Z280D_MOUSE
ID Z280D_MOUSE Reviewed; 974 AA.
AC Q68FE8; Q3T9B1; Q8BI82;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Zinc finger protein 280D;
DE AltName: Full=Suppressor of hairy wing homolog 4;
GN Name=Znf280d; Synonyms=Suhw4, Zfp280d;
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] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904 AND SER-907, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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=Q68FE8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68FE8-2; Sequence=VSP_017630, VSP_017633;
CC Name=3;
CC IsoId=Q68FE8-3; Sequence=VSP_017629, VSP_017631, VSP_017632;
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DR EMBL; AK045173; BAC32247.1; -; mRNA.
DR EMBL; AK172652; BAE43113.1; -; mRNA.
DR EMBL; BC079878; AAH79878.1; -; mRNA.
DR CCDS; CCDS40683.1; -. [Q68FE8-1]
DR RefSeq; NP_001298034.1; NM_001311105.1.
DR RefSeq; NP_666336.3; NM_146224.5. [Q68FE8-1]
DR RefSeq; XP_006511183.1; XM_006511120.2. [Q68FE8-2]
DR AlphaFoldDB; Q68FE8; -.
DR BioGRID; 231667; 4.
DR STRING; 10090.ENSMUSP00000096175; -.
DR iPTMnet; Q68FE8; -.
DR PhosphoSitePlus; Q68FE8; -.
DR EPD; Q68FE8; -.
DR jPOST; Q68FE8; -.
DR MaxQB; Q68FE8; -.
DR PaxDb; Q68FE8; -.
DR PeptideAtlas; Q68FE8; -.
DR PRIDE; Q68FE8; -.
DR ProteomicsDB; 302096; -. [Q68FE8-2]
DR ProteomicsDB; 302097; -. [Q68FE8-3]
DR DNASU; 235469; -.
DR Ensembl; ENSMUST00000098576; ENSMUSP00000096175; ENSMUSG00000038535. [Q68FE8-1]
DR Ensembl; ENSMUST00000184517; ENSMUSP00000138970; ENSMUSG00000038535. [Q68FE8-2]
DR GeneID; 235469; -.
DR KEGG; mmu:235469; -.
DR UCSC; uc009qpo.1; mouse. [Q68FE8-2]
DR UCSC; uc009qpp.1; mouse. [Q68FE8-3]
DR UCSC; uc009qpq.1; mouse. [Q68FE8-1]
DR CTD; 235469; -.
DR MGI; MGI:2384583; Zfp280d.
DR VEuPathDB; HostDB:ENSMUSG00000038535; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158889; -.
DR HOGENOM; CLU_010097_1_0_1; -.
DR InParanoid; Q68FE8; -.
DR OMA; MQIYLKA; -.
DR OrthoDB; 105829at2759; -.
DR PhylomeDB; Q68FE8; -.
DR TreeFam; TF331707; -.
DR BioGRID-ORCS; 235469; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Zfp280d; mouse.
DR PRO; PR:Q68FE8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q68FE8; protein.
DR Bgee; ENSMUSG00000038535; Expressed in undifferentiated genital tubercle and 257 other tissues.
DR ExpressionAtlas; Q68FE8; baseline and differential.
DR Genevisible; Q68FE8; 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; 9.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..974
FT /note="Zinc finger protein 280D"
FT /id="PRO_0000227978"
FT ZN_FING 333..355
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..393
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..424
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..453
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 188..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT CROSSLNK 752
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6N043"
FT VAR_SEQ 1..270
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017629"
FT VAR_SEQ 751..787
FT /note="IKTEAPTKGQEPVSKETARHSRAEGEPGASHSGSKQD -> CRSSPEISKHV
FT QGVPGQCPLRWTQVLPVLSFPGMRMN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017630"
FT VAR_SEQ 784
FT /note="S -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017631"
FT VAR_SEQ 785..974
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017632"
FT VAR_SEQ 788..974
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017633"
SQ SEQUENCE 974 AA; 107836 MW; 1207D9ADBE551229 CRC64;
MVTTYIKSDL QLDGRQFFQP KDNLKMAELF MECEEEELEP WQKKVKEVEE DDDDEPIFVA
EIASSKPAIS NILNRVNPSS HSRGIKNGIL NRGFTASFKP TSQRCLNSAS NPVAALPVNF
HPESRSSDSS VIVQPFSKPG YVTNSPRVLS NNSSELLFDL TQDTGLSHYQ GGPTLSIAGL
NETSFLSKRP SGSDISSVNP KKPKPSENTS GIDASSVISS EKSPSVISLQ VVPSQGANCS
SSQSKNGTTF PRACPKCDIH FNLLDPLKNH MTYCCPDMIN NFLGLTKADN LNSANEAKTL
ESEKGKLIML VNDFYYGKHE GDVLEEQKTH TTFKCFSCLK VLKNNIRFMN HMKHHLELEK
QSSESWEKHT TCQHCYRQFP TPFQLQCHIE STHTPHEFST ICKICELSFE TEQILLQHMK
DNHKPGEMPY ICQVCNYRSS LFSEVESHFR TSHENTKNLL CPFCLKVIKI ATPYMHHYMK
HQKKGIHRCT KCRLQFLTCK EKMDHKTQHH RTFVKPKQLE GLPPGTKVTI RASVGPLQSG
SSVTPSISPS TSTLQLSPPE PDNVTAKNHV KLTTSTPNTT ISDPSKANET KSNGSKSKNK
SKVSNMQKKQ STLSSSNKKS KVNTALRNLR LRRGVHECIE CSSEVKDFAN HFPTYVHCSF
CRYNTSCSKA YVNHMMSFHS NRPSKRYCIF KKHSENLRGI SLVCLNCDFL TDVSGLDNMA
THLSQHETHS CRVLVEQVSV CIPTSERLSE IKTEAPTKGQ EPVSKETARH SRAEGEPGAS
HSGSKQDKVP SSEEGTGCDA SVCEAAAATH CEKDVTVSDT ENVSSSKNIL SHDPDVGTDT
MEKEEKTHHA CQEMELKVDQ SSESTNPTEA ELSSETRQGL QLTSGDVGID QFLRQGDEPK
SVNSDASDPG SVRLEPLTPS EVLEYEATEI LHDGDDPSAN TSDTVSDQTG GSPGGSNPCR
AETAVDLADG EERS
