NKAP_RAT
ID NKAP_RAT Reviewed; 415 AA.
AC Q4V7C9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=NF-kappa-B-activating protein;
GN Name=Nkap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND THR-159, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC098011; AAH98011.1; -; mRNA.
DR RefSeq; NP_001020043.1; NM_001024872.1.
DR AlphaFoldDB; Q4V7C9; -.
DR SMR; Q4V7C9; -.
DR STRING; 10116.ENSRNOP00000039435; -.
DR iPTMnet; Q4V7C9; -.
DR PhosphoSitePlus; Q4V7C9; -.
DR PaxDb; Q4V7C9; -.
DR PRIDE; Q4V7C9; -.
DR GeneID; 298342; -.
DR KEGG; rno:298342; -.
DR UCSC; RGD:1565955; rat.
DR CTD; 79576; -.
DR RGD; 1565955; Nkap.
DR eggNOG; KOG2812; Eukaryota.
DR InParanoid; Q4V7C9; -.
DR OrthoDB; 1561377at2759; -.
DR PhylomeDB; Q4V7C9; -.
DR TreeFam; TF315333; -.
DR PRO; PR:Q4V7C9; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR GO; GO:0030851; P:granulocyte differentiation; ISO:RGD.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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:0019827; P:stem cell population maintenance; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR InterPro; IPR040466; NKAP.
DR InterPro; IPR009269; NKAP_C.
DR PANTHER; PTHR13087; PTHR13087; 1.
DR Pfam; PF06047; Nkap_C; 1.
PE 1: Evidence at protein 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_0000259647"
FT REGION 1..309
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..100
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:0007744|PubMed:22673903"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
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"
SQ SEQUENCE 415 AA; 47267 MW; DD45D1E4F1C93A05 CRC64;
MAPVSGSRSP VREASGGKRR SSSRSPKSIK SSRSPRCRRS RSRSCSRFGD RNGLSHSLSG
FSQSSRNQSY RSRSRSRSRE RPSAQRSAPF ASSSSSAYYG GYSRPYGGDK PWPSLLDKER
EESLRQKRLS ERERIGELGA PEVWGLSPKN PEPDSDEHTP VEDEEPKKST TSASSSEDDK
KKKRKSSRSK ERAKKKRKKK SSKRKHKKYS EDSDSDSESD TDSSDEDSKR RAKKAKKKEK
KKKRRGKKYK KKKSKKNRKE SSDSSSKESQ EEFLENPWKD RSKTEEPSDL IGPEAPKTLA
SQDDKPLNYG HALLPGEGAA MAEYVKAGKR IPRRGEIGLT SEEIASFECS GYVMSGSRHR
RMEAVRLRKE NQIYSADEKR ALASFNQEER RKRENKILAS FREMVYRKTK GKDDK
