ZN529_HUMAN
ID ZN529_HUMAN Reviewed; 563 AA.
AC Q6P280; K7EKE1; Q9H731; Q9HCF7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger protein 529;
GN Name=ZNF529; Synonyms=KIAA1615;
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=Colon;
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 MRNA], AND VARIANT VAL-131.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-563, AND VARIANT VAL-131.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87 AND LYS-268, 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 -!- 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=AAH64690.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15068.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK025110; BAB15068.1; ALT_FRAME; mRNA.
DR EMBL; AC092295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064690; AAH64690.1; ALT_INIT; mRNA.
DR EMBL; AB046835; BAB13441.1; -; mRNA.
DR CCDS; CCDS54256.1; -.
DR RefSeq; NP_001139121.1; NM_001145649.1.
DR RefSeq; NP_001308280.1; NM_001321351.1.
DR RefSeq; NP_066002.3; NM_020951.4.
DR RefSeq; XP_006723365.1; XM_006723302.3.
DR RefSeq; XP_011525466.1; XM_011527164.2.
DR RefSeq; XP_011525469.1; XM_011527167.2.
DR RefSeq; XP_016882530.1; XM_017027041.1.
DR RefSeq; XP_016882531.1; XM_017027042.1.
DR RefSeq; XP_016882532.1; XM_017027043.1.
DR RefSeq; XP_016882533.1; XM_017027044.1.
DR AlphaFoldDB; Q6P280; -.
DR SMR; Q6P280; -.
DR BioGRID; 121735; 3.
DR IntAct; Q6P280; 1.
DR STRING; 9606.ENSP00000465578; -.
DR GlyGen; Q6P280; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P280; -.
DR PhosphoSitePlus; Q6P280; -.
DR BioMuta; ZNF529; -.
DR DMDM; 519668652; -.
DR jPOST; Q6P280; -.
DR MassIVE; Q6P280; -.
DR MaxQB; Q6P280; -.
DR PaxDb; Q6P280; -.
DR PeptideAtlas; Q6P280; -.
DR PRIDE; Q6P280; -.
DR ProteomicsDB; 66882; -.
DR Antibodypedia; 29796; 98 antibodies from 18 providers.
DR DNASU; 57711; -.
DR Ensembl; ENST00000591340.6; ENSP00000465578.1; ENSG00000186020.13.
DR GeneID; 57711; -.
DR KEGG; hsa:57711; -.
DR MANE-Select; ENST00000591340.6; ENSP00000465578.1; NM_020951.5; NP_066002.3.
DR UCSC; uc002oeg.5; human.
DR CTD; 57711; -.
DR GeneCards; ZNF529; -.
DR HGNC; HGNC:29328; ZNF529.
DR HPA; ENSG00000186020; Low tissue specificity.
DR neXtProt; NX_Q6P280; -.
DR OpenTargets; ENSG00000186020; -.
DR PharmGKB; PA134910867; -.
DR VEuPathDB; HostDB:ENSG00000186020; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163735; -.
DR InParanoid; Q6P280; -.
DR OMA; NYACNQC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6P280; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q6P280; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q6P280; -.
DR BioGRID-ORCS; 57711; 16 hits in 1068 CRISPR screens.
DR ChiTaRS; ZNF529; human.
DR GenomeRNAi; 57711; -.
DR Pharos; Q6P280; Tdark.
DR PRO; PR:Q6P280; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6P280; protein.
DR Bgee; ENSG00000186020; Expressed in endothelial cell and 194 other tissues.
DR ExpressionAtlas; Q6P280; baseline and differential.
DR Genevisible; Q6P280; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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 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; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
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..563
FT /note="Zinc finger protein 529"
FT /id="PRO_0000280419"
FT DOMAIN 39..119
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 199..221
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 254..276
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..304
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 338..360
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 394..416
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 422..444
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 450..472
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 478..500
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 506..528
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 534..556
FT /note="C2H2-type 12; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 131
FT /note="L -> V (in dbSNP:rs2912444)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031147"
FT CONFLICT 79
FT /note="D -> N (in Ref. 1; BAB15068)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> P (in Ref. 2; BAB13441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 65865 MW; F59AA85D249C1A9E CRC64;
MANSSFIGDH VHGAPHAVMP EVEFPDQFFT VLTMDHELVT LRDVVINFSQ EEWEYLDSAQ
RNLYWDVMME NYSNLLSLDL ESRNETKHLS VGKDIIQNTG SQWEVMESSK LCGLEGSIFR
NDWQSKSKID LQGPEVGYFS QMKIISENVP SYKTHESLTL PRRTHDSEKP YEYKEYEKVF
SCDLEFDEYQ KIHTGGKNYE CNQCWKTFGI DNSSMLQLNI HTGVKPCKYM EYGNTCSFYK
DFNVYQKIHN EKFYKCKEYR RTFERVGKVT PLQRVHDGEK HFECSFCGKS FRVHAQLTRH
QKIHTDEKTY KCMECGKDFR FHSQLTEHQR IHTGEKPYKC MHCEKVFRIS SQLIEHQRIH
TGEKPYACKE CGKAFGVCRE LARHQRIHTG KKPYECKACG KVFRNSSSLT RHQRIHTGEK
PYKCKECEKA FGVGSELTRH ERIHSGQKPY ECKECGKFFR LTSALIQHQR IHSGEKPYEC
KVCGKAFRHS SALTEHQRIH TGEKPYECKA CGKAFRHSSS FTKHQRIHTD DKPYECKECG
NSFSVVGHLT CQPKIYTGEK SFD
