ZN181_HUMAN
ID ZN181_HUMAN Reviewed; 571 AA.
AC Q2M3W8; B7ZKX3; Q49A75;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Zinc finger protein 181;
DE AltName: Full=HHZ181;
GN Name=ZNF181;
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] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Lung, and 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).
RN [3]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-126, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2M3W8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2M3W8-2; Sequence=VSP_017824;
CC Name=3;
CC IsoId=Q2M3W8-3; Sequence=VSP_043416;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AC020910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043228; AAH43228.1; -; mRNA.
DR EMBL; BC104759; AAI04760.1; -; mRNA.
DR EMBL; BC143442; AAI43443.1; -; mRNA.
DR CCDS; CCDS32990.2; -. [Q2M3W8-1]
DR CCDS; CCDS46043.1; -. [Q2M3W8-3]
DR RefSeq; NP_001025168.2; NM_001029997.3. [Q2M3W8-1]
DR RefSeq; NP_001139137.1; NM_001145665.1. [Q2M3W8-3]
DR RefSeq; XP_005258906.1; XM_005258849.2. [Q2M3W8-1]
DR RefSeq; XP_005258907.1; XM_005258850.2. [Q2M3W8-3]
DR RefSeq; XP_006723246.1; XM_006723183.3. [Q2M3W8-1]
DR RefSeq; XP_016882228.1; XM_017026739.1. [Q2M3W8-3]
DR AlphaFoldDB; Q2M3W8; -.
DR SMR; Q2M3W8; -.
DR BioGRID; 130866; 5.
DR IntAct; Q2M3W8; 7.
DR STRING; 9606.ENSP00000420727; -.
DR iPTMnet; Q2M3W8; -.
DR PhosphoSitePlus; Q2M3W8; -.
DR BioMuta; ZNF181; -.
DR DMDM; 91208389; -.
DR jPOST; Q2M3W8; -.
DR MassIVE; Q2M3W8; -.
DR PaxDb; Q2M3W8; -.
DR PeptideAtlas; Q2M3W8; -.
DR PRIDE; Q2M3W8; -.
DR ProteomicsDB; 61384; -. [Q2M3W8-1]
DR ProteomicsDB; 61385; -. [Q2M3W8-2]
DR ProteomicsDB; 61386; -. [Q2M3W8-3]
DR Antibodypedia; 29203; 67 antibodies from 14 providers.
DR DNASU; 339318; -.
DR Ensembl; ENST00000459757.6; ENSP00000419435.1; ENSG00000197841.15. [Q2M3W8-3]
DR Ensembl; ENST00000492450.3; ENSP00000420727.1; ENSG00000197841.15. [Q2M3W8-1]
DR GeneID; 339318; -.
DR KEGG; hsa:339318; -.
DR MANE-Select; ENST00000492450.3; ENSP00000420727.1; NM_001029997.4; NP_001025168.2.
DR UCSC; uc002nvu.4; human. [Q2M3W8-1]
DR CTD; 339318; -.
DR DisGeNET; 339318; -.
DR GeneCards; ZNF181; -.
DR HGNC; HGNC:12971; ZNF181.
DR HPA; ENSG00000197841; Low tissue specificity.
DR MIM; 606741; gene.
DR neXtProt; NX_Q2M3W8; -.
DR OpenTargets; ENSG00000197841; -.
DR PharmGKB; PA37553; -.
DR VEuPathDB; HostDB:ENSG00000197841; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161431; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q2M3W8; -.
DR OMA; KEDICDE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q2M3W8; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q2M3W8; -.
DR SignaLink; Q2M3W8; -.
DR BioGRID-ORCS; 339318; 23 hits in 1097 CRISPR screens.
DR ChiTaRS; ZNF181; human.
DR GenomeRNAi; 339318; -.
DR Pharos; Q2M3W8; Tdark.
DR PRO; PR:Q2M3W8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q2M3W8; protein.
DR Bgee; ENSG00000197841; Expressed in calcaneal tendon and 98 other tissues.
DR ExpressionAtlas; Q2M3W8; 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 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; 10.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..571
FT /note="Zinc finger protein 181"
FT /id="PRO_0000230666"
FT DOMAIN 4..76
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 237..259
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 265..287
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 293..315
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..343
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 349..371
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..427
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..455
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 489..511
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..539
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017824"
FT VAR_SEQ 44
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043416"
SQ SEQUENCE 571 AA; 65842 MW; 8E69CEBA9B0E9720 CRC64;
MPQVTFNDVA IDFTHEEWGW LSSAQRDLYK DVMVQNYENL VSVAGLSVTK PYVITLLEDG
KEPWMMEKKL SKGMIPDWES RWENKELSTK KDNYDEDSPQ TVIIEKVVKQ SYEFSNSKKN
LEYIEKLEGK HGSQVDHFRP AILTSRESPT ADSVYKYNIF RSTFHSKSTL SEPQKISAEG
NSHKYDILKK NLPKKSVIKN EKVNGGKKLL NSNKSGAAFS QGKSLTLPQT CNREKIYTCS
ECGKAFGKQS ILNRHWRIHT GEKPYECREC GKTFSHGSSL TRHLISHSGE KPYKCIECGK
AFSHVSSLTN HQSTHTGEKP YECMNCGKSF SRVSHLIEHL RIHTQEKLYE CRICGKAFIH
RSSLIHHQKI HTGEKPYECR ECGKAFCCSS HLTRHQRIHT MEKQYECNKC LKVFSSLSFL
VQHQSIHTEE KPFECQKCRK SFNQLESLNM HLRNHIRLKP YECSICGKAF SHRSSLLQHH
RIHTGEKPYE CIKCGKTFSC SSNLTVHQRI HTGEKPYKCN ECGKAFSKGS NLTAHQRVHN
GEKPNSVVSV EKPLDYMNHY TCEKSYRRET V
