Z280C_MOUSE
ID Z280C_MOUSE Reviewed; 742 AA.
AC Q6P3Y5; B1AU28; B1AU29; Q6ZPM2; Q8K145;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zinc finger protein 280C;
DE AltName: Full=Suppressor of hairy wing homolog 3;
GN Name=Znf280c; Synonyms=Kiaa1584, Suhw3, Zfp280c;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as a transcription factor.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P3Y5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P3Y5-2; Sequence=VSP_017620, VSP_017621;
CC Name=3;
CC IsoId=Q6P3Y5-3; Sequence=VSP_017619;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129399; BAC98209.1; ALT_INIT; mRNA.
DR EMBL; AK141491; BAE24700.1; -; mRNA.
DR EMBL; AL669901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028839; AAH28839.1; -; mRNA.
DR EMBL; BC051397; AAH51397.1; -; mRNA.
DR EMBL; BC063775; AAH63775.1; -; mRNA.
DR CCDS; CCDS30111.1; -. [Q6P3Y5-1]
DR CCDS; CCDS53064.1; -. [Q6P3Y5-3]
DR CCDS; CCDS53065.1; -. [Q6P3Y5-2]
DR RefSeq; NP_001160120.1; NM_001166648.1. [Q6P3Y5-1]
DR RefSeq; NP_001160121.1; NM_001166649.1. [Q6P3Y5-3]
DR RefSeq; NP_001160122.1; NM_001166650.1. [Q6P3Y5-2]
DR RefSeq; NP_705760.2; NM_153532.3. [Q6P3Y5-1]
DR RefSeq; XP_006541521.1; XM_006541458.3. [Q6P3Y5-1]
DR RefSeq; XP_006541522.1; XM_006541459.3. [Q6P3Y5-1]
DR RefSeq; XP_006541524.1; XM_006541461.3. [Q6P3Y5-1]
DR RefSeq; XP_006541528.1; XM_006541465.3. [Q6P3Y5-2]
DR AlphaFoldDB; Q6P3Y5; -.
DR BioGRID; 229030; 3.
DR STRING; 10090.ENSMUSP00000075933; -.
DR iPTMnet; Q6P3Y5; -.
DR PhosphoSitePlus; Q6P3Y5; -.
DR EPD; Q6P3Y5; -.
DR jPOST; Q6P3Y5; -.
DR MaxQB; Q6P3Y5; -.
DR PaxDb; Q6P3Y5; -.
DR PeptideAtlas; Q6P3Y5; -.
DR PRIDE; Q6P3Y5; -.
DR ProteomicsDB; 275255; -. [Q6P3Y5-1]
DR ProteomicsDB; 275256; -. [Q6P3Y5-2]
DR ProteomicsDB; 275257; -. [Q6P3Y5-3]
DR Antibodypedia; 30167; 74 antibodies from 22 providers.
DR DNASU; 208968; -.
DR Ensembl; ENSMUST00000072292; ENSMUSP00000072138; ENSMUSG00000036916. [Q6P3Y5-3]
DR Ensembl; ENSMUST00000076635; ENSMUSP00000075933; ENSMUSG00000036916. [Q6P3Y5-1]
DR Ensembl; ENSMUST00000088898; ENSMUSP00000086288; ENSMUSG00000036916. [Q6P3Y5-1]
DR Ensembl; ENSMUST00000114940; ENSMUSP00000110590; ENSMUSG00000036916. [Q6P3Y5-2]
DR GeneID; 208968; -.
DR KEGG; mmu:208968; -.
DR UCSC; uc009tcj.1; mouse. [Q6P3Y5-2]
DR UCSC; uc009tck.1; mouse. [Q6P3Y5-1]
DR UCSC; uc009tcm.2; mouse. [Q6P3Y5-3]
DR CTD; 208968; -.
DR MGI; MGI:2387585; Zfp280c.
DR VEuPathDB; HostDB:ENSMUSG00000036916; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162128; -.
DR HOGENOM; CLU_010097_1_0_1; -.
DR InParanoid; Q6P3Y5; -.
DR OMA; PKCNIQF; -.
DR OrthoDB; 105829at2759; -.
DR PhylomeDB; Q6P3Y5; -.
DR TreeFam; TF331707; -.
DR BioGRID-ORCS; 208968; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Zfp280c; mouse.
DR PRO; PR:Q6P3Y5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6P3Y5; protein.
DR Bgee; ENSMUSG00000036916; Expressed in humerus cartilage element and 239 other tissues.
DR Genevisible; Q6P3Y5; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR025243; DUF4195.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF13836; DUF4195; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..742
FT /note="Zinc finger protein 280C"
FT /id="PRO_0000227976"
FT ZN_FING 323..345
FT /note="C2H2-type 1"
FT ZN_FING 360..383
FT /note="C2H2-type 2"
FT ZN_FING 390..413
FT /note="C2H2-type 3"
FT ZN_FING 420..443
FT /note="C2H2-type 4"
FT ZN_FING 477..499
FT /note="C2H2-type 5"
FT REGION 138..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 23
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 85
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT CROSSLNK 580
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8ND82"
FT VAR_SEQ 11..19
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_017619"
FT VAR_SEQ 686..693
FT /note="RGITLVCL -> SYRKSRNF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017620"
FT VAR_SEQ 694..742
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017621"
SQ SEQUENCE 742 AA; 83146 MW; 04A82F753CAD6C10 CRC64;
MDKDNSVQEK GLFLSSWKLD NSKMAELFME CEEEELEPWQ QKVEESQSKD DDDELIFVGE
ISSSKPAISN ILNRCSPGSS SKGLKNGSFN PAISNIFKPT SQHYRNPSSN ALVALPSFHP
ALKSSESSDG QTVSKLDFTK TSPQEDSGAC SVSQSDSTQD IPSSNILQPR TGVDQTLGLK
HPSTSKVNSV NPKKPKTSAS ISETRPCSSS SSQTAPSGAS SQTVLSNVNT SSVQSAPGSS
SLRSCPKCNV KFRLLDPLKC HMKRCCPDMI NKFLETLKSE NSKAVSKATT DSDKEKLIML
VSDFYYGRHE GTIEESQKTH TTFKCFSCTK VLKNNIRFMN HMKHHLELEK QNNETWESHT
TCQHCYRQYP NPFQLQCHIE STHTPHDFST ICKICELSFE TEHMLLQHMK DTHKPGEMPY
ICQVCQFRSS IFSDVETHFR SSHENTKNLL CPFCLKVSRM ATPYMNHYMR HQKKGIYRCP
KCRLQFLTSK EKTEHKLEHR TFIKPKELEG LPPGTKVIIR ASLGSSQSRA SSPPSSTIPS
TSLQLSVPKS KSTTTKNNSK VSANKATTTS PQTVATTTGK PSASKPGTGT TKSKAKPSYK
QKRQRTRKNK FSIDLKNLRC HQGSHMCIEC RSKIKDFSSH FSTHINCDFC KYTTNCNKAF
TNHMSSHNDH PSKQLYIFKK QSRARRGITL VCLKCDFLAD TSGLDRMAKH LNQRKTHTCQ
VVIENVTERA VTSESASDGL FK
