ZN888_HUMAN
ID ZN888_HUMAN Reviewed; 718 AA.
AC P0CJ79; A0A1W2PQ69;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Zinc finger protein 888 {ECO:0000305};
GN Name=ZNF888 {ECO:0000312|HGNC:HGNC:38695};
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).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AC010487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS86801.1; -.
DR RefSeq; NP_001297056.1; NM_001310127.1.
DR RefSeq; XP_005259508.1; XM_005259451.4.
DR RefSeq; XP_016882288.1; XM_017026799.1.
DR AlphaFoldDB; P0CJ79; -.
DR SMR; P0CJ79; -.
DR IntAct; P0CJ79; 4.
DR iPTMnet; P0CJ79; -.
DR PhosphoSitePlus; P0CJ79; -.
DR BioMuta; ZNF888; -.
DR DMDM; 322967617; -.
DR EPD; P0CJ79; -.
DR jPOST; P0CJ79; -.
DR MassIVE; P0CJ79; -.
DR PeptideAtlas; P0CJ79; -.
DR PRIDE; P0CJ79; -.
DR ProteomicsDB; 52493; -.
DR DNASU; 388559; -.
DR Ensembl; ENST00000638862.2; ENSP00000491567.1; ENSG00000213793.6.
DR GeneID; 388559; -.
DR KEGG; hsa:388559; -.
DR MANE-Select; ENST00000638862.2; ENSP00000491567.1; NM_001393938.1; NP_001380867.1.
DR CTD; 388559; -.
DR GeneCards; ZNF888; -.
DR HGNC; HGNC:38695; ZNF888.
DR HPA; ENSG00000213793; Low tissue specificity.
DR neXtProt; NX_P0CJ79; -.
DR VEuPathDB; HostDB:ENSG00000213793; -.
DR GeneTree; ENSGT00940000154397; -.
DR InParanoid; P0CJ79; -.
DR OMA; QDVHMKV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P0CJ79; -.
DR PathwayCommons; P0CJ79; -.
DR SignaLink; P0CJ79; -.
DR ChiTaRS; ZNF888; human.
DR GenomeRNAi; 388559; -.
DR Pharos; P0CJ79; Tdark.
DR PRO; PR:P0CJ79; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P0CJ79; protein.
DR Bgee; ENSG00000213793; Expressed in cerebellar vermis and 105 other tissues.
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 InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 17.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 18.
PE 3: Inferred from homology;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..718
FT /note="Zinc finger protein 888"
FT /id="PRO_0000404597"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 214..236
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 242..264
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 270..292
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..320
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 326..348
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 382..404
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..488
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 690..712
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N823"
SQ SEQUENCE 718 AA; 83549 MW; 285E27DC2F7E5E8E CRC64;
MALPQGLLTF RDVAIEFSQE EWKCLDPAQR TLYRDVMLEN YRNLVSLDIS SKCMMEFSSI
GKGNTEVIHT GTLQRLASHH IGECCFQEIE KDIHDFVFQW QEDETNGHEA PMTEIKELTG
STDQYDQRHA GNKPIKYQLG SSFHSHLPEL HIFQPEGKIG NQLEKSINNA SSVSTSQRIS
CRPKTHISNN YGNNFFHSSL LTQKQDVHRK EKSFQFNESG KSFNCSSLFK KHQIIHLGEK
QYKCDVCGKD FNQKRYLAHH RRCHTGEKPY MCNKCGKVFN KKAYLARHYR RHTGEKPYKC
NECGKTFSDK SALLVHKTIH TGEKPYKCNE CGKVFNQQSN LARHHRVHTG EKPYQCKECD
KVFSRKSYLE RHRRIHTGEK PYKCKVCDKA FRHDSHLAQH IVIHTREKPY KCNECGKTFG
ENSALLVHKT IHTGEKPYKC NECGKVFNQQ SNLARHHRLH TGEKPYKCKE CDKVFSRKSH
LERHRRIHTG EKPYKCKVCD KAFRRDSHLA QHTVIHTGEK PYKCNECGKT FVQNSSLVMH
KVIHTGEKRY KCNECGKSFN HKSSLAYHHR LHTGEKPYKC NECGKVFRTQ SQLACHHRLH
TGEKPYKCEE CDKVFNIKSH LEIHRRVHTG EKPYKCRVCD KAFGRDSYLA QHQRVHTGEK
PYKCKVCDKA FKCYSHLAQH TRIHTGEKPF KCSECGKAFR AQSTLIHHQA IHGVGKLD
