ZN549_HUMAN
ID ZN549_HUMAN Reviewed; 640 AA.
AC Q6P9A3; B3KV91; O43336; Q8NAR4;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zinc finger protein 549;
GN Name=ZNF549;
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 1 AND 2).
RC TISSUE=Teratocarcinoma;
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-223, 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 -!- INTERACTION:
CC Q6P9A3; P50402: EMD; NbExp=3; IntAct=EBI-13046342, EBI-489887;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P9A3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P9A3-2; Sequence=VSP_018379;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24605.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK092236; BAC03834.1; -; mRNA.
DR EMBL; AK122749; BAG53703.1; -; mRNA.
DR EMBL; AC003682; AAC24605.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471135; EAW72511.1; -; Genomic_DNA.
DR EMBL; BC060863; AAH60863.1; -; mRNA.
DR CCDS; CCDS12952.1; -. [Q6P9A3-2]
DR CCDS; CCDS56106.1; -. [Q6P9A3-1]
DR RefSeq; NP_001186224.1; NM_001199295.1. [Q6P9A3-1]
DR RefSeq; NP_694995.2; NM_153263.2. [Q6P9A3-2]
DR AlphaFoldDB; Q6P9A3; -.
DR SMR; Q6P9A3; -.
DR BioGRID; 129133; 9.
DR IntAct; Q6P9A3; 2.
DR STRING; 9606.ENSP00000365407; -.
DR iPTMnet; Q6P9A3; -.
DR PhosphoSitePlus; Q6P9A3; -.
DR BioMuta; ZNF549; -.
DR DMDM; 311033505; -.
DR EPD; Q6P9A3; -.
DR MassIVE; Q6P9A3; -.
DR MaxQB; Q6P9A3; -.
DR PaxDb; Q6P9A3; -.
DR PeptideAtlas; Q6P9A3; -.
DR PRIDE; Q6P9A3; -.
DR ProteomicsDB; 67033; -. [Q6P9A3-1]
DR ProteomicsDB; 67034; -. [Q6P9A3-2]
DR Antibodypedia; 33267; 63 antibodies from 18 providers.
DR DNASU; 256051; -.
DR Ensembl; ENST00000240719.7; ENSP00000240719.2; ENSG00000121406.9. [Q6P9A3-2]
DR Ensembl; ENST00000376233.8; ENSP00000365407.2; ENSG00000121406.9. [Q6P9A3-1]
DR GeneID; 256051; -.
DR KEGG; hsa:256051; -.
DR MANE-Select; ENST00000376233.8; ENSP00000365407.2; NM_001199295.2; NP_001186224.2.
DR UCSC; uc002qpa.3; human. [Q6P9A3-1]
DR CTD; 256051; -.
DR GeneCards; ZNF549; -.
DR HGNC; HGNC:26632; ZNF549.
DR HPA; ENSG00000121406; Low tissue specificity.
DR neXtProt; NX_Q6P9A3; -.
DR PharmGKB; PA134905435; -.
DR VEuPathDB; HostDB:ENSG00000121406; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164088; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; Q6P9A3; -.
DR OMA; HQVIPSR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6P9A3; -.
DR TreeFam; TF339848; -.
DR PathwayCommons; Q6P9A3; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q6P9A3; -.
DR BioGRID-ORCS; 256051; 15 hits in 1093 CRISPR screens.
DR ChiTaRS; ZNF549; human.
DR GenomeRNAi; 256051; -.
DR Pharos; Q6P9A3; Tdark.
DR PRO; PR:Q6P9A3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6P9A3; protein.
DR Bgee; ENSG00000121406; Expressed in cortical plate and 97 other tissues.
DR ExpressionAtlas; Q6P9A3; baseline and differential.
DR Genevisible; Q6P9A3; 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 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; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
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..640
FT /note="Zinc finger protein 549"
FT /id="PRO_0000234583"
FT DOMAIN 27..140
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 217..241
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 247..269
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 275..298
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 304..326
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 332..355
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..383
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 389..411
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 417..439
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 445..467
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 473..495
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 501..523
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 529..551
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 557..579
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 585..607
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 613..635
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 223
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 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018379"
FT VARIANT 8
FT /note="I -> N (in dbSNP:rs12461014)"
FT /id="VAR_059921"
FT CONFLICT 84
FT /note="S -> P (in Ref. 1; BAC03834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 74439 MW; CED338B5CC75DD97 CRC64;
MAEAALVITP QIPMVTEEFV KPSQGHVTFE DIAVYFSQEE WGLLDEAQRC LYHDVMLENF
SLMASVGCLH GIEAEEAPSE QTLSAQGVSQ ARTPKLGPSI PNAHSCEMCI LVMKDILYLS
EHQGTLPWQK PYTSVASGKW FSFGSNLQQH QNQDSGEKHI RKEESSALLL NSCKIPLSDN
LFPCKDVEKD FPTILGLLQH QTTHSRQEYA HRSRETFQQR RYKCEQVFNE KVHVTEHQRV
HTGEKAYKRR EYGKSLNSKY LFVEHQRTHN AEKPYVCNIC GKSFLHKQTL VGHQQRIHTR
ERSYVCIECG KSLSSKYSLV EHQRTHNGEK PYVCNVCGKS FRHKQTFVGH QQRIHTGERP
YVCMECGKSF IHSYDRIRHQ RVHTGEGAYQ CSECGKSFIY KQSLLDHHRI HTGERPYECK
ECGKAFIHKK RLLEHQRIHT GEKPYVCIIC GKSFIRSSDY MRHQRIHTGE RAYECSDCGK
AFISKQTLLK HHKIHTRERP YECSECGKGF YLEVKLLQHQ RIHTREQLCE CNECGKVFSH
QKRLLEHQKV HTGEKPCECS ECGKCFRHRT SLIQHQKVHS GERPYNCTAC EKAFIYKNKL
VEHQRIHTGE KPYECGKCGK AFNKRYSLVR HQKVHITEEP
