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IKIP_RAT
ID   IKIP_RAT                Reviewed;         373 AA.
AC   Q5EAJ6; Q5M859;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   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 [MRNA] (ISOFORMS 1 AND 2).
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] (ISOFORM 2).
RC   TISSUE=Thymus;
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: 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=Q5EAJ6-1; Sequence=Displayed;
CC       Name=2; Synonyms=Ikip2;
CC         IsoId=Q5EAJ6-2; Sequence=VSP_034412;
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.
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DR   EMBL; BN000112; CAD62384.1; -; mRNA.
DR   EMBL; BN000113; CAD62385.1; -; mRNA.
DR   EMBL; BC088210; AAH88210.1; -; mRNA.
DR   RefSeq; NP_001009430.2; NM_001009430.2. [Q5EAJ6-1]
DR   RefSeq; XP_006241312.1; XM_006241250.3. [Q5EAJ6-2]
DR   AlphaFoldDB; Q5EAJ6; -.
DR   SMR; Q5EAJ6; -.
DR   BioGRID; 260816; 1.
DR   STRING; 10116.ENSRNOP00000010913; -.
DR   GlyGen; Q5EAJ6; 1 site.
DR   jPOST; Q5EAJ6; -.
DR   PaxDb; Q5EAJ6; -.
DR   PRIDE; Q5EAJ6; -.
DR   Ensembl; ENSRNOT00000010914; ENSRNOP00000010913; ENSRNOG00000008247. [Q5EAJ6-1]
DR   Ensembl; ENSRNOT00000010929; ENSRNOP00000010929; ENSRNOG00000008247. [Q5EAJ6-2]
DR   GeneID; 314730; -.
DR   KEGG; rno:314730; -.
DR   UCSC; RGD:1305457; rat. [Q5EAJ6-1]
DR   CTD; 121457; -.
DR   RGD; 1305457; Ikbip.
DR   eggNOG; ENOG502RXC3; Eukaryota.
DR   GeneTree; ENSGT00500000045001; -.
DR   HOGENOM; CLU_061486_1_0_1; -.
DR   InParanoid; Q5EAJ6; -.
DR   OMA; EKTWNLM; -.
DR   OrthoDB; 1191353at2759; -.
DR   PhylomeDB; Q5EAJ6; -.
DR   TreeFam; TF331715; -.
DR   PRO; PR:Q5EAJ6; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000008247; Expressed in ovary and 19 other tissues.
DR   Genevisible; Q5EAJ6; RN.
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   2: Evidence at transcript 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_0000342263"
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          64..257
FT                   /evidence="ECO:0000255"
FT   COILED          290..325
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..29
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="LESTENTLQEATSSMSLMTQFEQEVAGLQRSIHDIENSEEMLTQKLQNLNEK
FT                   FQNITDLWKRTLVEMSDNTAVFKSEAKSTHSEVTLKINSAEQEIKLLTERLKDLEDSTL
FT                   RNIRTVSRQEEEDLLRVEAQLSSDTKAVEKLEEEQRTLLARDEDLTDKLSSYEPKVEEC
FT                   KAHLPTIENAVHSVLRVSQDLIGTERKMEELTVQMFNMEDDMLKAVSEIMEMQNTLEGI
FT                   QYDNSLLKMQNELVVLKGKVHDFMAYSSAGEKGTLEEYNLENKGTDDY -> YQKCEAL
FT                   LEQLKAFQIVAHLKLLQEEIHGMKTWSIGITEKQKILNNTLTSLSEDIIKVDQGTASVA
FT                   KDMGLKITSVKTDVRRISGLVTEVESLTDAVQALENKVKKVETATVESIGDLLSSSIDR
FT                   TTALRKTASENSRRIDSVTKRLAELQGDFDEHTDRFLSLESERAKVLKAVSFANDLKPK
FT                   VYNLKKDFSRLEPLVNDLTLRIGRLGSDLMQREKEIASLKEKISNLTIVQAAIKDMKDE
FT                   ITHISG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15389287,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_034412"
SQ   SEQUENCE   373 AA;  42361 MW;  C6BA554B510E4E38 CRC64;
     MSEVKSRKKP GPKVAAPEPE KRSDGRKNPE ARGGAGWADP RTGLSLLSLA TSLGLAWLVF
     QQSEKFAKVE NQYRLLQTES SEFQGLQSKI SLISNKLEST ENTLQEATSS MSLMTQFEQE
     VAGLQRSIHD IENSEEMLTQ KLQNLNEKFQ NITDLWKRTL VEMSDNTAVF KSEAKSTHSE
     VTLKINSAEQ EIKLLTERLK DLEDSTLRNI RTVSRQEEED LLRVEAQLSS DTKAVEKLEE
     EQRTLLARDE DLTDKLSSYE PKVEECKAHL PTIENAVHSV LRVSQDLIGT ERKMEELTVQ
     MFNMEDDMLK AVSEIMEMQN TLEGIQYDNS LLKMQNELVV LKGKVHDFMA YSSAGEKGTL
     EEYNLENKGT DDY
 
 
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