ZFP82_HUMAN
ID ZFP82_HUMAN Reviewed; 532 AA.
AC Q8N141; Q8NC63; Q8TF53;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Zinc finger protein 82 homolog;
DE Short=Zfp-82;
DE AltName: Full=Zinc finger protein 545;
GN Name=ZFP82; Synonyms=KIAA1948, ZNF545;
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=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 77-532.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-126 AND LYS-142, 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=BAB85534.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB85534.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AK074942; BAC11308.1; -; mRNA.
DR EMBL; AL834267; CAD38942.1; -; mRNA.
DR EMBL; BC032577; AAH32577.1; -; mRNA.
DR EMBL; AB075828; BAB85534.1; ALT_SEQ; mRNA.
DR CCDS; CCDS12493.1; -.
DR RefSeq; NP_597723.1; NM_133466.3.
DR AlphaFoldDB; Q8N141; -.
DR SMR; Q8N141; -.
DR BioGRID; 129864; 11.
DR IntAct; Q8N141; 1.
DR STRING; 9606.ENSP00000431265; -.
DR iPTMnet; Q8N141; -.
DR PhosphoSitePlus; Q8N141; -.
DR BioMuta; ZFP82; -.
DR DMDM; 74762511; -.
DR EPD; Q8N141; -.
DR jPOST; Q8N141; -.
DR MassIVE; Q8N141; -.
DR MaxQB; Q8N141; -.
DR PaxDb; Q8N141; -.
DR PeptideAtlas; Q8N141; -.
DR PRIDE; Q8N141; -.
DR ProteomicsDB; 71549; -.
DR Antibodypedia; 16307; 131 antibodies from 20 providers.
DR DNASU; 284406; -.
DR Ensembl; ENST00000392161.4; ENSP00000431265.1; ENSG00000181007.9.
DR GeneID; 284406; -.
DR KEGG; hsa:284406; -.
DR MANE-Select; ENST00000392161.4; ENSP00000431265.1; NM_133466.4; NP_597723.1.
DR UCSC; uc002ody.2; human.
DR CTD; 284406; -.
DR DisGeNET; 284406; -.
DR GeneCards; ZFP82; -.
DR HGNC; HGNC:28682; ZFP82.
DR HPA; ENSG00000181007; Low tissue specificity.
DR neXtProt; NX_Q8N141; -.
DR OpenTargets; ENSG00000181007; -.
DR PharmGKB; PA162409714; -.
DR VEuPathDB; HostDB:ENSG00000181007; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162531; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q8N141; -.
DR OMA; QHQSIHV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8N141; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q8N141; -.
DR SignaLink; Q8N141; -.
DR BioGRID-ORCS; 284406; 45 hits in 1067 CRISPR screens.
DR GenomeRNAi; 284406; -.
DR Pharos; Q8N141; Tbio.
DR PRO; PR:Q8N141; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N141; protein.
DR Bgee; ENSG00000181007; Expressed in secondary oocyte and 179 other tissues.
DR ExpressionAtlas; Q8N141; baseline and differential.
DR Genevisible; Q8N141; 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; 10.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
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..532
FT /note="Zinc finger protein 82 homolog"
FT /id="PRO_0000233164"
FT DOMAIN 6..77
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 170..192
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 198..220
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 226..248
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 254..276
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..304
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 338..360
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 394..416
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 422..444
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 450..472
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 478..500
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 506..528
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 128
FT /note="E -> G (in Ref. 1; BAC11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> A (in Ref. 1; BAC11308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 62578 MW; 39B18CE288A82DDC CRC64;
MALRSVMFSD VSIDFSPEEW EYLDLEQKDL YRDVMLENYS NLVSLGCFIS KPDVISSLEQ
GKEPWKVVRK GRRQYPDLET KYETKKLSLE NDIYEINLSQ WKIMERIENH GLKGLILKND
WESTGKIEGQ ERPQEGYFSS VKMPSEKVSS YQKRTSVTPH QRLHFVDKPY ECKECGKAFR
VRQQLTFHHR IHTGEKPYEC KECGMAFRQT AHLTRHQRLH SGEKLYECKE CGEAFICGAD
LRVHQKMHIG EKPYECKECG KAFRVRGQLT LHQRIHTGEK PYVCKECGKA FRQYAHLTRH
QKLNSADRLY ECKECGKAFL CGSGLRVHHK LHTGEKPYEC KECGKAFRVR QQLTLHQRIH
TGEKPYECKE CGKTFSRGYH LILHHRIHTG EKPYECKECW KAFSRYSQLI SHQSIHIGVK
PYDCKECGKA FRLLSQLTQH QSIHIGEKPY KCKECGKAFR LRQKLTLHQS IHTGEKPFEC
KECRKAFRLN SSLIQHLRIH SGEKPYECKE CKKAFRQHSH LTHHLKIHNV KI
