKHVC KICSKAFKRQ
DHLTGHMLTH QKTKPFVCIE QGCSKSYCDY RSLRRHYEVH HGLCILKEAP PEEEACGDSP
HAHESAGQPP PSSLRSLVPP EARSPGSLLP HRDLLRRIVS SIVHQKTPSP GPAPAGASDS
EGRNTACPCP ASSGSSSCTP AGPHAAPAAL DTELPEEPCL PQKEPATDVF TAPNSRAAEN
GAPDPPEPEP DTALLQARST AECWPEGGSV PACLPLFRGQ TVPASSQPSS HSFQWLRNLP
GCPKSKGNNV FVVHKPSAVP SREGSESGPG PSSGSPSEES PPGPGGGLED ALPFPAALLR
VPAEAPSDPR SASGEDDPCA PKKVKVDCDS FLCQNPGEPG LQEAQKAGGL PADASPLFRQ
LFLKSQEPLV SHEQMQVFQM ITKSQRIFSH AQVAAVSSQL PAPEGKPAAL RPLQGPWPQQ
PPPLAPAVDS LHAGPGNPEA EGSPARRRKT TPGVPREASP GSTRRDAKGG LKVAAVPTPL
AAPSLDPSRN PDISSLAKQL RSSKGTLDLE DIFPSTGQRQ TQLGGEEPPG ASLPGKQAPA
ENGAASRITK GEKGPACSRG GGYRLLGNPR APRFSGFRKE KAKMDMCCAA SPSQVAMASF
SSAGPPADPS KSKLTIFSRI QGGNIYRLPH PVKEENVAGR GNQQNGSPTD WTKPRSTFVC
KNCSQMFYTE KGLSSHMCFH SDQWPSPRGK QEPQVFGTEF CKPLRQVLRP EGDRHSPPGT
KKPLDPTAAA PLVVPQSIPV VPVTRHIGSM AMGQEKDGEE RDSKESSQQR KRKKRPPPST
AGEPGPAGCH QSRLRSPMFL VDCLLKGLFQ CSPYTPPPML SPIREGSGVY FNTLCSTSTQ
ASPDQLISSM LDQVDGSFGI CVVKDDTKIS IEPHINIGSR FQAEIPELQE RSLAGTDEHV
ASLVWKPWGD MMISSETQDR VTELCNVACS SVMPGGGTNL ELALHCLHEA QGNVQVALET
LLLRGPHKPR THLLADYRYT GSDVWTPIEK RLFKKAFYAH KKDFYLIHKM IQTKTVAQCV
EYYYIWKKMI KFDCGRAPGL EKRVKREPEE VERTEEKVPC SPRERPSHHP TPKLKTKSYR
RESILSSSPN AGSKRTPELL GSAESQGIFP CRECERVFDK IKSRNAHMKR HRLQDHVEPI
IRVKWPVKPF QLKEEELGAD IGPLQW
