IKIP_MOUSE
ID IKIP_MOUSE Reviewed; 373 AA.
AC Q9DBZ1; Q7TMH1; Q8K1Z4; Q9DA09;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Inhibitor of nuclear factor kappa-B kinase-interacting protein;
DE Short=I kappa-B kinase-interacting protein;
DE Short=IKBKB-interacting protein;
DE Short=IKK-interacting protein;
GN Name=Ikbip; Synonyms=Ikip;
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 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Testis;
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] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and 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: Target of p53/TP53 with pro-apoptotic function.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ikip1;
CC IsoId=Q9DBZ1-1; Sequence=Displayed;
CC Name=2; Synonyms=Ikip2;
CC IsoId=Q9DBZ1-2; Sequence=VSP_034411;
CC -!- PTM: N-glycosylated at Asn-151. {ECO:0000250}.
CC -!- MISCELLANEOUS: Shares a common promoter with APAF1 from which the 2
CC genes are transcribed in opposite directions.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23459.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004670; BAB23459.1; ALT_FRAME; mRNA.
DR EMBL; AK006283; BAB24502.1; -; mRNA.
DR EMBL; BC034890; AAH34890.1; -; mRNA.
DR EMBL; BC055834; AAH55834.1; -; mRNA.
DR CCDS; CCDS24119.1; -. [Q9DBZ1-2]
DR CCDS; CCDS36031.1; -. [Q9DBZ1-1]
DR RefSeq; NP_081354.1; NM_027078.2. [Q9DBZ1-2]
DR AlphaFoldDB; Q9DBZ1; -.
DR SMR; Q9DBZ1; -.
DR BioGRID; 212198; 7.
DR IntAct; Q9DBZ1; 8.
DR STRING; 10090.ENSMUSP00000020149; -.
DR GlyGen; Q9DBZ1; 1 site.
DR iPTMnet; Q9DBZ1; -.
DR PhosphoSitePlus; Q9DBZ1; -.
DR EPD; Q9DBZ1; -.
DR MaxQB; Q9DBZ1; -.
DR PaxDb; Q9DBZ1; -.
DR PeptideAtlas; Q9DBZ1; -.
DR PRIDE; Q9DBZ1; -.
DR ProteomicsDB; 267038; -. [Q9DBZ1-1]
DR ProteomicsDB; 267039; -. [Q9DBZ1-2]
DR Antibodypedia; 44824; 208 antibodies from 26 providers.
DR DNASU; 67454; -.
DR Ensembl; ENSMUST00000020150; ENSMUSP00000020150; ENSMUSG00000019975. [Q9DBZ1-2]
DR GeneID; 67454; -.
DR KEGG; mmu:67454; -.
DR UCSC; uc007gtm.1; mouse. [Q9DBZ1-2]
DR CTD; 121457; -.
DR MGI; MGI:1914704; Ikbip.
DR VEuPathDB; HostDB:ENSMUSG00000019975; -.
DR eggNOG; ENOG502RXC3; Eukaryota.
DR GeneTree; ENSGT00500000045001; -.
DR HOGENOM; CLU_061486_0_0_1; -.
DR InParanoid; Q9DBZ1; -.
DR PhylomeDB; Q9DBZ1; -.
DR BioGRID-ORCS; 67454; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Ikbip; mouse.
DR PRO; PR:Q9DBZ1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DBZ1; protein.
DR Bgee; ENSMUSG00000019975; Expressed in vault of skull and 258 other tissues.
DR ExpressionAtlas; Q9DBZ1; baseline and differential.
DR Genevisible; Q9DBZ1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR024152; Inh_kappa-B_kinase-int.
DR PANTHER; PTHR21734; PTHR21734; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..373
FT /note="Inhibitor of nuclear factor kappa-B kinase-
FT interacting protein"
FT /id="PRO_0000342262"
FT TRANSMEM 43..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..257
FT /evidence="ECO:0000255"
FT COILED 285..324
FT /evidence="ECO:0000255"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 97..373
FT /note="LESTENTLQEATSSISLMTQFEQEVSGLQRSIRDIETSEEMLTQKMQNLNEK
FT FQNITDFWKRTLAEMIDDTAVFKSEVKDTHSEVTLKINSADQEIKSLTERLKDLEDSTL
FT RNIRTVSRQEEEDLLRVEAQLSSDTKAVKKLEEEQHTLLARDEDLTNKLSSYEPKVEEC
FT KAHFPTIENAVHSVLRVSQDLIGTERKMEELTMQMFNMEDDMLRAVSEIMEMQKTLEGI
FT QYDNSLLKMQNELVVLKGKVHDFIAYSSAREKGTLGEYSLGNKGTDEY -> YQECEAL
FT VEQLKAFQIAAHLKLLQEEIHEMKTWSNRITERQGTLNNTLTRLSEDIIKVDQGTASMA
FT KDMGLKITSVKTDVRRISGLVTEVESLTDAVQALGNKVKKVETATVENIGDLLSSSIDR
FT TSALRKTASENAKRIDSVAQRLAELQGDFDEHTDRFLSLESDRAKVLKAVSFANDLKPK
FT VSNLKKDFSRLEPLVDDLTLRIGRLGSDLMQREKEIAFLKEKISNLTVVQAAIKDIKDE
FT ITHISD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034411"
FT CONFLICT 17
FT /note="P -> H (in Ref. 1; BAB23459)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="M -> T (in Ref. 2; AAH55834)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="I -> M (in Ref. 2; AAH55834)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="I -> S (in Ref. 2; AAH55834)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="V -> I (in Ref. 2; AAH55834)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="D -> E (in Ref. 2; AAH55834)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="F -> L (in Ref. 2; AAH55834)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="A -> T (in Ref. 2; AAH55834)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9DBZ1-2:197
FT /note="G -> E (in Ref. 2; AAH34890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42532 MW; 9F42D944855ADA8A CRC64;
MSEVKSRKKP GPKVAAPEPE KRSDGRKNPE ARGDAGWADP RTGLSLLSLA MTLGLAWLVF
QQSEKFAKVE KQYRLLQTES SEFQGLQSKI SLISSKLEST ENTLQEATSS ISLMTQFEQE
VSGLQRSIRD IETSEEMLTQ KMQNLNEKFQ NITDFWKRTL AEMIDDTAVF KSEVKDTHSE
VTLKINSADQ EIKSLTERLK DLEDSTLRNI RTVSRQEEED LLRVEAQLSS DTKAVKKLEE
EQHTLLARDE DLTNKLSSYE PKVEECKAHF PTIENAVHSV LRVSQDLIGT ERKMEELTMQ
MFNMEDDMLR AVSEIMEMQK TLEGIQYDNS LLKMQNELVV LKGKVHDFIA YSSAREKGTL
GEYSLGNKGT DEY
