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Protein

NF-kappa-B-activating protein

Gene

Nkap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Acts as a transcriptional repressor. Plays a role as a transcriptional corepressor of the Notch-mediated signaling required for T-cell development. Also involved in the TNF and IL-1 induced NF-kappa-B activation. Associates with chromatin at the Notch-regulated SKP2 promoter (By similarity).By similarity

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • chromatin DNA binding Source: MGI
  • poly(A) RNA binding Source: MGI

GO - Biological processi

  • granulocyte differentiation Source: MGI
  • hematopoietic stem cell proliferation Source: MGI
  • hemopoiesis Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • Notch signaling pathway Source: UniProtKB-KW
  • positive regulation of alpha-beta T cell differentiation Source: UniProtKB
  • positive regulation of protein targeting to mitochondrion Source: MGI
  • stem cell population maintenance Source: MGI
  • T cell differentiation in thymus Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Notch signaling pathway, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
NF-kappa-B-activating protein
Gene namesi
Name:Nkap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1914300. Nkap.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415NF-kappa-B-activating proteinPRO_0000259646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101N6-acetyllysineBy similarity
Modified residuei147 – 1471PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9D0F4.
MaxQBiQ9D0F4.
PaxDbiQ9D0F4.
PRIDEiQ9D0F4.

PTM databases

iPTMnetiQ9D0F4.
PhosphoSiteiQ9D0F4.

Expressioni

Gene expression databases

BgeeiQ9D0F4.
CleanExiMM_NKAP.
GenevisibleiQ9D0F4. MM.

Interactioni

Subunit structurei

Component of the Notch corepressor complex. Interacts with CIR1 and HDAC3 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9D0F4. 2 interactions.
MINTiMINT-4126413.
STRINGi10090.ENSMUSP00000016553.

Structurei

3D structure databases

ProteinModelPortaliQ9D0F4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 27296Necessary for interaction with CIR1By similarityAdd
BLAST
Regioni273 – 415143Necessary for interaction with HDAC3 and transcriptional repressionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 8679Arg-richAdd
BLAST
Compositional biasi180 – 25980Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the UPF0396 family.Curated

Phylogenomic databases

eggNOGiKOG2812. Eukaryota.
ENOG4111VW4. LUCA.
GeneTreeiENSGT00510000047021.
HOGENOMiHOG000049099.
HOVERGENiHBG068915.
InParanoidiQ9D0F4.
OMAiRRGKKYK.
OrthoDBiEOG700898.
PhylomeDBiQ9D0F4.
TreeFamiTF315333.

Family and domain databases

InterProiIPR009269. NKAP/UPF0396.
[Graphical view]
PANTHERiPTHR13087. PTHR13087. 1 hit.
PfamiPF06047. SynMuv_product. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D0F4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPVSGSRSP EREASGAKRR SPSRSPKSIK SSRSPRCRRS RSRSCSRFGD
60 70 80 90 100
RNGLSHSLSG FSQSSRNQSY RSRSRSRSRE RPSAQRSAPF ASASSSAYYG
110 120 130 140 150
GYSRPYGGDK PWPSLLDKER EESLRQKRLS ERERIGELGA PEVWGLSPKN
160 170 180 190 200
PEPDSDEHTP VEDEEPKKST TSASSSEDDK KKKRKSSHSK DRAKKKRKKK
210 220 230 240 250
SSKRKHKKYS EDSDSDSESD TDSSDEDSKR RAKKAKKKDK KKKRRGKKYK
260 270 280 290 300
KKKSKKNRKE SSDSSSKESQ EEFLENPWKD RSKAEEPSDL IGPEAPKTLA
310 320 330 340 350
SQDDKPLNYG HALLPGEGAA MAEYVKAGKR IPRRGEIGLT SEEIASFECS
360 370 380 390 400
GYVMSGSRHR RMEAVRLRKE NQIYSADEKR ALASFNQEER RKRENKILAS
410
FREMVYRKTK GKDDK
Length:415
Mass (Da):47,227
Last modified:June 1, 2001 - v1
Checksum:iF9B254B486CD363C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851K → E in BAC41010 (PubMed:16141072).Curated
Sequence conflicti191 – 1911D → E in AAH26774 (PubMed:15489334).Curated
Sequence conflicti194 – 1952KK → QE in BAC41010 (PubMed:16141072).Curated
Sequence conflicti293 – 2931P → A in BAC29972 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY388959 mRNA. Translation: AAQ90403.1.
AK011492 mRNA. Translation: BAB27654.1.
AK012826 mRNA. Translation: BAB28497.3.
AK038344 mRNA. Translation: BAC29972.1.
AK089943 mRNA. Translation: BAC41010.1.
BC026774 mRNA. Translation: AAH26774.1.
CCDSiCCDS30069.1.
RefSeqiNP_080213.3. NM_025937.4.
UniGeneiMm.55422.

Genome annotation databases

EnsembliENSMUST00000016553; ENSMUSP00000016553; ENSMUSG00000016409.
GeneIDi67050.
KEGGimmu:67050.
UCSCiuc009syg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY388959 mRNA. Translation: AAQ90403.1.
AK011492 mRNA. Translation: BAB27654.1.
AK012826 mRNA. Translation: BAB28497.3.
AK038344 mRNA. Translation: BAC29972.1.
AK089943 mRNA. Translation: BAC41010.1.
BC026774 mRNA. Translation: AAH26774.1.
CCDSiCCDS30069.1.
RefSeqiNP_080213.3. NM_025937.4.
UniGeneiMm.55422.

3D structure databases

ProteinModelPortaliQ9D0F4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D0F4. 2 interactions.
MINTiMINT-4126413.
STRINGi10090.ENSMUSP00000016553.

PTM databases

iPTMnetiQ9D0F4.
PhosphoSiteiQ9D0F4.

Proteomic databases

EPDiQ9D0F4.
MaxQBiQ9D0F4.
PaxDbiQ9D0F4.
PRIDEiQ9D0F4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016553; ENSMUSP00000016553; ENSMUSG00000016409.
GeneIDi67050.
KEGGimmu:67050.
UCSCiuc009syg.2. mouse.

Organism-specific databases

CTDi79576.
MGIiMGI:1914300. Nkap.

Phylogenomic databases

eggNOGiKOG2812. Eukaryota.
ENOG4111VW4. LUCA.
GeneTreeiENSGT00510000047021.
HOGENOMiHOG000049099.
HOVERGENiHBG068915.
InParanoidiQ9D0F4.
OMAiRRGKKYK.
OrthoDBiEOG700898.
PhylomeDBiQ9D0F4.
TreeFamiTF315333.

Miscellaneous databases

PROiQ9D0F4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0F4.
CleanExiMM_NKAP.
GenevisibleiQ9D0F4. MM.

Family and domain databases

InterProiIPR009269. NKAP/UPF0396.
[Graphical view]
PANTHERiPTHR13087. PTHR13087. 1 hit.
PfamiPF06047. SynMuv_product. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a nuclear protein that promotes NF-kappaB activation."
    Chen D., Li Z., Yang Q., Zhang J., Zhai Z., Shu H.-B.
    Biochem. Biophys. Res. Commun. 310:720-724(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.

Entry informationi

Entry nameiNKAP_MOUSE
AccessioniPrimary (citable) accession number: Q9D0F4
Secondary accession number(s): Q8BTK6
, Q8BYT5, Q8R324, Q9CSH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
  3. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.