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ZN667_MOUSE
ID   ZN667_MOUSE             Reviewed;         609 AA.
AC   Q2TL60; B2RUH6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Zinc finger protein 667;
DE   AltName: Full=Myocardial ischemic preconditioning up-regulated protein 1;
GN   Name=Znf667; Synonyms=Mip1, Zfp667;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yuan C., Zhang H., Liu Y., Wang Q., Xiao X.;
RT   "Cloning and characteration of a new gene Mip1 up-regulated during
RT   myocardial ischemia-reperfusion.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 31:231-236(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
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; AY850275; AAX45071.1; -; mRNA.
DR   EMBL; BC141152; AAI41153.1; -; mRNA.
DR   EMBL; BC141153; AAI41154.1; -; mRNA.
DR   CCDS; CCDS20773.1; -.
DR   RefSeq; NP_001020099.1; NM_001024928.2.
DR   RefSeq; XP_006540216.1; XM_006540153.3.
DR   RefSeq; XP_006540217.1; XM_006540154.2.
DR   RefSeq; XP_006540218.1; XM_006540155.1.
DR   RefSeq; XP_006540219.1; XM_006540156.3.
DR   AlphaFoldDB; Q2TL60; -.
DR   SMR; Q2TL60; -.
DR   BioGRID; 239298; 51.
DR   STRING; 10090.ENSMUSP00000083507; -.
DR   iPTMnet; Q2TL60; -.
DR   PhosphoSitePlus; Q2TL60; -.
DR   PaxDb; Q2TL60; -.
DR   PeptideAtlas; Q2TL60; -.
DR   PRIDE; Q2TL60; -.
DR   ProteomicsDB; 275091; -.
DR   Antibodypedia; 33211; 106 antibodies from 20 providers.
DR   DNASU; 384763; -.
DR   Ensembl; ENSMUST00000086327; ENSMUSP00000083507; ENSMUSG00000054893.
DR   Ensembl; ENSMUST00000108562; ENSMUSP00000104202; ENSMUSG00000054893.
DR   Ensembl; ENSMUST00000170776; ENSMUSP00000128658; ENSMUSG00000054893.
DR   GeneID; 384763; -.
DR   KEGG; mmu:384763; -.
DR   UCSC; uc009fbb.1; mouse.
DR   CTD; 384763; -.
DR   MGI; MGI:2442757; Zfp667.
DR   VEuPathDB; HostDB:ENSMUSG00000054893; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00390000021477; -.
DR   HOGENOM; CLU_002678_57_1_1; -.
DR   InParanoid; Q2TL60; -.
DR   OMA; HQNSHSE; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q2TL60; -.
DR   TreeFam; TF341817; -.
DR   Reactome; R-MMU-212436; Generic Transcription Pathway.
DR   BioGRID-ORCS; 384763; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Zfp667; mouse.
DR   PRO; PR:Q2TL60; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q2TL60; protein.
DR   Bgee; ENSMUSG00000054893; Expressed in otolith organ and 215 other tissues.
DR   ExpressionAtlas; Q2TL60; baseline and differential.
DR   Genevisible; Q2TL60; MM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; 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; 14.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 9.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..609
FT                   /note="Zinc finger protein 667"
FT                   /id="PRO_0000251898"
FT   DOMAIN          14..85
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         144..166
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         172..194
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         200..222
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         253..275
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         329..351
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         357..379
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         385..407
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         414..436
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         442..464
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         470..492
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         498..520
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         526..548
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         554..576
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         582..604
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          81..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  70263 MW;  9F9559840C769097 CRC64;
     MPAVRGKSKS KAPVTFGDLA IYFSQEEWEW LSPMQKDLYE DVMLENYHNL VSVGLACRRP
     NIIALLEKGK APWVIEPSRR RWGPESGSKY ETKKLPPNSC HKSGPSICEK PTSSQQKVPT
     EKAKHNKSSV PSKSKKEHSG KKSLKCNLCG KTFFRSLSLK LHQDFHTGER SYECSTCRHV
     FRQILSLILH QRVHNWNKSY ECDKCGDIFN KKLTLMIHRR IHNGKESFHH EKASDSCPSL
     SLHRNNHTTD SVHQCRKCGK VFSRMSSLLL HKRSHNRKKI QKYNKYKRGF KKQPVLVHKR
     VCIGKKTHES KKALIQSARQ KTCQSENPFM CGKCGKSFSR ISALMLHQRI HTSGNPYKCD
     KCQKDFGRLS TLILHLRIHS GEKQFKCSKC EKVCSRLSSF IQHQKIHKRK KKLIACKECG
     KMFGGMKNLK VHLNIHSEEK PFKCNKCSKV FGRQSFLSEH QRIHTGEKPY QCEECGKAFS
     HRISLTRHKR IHSEDRPYEC DLCGKAFSQS AHLAQHERIH TGEKPYACKI CKKSFAQRIS
     LILHERSHTG ERPYECNECG KAFSSGSDLI RHQRSHSSEK PYECSKCGKA YSRSSSLIRH
     QSIHSEETP
 
 
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