ZNF7_HUMAN
ID ZNF7_HUMAN Reviewed; 686 AA.
AC P17097; B4DT08; D3DWN6; P17015; Q8N8Y4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Zinc finger protein 7;
DE AltName: Full=Zinc finger protein HF.16;
DE AltName: Full=Zinc finger protein KOX4;
GN Name=ZNF7; Synonyms=KOX4;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=2106481; DOI=10.1016/0888-7543(90)90574-e;
RA Lania L., Donti E., Pannuti A., Pascucci A., Pengue G., Feliciello I.,
RA la Mantia G., Lanfrancone L., Pelicci P.-G.;
RT "cDNA isolation, expression analysis, and chromosomal localization of two
RT human zinc finger genes.";
RL Genomics 6:333-340(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-188.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 413-468.
RC TISSUE=Lymphoid tissue;
RX PubMed=2288909;
RA Thiesen H.-J.;
RT "Multiple genes encoding zinc finger domains are expressed in human T
RT cells.";
RL New Biol. 2:363-374(1990).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY MASS
RP 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-101; LYS-279; LYS-292 AND
RP LYS-393, AND 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P17097-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17097-2; Sequence=VSP_054822;
CC Name=3;
CC IsoId=P17097-3; Sequence=VSP_054823, VSP_054824;
CC -!- TISSUE SPECIFICITY: Ubiquitously present in many human cell lines of
CC different embryological derivation.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; M29580; AAA61313.1; -; mRNA.
DR EMBL; AK096025; BAC04677.1; -; mRNA.
DR EMBL; AK300001; BAG61820.1; -; mRNA.
DR EMBL; AF235103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471162; EAW82039.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82040.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82041.1; -; Genomic_DNA.
DR EMBL; BC058923; AAH58923.1; -; mRNA.
DR EMBL; X52335; CAA36561.1; -; mRNA.
DR CCDS; CCDS6435.1; -. [P17097-1]
DR CCDS; CCDS64996.1; -. [P17097-2]
DR CCDS; CCDS64998.1; -. [P17097-3]
DR PIR; A34612; A34612.
DR RefSeq; NP_001269724.1; NM_001282795.1. [P17097-2]
DR RefSeq; NP_001269725.1; NM_001282796.1. [P17097-3]
DR RefSeq; NP_001269726.1; NM_001282797.1.
DR RefSeq; NP_001317552.1; NM_001330623.1.
DR RefSeq; NP_003407.1; NM_003416.3. [P17097-1]
DR RefSeq; XP_011515594.1; XM_011517292.2. [P17097-2]
DR RefSeq; XP_011515595.1; XM_011517293.2. [P17097-1]
DR RefSeq; XP_011515596.1; XM_011517294.2. [P17097-1]
DR AlphaFoldDB; P17097; -.
DR SMR; P17097; -.
DR BioGRID; 113385; 23.
DR IntAct; P17097; 8.
DR STRING; 9606.ENSP00000393260; -.
DR iPTMnet; P17097; -.
DR PhosphoSitePlus; P17097; -.
DR BioMuta; ZNF7; -.
DR DMDM; 141685; -.
DR EPD; P17097; -.
DR jPOST; P17097; -.
DR MassIVE; P17097; -.
DR MaxQB; P17097; -.
DR PaxDb; P17097; -.
DR PeptideAtlas; P17097; -.
DR PRIDE; P17097; -.
DR ProteomicsDB; 5062; -.
DR ProteomicsDB; 53456; -. [P17097-1]
DR ProteomicsDB; 72474; -.
DR Antibodypedia; 15006; 155 antibodies from 26 providers.
DR DNASU; 7553; -.
DR Ensembl; ENST00000446747.7; ENSP00000393260.2; ENSG00000147789.16. [P17097-2]
DR Ensembl; ENST00000525266.5; ENSP00000435252.1; ENSG00000147789.16. [P17097-3]
DR Ensembl; ENST00000528372.5; ENSP00000432724.1; ENSG00000147789.16. [P17097-1]
DR Ensembl; ENST00000532777.6; ENSP00000432641.2; ENSG00000147789.16. [P17097-1]
DR GeneID; 7553; -.
DR KEGG; hsa:7553; -.
DR MANE-Select; ENST00000532777.6; ENSP00000432641.2; NM_003416.4; NP_003407.1.
DR UCSC; uc003zeh.4; human. [P17097-1]
DR CTD; 7553; -.
DR DisGeNET; 7553; -.
DR GeneCards; ZNF7; -.
DR HGNC; HGNC:13139; ZNF7.
DR HPA; ENSG00000147789; Low tissue specificity.
DR MIM; 194531; gene.
DR neXtProt; NX_P17097; -.
DR OpenTargets; ENSG00000147789; -.
DR PharmGKB; PA37713; -.
DR VEuPathDB; HostDB:ENSG00000147789; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161563; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; P17097; -.
DR OMA; TRAQWYY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P17097; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; P17097; -.
DR SignaLink; P17097; -.
DR BioGRID-ORCS; 7553; 13 hits in 1106 CRISPR screens.
DR ChiTaRS; ZNF7; human.
DR GeneWiki; ZNF7; -.
DR GenomeRNAi; 7553; -.
DR Pharos; P17097; Tbio.
DR PRO; PR:P17097; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P17097; protein.
DR Bgee; ENSG00000147789; Expressed in right hemisphere of cerebellum and 190 other tissues.
DR ExpressionAtlas; P17097; baseline and differential.
DR Genevisible; P17097; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
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; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..686
FT /note="Zinc finger protein 7"
FT /id="PRO_0000047330"
FT DOMAIN 4..76
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 223..245
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 413..435
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 441..463
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..491
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..547
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..575
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..603
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 279
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 292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 393
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 -> MGFLGCWCVSFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054822"
FT VAR_SEQ 83..148
FT /note="DSTIRTENEQACEDMDILKSESYGTVVRISPQDFPQNPGFGDVSDSEVWLDS
FT HLGSPGLKVTGFTF -> GFLGRPTMGQEPRHPHAPPATPVPGLPKHCSQRLTLPPPGL
FT SSSPLGHFLVHDQDRRRGTSAIWMV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054823"
FT VAR_SEQ 149..686
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054824"
FT VARIANT 188
FT /note="G -> R (in dbSNP:rs1735169)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_024191"
FT VARIANT 347
FT /note="S -> L (in dbSNP:rs2228180)"
FT /id="VAR_052744"
FT VARIANT 596
FT /note="L -> F (in dbSNP:rs1735170)"
FT /id="VAR_052745"
SQ SEQUENCE 686 AA; 77887 MW; 0397ADDABEFD4FBF CRC64;
MEVVTFGDVA VHFSREEWQC LDPGQRALYR EVMLENHSSV AGLAGFLVFK PELISRLEQG
EEPWVLDLQG AEGTEAPRTS KTDSTIRTEN EQACEDMDIL KSESYGTVVR ISPQDFPQNP
GFGDVSDSEV WLDSHLGSPG LKVTGFTFQN NCLNEETVVP KTFTKDAPQG CKELGSSGLD
CQPLESQGES AEGMSQRCEE CGKGIRATSD IALHWEINTQ KISRCQECQK KLSDCLQGKH
TNNCHGEKPY ECAECGKVFR LCSQLNQHQR IHTGEKPFKC TECGKAFRLS SKLIQHQRIH
TGEKPYRCEE CGKAFGQSSS LIHHQRIHTG ERPYGCRECG KAFSQQSQLV RHQRTHTGER
PYPCKECGKA FSQSSTLAQH QRMHTGEKAQ ILKASDSPSL VAHQRIHAVE KPFKCDECGK
AFRWISRLSQ HQLIHTGEKP YKCNKCTKAF GCSSRLIRHQ RTHTGEKPFK CDECGKGFVQ
GSHLIQHQRI HTGEKPYVCN DCGKAFSQSS SLIYHQRIHK GEKPYECLQC GKAFSMSTQL
TIHQRVHTGE RPYKCNECGK AFSQNSTLFQ HQIIHAGVKP YECSECGKAF SRSSYLIEHQ
RIHTRAQWFY EYGNALEGST FVSRKKVNTI KKLHQCEDCE KIFRWRSHLI IHQRIHTGEK
PYKCNDCGKA FNRSSRLTQH QKIHMG
