IKIP_HUMAN
ID IKIP_HUMAN Reviewed; 350 AA.
AC Q70UQ0; Q6ZWH4; Q70UP9; Q86V91; Q96ND2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), INDUCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, AND FUNCTION.
RX PubMed=15389287; DOI=10.1038/sj.cdd.4401502;
RA Hofer-Warbinek R., Schmid J.A., Mayer H., Winsauer G., Orel L., Mueller B.,
RA Wiesner C., Binder B.R., de Martin R.;
RT "A highly conserved proapoptotic gene, IKIP, located next to the APAF1 gene
RT locus, is regulated by p53.";
RL Cell Death Differ. 11:1317-1325(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Prostate, Skin, and 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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144 AND ASN-328.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Target of p53/TP53 with pro-apoptotic function.
CC {ECO:0000269|PubMed:15389287}.
CC -!- INTERACTION:
CC Q70UQ0; Q9BUW7: BBLN; NbExp=3; IntAct=EBI-2557212, EBI-752084;
CC Q70UQ0; P19012: KRT15; NbExp=3; IntAct=EBI-2557212, EBI-739566;
CC Q70UQ0; P15173: MYOG; NbExp=4; IntAct=EBI-2557212, EBI-3906629;
CC Q70UQ0; P37198: NUP62; NbExp=3; IntAct=EBI-2557212, EBI-347978;
CC Q70UQ0; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2557212, EBI-1105213;
CC Q70UQ0; Q5VU62: TPM3; NbExp=3; IntAct=EBI-2557212, EBI-10184033;
CC Q70UQ0-4; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-12190633, EBI-7247651;
CC Q70UQ0-4; O00155: GPR25; NbExp=3; IntAct=EBI-12190633, EBI-10178951;
CC Q70UQ0-4; O95447: LCA5L; NbExp=3; IntAct=EBI-12190633, EBI-8473670;
CC Q70UQ0-4; P15173: MYOG; NbExp=4; IntAct=EBI-12190633, EBI-3906629;
CC Q70UQ0-4; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-12190633, EBI-358489;
CC Q70UQ0-4; O95295: SNAPIN; NbExp=4; IntAct=EBI-12190633, EBI-296723;
CC Q70UQ0-4; Q9Y3C0: WASHC3; NbExp=4; IntAct=EBI-12190633, EBI-712969;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15389287}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15389287}. Note=Isoform 4 deletion of the
CC hydrophobic, or transmembrane region between AA 45-63 results in
CC uniform distribution throughout the cell, suggesting that this region
CC is responsible for endoplasmic reticulum localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=IKIP2;
CC IsoId=Q70UQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q70UQ0-2; Sequence=VSP_034407;
CC Name=3; Synonyms=IKIP3;
CC IsoId=Q70UQ0-3; Sequence=VSP_034408, VSP_034409;
CC Name=4; Synonyms=IKIP1;
CC IsoId=Q70UQ0-4; Sequence=VSP_034410;
CC -!- TISSUE SPECIFICITY: Expressed in vein endothelial cells. Isoform 4 is
CC expressed in lung, kidney, spleen, thymus and skeletal muscle.
CC {ECO:0000269|PubMed:15389287}.
CC -!- INDUCTION: By X-ray irradiation. {ECO:0000269|PubMed:15389287}.
CC -!- PTM: N-glycosylated. Isoform 4 is glycosylated at Asn-154.
CC {ECO:0000269|PubMed:15389287, ECO:0000269|PubMed:19159218}.
CC -!- MISCELLANEOUS: Shares a common promoter with APAF1 from which the 2
CC genes are transcribed in opposite directions.
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DR EMBL; AJ539425; CAD62380.1; -; mRNA.
DR EMBL; AJ539426; CAD62381.1; -; mRNA.
DR EMBL; AJ539427; CAD62382.1; -; mRNA.
DR EMBL; AJ539427; CAD62383.1; -; mRNA.
DR EMBL; AK055613; BAB70970.1; -; mRNA.
DR EMBL; AK123069; BAC85528.1; -; mRNA.
DR EMBL; CH471054; EAW97601.1; -; Genomic_DNA.
DR EMBL; BC029415; AAH29415.2; -; mRNA.
DR EMBL; BC051372; AAH51372.2; -; mRNA.
DR EMBL; BC058933; AAH58933.1; -; mRNA.
DR CCDS; CCDS41822.1; -. [Q70UQ0-3]
DR CCDS; CCDS9067.1; -. [Q70UQ0-1]
DR CCDS; CCDS9068.1; -. [Q70UQ0-4]
DR RefSeq; NP_710154.1; NM_153687.3. [Q70UQ0-4]
DR RefSeq; NP_963906.1; NM_201612.2. [Q70UQ0-1]
DR RefSeq; NP_963907.1; NM_201613.2. [Q70UQ0-3]
DR AlphaFoldDB; Q70UQ0; -.
DR SMR; Q70UQ0; -.
DR BioGRID; 125730; 162.
DR IntAct; Q70UQ0; 79.
DR MINT; Q70UQ0; -.
DR GlyConnect; 1398; 2 N-Linked glycans (2 sites).
DR GlyGen; Q70UQ0; 4 sites, 3 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q70UQ0; -.
DR PhosphoSitePlus; Q70UQ0; -.
DR SwissPalm; Q70UQ0; -.
DR BioMuta; IKBIP; -.
DR DMDM; 74712656; -.
DR EPD; Q70UQ0; -.
DR jPOST; Q70UQ0; -.
DR MassIVE; Q70UQ0; -.
DR MaxQB; Q70UQ0; -.
DR PeptideAtlas; Q70UQ0; -.
DR PRIDE; Q70UQ0; -.
DR ProteomicsDB; 68566; -. [Q70UQ0-1]
DR ProteomicsDB; 68567; -. [Q70UQ0-2]
DR ProteomicsDB; 68568; -. [Q70UQ0-3]
DR ProteomicsDB; 68569; -. [Q70UQ0-4]
DR Antibodypedia; 44824; 208 antibodies from 26 providers.
DR DNASU; 121457; -.
DR Ensembl; ENST00000299157.5; ENSP00000299157.4; ENSG00000166130.15. [Q70UQ0-4]
DR Ensembl; ENST00000342502.6; ENSP00000343471.2; ENSG00000166130.15. [Q70UQ0-1]
DR Ensembl; ENST00000393042.3; ENSP00000376762.3; ENSG00000166130.15. [Q70UQ0-3]
DR GeneID; 121457; -.
DR KEGG; hsa:121457; -.
DR MANE-Select; ENST00000299157.5; ENSP00000299157.4; NM_153687.4; NP_710154.1. [Q70UQ0-4]
DR UCSC; uc001tfv.5; human. [Q70UQ0-1]
DR CTD; 121457; -.
DR DisGeNET; 121457; -.
DR GeneCards; IKBIP; -.
DR HGNC; HGNC:26430; IKBIP.
DR HPA; ENSG00000166130; Low tissue specificity.
DR MIM; 609861; gene.
DR neXtProt; NX_Q70UQ0; -.
DR OpenTargets; ENSG00000166130; -.
DR PharmGKB; PA165512948; -.
DR VEuPathDB; HostDB:ENSG00000166130; -.
DR GeneTree; ENSGT00500000045001; -.
DR HOGENOM; CLU_2757083_0_0_1; -.
DR InParanoid; Q70UQ0; -.
DR OMA; EKTWNLM; -.
DR OrthoDB; 1191353at2759; -.
DR PhylomeDB; Q70UQ0; -.
DR TreeFam; TF331715; -.
DR PathwayCommons; Q70UQ0; -.
DR SignaLink; Q70UQ0; -.
DR BioGRID-ORCS; 121457; 7 hits in 1069 CRISPR screens.
DR ChiTaRS; IKBIP; human.
DR GenomeRNAi; 121457; -.
DR Pharos; Q70UQ0; Tbio.
DR PRO; PR:Q70UQ0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q70UQ0; protein.
DR Bgee; ENSG00000166130; Expressed in stromal cell of endometrium and 159 other tissues.
DR Genevisible; Q70UQ0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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 GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0010165; P:response to X-ray; TAS:BHF-UCL.
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..350
FT /note="Inhibitor of nuclear factor kappa-B kinase-
FT interacting protein"
FT /id="PRO_0000342261"
FT TRANSMEM 46..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..217
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15389287"
FT /id="VSP_034407"
FT VAR_SEQ 60..70
FT /note="WFVFQQSEKFA -> CGRNLKLSWNN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15389287,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_034408"
FT VAR_SEQ 71..350
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15389287,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_034409"
FT VAR_SEQ 100..350
FT /note="WQKSEAIMEQLKSFQIIAHLKRLQEEINEVKTWSNRITEKQDILNNSLTTLS
FT QDITKVDQSTTSMAKDVGLKITSVKTDIRRISGLVTDVISLTDSVQELENKIEKVEKNT
FT VKNIGDLLSSSIDRTATLRKTASENSQRINSVKKTLTELKSDFDKHTDRFLSLEGDRAK
FT VLKTVTFANDLKPKVYNLKKDFSRLEPLVNDLTLRIGRLVTDLLQREKEIAFLSEKISN
FT LTIVQAEIKDIKDEIAHISDMN -> LESTESILQEATSSMSLMTQFEQEVSNLQDIMH
FT DIQNNEEVLTQRMQSLNEKFQNITDFWKRSLEEMNINTDIFKSEAKHIHSQVTVQINSA
FT EQEIKLLTERLKDLEDSTLRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKLEEEQHALFA
FT RDEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLRVSQDLIETEKKMEDLTMQMFNMED
FT DMLKAVSEIMEMQKTLEGIQYDNSILKMQNELDILKEKVHDFIAYSSTGEKGTLKEYNI
FT ENKGIGGDF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15389287, ECO:0000303|PubMed:15489334"
FT /id="VSP_034410"
FT VARIANT 265
FT /note="G -> S (in dbSNP:rs1048906)"
FT /id="VAR_051067"
FT VARIANT Q70UQ0-4:122
FT /note="Q -> H (in dbSNP:rs12322444)"
FT /evidence="ECO:0000305"
FT /id="VAR_082882"
SQ SEQUENCE 350 AA; 39309 MW; 98BDA498C7BA1D0A CRC64;
MSEVKSRKKS GPKGAPAAEP GKRSEGGKTP VARSSGGGGW ADPRTCLSLL SLGTCLGLAW
FVFQQSEKFA KVENQYQLLK LETNEFQQLQ SKISLISEKW QKSEAIMEQL KSFQIIAHLK
RLQEEINEVK TWSNRITEKQ DILNNSLTTL SQDITKVDQS TTSMAKDVGL KITSVKTDIR
RISGLVTDVI SLTDSVQELE NKIEKVEKNT VKNIGDLLSS SIDRTATLRK TASENSQRIN
SVKKTLTELK SDFDKHTDRF LSLEGDRAKV LKTVTFANDL KPKVYNLKKD FSRLEPLVND
LTLRIGRLVT DLLQREKEIA FLSEKISNLT IVQAEIKDIK DEIAHISDMN
