ZN552_HUMAN
ID ZN552_HUMAN Reviewed; 407 AA.
AC Q9H707; B3KUE9; Q6P5A6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc finger protein 552;
GN Name=ZNF552;
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 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Small intestine;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-407.
RC TISSUE=Prostate;
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-198; LYS-251 AND LYS-266, AND
RP IDENTIFICATION BY MASS 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-176; LYS-198 AND LYS-308, 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 Q9H707; X5D778: ANKRD11; NbExp=3; IntAct=EBI-2555731, EBI-17183751;
CC Q9H707; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-2555731, EBI-541426;
CC Q9H707; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2555731, EBI-3866279;
CC Q9H707; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-2555731, EBI-11977221;
CC Q9H707; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2555731, EBI-10961624;
CC Q9H707; O95273: CCNDBP1; NbExp=3; IntAct=EBI-2555731, EBI-748961;
CC Q9H707; Q96Q77: CIB3; NbExp=3; IntAct=EBI-2555731, EBI-10292696;
CC Q9H707; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-2555731, EBI-11962928;
CC Q9H707; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2555731, EBI-3867333;
CC Q9H707; Q92997: DVL3; NbExp=3; IntAct=EBI-2555731, EBI-739789;
CC Q9H707; O43559: FRS3; NbExp=3; IntAct=EBI-2555731, EBI-725515;
CC Q9H707; P55040: GEM; NbExp=3; IntAct=EBI-2555731, EBI-744104;
CC Q9H707; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2555731, EBI-5916454;
CC Q9H707; P13807: GYS1; NbExp=3; IntAct=EBI-2555731, EBI-740553;
CC Q9H707; P09067: HOXB5; NbExp=3; IntAct=EBI-2555731, EBI-3893317;
CC Q9H707; Q9C086: INO80B; NbExp=3; IntAct=EBI-2555731, EBI-715611;
CC Q9H707; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-2555731, EBI-11954971;
CC Q9H707; Q9BYQ6: KRTAP4-11; NbExp=6; IntAct=EBI-2555731, EBI-10302392;
CC Q9H707; Q9BYR2: KRTAP4-5; NbExp=6; IntAct=EBI-2555731, EBI-11993254;
CC Q9H707; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2555731, EBI-739832;
CC Q9H707; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2555731, EBI-10172526;
CC Q9H707; Q9UPV7: PHF24; NbExp=3; IntAct=EBI-2555731, EBI-17717171;
CC Q9H707; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-2555731, EBI-748391;
CC Q9H707; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-2555731, EBI-750487;
CC Q9H707; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-2555731, EBI-11952721;
CC Q9H707; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-2555731, EBI-725997;
CC Q9H707; Q05516: ZBTB16; NbExp=3; IntAct=EBI-2555731, EBI-711925;
CC Q9H707; Q5T619: ZNF648; NbExp=3; IntAct=EBI-2555731, EBI-11985915;
CC Q9H707; Q8N720: ZNF655; NbExp=3; IntAct=EBI-2555731, EBI-625509;
CC Q9H707; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-2555731, EBI-10240849;
CC Q9H707; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-2555731, EBI-5667516;
CC Q9H707; Q96EG3: ZNF837; NbExp=6; IntAct=EBI-2555731, EBI-11962574;
CC Q9H707; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2555731, EBI-527853;
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=BAB15093.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC010645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DA345819; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK025256; BAB15093.1; ALT_SEQ; mRNA.
DR EMBL; AK097041; BAG53411.1; -; mRNA.
DR EMBL; CH471135; EAW72535.1; -; Genomic_DNA.
DR EMBL; BC046237; AAH46237.1; -; mRNA.
DR EMBL; BC062982; AAH62982.1; -; mRNA.
DR EMBL; BC082767; AAH82767.1; -; mRNA.
DR CCDS; CCDS12963.1; -.
DR RefSeq; NP_079038.2; NM_024762.3.
DR AlphaFoldDB; Q9H707; -.
DR SMR; Q9H707; -.
DR BioGRID; 122913; 38.
DR IntAct; Q9H707; 37.
DR STRING; 9606.ENSP00000375582; -.
DR iPTMnet; Q9H707; -.
DR PhosphoSitePlus; Q9H707; -.
DR BioMuta; ZNF552; -.
DR DMDM; 147742907; -.
DR EPD; Q9H707; -.
DR MassIVE; Q9H707; -.
DR MaxQB; Q9H707; -.
DR PaxDb; Q9H707; -.
DR PeptideAtlas; Q9H707; -.
DR PRIDE; Q9H707; -.
DR ProteomicsDB; 81071; -.
DR Antibodypedia; 71188; 11 antibodies from 6 providers.
DR DNASU; 79818; -.
DR Ensembl; ENST00000391701.1; ENSP00000375582.1; ENSG00000178935.5.
DR GeneID; 79818; -.
DR KEGG; hsa:79818; -.
DR MANE-Select; ENST00000391701.1; ENSP00000375582.1; NM_024762.3; NP_079038.2.
DR UCSC; uc002qqg.3; human.
DR CTD; 79818; -.
DR GeneCards; ZNF552; -.
DR HGNC; HGNC:26135; ZNF552.
DR HPA; ENSG00000178935; Low tissue specificity.
DR neXtProt; NX_Q9H707; -.
DR OpenTargets; ENSG00000178935; -.
DR PharmGKB; PA134986961; -.
DR VEuPathDB; HostDB:ENSG00000178935; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164660; -.
DR HOGENOM; CLU_002678_0_2_1; -.
DR InParanoid; Q9H707; -.
DR OMA; FRGGKTH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9H707; -.
DR TreeFam; TF341078; -.
DR PathwayCommons; Q9H707; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9H707; -.
DR BioGRID-ORCS; 79818; 19 hits in 1097 CRISPR screens.
DR ChiTaRS; ZNF552; human.
DR GenomeRNAi; 79818; -.
DR Pharos; Q9H707; Tdark.
DR PRO; PR:Q9H707; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H707; protein.
DR Bgee; ENSG00000178935; Expressed in buccal mucosa cell and 130 other tissues.
DR ExpressionAtlas; Q9H707; baseline and differential.
DR Genevisible; Q9H707; 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; 5.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
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..407
FT /note="Zinc finger protein 552"
FT /id="PRO_0000286810"
FT DOMAIN 14..90
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 91..113
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 119..141
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..262
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..290
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 296..318
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 324..346
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 352..374
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 380..402
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 198
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 CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 242
FT /note="W -> C (in dbSNP:rs2288538)"
FT /id="VAR_032177"
FT CONFLICT 286
FT /note="H -> R (in Ref. 3; BAB15093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46198 MW; A2D6783033EEDC61 CRC64;
MAAAALRFPV QGTVTFEDVA VKFTQEEWNL LSEAQRCLYR DVTLENLALM SSLGCWCGVE
DEAAPSKQSI YIQRETQVRT PMAGVSPKKA HPCEMCGPIL GDILHVADHQ GTHHKQKLHR
CEAWGNKLYD SGNFHQHQNE HIGEKPYRGS VEEALFAKRC KLHVSGESSV FSESGKDFLL
RSGLLQQEAT HTGKSNSKTE CVSLFHGGKS HYSCGGCMKH FSTKDILSQH ERLLPTEEPS
VWCECGKSSS KYDSFSNHQG VHTREKPYTC GICGKLFNSK SHLLVHQRIH TGEKPYECEV
CQKFFRHKYH LIAHQRVHTG ERPYECSDCG KSFTHSSTFR VHKRVHTGQK PYECSECGKS
FAESSSLTKH RRVHTGEKPY GCSECEKKFR QISSLRHHQR VHKRKGL
