ID ZN544_HUMAN Reviewed; 715 AA. AC Q6NX49; A8K6J1; Q9UEX4; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-NOV-2024, entry version 175. DE RecName: Full=Zinc finger protein 544; GN Name=ZNF544; 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 [MRNA], AND VARIANT ARG-700. RA Hu P., Yu L., Zhang M.; RT "Cloning of a novel human gene coding a zinc finger protein."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-700. RC TISSUE=Placenta; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-700. 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]. RC TISSUE=PNS; 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-534, 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 [6] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-273; LYS-289 AND LYS-534, 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 Q6NX49; O76003: GLRX3; NbExp=3; IntAct=EBI-2841978, EBI-374781; CC Q6NX49; Q9GZM8: NDEL1; NbExp=5; IntAct=EBI-2841978, EBI-928842; CC Q6NX49; Q12933: TRAF2; NbExp=4; IntAct=EBI-2841978, EBI-355744; CC Q6NX49; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-2841978, EBI-744794; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF020591; AAC01956.1; -; mRNA. DR EMBL; AK291656; BAF84345.1; -; mRNA. DR EMBL; CH471135; EAW72568.1; -; Genomic_DNA. DR EMBL; BC067271; AAH67271.1; -; mRNA. DR CCDS; CCDS12973.1; -. DR RefSeq; NP_001307696.1; NM_001320767.1. DR RefSeq; NP_001307698.1; NM_001320769.1. DR RefSeq; NP_001307699.1; NM_001320770.1. DR RefSeq; NP_001307700.1; NM_001320771.1. DR RefSeq; NP_001307702.1; NM_001320773.1. DR RefSeq; NP_001307705.1; NM_001320776.1. DR RefSeq; NP_001307706.1; NM_001320777.1. DR RefSeq; NP_001307709.1; NM_001320780.1. DR RefSeq; NP_001307712.1; NM_001320783.1. DR RefSeq; NP_001307714.1; NM_001320785.1. DR RefSeq; NP_001307715.1; NM_001320786.1. DR RefSeq; NP_001307720.1; NM_001320791.1. DR RefSeq; NP_055295.2; NM_014480.3. DR AlphaFoldDB; Q6NX49; -. DR SMR; Q6NX49; -. DR BioGRID; 118123; 16. DR IntAct; Q6NX49; 12. DR MINT; Q6NX49; -. DR STRING; 9606.ENSP00000269829; -. DR GlyCosmos; Q6NX49; 1 site, 2 glycans. DR GlyGen; Q6NX49; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q6NX49; -. DR PhosphoSitePlus; Q6NX49; -. DR BioMuta; ZNF544; -. DR DMDM; 74762345; -. DR jPOST; Q6NX49; -. DR MassIVE; Q6NX49; -. DR PaxDb; 9606-ENSP00000269829; -. DR PeptideAtlas; Q6NX49; -. DR ProteomicsDB; 66747; -. DR Antibodypedia; 1170; 68 antibodies from 18 providers. DR DNASU; 27300; -. DR Ensembl; ENST00000269829.5; ENSP00000269829.4; ENSG00000198131.15. DR Ensembl; ENST00000596652.5; ENSP00000469635.1; ENSG00000198131.15. DR Ensembl; ENST00000687789.1; ENSP00000510489.1; ENSG00000198131.15. DR GeneID; 27300; -. DR KEGG; hsa:27300; -. DR MANE-Select; ENST00000687789.1; ENSP00000510489.1; NM_014480.4; NP_055295.2. DR UCSC; uc061dqq.1; human. DR AGR; HGNC:16759; -. DR CTD; 27300; -. DR DisGeNET; 27300; -. DR GeneCards; ZNF544; -. DR HGNC; HGNC:16759; ZNF544. DR HPA; ENSG00000198131; Low tissue specificity. DR neXtProt; NX_Q6NX49; -. DR OpenTargets; ENSG00000198131; -. DR PharmGKB; PA134871299; -. DR VEuPathDB; HostDB:ENSG00000198131; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000164425; -. DR InParanoid; Q6NX49; -. DR OMA; RCQLIRH; -. DR OrthoDB; 5259213at2759; -. DR PhylomeDB; Q6NX49; -. DR TreeFam; TF341817; -. DR PathwayCommons; Q6NX49; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q6NX49; -. DR BioGRID-ORCS; 27300; 9 hits in 1173 CRISPR screens. DR ChiTaRS; ZNF544; human. DR GenomeRNAi; 27300; -. DR Pharos; Q6NX49; Tdark. DR PRO; PR:Q6NX49; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q6NX49; protein. DR Bgee; ENSG00000198131; Expressed in buccal mucosa cell and 200 other cell types or tissues. DR ExpressionAtlas; Q6NX49; baseline and differential. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0001228; F:DNA-binding transcription activator 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 FunFam; 3.30.160.60:FF:000478; Zinc finger protein 133; 1. DR FunFam; 3.30.160.60:FF:000506; Zinc finger protein 23; 1. DR FunFam; 3.30.160.60:FF:002343; Zinc finger protein 33A; 4. DR FunFam; 3.30.160.60:FF:000848; Zinc finger protein 35; 2. DR FunFam; 3.30.160.60:FF:002254; Zinc finger protein 540; 2. DR FunFam; 3.30.160.60:FF:000953; Zinc finger protein 691; 1. DR FunFam; 3.30.160.60:FF:000934; zinc finger protein 90 homolog; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 14. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR23235:SF149; LOW QUALITY PROTEIN: ZINC FINGER PROTEIN 239-RELATED; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 12. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 12. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 9. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13. PE 1: Evidence at protein level; KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Proteomics identification; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..715 FT /note="Zinc finger protein 544" FT /id="PRO_0000047643" FT DOMAIN 14..85 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 354..374 FT /note="C2H2-type 1; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 380..402 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 408..430 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 436..458 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 464..486 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 492..514 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 520..542 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 548..570 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 576..598 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 604..626 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 632..654 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 660..682 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 688..710 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT CROSSLNK 273 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 289 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 534 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VARIANT 203 FT /note="H -> D (in dbSNP:rs6510130)" FT /id="VAR_052859" FT VARIANT 700 FT /note="Q -> R (in dbSNP:rs260462)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1, FT ECO:0000269|Ref.3" FT /id="VAR_052860" FT CONFLICT 86 FT /note="T -> P (in Ref. 1; AAC01956)" FT /evidence="ECO:0000305" FT CONFLICT 91 FT /note="R -> G (in Ref. 1; AAC01956)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="Q -> L (in Ref. 1; AAC01956)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="R -> T (in Ref. 1; AAC01956)" FT /evidence="ECO:0000305" FT CONFLICT 590 FT /note="Q -> R (in Ref. 1; AAC01956)" FT /evidence="ECO:0000305" SQ SEQUENCE 715 AA; 81742 MW; D0F6F775D9741E03 CRC64; MEARSMLVPP QASVCFEDVA MAFTQEEWEQ LDLAQRTLYR EVTLETWEHI VSLGLFLSKS DVISQLEQEE DLCRAEQEAP RDWKATLEEN RLNSEKDRAR EELSHHVEVY RSGPEEPPSL VLGKVQDQSN QLREHQENSL RFMVLTSERL FAQREHCELE LGGGYSLPST LSLLPTTLPT STGFPKPNSQ VKELKQNSAF INHEKNGADG KHCESHQCAR AFCQSIYLSK LGNVETGKKN PYEYIVSGDS LNYGSSLCFH GRTFSVKKSD DCKDYGNLFS HSVSLNEQKP VHFGKSQYEC DECRETCSES LCLVQTERSG PGETPFRCEE RCAAFPMASS FSDCNIIQTT EKPSVCNQCG KSFSCCKLIH QRTHTGEKPF ECTQCGKSFS QSYDLVIHQR THTGEKPYEC DLCGKSFTQR SKLITHQRIH TGEKPYQCIE CRKSFRWNSN LIVHQRIHTG EKPYECTHCG KSFSQSYELV THKRTHTGEK PFKCTQCGKS FSQKYDLVVH QRTHTGEKPY ECNLCGKSFS QSSKLITHQR IHTGEKPYQC IECGKSFRWN SNLVIHQRIH TGEKPYDCTH CGKSFSQSYQ LVAHKRTHTG EKPYECNECG KAFNRSTQLI RHLQIHTGEK PYKCNQCNKA FARSSYLVMH QRTHTGEKPF ECSQCGKAFS GSSNLLSHHR IHSGEKPYEC SDCGKSFRQQ SQLVVHRRTH TGEKP //