ID ZN419_HUMAN Reviewed; 510 AA.
AC Q96HQ0; B4DXU7; B4E348; B7ZA41; E9PCP4; E9PED0; E9PET3; E9PFX9; Q9H5P0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 27-MAR-2024, entry version 178.
DE RecName: Full=Zinc finger protein 419;
GN Name=ZNF419; Synonyms=ZNF419A;
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] (ISOFORMS 2; 3 AND 6), AND VARIANTS
RP GLN-141 AND VAL-336.
RC TISSUE=Brain, Coronary arterial endothelium, Testis, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-141
RP AND VAL-336.
RC TISSUE=Skin, and Uterus;
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-166 AND LYS-176, AND
RP IDENTIFICATION BY MASS 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 -!- INTERACTION:
CC Q96HQ0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10288482, EBI-3867333;
CC Q96HQ0; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10288482, EBI-10172290;
CC Q96HQ0; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10288482, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96HQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HQ0-2; Sequence=VSP_016034, VSP_016033;
CC Name=3;
CC IsoId=Q96HQ0-3; Sequence=VSP_046149;
CC Name=4;
CC IsoId=Q96HQ0-4; Sequence=VSP_047106;
CC Name=5;
CC IsoId=Q96HQ0-5; Sequence=VSP_016034;
CC Name=6;
CC IsoId=Q96HQ0-6; Sequence=VSP_046149, VSP_016033;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK026886; BAB15582.1; -; mRNA.
DR EMBL; AK302135; BAG63509.1; -; mRNA.
DR EMBL; AK304569; BAG65360.1; -; mRNA.
DR EMBL; AK316156; BAH14527.1; -; mRNA.
DR EMBL; AK316297; BAH14668.1; -; mRNA.
DR EMBL; AC003005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008297; AAH08297.1; -; mRNA.
DR EMBL; BC024259; AAH24259.1; -; mRNA.
DR CCDS; CCDS42637.1; -. [Q96HQ0-2]
DR CCDS; CCDS46211.1; -. [Q96HQ0-6]
DR CCDS; CCDS54325.1; -. [Q96HQ0-5]
DR CCDS; CCDS54326.1; -. [Q96HQ0-1]
DR CCDS; CCDS54327.1; -. [Q96HQ0-4]
DR CCDS; CCDS54328.1; -. [Q96HQ0-3]
DR RefSeq; NP_001091961.1; NM_001098491.1. [Q96HQ0-5]
DR RefSeq; NP_001091962.1; NM_001098492.1. [Q96HQ0-4]
DR RefSeq; NP_001091963.1; NM_001098493.1. [Q96HQ0-3]
DR RefSeq; NP_001091964.1; NM_001098494.1. [Q96HQ0-2]
DR RefSeq; NP_001091965.1; NM_001098495.1.
DR RefSeq; NP_001091966.1; NM_001098496.1. [Q96HQ0-6]
DR RefSeq; NP_001278672.1; NM_001291743.1.
DR RefSeq; NP_001278673.1; NM_001291744.1.
DR RefSeq; NP_001278674.1; NM_001291745.1.
DR RefSeq; NP_078967.3; NM_024691.3. [Q96HQ0-1]
DR AlphaFoldDB; Q96HQ0; -.
DR SMR; Q96HQ0; -.
DR BioGRID; 122856; 23.
DR IntAct; Q96HQ0; 5.
DR STRING; 9606.ENSP00000388864; -.
DR iPTMnet; Q96HQ0; -.
DR PhosphoSitePlus; Q96HQ0; -.
DR BioMuta; ZNF419; -.
DR DMDM; 209572704; -.
DR EPD; Q96HQ0; -.
DR MassIVE; Q96HQ0; -.
DR MaxQB; Q96HQ0; -.
DR PaxDb; 9606-ENSP00000388864; -.
DR PeptideAtlas; Q96HQ0; -.
DR ProteomicsDB; 19485; -.
DR ProteomicsDB; 19860; -.
DR ProteomicsDB; 19957; -.
DR ProteomicsDB; 20201; -.
DR ProteomicsDB; 76774; -. [Q96HQ0-1]
DR ProteomicsDB; 76775; -. [Q96HQ0-2]
DR Antibodypedia; 826; 158 antibodies from 21 providers.
DR DNASU; 79744; -.
DR Ensembl; ENST00000221735.12; ENSP00000221735.7; ENSG00000105136.22. [Q96HQ0-1]
DR Ensembl; ENST00000347466.10; ENSP00000299860.9; ENSG00000105136.22. [Q96HQ0-2]
DR Ensembl; ENST00000415379.6; ENSP00000392129.2; ENSG00000105136.22. [Q96HQ0-6]
DR Ensembl; ENST00000424930.6; ENSP00000388864.1; ENSG00000105136.22. [Q96HQ0-5]
DR Ensembl; ENST00000426954.6; ENSP00000390916.1; ENSG00000105136.22. [Q96HQ0-4]
DR Ensembl; ENST00000442920.6; ENSP00000414709.2; ENSG00000105136.22. [Q96HQ0-3]
DR GeneID; 79744; -.
DR KEGG; hsa:79744; -.
DR MANE-Select; ENST00000221735.12; ENSP00000221735.7; NM_024691.4; NP_078967.3.
DR UCSC; uc002qov.3; human. [Q96HQ0-1]
DR AGR; HGNC:20648; -.
DR CTD; 79744; -.
DR DisGeNET; 79744; -.
DR GeneCards; ZNF419; -.
DR HGNC; HGNC:20648; ZNF419.
DR HPA; ENSG00000105136; Low tissue specificity.
DR MIM; 617410; gene.
DR neXtProt; NX_Q96HQ0; -.
DR OpenTargets; ENSG00000105136; -.
DR PharmGKB; PA134871733; -.
DR VEuPathDB; HostDB:ENSG00000105136; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164209; -.
DR HOGENOM; CLU_002678_0_9_1; -.
DR InParanoid; Q96HQ0; -.
DR OMA; CGAEADE; -.
DR OrthoDB; 4305202at2759; -.
DR PhylomeDB; Q96HQ0; -.
DR TreeFam; TF339848; -.
DR PathwayCommons; Q96HQ0; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q96HQ0; -.
DR BioGRID-ORCS; 79744; 12 hits in 1176 CRISPR screens.
DR GenomeRNAi; 79744; -.
DR Pharos; Q96HQ0; Tdark.
DR PRO; PR:Q96HQ0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96HQ0; Protein.
DR Bgee; ENSG00000105136; Expressed in olfactory bulb and 200 other cell types or tissues.
DR ExpressionAtlas; Q96HQ0; baseline and differential.
DR Genevisible; Q96HQ0; HS.
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; 11.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR14003:SF22; GASTRULA ZINC FINGER PROTEIN XLCGF49.1-LIKE-RELATED; 1.
DR PANTHER; PTHR14003; TRANSCRIPTIONAL REPRESSOR PROTEIN YY; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
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..510
FT /note="Zinc finger protein 419"
FT /id="PRO_0000047574"
FT DOMAIN 27..98
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 203..225
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 231..253
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 259..281
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 287..309
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 315..337
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 343..365
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 371..393
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 399..421
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 427..449
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 455..477
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 483..505
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 12..24
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046149"
FT VAR_SEQ 12..24
FT /note="VPVAADLLTDHEE -> Q (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047106"
FT VAR_SEQ 24
FT /note="E -> EQ (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016034"
FT VAR_SEQ 67..99
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016033"
FT VARIANT 141
FT /note="E -> Q (in dbSNP:rs2074076)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_046651"
FT VARIANT 336
FT /note="I -> V (in dbSNP:rs2074077)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_046652"
FT CONFLICT 194
FT /note="E -> G (in Ref. 1; BAG65360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 58564 MW; 4B4EDB2D92053826 CRC64;
MAAAALRDPA QVPVAADLLT DHEEGYVTFE DVAVYFSQEE WRLLDDAQRL LYRNVMLENF
TLLASLGLAS SKTHEITQLE SWEEPFMPAW EVVTSAIPRG CWHGAEAEEA PEQIASVGLL
SSNIQQHQKQ HCGEKPLKRQ EGRVPVLRSC KVHLSEKSLQ SREVGKALLI SSGVLKHQVT
HTGEKSHRSS KSREAFHAGK RHYKCSECGK AFGQKYLLVQ HQRLHAGKKT YECSECGKLF
RDMSNLFIHQ IVHTGERPYG CSNCGKSFSR NAHLIEHQRV HTGEKPFTCS ECGKAFRHNS
TLVQHHKIHT GVRPYECSEC GKLFSFNSSL MKHQRIHTGE RPYKCSECGK FYSHKSNLIK
HWRVHTGERP YKCSDCGKFF TQCSSLMQHQ KVHTGEKPFK CNECGRFFRE NSTLVRHQRV
HTGAKPYECR ECGKFFSQSS TLMQHRKVHI GEKPFKCNEC GRLFRENSSL VKHQRVHTGA
KPYECRECGK FFRHNSSLFK HRRIHTGEMQ
//
