(data stored in ACNUC31965 zone)

HOGENOM: RATX_PE1364

ID   RATX_PE1364                          STANDARD;      PRT;   350 AA.
AC   RATX_PE1364; Q6TMG5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   Flags: Fragments;
DE   RecName: Full=NF-kappa-B essential modulator; Short=NEMO;AltName:
DE   Full=IkB kinase-associated protein 1; Short=IKKAP1;AltName:
DE   Full=Inhibitor of nuclear factor kappa-B kinase subunit gamma;
DE   Short=I-kappa-B kinase subunit gamma; Short=IKK-gamma; Short=IKKG;
DE   Short=IkB kinase subunit gamma;AltName: Full=NF-kappa-B essential
DE   modifier; (RATX.PE1364).
GN   Name=Ikbkg; Synonyms=Nemo;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RATX.PE1364.
CC       Rattus norvegicus chromosome X RGSC3.4  sequence 1..160699376
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:NEMO_RAT
CC   -!- FUNCTION: Regulatory subunit of the IKK core complex which
CC       phosphorylates inhibitors of NF-kappa-B thus leading to the
CC       dissociation of the inhibitor/NF-kappa-B complex and ultimately
CC       the degradation of the inhibitor. Also considered to be a mediator
CC       for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-
CC       B-mediated protection from cytokine toxicity. Essential for viral
CC       activation of IRF3 (By similarity).
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Component of the I-kappa-B-
CC       kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG;
CC       probably four alpha/CHUK-beta/IKBKB dimers are associated with
CC       four gamma/IKBKG subunits. The IKK core complex seems to associate
CC       with regulatory or adapter proteins to form a IKK-signalosome
CC       holo-complex. The IKK complex associates with TERF2IP/RAP1,
CC       leading to promote IKK-mediated phosphorylation of RELA/p65. Part
CC       of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and
CC       CREBBP. Interacts with COPS3, CYLD, NALP2, TRPC4AP and LRDD.
CC       Interacts with ATM; the complex is exported from the nucleus.
CC       Interacts with TRAF6. Interacts with TANK; the interaction is
CC       enhanced by IKBKE and TBK1. Part of a ternary complex consisting
CC       of TANK, IKBKB and IKBKG (By similarity). Interacts with ZFAND5
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- DOMAIN: The leucine-zipper domain and the C2HC-type zinc-finger
CC       are essential for polyubiquitin binding and for the activation of
CC       IRF3 (By similarity).
CC   -!- PTM: Phosphorylation at Ser-68 attenuates aminoterminal
CC       homodimerization (By similarity).
CC   -!- PTM: Polyubiquitinated on Lys-278 through 'Lys-63'; the
CC       ubiquitination is mediated by NOD2 and RIPK2 and probably plays a
CC       role in signaling by facilitating interactions with ubiquitin
CC       domain-containing proteins and activates the NF-kappa-B
CC       pathway.Polyubiquitinated on Lys-392 through 'Lys-63'; the
CC       ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably
CC       plays a role in signaling by facilitating interactions with
CC       ubiquitin domain-containing proteins and activates the NF-kappa-B
CC       pathway. Monoubiquitinated on Lys-270 and Lys-302; promotes
CC       nuclear export. Linear polyubiquitinated on Lys-111, Lys-143, Lys-
CC       226, Lys-246, Lys-270, Lys-278, Lys-285, Lys-295, Lys-302 and Lys-
CC       319; the head-to-tail polyubiquitination is mediated by the LUBAC
CC       complex and plays a key role in NF-kappa-B activation (By
CC       similarity).
CC   -!- PTM: Sumoylated on Lys-270 and Lys-302 by SUMO1; the modification
CC       results in phosphorylation of Ser-85 by ATM leading to a
CC       replacement of the sumoylation by mono-ubiquitination on these
CC       residues (By similarity).
CC   -!- SIMILARITY: Contains 1 C2HC-type zinc finger.
CC   -!- GENE_FAMILY: HOG000293233 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000037237;ENSRNOT00000056275;ENSRNOP00000053114.
DR   EMBL; AY392762; - ;
DR   UniProtKB/Swiss-Prot; Q6TMG5; -.
DR   EMBL; AY392762; AAQ94056.1; -; mRNA.
DR   IPI; IPI00400576; -.
DR   RefSeq; NP_954534.1; NM_199103.1.
DR   UniGene; Rn.214715; -.
DR   ProteinModelPortal; Q6TMG5; -.
DR   SMR; Q6TMG5; 49-109, 193-248, 387-412.
DR   STRING; Q6TMG5; -.
DR   GeneID; 309295; -.
DR   KEGG; rno:309295; -.
DR   CTD; 8517; -.
DR   RGD; 735223; Ikbkg.
DR   eggNOG; roNOG09128; -.
DR   GeneTree; ENSGT00530000063808; -.
DR   InParanoid; Q6TMG5; -.
DR   OrthoDB; EOG42BX8V; -.
DR   NextBio; 660548; -.
DR   Genevestigator; Q6TMG5; -.
DR   GO; GO:0008385; C:IkappaB kinase complex; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042348; P:NF-kappaB import into nucleus; TAS:RGD.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:RGD.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR021063; NEMO_N.
DR   Pfam; PF11577; NEMO; 1.
DR   HOGENOMDNA; RATX.PE1364; -.
KW   ENSRNOG00000037237820036002503210000011;
KW   Ikbkg; NEMO_RAT; AY392762;
KW   Coiled coil; Complete proteome; Cytoplasm; Disulfide bond;
KW   Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
SQ   SEQUENCE   350 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     DAIRQSNQML RERCEELLHF QVSQREEKEF LMCKFQEARK LVERLSLEKL DLRRQREQAL
     EDLEHLKKCQ QQMAEDKASV KAQVTSLLGE LQESQSRLEA ATKERQTLEG RIRAVSEQVR
     QLESEREVLQ QQHSVQVDQL RMQNQSVEAA LRMERQAASE EKRKLAQLQA AYHQLFQDYD
     SHIKSSKGMQ LEDLRQQLQQ AEEALVAKQE LIDKLKEEAE QHKIVMETVP VLKAQADIYK
     ADFQAERHAR EKLVERKELL QEQLEQLQRE FNKLKVGCHE SARIEDMRKR HVETSQPPLL
     PAPAHHSFHL ALSNQRRSPP EEPPDFCCPK CQYQAPDMDT LQIHVMECIE
//

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