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DescriptionRecName: Full=Zinc finger protein 276; Short=Zfp-276;
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MyHits synonymsZN276_MOUSE , Q8CE64 , Q3TQL7 , Q3V088 , Q80ZN3 , Q8C912 , Q9ESV2 , 1F5716CFADE16533
match map segment
iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 ismart:ZnF_C2H2 iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 iprf:ZINC_FINGER_C2H2_2 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ipfam:zf-AD  
Legends: 1, CONFLICT K -> R (in Ref. 1; BAC26204). {ECO:0000305}; 2, CONFLICT A -> G (in Ref. 2; AAG01634). {ECO:0000305}; 3, CONFLICT L -> W (in Ref. 2; AAG01634). {ECO:0000305}; 4, ZN_FING C2H2-type 1. {ECO:0000255|PROSITE- ProRule:PRU00042}; 5, ZN_FING C2H2-type 2. {ECO:0000255|PROSITE- ProRule:PRU00042}; 6, ZN_FING C2H2-type 3. {ECO:0000255|PROSITE- ProRule:PRU00042}; 7, ZN_FING C2H2-type 4. {ECO:0000255|PROSITE- ProRule:PRU00042}; 8, ZN_FING C2H2-type 5. {ECO:0000255|PROSITE- ProRule:PRU00042}; 9, VAR_SEQ QLGETQVPSSTSDD -> KQHLWLMLEQDSVF (in isoform 2). {ECO:0000303|PubMed:16141072}; 10, VAR_SEQ Missing (in isoform 2). {ECO:0000303|PubMed:16141072}; 11, CONFLICT KH -> ND (in Ref. 2; AAG01634). {ECO:0000305}; 12, iprf:ZINC_FINGER_C2H2_2 [T]; 13, ismart:ZnF_C2H2 [T]; 14, ipat:ZINC_FINGER_C2H2_1 [T]; 15, ipfam:zf-AD [T].
ID   ZN276_MOUSE             Reviewed;         614 AA.
AC   Q8CE64; Q3TQL7; Q3V088; Q80ZN3; Q8C912; Q9ESV2;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 3.
DT   30-NOV-2016, entry version 115.
DE   RecName: Full=Zinc finger protein 276;
DE            Short=Zfp-276;
GN   Name=Znf276; Synonyms=Zfp276;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 149-614 (ISOFORM 1), TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J;
RX   PubMed=10936049; DOI=10.1006/geno.2000.6252;
RA   Wong J.C., Alon N., Norga K., Kruyt F.A.E., Youssoufian H.,
RA   Buchwald M.;
RT   "Cloning and analysis of the mouse Fanconi anemia group A cDNA and an
RT   overlapping penta zinc finger cDNA.";
RL   Genomics 67:273-283(2000).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome,
CC       centromere, kinetochore {ECO:0000250|UniProtKB:Q8N554}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CE64-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CE64-2; Sequence=VSP_026106, VSP_026107;
CC   -!- TISSUE SPECIFICITY: Found in all the examined tissues, with
CC       highest levels in kidney, liver, lung, and spleen.
CC       {ECO:0000269|PubMed:10936049}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at low levels in all stages of
CC       embryonic development examined. {ECO:0000269|PubMed:10936049}.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 1 ZAD (zinc-finger associated) domain.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG01634.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAC31505.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AK028939; BAC26204.1; -; mRNA.
DR   EMBL; AK043258; BAC31505.1; ALT_INIT; mRNA.
DR   EMBL; AK133363; BAE21616.1; -; mRNA.
DR   EMBL; AK163486; BAE37365.1; -; mRNA.
DR   EMBL; AF178935; AAG01634.1; ALT_INIT; mRNA.
DR   CCDS; CCDS52699.1; -. [Q8CE64-1]
DR   RefSeq; NP_065243.2; NM_020497.2. [Q8CE64-1]
DR   UniGene; Mm.379084; -.
DR   ProteinModelPortal; Q8CE64; -.
DR   SMR; Q8CE64; -.
DR   BioGrid; 208217; 1.
DR   STRING; 10090.ENSMUSP00000001092; -.
DR   iPTMnet; Q8CE64; -.
DR   PhosphoSitePlus; Q8CE64; -.
DR   PaxDb; Q8CE64; -.
DR   PeptideAtlas; Q8CE64; -.
DR   PRIDE; Q8CE64; -.
DR   Ensembl; ENSMUST00000001092; ENSMUSP00000001092; ENSMUSG00000001065. [Q8CE64-1]
DR   GeneID; 57247; -.
DR   KEGG; mmu:57247; -.
DR   UCSC; uc009nva.2; mouse. [Q8CE64-2]
DR   UCSC; uc009nvb.2; mouse. [Q8CE64-1]
DR   CTD; 57247; -.
DR   MGI; MGI:1888495; Zfp276.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00530000063153; -.
DR   HOGENOM; HOG000155790; -.
DR   HOVERGEN; HBG061026; -.
DR   InParanoid; Q8CE64; -.
DR   OMA; GCDQGHD; -.
DR   OrthoDB; EOG091G04WK; -.
DR   PhylomeDB; Q8CE64; -.
DR   TreeFam; TF332664; -.
DR   PRO; PR:Q8CE64; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000001065; -.
DR   CleanEx; MM_ZFP276; -.
DR   ExpressionAtlas; Q8CE64; baseline and differential.
DR   Genevisible; Q8CE64; MM.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 5.
DR   InterPro; IPR012934; Znf_AD.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF07776; zf-AD; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Centromere; Chromosome; Complete proteome;
KW   DNA-binding; Kinetochore; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    614       Zinc finger protein 276.
FT                                /FTId=PRO_0000047324.
FT   DOMAIN       79    153       ZAD.
FT   ZN_FING     434    458       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     465    490       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     496    518       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     524    546       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     554    577       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   VAR_SEQ     337    350       QLGETQVPSSTSDD -> KQHLWLMLEQDSVF (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_026106.
FT   VAR_SEQ     351    614       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_026107.
FT   CONFLICT    353    353       K -> R (in Ref. 1; BAC26204).
FT                                {ECO:0000305}.
FT   CONFLICT    509    510       KH -> ND (in Ref. 2; AAG01634).
FT                                {ECO:0000305}.
FT   CONFLICT    521    521       A -> G (in Ref. 2; AAG01634).
FT                                {ECO:0000305}.
FT   CONFLICT    579    579       L -> W (in Ref. 2; AAG01634).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       554    582       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       524    546       ismart:ZnF_C2H2 [T]
FT   MYHIT       496    518       ismart:ZnF_C2H2 [T]
FT   MYHIT       524    551       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       496    523       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       498    518       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       434    458       ismart:ZnF_C2H2 [T]
FT   MYHIT       556    577       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       465    495       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       436    459       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       554    577       ismart:ZnF_C2H2 [T]
FT   MYHIT       465    490       ismart:ZnF_C2H2 [T]
FT   MYHIT        79    156       ipfam:zf-AD [T]
SQ   SEQUENCE   614 AA;  67339 MW;  1F5716CFADE16533 CRC64;
     MKRDRLGRFL SPGIARQRGG SGGGCGSGRT RGRPSRSGGT SADGAAAQLS WGSMTRSCGD
     TGDDGTDEAG AGRTLAMGHC RLCHGKFSSR SLRSISDRVP GETSERLSPG ERVFIRDFQR
     LLGVAVHQDP ALPQSVCKNC YTQFYQCHSL LRTFLQRVNV SPAGQRKPCT KVGVQPTTVA
     EEGACVADLI ASSPRCLHGL VGWVHEHAVS CGSLPSLQRT LSSEYCGIIQ AVWGCDQGHD
     FTMDTASSCR ALFLDSALAV KWAWGKDLSP RLAQNSESNP TGAASRLCQA RETQVGSETK
     TLPSVDVALL HSHGDSVGPG LGPCTQPHLA PSEAPGQLGE TQVPSSTSDD RVKDEFSDLS
     EGDFLSEDES DKKQTPQSSD ESFEPYPEKK VSGKKSEGRE AKRPEEPKIR KKPGPKPGWK
     KKLRCEREEL PTIYKCPYQG CTAVYRGADG MKKHIKEHHE EVRERPCPHP GCNKVFMIDR
     YLQRHVKLIH TEVRNYICDE CGQTFKQRKH LLVHQMRHSG AKPLQCEVCG FQCRQRASLK
     YHMTKHKAET ELDFACDQCG RRFEKAHNLN VHMSMVHPLT QAQDRALPLE AEPPPGPLSP
     SGTMEGQAVK PEPT
//