Nuclear factor NF-kappa-B p100 subunit

Sequence length	900 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Function	NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. Ref.12
Subunit structure	Component of the NF-kappa-B RelB-p52 complex. Homodimer; component of the NF-kappa-B p52-p52 complex. Component of the NF-kappa-B p65-p52 complex. Component of the NF-kappa-B p52-c-Rel complex. NFKB2/p52 interacts with NFKBIE. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Ref.14 Ref.16
Subcellular location	Nucleus. Cytoplasm. Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).
Domain	The C-terminus of p100 might be involved in cytoplasmic retention, inhibition of DNA-binding by p52 homodimers, and/or transcription activation By similarity. The glycine-rich region (GRR) appears to be a critical element in the generation of p52.
Post-translational modification	While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p52 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing. Subsequent to MAP3K14-dependent serine phosphorylation, p100 polyubiquitination occurs then triggering its proteasome-dependent processing. Constitutive processing is tightly suppressed by its C-terminal processing inhibitory domain, named PID, which contains the death domain.
Involvement in disease	A chromosomal aberration involving NFKB2 is found in a case of B-cell non Hodgkin lymphoma (B-NHL). Translocation t(10;14)(q24;q32) with IGHA1. The resulting oncogene is also called Lyt-10C alpha variant. A chromosomal aberration involving NFKB2 is found in a cutaneous T-cell leukemia (C-TCL) cell line. This rearrangement produces the p80HT gene which encodes for a truncated 80 kDa protein (p80HT). In B-cell leukemia (B-CLL) cell line, LB40 and EB308, can be found after heterogeneous chromosomal aberrations, such as internal deletions.
Sequence similarities	Contains 7 ANK repeats. Contains 1 death domain. Contains 1 RHD (Rel-like) domain.
Sequence caution	The sequence CAA43715.1 differs from that shown. Reason: Frameshift at positions 455, 470 and 899.

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation Proto-oncogene
Domain	ANK repeat Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Ref.10 Inferred from direct assay. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Bcl3/NF-kappaB2 complex Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	transcription coactivator activity Ref.1 Traceable author statement. Source: ProtInc transcription factor activity Ref.1 Ref.18 Traceable author statement. Source: ProtInc
Complete GO annotation...

With	Entry	#Exp.	IntAct	Notes
COMMD1	Q8N668	1	EBI-307345,EBI-1550112

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 900

900

Nuclear factor NF-kappa-B p100 subunit

PRO_0000030321

Chain

1 – 454

454

Nuclear factor NF-kappa-B p52 subunit

PRO_0000030322

Domain

38 – 343

306

RHD

Repeat

487 – 519

33

ANK 1

Repeat

526 – 555

30

ANK 2

Repeat

559 – 591

33

ANK 3

Repeat

599 – 628

30

ANK 4

Repeat

633 – 663

31

ANK 5

Repeat

667 – 696

30

ANK 6

Repeat

729 – 758

30

ANK 7

Domain

764 – 851

88

Death

Region

346 – 377

32

GRR

Motif

337 – 341

5

Nuclear localization signal Potential

Compositional bias

350 – 400

51

Gly-rich

Site

454 – 455

2

Cleavage (when cotranslationally processed)

Site

490 – 491

2

Breakpoint for translocation to form NFKB2-IGHA1 oncogene

Modified residue

429

1

Phosphothreonine Ref.23

Modified residue

713

1

Phosphoserine Ref.16

Modified residue

715

1

Phosphoserine Ref.16

Modified residue

717

1

Phosphoserine Ref.16

Modified residue

866

1

Phosphoserine; by MAP3K14 Ref.17

Modified residue

870

1

Phosphoserine; by MAP3K14 Ref.17

Cross-link

855

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21

Alternative sequence

374 – 403

30

GSLGF…PGGGG → EGVLMEGGVKVREAVEEKNL GEAGRGGSRL in isoform 2.

VSP_005585

Alternative sequence

404 – 900

497

Missing in isoform 2.

VSP_005586

Natural variant

14

1

E → K Ref.6

VAR_022223

Natural variant

351

1

G → R Ref.6

VAR_022224

Natural variant

392

1

A → G: dbSNP rs11574848.

VAR_051781

Natural variant

452

1

G → R Ref.6

VAR_022225

Natural variant

618 – 900

283

Missing in truncated form EB308.

VAR_018452

Natural variant

667 – 669

3

AGN → SAS in truncated form p80HT.

VAR_006909

Natural variant

670 – 900

231

Missing in truncated form p80HT.

VAR_006910

Natural variant

703 – 900

198

Missing in truncated form LB40.

VAR_018453

Mutagenesis

247 – 249

3

YLL → AAA: Two-fold reduction in heterodimerization with RelA.

Mutagenesis

399

1

P → A: No change in cleavage rate or products.

Mutagenesis

404

1

G → A: No change in cleavage rate or products.

Mutagenesis

405

1

A → P: No change in cleavage rate or products.

Mutagenesis

406

1

Q → N: No change in cleavage rate or products.

Mutagenesis

713

1

S → G: Loss of phosphorylation; when associated with A-715 and A-717.

Mutagenesis

715

1

S → A: Loss of phosphorylation; when associated with G-713 and A-717.

Mutagenesis

717

1

S → A: Loss of phosphorylation; when associated with G-713 and A-715.

Mutagenesis

866

1

S → A: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-869. Ref.17

Mutagenesis

870

1

S → A: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-865. Ref.17

Sequence conflict

144

1

K → E in AAB21124. Ref.2

Sequence conflict

213

1

I → T Ref.1

Sequence conflict

213

1

I → T Ref.3

Sequence conflict

213

1

I → T Ref.9

Sequence conflict

396

1

G → R Ref.1

Sequence conflict

396

1

G → R Ref.3

Sequence conflict

433 – 434

2

EP → DA in AAB21124. Ref.2

Sequence conflict

459

1

R → K AA sequence Ref.10

Sequence conflict

470

1

A → R in AAB21124. Ref.2

Sequence conflict

741

1

K → L in CAA43715. Ref.1

Sequence conflict

1

A → T in AAB21124. Ref.2

Sequence conflict

1

Missing in CAA43715. Ref.1

Sequence conflict

1

Missing in AAP88771. Ref.5

Sequence conflict

1

Missing in AAH02844. Ref.8

Sequence conflict

876

1

E → K in AAB21124. Ref.2

Sequence conflict

891

1

C → S in CAA43715. Ref.1

1

.

900

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform 1 (p100) [UniParc]. Last modified October 17, 2006. Version 4. Checksum: 6BAD7038834783CA Show »	FASTA	900	96,749
10 20 30 40 50 60 MESCYNPGLD GIIEYDDFKL NSSIVEPKEP APETADGPYL VIVEQPKQRG FRFRYGCEGP 70 80 90 100 110 120 SHGGLPGASS EKGRKTYPTV KICNYEGPAK IEVDLVTHSD PPRAHAHSLV GKQCSELGIC 130 140 150 160 170 180 AVSVGPKDMT AQFNNLGVLH VTKKNMMGTM IQKLQRQRLR SRPQGLTEAE QRELEQEAKE 190 200 210 220 230 240 LKKVMDLSIV RLRFSAFLRA SDGSFSLPLK PVISQPIHDS KSPGASNLKI SRMDKTAGSV 250 260 270 280 290 300 RGGDEVYLLC DKVQKDDIEV RFYEDDENGW QAFGDFSPTD VHKQYAIVFR TPPYHKMKIE 310 320 330 340 350 360 RPVTVFLQLK RKRGGDVSDS KQFTYYPLVE DKEEVQRKRR KALPTFSQPF GGGSHMGGGS 370 380 390 400 410 420 GGAAGGYGGA GGGGSLGFFP SSLAYSPYQS GAGPMGCYPG GGGGAQMAAT VPSRDSGEEA 430 440 450 460 470 480 AEPSAPSRTP QCEPQAPEML QRAREYNARL FGLAQRSARA LLDYGVTADA RALLAGQRHL 490 500 510 520 530 540 LTAQDENGDT PLHLAIIHGQ TSVIEQIVYV IHHAQDLGVV NLTNHLHQTP LHLAVITGQT 550 560 570 580 590 600 SVVSFLLRVG ADPALLDRHG DSAMHLALRA GAGAPELLRA LLQSGAPAVP QLLHMPDFEG 610 620 630 640 650 660 LYPVHLAVRA RSPECLDLLV DSGAEVEATE RQGGRTALHL ATEMEELGLV THLVTKLRAN 670 680 690 700 710 720 VNARTFAGNT PLHLAAGLGY PTLTRLLLKA GADIHAENEE PLCPLPSPPT SDSDSDSEGP 730 740 750 760 770 780 EKDTRSSFRG HTPLDLTCST KVKTLLLNAA QNTMEPPLTP PSPAGPGLSL GDTALQNLEQ 790 800 810 820 830 840 LLDGPEAQGS WAELAERLGL RSLVDTYRQT TSPSGSLLRS YELAGGDLAG LLEALSDMGL 850 860 870 880 890 900 EEGVRLLRGP ETRDKLPSTA EVKEDSAYGS QSVEQEAEKL GPPPEPPGGL CHGHPQPQVH « Hide
Isoform 2 (p49). Checksum: E6F7E2102EB686E5 Show »	FASTA	403	44,253
10 20 30 40 50 60 MESCYNPGLD GIIEYDDFKL NSSIVEPKEP APETADGPYL VIVEQPKQRG FRFRYGCEGP 70 80 90 100 110 120 SHGGLPGASS EKGRKTYPTV KICNYEGPAK IEVDLVTHSD PPRAHAHSLV GKQCSELGIC 130 140 150 160 170 180 AVSVGPKDMT AQFNNLGVLH VTKKNMMGTM IQKLQRQRLR SRPQGLTEAE QRELEQEAKE 190 200 210 220 230 240 LKKVMDLSIV RLRFSAFLRA SDGSFSLPLK PVISQPIHDS KSPGASNLKI SRMDKTAGSV 250 260 270 280 290 300 RGGDEVYLLC DKVQKDDIEV RFYEDDENGW QAFGDFSPTD VHKQYAIVFR TPPYHKMKIE 310 320 330 340 350 360 RPVTVFLQLK RKRGGDVSDS KQFTYYPLVE DKEEVQRKRR KALPTFSQPF GGGSHMGGGS 370 380 390 400 GGAAGGYGGA GGGEGVLMEG GVKVREAVEE KNLGEAGRGG SRL « Hide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of an NF-kappa B subunit which stimulates HIV transcription in synergy with p65." Schmid R.M., Perkins N.D., Duckett C.S., Andrews P.C., Nabel G.J. Nature 352:733-736(1991) [PubMed: 1876189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Leukemia.
[2]	"A novel mitogen-inducible gene product related to p50/p105-NF-kappa B participates in transactivation through a kappa B site." Bours V., Burd P.R., Brown K., Villalobos J., Park S., Ryseck R.P., Bravo R., Kelly K., Siebenlist U. Mol. Cell. Biol. 12:685-695(1992) [PubMed: 1531086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Rearrangement and altered expression of the NFKB-2 gene in human cutaneous T-lymphoma cells." Thakur S., Lin H.C., Tseng W.T., Kumar S., Bravo R., Foss F., Gelinas C., Rabson A.B. Oncogene 9:2335-2344(1994) [PubMed: 8036016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION, P80HT GENERATION.
[4]	Rabson A.B. Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	NIEHS SNPs program Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-14; ARG-351 AND ARG-452.
[7]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lymph.
[9]	"Transcriptional regulation of NF-kappa B2: evidence for kappa B-mediated positive and negative autoregulation." Liptay S., Schmid R.M., Nabel E.G., Nabel G.J. Mol. Cell. Biol. 14:7695-7703(1994) [PubMed: 7969113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-220.
[10]	"Purification of the major histocompatibility complex class I transcription factor H2TF1. The full-length product of the nfkb2 gene." Potter D.A., Larson C.J., Eckes P., Schmid R.M., Nabel G.J., Verdine G.L., Sharp P.A. J. Biol. Chem. 268:18882-18890(1993) [PubMed: 8360178] [Abstract] Cited for: PROTEIN SEQUENCE OF 459-470; 580-597 AND 636-647 (ISOFORM 1).
[11]	"The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers." Bours V., Franzoso G., Azarenko V., Park S., Kanno T., Brown K., Siebenlist U. Cell 72:729-739(1993) [PubMed: 8453667] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH BCL3.
[12]	"Differential interactions of Rel-NF-kappa B complexes with I kappa B alpha determine pools of constitutive and inducible NF-kappa B activity." Dobrzanski P., Ryseck R.P., Bravo R. EMBO J. 13:4608-4616(1994) [PubMed: 7925301] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
[13]	"Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor necrosis factor." Beg A.A., Baldwin A.S. Jr. Oncogene 9:1487-1492(1994) [PubMed: 8152812] [Abstract] Cited for: IDENTIFICATION IN THE NF-KAPPA-B P52-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
[14]	"A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription." Li Z., Nabel G.J. Mol. Cell. Biol. 17:6184-6190(1997) [PubMed: 9315679] [Abstract] Cited for: INTERACTION WITH NFKBIE.
[15]	"The generation of nfkb2 p52: mechanism and efficiency." Heusch M., Lin L., Geleziunas R., Greene W.C. Oncogene 18:6201-6208(1999) [PubMed: 10597218] [Abstract] Cited for: COTRANSLATIONAL FOLDING/PROCESSING OF P100, GENERATION OF P52/P100.
[16]	"Differential regulation of NF-kappaB2(p100) processing and control by amino-terminal sequences." Betts J.C., Nabel G.J. Mol. Cell. Biol. 16:6363-6371(1996) [PubMed: 8887665] [Abstract] Cited for: PHOSPHORYLATION AT SER-713; SER-715 AND SER-717, MUTAGENESIS, DIMERIZATION, PROTEOLYTIC PROCESSING OF P100.
[17]	"NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100." Xiao G., Harhaj E.W., Sun S.-C. Mol. Cell 7:401-409(2001) [PubMed: 11239468] [Abstract] Cited for: PHOSPHORYLATION AT SER-866 AND SER-870, MUTAGENESIS OF SER-866 AND SER-870, PROTEOLYTIC PROCESSING OF P100.
[18]	"B cell lymphoma-associated chromosomal translocation involves candidate oncogene lyt-10, homologous to NF-kappa B p50." Neri A., Chang C.C., Lombardi L., Salina M., Corradini P., Maiolo A.T., Chaganti R.S., Dalla-Favera R. Cell 67:1075-1087(1991) [PubMed: 1760839] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH IGHA1.
[19]	"Heterogeneous chromosomal aberrations generate 3' truncations of the NFKB2/lyt-10 gene in lymphoid malignancies." Migliazza A., Lombardi L., Rocchi M., Trecca D., Chang C.-C., Antonacci R., Fracchiolla N.S., Ciana P., Maiolo A.T., Neri A. Blood 84:3850-3860(1994) [PubMed: 7949142] [Abstract] Cited for: CHROMOSOMAL ABERRATIONS, GENERATION OF LB40 AND EB308.
[20]	"Structural and functional characterization of the promoter regions of the NFKB2 gene." Lombardi L., Ciana P., Cappellini C., Trecca D., Guerrini L., Migliazza A., Maiolo A.T., Neri A. Nucleic Acids Res. 23:2328-2336(1995) [PubMed: 7541912] [Abstract] Cited for: CHARACTERIZATION OF THE TWO PROMOTER REGIONS.
[21]	"Mechanism of processing of the NF-kappa B2 p100 precursor: identification of the specific polyubiquitin chain-anchoring lysine residue and analysis of the role of NEDD8-modification on the SCF(beta-TrCP) ubiquitin ligase." Amir R.E., Haecker H., Karin M., Ciechanover A. Oncogene 23:2540-2547(2004) [PubMed: 14676825] [Abstract] Cited for: UBIQUITINATION AT LYS-855.
[22]	"IL-1 receptor-associated kinase 1 is critical for latent membrane protein 1-induced p65/RelA serine 536 phosphorylation and NF-kappaB activation." Song Y.J., Jen K.Y., Soni V., Kieff E., Cahir-McFarland E. Proc. Natl. Acad. Sci. U.S.A. 103:2689-2694(2006) [PubMed: 16477006] [Abstract] Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
[23]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429, MASS SPECTROMETRY.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[25]	"Structure of the human NF-kappaB p52 homodimer-DNA complex at 2.1-A resolution." Cramer P., Larson C.J., Verdine G.L., Mueller C.W. EMBO J. 16:7078-7090(1997) [PubMed: 9384586] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 37-327.
[26]	"Solution structure of the death domain of nuclear factor NF-kappa-B p100." RIKEN structural genomics initiative (RSGI) Submitted (DEC-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 764-859.
+	Additional computationally mapped references.

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

X61498 mRNA. Translation: CAA43715.1. Frameshift.
X61499 mRNA. Translation: CAA43716.1. Sequence problems.
S76638 mRNA. Translation: AAB21124.1.
U09609 mRNA. Translation: AAA21462.2.
BT009769 mRNA. Translation: AAP88771.1.
AY865619 Genomic DNA. Translation: AAW56071.1.
AL121928 Genomic DNA. Translation: CAC08399.1.
BC002844 mRNA. Translation: AAH02844.1.
U20816 Genomic DNA. Translation: AAA68171.1.

IPI

IPI00411715.
IPI00845373.

PIR

A42024.
A57034.
I38609.
S17233.

RefSeq

NP_001070961.1.
NP_001070962.1.
NP_002493.3.

UniGene

Hs.73090

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A3Q	X-ray	2.10	A/B	37-327	[»]
2D96	NMR	-	A	766-859	[»]

ModBase

DIP

DIP:24239N.
DIP:27535N.

IntAct

Q00653. 171 interactions.

PhosphoSite

Q00653.

PRIDE

Q00653.

Ensembl

ENSG00000077150. Homo sapiens. [Contig view]

GeneID

4791.

KEGG

hsa:4791.

GeneCards

GC10P104144.

H-InvDB

HIX0009155.

HGNC

HGNC:7795. NFKB2.

HPA

HPA008422.

MIM

164012. gene.

PharmGKB

PA31600.

GenAtlas

HOVERGEN

Q00653.

OMA

Q00653. QTSVVSF.

Pathway_Interaction_DB

nfkappabalternativepathway. Alternative NF-kappaB pathway.
il12_2pathway. IL12-mediated signaling events.

Reactome

REACT_6900. Signaling in Immune system.

ArrayExpress

Q00653.

Bgee

Q00653.

CleanEx

HS_NFKB2.

GermOnline

ENSG00000077150. Homo sapiens.

InterPro

IPR002110. ANK.
IPR000488. Death.
IPR011029. DEATH-like.
IPR013783. Ig-like_fold.
IPR002909. IPT_TIG_rcpt.
IPR015682. NF-kappaB_related2.
IPR000451. NF_Rel_dor.
IPR011539. RHD.
[Graphical view]

Gene3D

G3DSA:1.25.40.20. ANK. 1 hit.
G3DSA:1.10.533.10. DEATH_like. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:2.60.40.340. RHD. 1 hit.

PANTHER

PTHR18958:SF244. NF_kB_related2. 1 hit.

Pfam

PF00023. Ank. 6 hits.
PF00531. Death. 1 hit.
PF00554. RHD. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]

PRINTS

PR00057. NFKBTNSCPFCT.

SMART

SM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50017. DEATH_DOMAIN. False negative.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

ProtoNet

NextBio

18458.

PMAP-CutDB

Q00653.

SOURCE