ZN544_HUMAN
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 03-AUG-2022, entry version 162.
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}.
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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; 15.
DR IntAct; Q6NX49; 11.
DR MINT; Q6NX49; -.
DR STRING; 9606.ENSP00000269829; -.
DR GlyGen; Q6NX49; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q6NX49; -.
DR PhosphoSitePlus; Q6NX49; -.
DR BioMuta; ZNF544; -.
DR DMDM; 74762345; -.
DR EPD; Q6NX49; -.
DR jPOST; Q6NX49; -.
DR MassIVE; Q6NX49; -.
DR MaxQB; Q6NX49; -.
DR PaxDb; Q6NX49; -.
DR PeptideAtlas; Q6NX49; -.
DR PRIDE; Q6NX49; -.
DR ProteomicsDB; 66747; -.
DR Antibodypedia; 1170; 77 antibodies from 19 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 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; KPCENHQ; -.
DR OrthoDB; 1318335at2759; -.
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 1095 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 198 other tissues.
DR ExpressionAtlas; Q6NX49; baseline and differential.
DR Genevisible; Q6NX49; HS.
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 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; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
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; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW 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
