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ZNF2_HUMAN
ID   ZNF2_HUMAN              Reviewed;         425 AA.
AC   Q9BSG1; A8MWV7; B0AZN8; B4DIR4; Q4ZFY6; Q96G44; Q9UMC5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 5.
DT   03-AUG-2022, entry version 172.
DE   RecName: Full=Zinc finger protein 2 {ECO:0000305};
DE   AltName: Full=Zinc finger protein 2.2;
DE   AltName: Full=Zinc finger protein 661;
GN   Name=ZNF2 {ECO:0000312|HGNC:HGNC:12991}; Synonyms=ZNF661;
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] (ISOFORMS 3 AND 4).
RC   TISSUE=Hippocampus;
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=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 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye, and Muscle;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-392 (ISOFORM 2).
RX   PubMed=1945843; DOI=10.1093/nar/19.20.5661;
RA   Rosati M., Marino M., Franze A., Tramontano A., Grimaldi G.;
RT   "Members of the zinc finger protein gene family sharing a conserved N-
RT   terminal module.";
RL   Nucleic Acids Res. 19:5661-5667(1991).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       Q9BSG1; Q92997: DVL3; NbExp=3; IntAct=EBI-8489229, EBI-739789;
CC       Q9BSG1; P42858: HTT; NbExp=3; IntAct=EBI-8489229, EBI-466029;
CC       Q9BSG1; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-8489229, EBI-12023934;
CC       Q9BSG1; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-8489229, EBI-725997;
CC       Q9BSG1-2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10297542, EBI-10172290;
CC       Q9BSG1-2; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-10297542, EBI-744794;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2;
CC         IsoId=Q9BSG1-2; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q9BSG1-3; Sequence=VSP_060238;
CC       Name=4;
CC         IsoId=Q9BSG1-4; Sequence=VSP_060237;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX88982.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK295739; BAG58576.1; -; mRNA.
DR   EMBL; AK315829; BAF98720.1; -; mRNA.
DR   EMBL; AC092835; AAX88982.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; KF459620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471219; EAX10715.1; -; Genomic_DNA.
DR   EMBL; BC005068; AAH05068.2; -; mRNA.
DR   EMBL; BC009976; AAH09976.2; -; mRNA.
DR   EMBL; X60152; CAB52138.1; -; mRNA.
DR   CCDS; CCDS42712.1; -. [Q9BSG1-2]
DR   CCDS; CCDS42713.1; -. [Q9BSG1-3]
DR   CCDS; CCDS62957.1; -. [Q9BSG1-4]
DR   RefSeq; NP_001017396.1; NM_001017396.2. [Q9BSG1-3]
DR   RefSeq; NP_001269327.1; NM_001282398.1. [Q9BSG1-4]
DR   RefSeq; NP_066574.2; NM_021088.3. [Q9BSG1-2]
DR   AlphaFoldDB; Q9BSG1; -.
DR   SMR; Q9BSG1; -.
DR   BioGRID; 113381; 78.
DR   IntAct; Q9BSG1; 73.
DR   MINT; Q9BSG1; -.
DR   STRING; 9606.ENSP00000480297; -.
DR   iPTMnet; Q9BSG1; -.
DR   PhosphoSitePlus; Q9BSG1; -.
DR   BioMuta; ZNF2; -.
DR   DMDM; 527504091; -.
DR   EPD; Q9BSG1; -.
DR   jPOST; Q9BSG1; -.
DR   MassIVE; Q9BSG1; -.
DR   MaxQB; Q9BSG1; -.
DR   PaxDb; Q9BSG1; -.
DR   PeptideAtlas; Q9BSG1; -.
DR   PRIDE; Q9BSG1; -.
DR   ProteomicsDB; 2270; -.
DR   ProteomicsDB; 4323; -.
DR   Antibodypedia; 72445; 153 antibodies from 23 providers.
DR   DNASU; 7549; -.
DR   Ensembl; ENST00000614034.5; ENSP00000480297.1; ENSG00000275111.5. [Q9BSG1-2]
DR   Ensembl; ENST00000617923.4; ENSP00000480057.1; ENSG00000275111.5. [Q9BSG1-3]
DR   Ensembl; ENST00000622059.4; ENSP00000483131.1; ENSG00000275111.5. [Q9BSG1-4]
DR   GeneID; 7549; -.
DR   KEGG; hsa:7549; -.
DR   MANE-Select; ENST00000614034.5; ENSP00000480297.1; NM_021088.4; NP_066574.2.
DR   UCSC; uc032nuy.2; human. [Q9BSG1-2]
DR   UCSC; uc032nva.2; human.
DR   CTD; 7549; -.
DR   DisGeNET; 7549; -.
DR   GeneCards; ZNF2; -.
DR   HGNC; HGNC:12991; ZNF2.
DR   HPA; ENSG00000275111; Low tissue specificity.
DR   MIM; 194500; gene.
DR   neXtProt; NX_Q9BSG1; -.
DR   OpenTargets; ENSG00000275111; -.
DR   PharmGKB; PA37571; -.
DR   VEuPathDB; HostDB:ENSG00000275111; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160826; -.
DR   HOGENOM; CLU_002678_44_0_1; -.
DR   InParanoid; Q9BSG1; -.
DR   OMA; TKPEIHG; -.
DR   TreeFam; TF340946; -.
DR   PathwayCommons; Q9BSG1; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q9BSG1; -.
DR   BioGRID-ORCS; 7549; 11 hits in 1097 CRISPR screens.
DR   GenomeRNAi; 7549; -.
DR   Pharos; Q9BSG1; Tbio.
DR   PRO; PR:Q9BSG1; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9BSG1; protein.
DR   Bgee; ENSG00000275111; Expressed in secondary oocyte and 124 other tissues.
DR   ExpressionAtlas; Q9BSG1; baseline and differential.
DR   Genevisible; Q9BSG1; 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
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; 5.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..425
FT                   /note="Zinc finger protein 2"
FT                   /id="PRO_0000274049"
FT   DOMAIN          14..85
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         173..195
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         201..223
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         229..251
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         257..279
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         285..307
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         313..335
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         341..363
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         369..391
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         397..419
FT                   /note="C2H2-type 9; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          86..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..42
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_060238"
FT   VAR_SEQ         54..91
FT                   /note="Missing (in isoform 4)"
FT                   /id="VSP_060237"
FT   CONFLICT        1..11
FT                   /note="MAAVSPTTRCQ -> RGAVFPGPEHSVPE (in Ref. 5; CAB52138)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="R -> RR (in Ref. 1; BAG58576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        369
FT                   /note="Y -> H (in Ref. 4; AAH05068)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   425 AA;  48707 MW;  8CB40D3EDB62147E CRC64;
     MAAVSPTTRC QESVTFEDVA VVFTDEEWSR LVPIQRDLYK EVMLENYNSI VSLGLPVPQP
     DVIFQLKRGD KPWMVDLHGS EEREWPESVS LDWETKPEIH DASDKKSEGS LRECLGRQSP
     LCPKFEVHTP NGRMGTEKQS PSGETRKKSL SRDKGLRRRS ALSREILTKE RHQECSDCGK
     TFFDHSSLTR HQRTHTGEKP YDCRECGKAF SHRSSLSRHL MSHTGESPYE CSVCSKAFFD
     RSSLTVHQRI HTGEKPFQCN ECGKAFFDRS SLTRHQRIHT GESPYECHQC GKAFSQKSIL
     TRHQLIHTGR KPYECNECGK AFYGVSSLNR HQKAHAGDPR YQCNECGKAF FDRSSLTQHQ
     KIHTGDKPYE CSECGKAFSQ RCRLTRHQRV HTGEKPFECT VCGKVFSSKS SVIQHQRRYA
     KQGID
 
 
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