NKAP_MOUSE
ID NKAP_MOUSE Reviewed; 415 AA.
AC Q9D0F4; Q8BTK6; Q8BYT5; Q8R324; Q9CSH4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=NF-kappa-B-activating protein;
GN Name=Nkap;
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].
RX PubMed=14550261; DOI=10.1016/j.bbrc.2003.09.074;
RA Chen D., Li Z., Yang Q., Zhang J., Zhai Z., Shu H.-B.;
RT "Identification of a nuclear protein that promotes NF-kappaB activation.";
RL Biochem. Biophys. Res. Commun. 310:720-724(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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: Acts as a transcriptional repressor. Plays a role as a
CC transcriptional corepressor of the Notch-mediated signaling required
CC for T-cell development. Also involved in the TNF and IL-1 induced NF-
CC kappa-B activation. Associates with chromatin at the Notch-regulated
CC SKP2 promoter (By similarity). {ECO:0000250|UniProtKB:Q8N5F7}.
CC -!- SUBUNIT: Component of the Notch corepressor complex. Interacts with
CC CIR1 and HDAC3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NKAP family. {ECO:0000305}.
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DR EMBL; AY388959; AAQ90403.1; -; mRNA.
DR EMBL; AK011492; BAB27654.1; -; mRNA.
DR EMBL; AK012826; BAB28497.3; -; mRNA.
DR EMBL; AK038344; BAC29972.1; -; mRNA.
DR EMBL; AK089943; BAC41010.1; -; mRNA.
DR EMBL; BC026774; AAH26774.1; -; mRNA.
DR CCDS; CCDS30069.1; -.
DR RefSeq; NP_080213.3; NM_025937.4.
DR AlphaFoldDB; Q9D0F4; -.
DR SMR; Q9D0F4; -.
DR BioGRID; 211903; 1.
DR IntAct; Q9D0F4; 2.
DR MINT; Q9D0F4; -.
DR STRING; 10090.ENSMUSP00000016553; -.
DR iPTMnet; Q9D0F4; -.
DR PhosphoSitePlus; Q9D0F4; -.
DR EPD; Q9D0F4; -.
DR jPOST; Q9D0F4; -.
DR MaxQB; Q9D0F4; -.
DR PaxDb; Q9D0F4; -.
DR PeptideAtlas; Q9D0F4; -.
DR PRIDE; Q9D0F4; -.
DR ProteomicsDB; 253078; -.
DR Antibodypedia; 364; 138 antibodies from 25 providers.
DR Ensembl; ENSMUST00000016553; ENSMUSP00000016553; ENSMUSG00000016409.
DR GeneID; 67050; -.
DR KEGG; mmu:67050; -.
DR UCSC; uc009syg.2; mouse.
DR CTD; 79576; -.
DR MGI; MGI:1914300; Nkap.
DR VEuPathDB; HostDB:ENSMUSG00000016409; -.
DR eggNOG; KOG2812; Eukaryota.
DR GeneTree; ENSGT00940000160787; -.
DR HOGENOM; CLU_032439_1_0_1; -.
DR InParanoid; Q9D0F4; -.
DR OMA; VERWPND; -.
DR OrthoDB; 1561377at2759; -.
DR PhylomeDB; Q9D0F4; -.
DR TreeFam; TF315333; -.
DR BioGRID-ORCS; 67050; 17 hits in 72 CRISPR screens.
DR ChiTaRS; Nkap; mouse.
DR PRO; PR:Q9D0F4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9D0F4; protein.
DR Bgee; ENSMUSG00000016409; Expressed in aortic valve and 223 other tissues.
DR Genevisible; Q9D0F4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0030851; P:granulocyte differentiation; IMP:MGI.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR InterPro; IPR040466; NKAP.
DR InterPro; IPR009269; NKAP_C.
DR PANTHER; PTHR13087; PTHR13087; 1.
DR Pfam; PF06047; Nkap_C; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Notch signaling pathway; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..415
FT /note="NF-kappa-B-activating protein"
FT /id="PRO_0000259646"
FT REGION 1..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..272
FT /note="Necessary for interaction with CIR1"
FT /evidence="ECO:0000250"
FT REGION 273..415
FT /note="Necessary for interaction with HDAC3 and
FT transcriptional repression"
FT /evidence="ECO:0000250"
FT COMPBIAS 23..42
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..257
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N5F7"
FT CONFLICT 185
FT /note="K -> E (in Ref. 2; BAC41010)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="D -> E (in Ref. 3; AAH26774)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..195
FT /note="KK -> QE (in Ref. 2; BAC41010)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="P -> A (in Ref. 2; BAC29972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47227 MW; F9B254B486CD363C CRC64;
MAPVSGSRSP EREASGAKRR SPSRSPKSIK SSRSPRCRRS RSRSCSRFGD RNGLSHSLSG
FSQSSRNQSY RSRSRSRSRE RPSAQRSAPF ASASSSAYYG GYSRPYGGDK PWPSLLDKER
EESLRQKRLS ERERIGELGA PEVWGLSPKN PEPDSDEHTP VEDEEPKKST TSASSSEDDK
KKKRKSSHSK DRAKKKRKKK SSKRKHKKYS EDSDSDSESD TDSSDEDSKR RAKKAKKKDK
KKKRRGKKYK KKKSKKNRKE SSDSSSKESQ EEFLENPWKD RSKAEEPSDL IGPEAPKTLA
SQDDKPLNYG HALLPGEGAA MAEYVKAGKR IPRRGEIGLT SEEIASFECS GYVMSGSRHR
RMEAVRLRKE NQIYSADEKR ALASFNQEER RKRENKILAS FREMVYRKTK GKDDK
