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ZN267_HUMAN
ID   ZN267_HUMAN             Reviewed;         743 AA.
AC   Q14586; A0JNZ9; Q8NE41; Q9NRJ0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   03-AUG-2022, entry version 212.
DE   RecName: Full=Zinc finger protein 267;
DE   AltName: Full=Zinc finger protein HZF2;
GN   Name=ZNF267;
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], AND VARIANT TYR-350.
RA   Schaefer U., Schneider A., Neugebauer E.;
RT   "Identification of a nitric oxide regulated krueppel-like zinc finger
RT   protein using motif directed differential display.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-350.
RC   TISSUE=Testis;
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 MRNA], AND VARIANT TYR-350.
RC   TISSUE=Testis;
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 [MRNA] OF 12-743, AND VARIANT TYR-350.
RX   PubMed=7865130; DOI=10.1089/dna.1995.14.125;
RA   Abrink M., Aveskogh M., Hellman L.;
RT   "Isolation of cDNA clones for 42 different Kruppel-related zinc finger
RT   proteins expressed in the human monoblast cell line U-937.";
RL   DNA Cell Biol. 14:125-136(1995).
RN   [5]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-135, 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}.
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DR   EMBL; AF220492; AAF73867.1; -; mRNA.
DR   EMBL; AK292573; BAF85262.1; -; mRNA.
DR   EMBL; BC036367; AAH36367.1; -; mRNA.
DR   EMBL; BC127088; AAI27089.1; -; mRNA.
DR   EMBL; BC127089; AAI27090.1; -; mRNA.
DR   EMBL; X78925; CAA55525.1; -; mRNA.
DR   CCDS; CCDS32440.1; -.
DR   PIR; S47073; S47073.
DR   RefSeq; NP_001252517.1; NM_001265588.1.
DR   RefSeq; NP_003405.3; NM_003414.5.
DR   AlphaFoldDB; Q14586; -.
DR   SMR; Q14586; -.
DR   BioGRID; 115594; 11.
DR   IntAct; Q14586; 9.
DR   STRING; 9606.ENSP00000300870; -.
DR   iPTMnet; Q14586; -.
DR   PhosphoSitePlus; Q14586; -.
DR   BioMuta; ZNF267; -.
DR   DMDM; 296453069; -.
DR   EPD; Q14586; -.
DR   jPOST; Q14586; -.
DR   MassIVE; Q14586; -.
DR   MaxQB; Q14586; -.
DR   PaxDb; Q14586; -.
DR   PeptideAtlas; Q14586; -.
DR   PRIDE; Q14586; -.
DR   ProteomicsDB; 60059; -.
DR   Antibodypedia; 833; 27 antibodies from 12 providers.
DR   DNASU; 10308; -.
DR   Ensembl; ENST00000300870.15; ENSP00000300870.10; ENSG00000185947.15.
DR   GeneID; 10308; -.
DR   KEGG; hsa:10308; -.
DR   MANE-Select; ENST00000300870.15; ENSP00000300870.10; NM_003414.6; NP_003405.4.
DR   UCSC; uc002ecs.6; human.
DR   CTD; 10308; -.
DR   DisGeNET; 10308; -.
DR   GeneCards; ZNF267; -.
DR   HGNC; HGNC:13060; ZNF267.
DR   HPA; ENSG00000185947; Low tissue specificity.
DR   MIM; 604752; gene.
DR   neXtProt; NX_Q14586; -.
DR   OpenTargets; ENSG00000185947; -.
DR   PharmGKB; PA37638; -.
DR   VEuPathDB; HostDB:ENSG00000185947; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000164593; -.
DR   HOGENOM; CLU_002678_0_12_1; -.
DR   InParanoid; Q14586; -.
DR   OMA; RHGNCDL; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q14586; -.
DR   TreeFam; TF341817; -.
DR   PathwayCommons; Q14586; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q14586; -.
DR   SIGNOR; Q14586; -.
DR   BioGRID-ORCS; 10308; 25 hits in 1096 CRISPR screens.
DR   GeneWiki; ZNF267; -.
DR   GenomeRNAi; 10308; -.
DR   Pharos; Q14586; Tdark.
DR   PRO; PR:Q14586; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q14586; protein.
DR   Bgee; ENSG00000185947; Expressed in oocyte and 194 other tissues.
DR   ExpressionAtlas; Q14586; baseline and differential.
DR   Genevisible; Q14586; 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   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; 15.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 10.
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   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..743
FT                   /note="Zinc finger protein 267"
FT                   /id="PRO_0000047494"
FT   DOMAIN          4..75
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         267..289
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         322..340
FT                   /note="C2H2-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         380..402
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         408..430
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         436..458
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         464..486
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         492..514
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         520..542
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         548..570
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         576..598
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         604..626
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         632..654
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         660..682
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         688..710
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         716..738
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        66
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        135
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         257
FT                   /note="M -> V (in dbSNP:rs7202455)"
FT                   /id="VAR_057414"
FT   VARIANT         350
FT                   /note="C -> Y (in dbSNP:rs3850114)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7865130,
FT                   ECO:0000269|Ref.1"
FT                   /id="VAR_059907"
FT   CONFLICT        31
FT                   /note="D -> N (in Ref. 3; AAH36367)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        567
FT                   /note="H -> Y (in Ref. 1; AAF73867 and 4; CAA55525)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        592
FT                   /note="T -> S (in Ref. 1; AAF73867 and 4; CAA55525)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   743 AA;  87376 MW;  66AA4EC827BEFAAF CRC64;
     MGLLTFRDVA VEFSLEEWEH LEPAQKNLYQ DVMLENYRNL VSLGLVVSKP DLITFLEQRK
     EPWNVKSEET VAIQPDVFSH YNKDLLTEHC TEASFQKVIS RRHGSCDLEN LHLRKRWKRE
     ECEGHNGCYD EKTFKYDQFD ESSVESLFHQ QILSSCAKSY NFDQYRKVFT HSSLLNQQEE
     IDIWGKHHIY DKTSVLFRQV STLNSYRNVF IGEKNYHCNN SEKTLNQSSS PKNHQENYFL
     EKQYKCKEFE EVFLQSMHGQ EKQEQSYKCN KCVEVCTQSL KHIQHQTIHI RENSYSYNKY
     DKDLSQSSNL RKQIIHNEEK PYKCEKCGDS LNHSLHLTQH QIIPTEEKPC KWKECGKVFN
     LNCSLYLTKQ QQIDTGENLY KCKACSKSFT RSSNLIVHQR IHTGEKPYKC KECGKAFRCS
     SYLTKHKRIH TGEKPYKCKE CGKAFNRSSC LTQHQTTHTG EKLYKCKVCS KSYARSSNLI
     MHQRVHTGEK PYKCKECGKV FSRSSCLTQH RKIHTGENLY KCKVCAKPFT CFSNLIVHER
     IHTGEKPYKC KECGKAFPYS SHLIRHHRIH TGEKPYKCKA CSKSFSDSSG LTVHRRTHTG
     EKPYTCKECG KAFSYSSDVI QHRRIHTGQR PYKCEECGKA FNYRSYLTTH QRSHTGERPY
     KCEECGKAFN SRSYLTTHRR RHTGERPYKC DECGKAFSYR SYLTTHRRSH SGERPYKCEE
     CGKAFNSRSY LIAHQRSHTR EKL
 
 
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