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Database: UniProt
Entry: Q86TJ5
LinkDB: Q86TJ5
Original site: Q86TJ5 
ID   ZN554_HUMAN             Reviewed;         538 AA.
AC   Q86TJ5; Q8NAT3; Q9BWN3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Zinc finger protein 554;
GN   Name=ZNF554;
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].
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 MRNA].
RC   TISSUE=Eye, and 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   [3]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, 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       Q86TJ5; O15160: POLR1C; NbExp=3; IntAct=EBI-19137100, EBI-1055079;
CC       Q86TJ5; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-19137100, EBI-372432;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH00113.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK092136; BAC03814.1; -; mRNA.
DR   EMBL; BC000113; AAH00113.1; ALT_INIT; mRNA.
DR   EMBL; BC047777; AAH47777.1; -; mRNA.
DR   CCDS; CCDS42462.1; -.
DR   RefSeq; NP_001096121.1; NM_001102651.1.
DR   AlphaFoldDB; Q86TJ5; -.
DR   SMR; Q86TJ5; -.
DR   BioGRID; 125417; 17.
DR   IntAct; Q86TJ5; 3.
DR   STRING; 9606.ENSP00000321132; -.
DR   iPTMnet; Q86TJ5; -.
DR   PhosphoSitePlus; Q86TJ5; -.
DR   BioMuta; ZNF554; -.
DR   DMDM; 74759371; -.
DR   EPD; Q86TJ5; -.
DR   jPOST; Q86TJ5; -.
DR   MassIVE; Q86TJ5; -.
DR   MaxQB; Q86TJ5; -.
DR   PaxDb; 9606-ENSP00000321132; -.
DR   PeptideAtlas; Q86TJ5; -.
DR   ProteomicsDB; 69708; -.
DR   Antibodypedia; 23070; 138 antibodies from 18 providers.
DR   DNASU; 115196; -.
DR   Ensembl; ENST00000317243.10; ENSP00000321132.4; ENSG00000172006.12.
DR   GeneID; 115196; -.
DR   KEGG; hsa:115196; -.
DR   MANE-Select; ENST00000317243.10; ENSP00000321132.4; NM_001102651.2; NP_001096121.1.
DR   UCSC; uc002lwm.3; human.
DR   AGR; HGNC:26629; -.
DR   CTD; 115196; -.
DR   GeneCards; ZNF554; -.
DR   HGNC; HGNC:26629; ZNF554.
DR   HPA; ENSG00000172006; Low tissue specificity.
DR   neXtProt; NX_Q86TJ5; -.
DR   PharmGKB; PA134915990; -.
DR   VEuPathDB; HostDB:ENSG00000172006; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163560; -.
DR   HOGENOM; CLU_002678_44_5_1; -.
DR   InParanoid; Q86TJ5; -.
DR   OMA; EKATAWH; -.
DR   OrthoDB; 5258420at2759; -.
DR   PhylomeDB; Q86TJ5; -.
DR   TreeFam; TF337055; -.
DR   PathwayCommons; Q86TJ5; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q86TJ5; -.
DR   BioGRID-ORCS; 115196; 6 hits in 1168 CRISPR screens.
DR   GenomeRNAi; 115196; -.
DR   Pharos; Q86TJ5; Tdark.
DR   PRO; PR:Q86TJ5; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q86TJ5; Protein.
DR   Bgee; ENSG00000172006; Expressed in buccal mucosa cell and 159 other cell types or tissues.
DR   ExpressionAtlas; Q86TJ5; baseline and differential.
DR   Genevisible; Q86TJ5; HS.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative 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; 7.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1.
DR   PANTHER; PTHR23232:SF141; KRAB DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   Pfam; PF13465; zf-H2C2_2; 1.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
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..538
FT                   /note="Zinc finger protein 554"
FT                   /id="PRO_0000274875"
FT   DOMAIN          45..148
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         271..292
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         324..346
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         352..374
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         380..402
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         408..430
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         436..458
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         464..486
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         492..514
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        178
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         190
FT                   /note="E -> G (in dbSNP:rs867168)"
FT                   /id="VAR_052861"
FT   VARIANT         211
FT                   /note="V -> I (in dbSNP:rs867169)"
FT                   /id="VAR_052862"
SQ   SEQUENCE   538 AA;  60582 MW;  00BF620D2028704C CRC64;
     MVTCAHLGRR ARLPAAQPSA CPGTCFSQEE RMAAGYLPRW SQELVTFEDV SMDFSQEEWE
     LLEPAQKNLY REVMLENYRN VVSLEALKNQ CTDVGIKEGP LSPAQTSQVT SLSSWTGYLL
     FQPVASSHLE QREALWIEEK GTPQASCSDW MTVLRNQDST YKKVALQEEP ASGINMIKLI
     REDGGWKQLE DSHEDPQGLL SQKASLHVVA VPQEKATAWH GFGENGNLSP ALVLSQGSSK
     GNHLCGSELD ITSLASDSVL NHHQLGYADR RPCESNECGN AIRQNSHFIQ HGGKMFVYLE
     NGQSLNHGMA LTIHNKINTA EKPFECHQCG KVFNRRHSLS EHQRIHTGEK PYECQECGRA
     FTHSSTLTRH LRTHTGEKPY GCGECGKAFN RISSLTQHQR IHTGEKPYKC EDCGKSFCQS
     SYLILHKRTH TGEKPYECSE CGKAFSDRSS LNQHERTHTG ENPYECKQCG RAFSQRSSLV
     RHERTHTGEK PYRCQECGKA FSQSSSLVTH QKTHSSQKTY KIIDCGKAFY QNRHLIGY
//
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