ID ZN595_HUMAN Reviewed; 648 AA.
AC Q8IYB9; Q7Z3I0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Zinc finger protein 595;
GN Name=ZNF595;
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].
RC TISSUE=Bone marrow {ECO:0000312|EMBL:CAD97883.1};
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q8IYB9; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-2682172, EBI-12012928;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BX537887; CAD97883.1; -; mRNA.
DR EMBL; AC253576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036110; AAH36110.1; -; mRNA.
DR EMBL; BC043151; AAH43151.1; -; mRNA.
DR CCDS; CCDS75075.1; -.
DR RefSeq; NP_001272981.1; NM_001286052.1.
DR RefSeq; NP_001272982.1; NM_001286053.1.
DR RefSeq; NP_001272983.1; NM_001286054.1.
DR RefSeq; NP_872330.1; NM_182524.3.
DR AlphaFoldDB; Q8IYB9; -.
DR SMR; Q8IYB9; -.
DR IntAct; Q8IYB9; 3.
DR MINT; Q8IYB9; -.
DR STRING; 9606.ENSP00000477392; -.
DR iPTMnet; Q8IYB9; -.
DR PhosphoSitePlus; Q8IYB9; -.
DR BioMuta; ZNF595; -.
DR EPD; Q8IYB9; -.
DR jPOST; Q8IYB9; -.
DR MassIVE; Q8IYB9; -.
DR PaxDb; 9606-ENSP00000477392; -.
DR PeptideAtlas; Q8IYB9; -.
DR ProteomicsDB; 71154; -.
DR Pumba; Q8IYB9; -.
DR Antibodypedia; 74373; 18 antibodies from 6 providers.
DR DNASU; 152687; -.
DR Ensembl; ENST00000610261.6; ENSP00000477392.1; ENSG00000272602.6.
DR GeneID; 152687; -.
DR KEGG; hsa:152687; -.
DR MANE-Select; ENST00000610261.6; ENSP00000477392.1; NM_182524.4; NP_872330.1.
DR UCSC; uc032szy.1; human.
DR AGR; HGNC:27196; -.
DR CTD; 152687; -.
DR DisGeNET; 152687; -.
DR GeneCards; ZNF595; -.
DR HGNC; HGNC:27196; ZNF595.
DR HPA; ENSG00000272602; Tissue enriched (placenta).
DR neXtProt; NX_Q8IYB9; -.
DR OpenTargets; ENSG00000272602; -.
DR VEuPathDB; HostDB:ENSG00000272602; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161765; -.
DR InParanoid; Q8IYB9; -.
DR OMA; CEKVISW; -.
DR OrthoDB; 5398495at2759; -.
DR PhylomeDB; Q8IYB9; -.
DR PathwayCommons; Q8IYB9; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q8IYB9; -.
DR BioGRID-ORCS; 152687; 27 hits in 298 CRISPR screens.
DR ChiTaRS; ZNF595; human.
DR GenomeRNAi; 152687; -.
DR Pharos; Q8IYB9; Tdark.
DR PRO; PR:Q8IYB9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8IYB9; Protein.
DR Bgee; ENSG00000272602; Expressed in placenta and 109 other cell types or tissues.
DR ExpressionAtlas; Q8IYB9; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 18.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24377; IP01015P-RELATED; 1.
DR PANTHER; PTHR24377:SF938; ZINC FINGER PROTEIN 93; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 17.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 18.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 17.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 18.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..648
FT /note="Zinc finger protein 595"
FT /id="PRO_0000047686"
FT DOMAIN 4..75
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 145..167
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 173..194
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 228..250
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 256..278
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 340..362
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 368..390
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 396..418
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 424..446
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..474
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 480..502
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 508..530
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 536..558
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 564..586
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 592..614
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 620..642
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VARIANT 628
FT /note="A -> G (in dbSNP:rs2006764)"
FT /id="VAR_061958"
FT CONFLICT 299
FT /note="L -> M (in Ref. 3; AAH36110/AAH43151)"
FT CONFLICT 397
FT /note="T -> A (in Ref. 3; AAH36110/AAH43151)"
SQ SEQUENCE 648 AA; 74302 MW; EBCB193E1D4660E1 CRC64;
MELVTFRDVA IEFSPEEWKC LDPAQQNLYR DVMLENYRNL VSLGFVISNP DLVTCLEQIK
EPCNLKIHET AAKPPAICSP FSQDLSPVQG IEDSFHKLIL KRYEKCGHEN LQLRKGCKRV
NECKVQKGVN NGVYQCLSTT QSKIFQCNTC VKVFSKFSNS NKHKIRHTGE KPFKCTECGR
SFYMSHLTQH TGIHAGEKPY KCEKCGKAFN RSTSLSKHKR IHTGEKPYTC EECGKAFRRS
TVLNEHKKIH TGEKPYKCEE CGKAFTRSTT LNEHKKIHTG EKPYKCKECG KAFRWSTSLN
EHKNIHTGEK PYKCKECGKA FRQSRSLNEH KNIHTGEKPY TCEKCGKAFN QSSSLIIHRS
IHSEQKLYKC EECGKAFTWS SSLNKHKRIH TGEKPYTCEE CGKAFYRSSH LAKHKRIHTG
EKPYTCEECG KAFNQSSTLI LHKRIHSGQK PYKCEECGKA FTRSTTLNEH KKIHTGEKPY
KCEECGKAFI WSASLNEHKN IHTGEKPYKC KECGKAFNQS SGLIIHRSIH SEQKLYKCEE
CGKAFTRSTA LNEHKKIHSG EKPYKCKECG KAYNLSSTLT KHKRIHTGEK PFTCEECGKA
FNWSSSLTKH KIIHTGEKSY KCEECGKAFN RPSTLTVHKR IHTGKEHS
//
