ZN721_HUMAN
ID ZN721_HUMAN Reviewed; 911 AA.
AC Q8TF20; Q69YG7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Zinc finger protein 721;
GN Name=ZNF721; Synonyms=KIAA1982;
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] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-123 (ISOFORM 2).
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 313-911.
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-478; LYS-649 AND LYS-786, 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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TF20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TF20-2; Sequence=VSP_040879;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH10687.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL834155; CAH10687.1; ALT_FRAME; mRNA.
DR EMBL; AC092574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DA309597; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB075862; BAB85568.1; -; mRNA.
DR CCDS; CCDS46991.1; -. [Q8TF20-2]
DR RefSeq; NP_597731.2; NM_133474.3. [Q8TF20-2]
DR AlphaFoldDB; Q8TF20; -.
DR SMR; Q8TF20; -.
DR BioGRID; 128095; 7.
DR IntAct; Q8TF20; 4.
DR STRING; 9606.ENSP00000428878; -.
DR iPTMnet; Q8TF20; -.
DR PhosphoSitePlus; Q8TF20; -.
DR BioMuta; ZNF721; -.
DR DMDM; 158706490; -.
DR EPD; Q8TF20; -.
DR jPOST; Q8TF20; -.
DR MassIVE; Q8TF20; -.
DR PaxDb; Q8TF20; -.
DR PeptideAtlas; Q8TF20; -.
DR PRIDE; Q8TF20; -.
DR ProteomicsDB; 74540; -. [Q8TF20-1]
DR ProteomicsDB; 74541; -. [Q8TF20-2]
DR Antibodypedia; 77821; 4 antibodies from 4 providers.
DR DNASU; 170960; -.
DR Ensembl; ENST00000338977.5; ENSP00000340524.5; ENSG00000182903.16. [Q8TF20-1]
DR Ensembl; ENST00000511833.3; ENSP00000428878.1; ENSG00000182903.16. [Q8TF20-2]
DR GeneID; 170960; -.
DR KEGG; hsa:170960; -.
DR MANE-Select; ENST00000511833.3; ENSP00000428878.1; NM_133474.4; NP_597731.2. [Q8TF20-2]
DR UCSC; uc003gag.5; human. [Q8TF20-1]
DR CTD; 170960; -.
DR GeneCards; ZNF721; -.
DR HGNC; HGNC:29425; ZNF721.
DR HPA; ENSG00000182903; Low tissue specificity.
DR neXtProt; NX_Q8TF20; -.
DR OpenTargets; ENSG00000182903; -.
DR VEuPathDB; HostDB:ENSG00000182903; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT01050000244829; -.
DR HOGENOM; CLU_002678_17_4_1; -.
DR InParanoid; Q8TF20; -.
DR OMA; KCEDHGR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8TF20; -.
DR TreeFam; TF343410; -.
DR PathwayCommons; Q8TF20; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q8TF20; -.
DR BioGRID-ORCS; 170960; 41 hits in 1076 CRISPR screens.
DR ChiTaRS; ZNF721; human.
DR GenomeRNAi; 170960; -.
DR Pharos; Q8TF20; Tdark.
DR PRO; PR:Q8TF20; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TF20; protein.
DR Bgee; ENSG00000182903; Expressed in oocyte and 181 other tissues.
DR ExpressionAtlas; Q8TF20; baseline and differential.
DR Genevisible; Q8TF20; 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 InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 19.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 25.
DR SUPFAM; SSF57667; SSF57667; 15.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 23.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 28.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..911
FT /note="Zinc finger protein 721"
FT /id="PRO_0000306879"
FT ZN_FING 69..91
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 97..119
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 125..147
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 153..175
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 181..203
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 209..231
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 237..259
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 265..287
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 293..315
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..343
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 349..371
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..427
FT /note="C2H2-type 13; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..455
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 489..511
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..539
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 545..567
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 573..595
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 601..623
FT /note="C2H2-type 20; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 629..651
FT /note="C2H2-type 21; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 657..679
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 685..707
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 713..735
FT /note="C2H2-type 24; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 741..763
FT /note="C2H2-type 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 769..791
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 797..819
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 825..847
FT /note="C2H2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 853..875
FT /note="C2H2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 881..903
FT /note="C2H2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 786
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MLENYRNLVSLAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040879"
FT CONFLICT 210
FT /note="K -> T (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..249
FT /note="SSS -> LIL (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="N -> I (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="G -> E (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="A -> D (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..388
FT /note="NS -> VC (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="N -> D (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="H -> M (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="R -> C (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="L -> M (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="H -> HS (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="Q -> E (in Ref. 1; CAH10687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 911 AA; 105084 MW; AA0D3FBAC9C789AA CRC64;
MCSHFTQDFL PVQGIEDSFH KLILRRYEKC GHDNLQLRKG CKSMNVCKVQ KGVYNGINKC
LSNTQSKIFQ CNARVKVFSK FANSNKDKTR HTGEKHFKCN ECGKSFQKFS DLTQHKGIHA
GEKPYTCEER GKDFGWYTDL NQHKKIHTGE KPYKCEECGK AFNRSTNLTA HKRIHNREKA
YTGEDRDRAF GWSTNLNEYK KIHTGDKPYK CKECGKAFMH SSHLNKHEKI HTGEKPYKCK
ECGKVISSSS SFAKHKRIHT GEKPFKCLEC GKAFNISTTL TKHRRIHTGE KPYTCEVCGK
AFRQSANLYV HRRIHTGEKP YTCGECGKTF RQSANLYVHR RIHTGEKPYK CEDCGKAFGR
YTALNQHKKI HTGEKPYKCE ECGKAFNSST NLTAHKRIHT REKPYTCEDR GRAFGLSTNL
NEYKKIHTGD KPYKCKECGK AFIHSLHLNK HEKIHTGKKP YKCKQCGKVI TSSSSFAKHK
RIHTGEKPFE CLECGKAFTS STTLTKHRRI HTGEKPYTCE VCGKAFRQSA ILYVHRRIHT
GEKPYTCEEC GKTFRQSANL YVHRRIHTGE KPYKCEECGK AFGRYTDLNQ HKKIHTGEKL
YKCEECGKDF VWYTDLNQQK KIYTGEKPYK CEECGKAFAP STDLNQHTKI LTGEQSYKCE
ECGKAFGWSI ALNQHKKIHT GEKPYKCEEC GKAFSRSRNL TTHRRVHTRE KPYKCEDRGR
SFGWSTNLNE YKKIHTGDKL YKCKECGKVF KQSSHLNRHE KIHTGKKPYK CKECGKVITS
SSSFAKHKRI HTGEKPFKCL ECGKAFTSST TLTKHRRIHT GEKPYTCEEC GKAFRQSAIL
YVHRRIHTGE KPYTCGECGK TFRQSANLYA HKKIHTGEKP YTCGDCGKTF RQSANLYAHK
KIHTGDKTIQ V
