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Q00653

- NFKB2_HUMAN

UniProt

Q00653 - NFKB2_HUMAN

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Protein
Nuclear factor NF-kappa-B p100 subunit
Gene
NFKB2, LYT10
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes 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 p65.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei454 – 4552Cleavage (when cotranslationally processed)
Sitei490 – 4912Breakpoint for translocation to form NFKB2-IGHA1 oncogene

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. protein binding Source: BHF-UCL
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc
  4. transcription coactivator activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  2. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  3. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  4. extracellular matrix organization Source: Ensembl
  5. follicular dendritic cell differentiation Source: Ensembl
  6. germinal center formation Source: Ensembl
  7. innate immune response Source: Reactome
  8. positive regulation of NF-kappaB transcription factor activity Source: Reactome
  9. positive regulation of type I interferon production Source: Reactome
  10. regulation of transcription, DNA-templated Source: UniProtKB
  11. spleen development Source: Ensembl
  12. toll-like receptor 10 signaling pathway Source: Reactome
  13. toll-like receptor 2 signaling pathway Source: Reactome
  14. toll-like receptor 3 signaling pathway Source: Reactome
  15. toll-like receptor 4 signaling pathway Source: Reactome
  16. toll-like receptor 5 signaling pathway Source: Reactome
  17. toll-like receptor 9 signaling pathway Source: Reactome
  18. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  19. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  20. toll-like receptor signaling pathway Source: Reactome
  21. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_23950. Interleukin-1 processing.
REACT_24969. TRAF6 mediated NF-kB activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor NF-kappa-B p100 subunit
Alternative name(s):
DNA-binding factor KBF2
H2TF1
Lymphocyte translocation chromosome 10 protein
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2
Oncogene Lyt-10
Short name:
Lyt10
Cleaved into the following chain:
Gene namesi
Name:NFKB2
Synonyms:LYT10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:7795. NFKB2.

Subcellular locationi

Nucleus. Cytoplasm
Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).

GO - Cellular componenti

  1. Bcl3/NF-kappaB2 complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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 codes 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.
Immunodeficiency, common variable, 10 (CVID10) [MIM:615577]: A primary immunodeficiency characterized by childhood-onset of recurrent infections, hypogammaglobulinemia, and decreased numbers of memory and marginal zone B-cells. Some patients may develop autoimmune features and have circulating autoantibodies. An unusual feature is central adrenal insufficiency.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi247 – 2493YLL → AAA: Two-fold reduction in heterodimerization with RelA.
Mutagenesisi399 – 3991P → A: No change in cleavage rate or products.
Mutagenesisi404 – 4041G → A: No change in cleavage rate or products.
Mutagenesisi405 – 4051A → P: No change in cleavage rate or products.
Mutagenesisi406 – 4061Q → N: No change in cleavage rate or products.
Mutagenesisi713 – 7131S → G: Loss of phosphorylation; when associated with A-715 and A-717.
Mutagenesisi715 – 7151S → A: Loss of phosphorylation; when associated with G-713 and A-717.
Mutagenesisi717 – 7171S → A: Loss of phosphorylation; when associated with G-713 and A-715.
Mutagenesisi866 – 8661S → A: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-869. 1 Publication
Mutagenesisi870 – 8701S → A: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-865. 1 Publication

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

MIMi615577. phenotype.
Orphaneti1572. Common variable immunodeficiency.
PharmGKBiPA31600.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 900900Nuclear factor NF-kappa-B p100 subunit
PRO_0000030321Add
BLAST
Chaini1 – 454454Nuclear factor NF-kappa-B p52 subunit
PRO_0000030322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei429 – 4291Phosphothreonine1 Publication
Modified residuei713 – 7131Phosphoserine1 Publication
Modified residuei715 – 7151Phosphoserine1 Publication
Modified residuei717 – 7171Phosphoserine1 Publication
Cross-linki855 – 855Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei866 – 8661Phosphoserine; by MAP3K141 Publication
Modified residuei870 – 8701Phosphoserine; by MAP3K141 Publication

Post-translational modificationi

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.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ00653.
PaxDbiQ00653.
PRIDEiQ00653.

PTM databases

PhosphoSiteiQ00653.

Miscellaneous databases

PMAP-CutDBQ00653.

Expressioni

Gene expression databases

ArrayExpressiQ00653.
BgeeiQ00653.
CleanExiHS_NFKB2.
GenevestigatoriQ00653.

Organism-specific databases

HPAiCAB022098.
HPA008422.
HPA023900.

Interactioni

Subunit structurei

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. Directly interacts with MEN1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NFKB1P198384EBI-307326,EBI-300010
RELQ048643EBI-307326,EBI-307352
RELBQ012013EBI-307326,EBI-357837
SUMO1P631652EBI-307326,EBI-80140

Protein-protein interaction databases

BioGridi110858. 48 interactions.
DIPiDIP-24239N.
DIP-27535N.
IntActiQ00653. 30 interactions.
MINTiMINT-7944680.
STRINGi9606.ENSP00000189444.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 446
Beta strandi48 – 514
Turni56 – 583
Beta strandi79 – 835
Beta strandi87 – 9610
Beta strandi98 – 1014
Beta strandi106 – 1116
Beta strandi116 – 1183
Beta strandi120 – 1245
Beta strandi130 – 1323
Beta strandi136 – 1405
Turni143 – 1453
Helixi146 – 15813
Turni159 – 1613
Helixi168 – 18215
Beta strandi189 – 19810
Beta strandi205 – 2073
Beta strandi217 – 2193
Beta strandi220 – 2223
Turni223 – 2253
Beta strandi230 – 2345
Beta strandi236 – 2394
Beta strandi240 – 2423
Beta strandi245 – 2528
Turni255 – 2573
Beta strandi258 – 2647
Beta strandi266 – 2683
Beta strandi270 – 2734
Helixi278 – 2803
Turni283 – 2853
Beta strandi286 – 2905
Beta strandi303 – 3119
Turni312 – 3143
Beta strandi321 – 3266
Helixi772 – 78211
Beta strandi783 – 7864
Helixi791 – 7988
Helixi801 – 8088
Helixi813 – 82311
Helixi828 – 83811
Helixi841 – 8488

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3QX-ray2.10A/B37-327[»]
2D96NMR-A766-859[»]
3DO7X-ray3.05B37-329[»]
ProteinModelPortaliQ00653.
SMRiQ00653. Positions 37-329, 434-752, 772-859.

Miscellaneous databases

EvolutionaryTraceiQ00653.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 343306RHD
Add
BLAST
Repeati487 – 51933ANK 1
Add
BLAST
Repeati526 – 55530ANK 2
Add
BLAST
Repeati559 – 59133ANK 3
Add
BLAST
Repeati599 – 62830ANK 4
Add
BLAST
Repeati633 – 66331ANK 5
Add
BLAST
Repeati667 – 69630ANK 6
Add
BLAST
Repeati729 – 75830ANK 7
Add
BLAST
Domaini764 – 85188Death
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni346 – 37732GRR
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi337 – 3415Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi350 – 40051Gly-rich
Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 7 ANK repeats.
Contains 1 death domain.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000004822.
HOVERGENiHBG052613.
InParanoidiQ00653.
KOiK04469.
OMAiFRGHTPL.
OrthoDBiEOG7W154S.
PhylomeDBiQ00653.
TreeFamiTF325632.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamiPF00023. Ank. 5 hits.
PF00531. Death. 1 hit.
PF00554. RHD. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR00057. NFKBTNSCPFCT.
SMARTiSM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q00653-1) [UniParc]FASTAAdd to Basket

Also known as: p100

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MESCYNPGLD GIIEYDDFKL NSSIVEPKEP APETADGPYL VIVEQPKQRG    50
FRFRYGCEGP SHGGLPGASS EKGRKTYPTV KICNYEGPAK IEVDLVTHSD 100
PPRAHAHSLV GKQCSELGIC AVSVGPKDMT AQFNNLGVLH VTKKNMMGTM 150
IQKLQRQRLR SRPQGLTEAE QRELEQEAKE LKKVMDLSIV RLRFSAFLRA 200
SDGSFSLPLK PVISQPIHDS KSPGASNLKI SRMDKTAGSV RGGDEVYLLC 250
DKVQKDDIEV RFYEDDENGW QAFGDFSPTD VHKQYAIVFR TPPYHKMKIE 300
RPVTVFLQLK RKRGGDVSDS KQFTYYPLVE DKEEVQRKRR KALPTFSQPF 350
GGGSHMGGGS GGAAGGYGGA GGGGSLGFFP SSLAYSPYQS GAGPMGCYPG 400
GGGGAQMAAT VPSRDSGEEA AEPSAPSRTP QCEPQAPEML QRAREYNARL 450
FGLAQRSARA LLDYGVTADA RALLAGQRHL LTAQDENGDT PLHLAIIHGQ 500
TSVIEQIVYV IHHAQDLGVV NLTNHLHQTP LHLAVITGQT SVVSFLLRVG 550
ADPALLDRHG DSAMHLALRA GAGAPELLRA LLQSGAPAVP QLLHMPDFEG 600
LYPVHLAVRA RSPECLDLLV DSGAEVEATE RQGGRTALHL ATEMEELGLV 650
THLVTKLRAN VNARTFAGNT PLHLAAGLGY PTLTRLLLKA GADIHAENEE 700
PLCPLPSPPT SDSDSDSEGP EKDTRSSFRG HTPLDLTCST KVKTLLLNAA 750
QNTMEPPLTP PSPAGPGLSL GDTALQNLEQ LLDGPEAQGS WAELAERLGL 800
RSLVDTYRQT TSPSGSLLRS YELAGGDLAG LLEALSDMGL EEGVRLLRGP 850
ETRDKLPSTA EVKEDSAYGS QSVEQEAEKL GPPPEPPGGL CHGHPQPQVH 900
Length:900
Mass (Da):96,749
Last modified:October 17, 2006 - v4
Checksum:i6BAD7038834783CA
GO
Isoform 3 (identifier: Q00653-3) [UniParc]FASTAAdd to Basket

Also known as: p49

The sequence of this isoform differs from the canonical sequence as follows:
     374-428: GSLGFFPSSL...EAAEPSAPSR → EGVLMEGGVK...RSSRPAWPTA
     429-900: Missing.

Note: Ref.1 (CAA43716.1) sequence(s) differ(s) from that shown due to frameshifts in positions 407, 414.

Show »
Length:428
Mass (Da):47,021
Checksum:iE4D38A8635501807
GO
Isoform 4 (identifier: Q00653-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     860-860: Missing.

Show »
Length:899
Mass (Da):96,678
Checksum:iB3753FF15B7BDF57
GO

Sequence cautioni

The sequence CAA43715.1 differs from that shown. Reason: Frameshift at positions 456, 458, 470 and 900.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141E → K.1 Publication
Corresponds to variant rs45581936 [ dbSNP | Ensembl ].
VAR_022223
Natural varianti351 – 3511G → R.1 Publication
Corresponds to variant rs45580031 [ dbSNP | Ensembl ].
VAR_022224
Natural varianti392 – 3921A → G.
Corresponds to variant rs11574848 [ dbSNP | Ensembl ].
VAR_051781
Natural varianti452 – 4521G → R.1 Publication
Corresponds to variant rs45471103 [ dbSNP | Ensembl ].
VAR_022225
Natural varianti618 – 900283Missing in truncated form EB308.
VAR_018452Add
BLAST
Natural varianti667 – 6693AGN → SAS in truncated form p80HT.
VAR_006909
Natural varianti670 – 900231Missing in truncated form p80HT.
VAR_006910Add
BLAST
Natural varianti703 – 900198Missing in truncated form LB40.
VAR_018453Add
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei374 – 42855GSLGF…SAPSR → EGVLMEGGVKVREAVEEKNL GEAGRGLHACNPALWEAKAG RLPEIRSSRPAWPTA in isoform 3.
VSP_040082Add
BLAST
Alternative sequencei429 – 900472Missing in isoform 3.
VSP_040083Add
BLAST
Alternative sequencei860 – 8601Missing in isoform 4.
VSP_040084

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441K → E in AAB21124. 1 Publication
Sequence conflicti213 – 2131I → T in CAA43715. 1 Publication
Sequence conflicti213 – 2131I → T in CAA43716. 1 Publication
Sequence conflicti213 – 2131I → T in AAA68171. 1 Publication
Sequence conflicti396 – 3961G → R in CAA43715. 1 Publication
Sequence conflicti433 – 4342EP → DA in AAB21124. 1 Publication
Sequence conflicti459 – 4591R → K AA sequence 1 Publication
Sequence conflicti465 – 4651G → C in CAA43715. 1 Publication
Sequence conflicti470 – 4701A → R in CAA43715. 1 Publication
Sequence conflicti470 – 4701A → R in AAB21124. 1 Publication
Sequence conflicti741 – 7411K → L in CAA43715. 1 Publication
Sequence conflicti860 – 8601A → T in AAB21124. 1 Publication
Sequence conflicti876 – 8761E → K in AAB21124. 1 Publication
Sequence conflicti891 – 8911C → S in CAA43715. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61498 mRNA. Translation: CAA43715.1. Frameshift.
X61499 mRNA. Translation: CAA43716.1. Frameshift.
S76638 mRNA. Translation: AAB21124.1.
U09609 mRNA. Translation: AAA21462.2.
BT009769 mRNA. Translation: AAP88771.1.
AK292654 mRNA. Translation: BAF85343.1.
AY865619 Genomic DNA. Translation: AAW56071.1.
AL121928 Genomic DNA. Translation: CAC08399.1.
CH471066 Genomic DNA. Translation: EAW49700.1.
CH471066 Genomic DNA. Translation: EAW49701.1.
CH471066 Genomic DNA. Translation: EAW49702.1.
CH471066 Genomic DNA. Translation: EAW49704.1.
CH471066 Genomic DNA. Translation: EAW49706.1.
BC002844 mRNA. Translation: AAH02844.1.
U20816 Genomic DNA. Translation: AAA68171.1.
CCDSiCCDS41564.1. [Q00653-1]
CCDS41565.1. [Q00653-4]
PIRiA42024.
A57034.
I38609.
S17233.
RefSeqiNP_001070962.1. NM_001077494.3. [Q00653-1]
NP_001248332.1. NM_001261403.2. [Q00653-4]
NP_001275653.1. NM_001288724.1. [Q00653-4]
NP_002493.3. NM_002502.5. [Q00653-4]
XP_005269917.1. XM_005269860.1. [Q00653-1]
XP_005269918.1. XM_005269861.2. [Q00653-1]
UniGeneiHs.73090.

Genome annotation databases

EnsembliENST00000189444; ENSP00000189444; ENSG00000077150. [Q00653-4]
ENST00000369966; ENSP00000358983; ENSG00000077150. [Q00653-1]
ENST00000428099; ENSP00000410256; ENSG00000077150. [Q00653-4]
GeneIDi4791.
KEGGihsa:4791.
UCSCiuc001kva.4. human. [Q00653-4]
uc001kvb.4. human. [Q00653-1]

Polymorphism databases

DMDMi116242678.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61498 mRNA. Translation: CAA43715.1 . Frameshift.
X61499 mRNA. Translation: CAA43716.1 . Frameshift.
S76638 mRNA. Translation: AAB21124.1 .
U09609 mRNA. Translation: AAA21462.2 .
BT009769 mRNA. Translation: AAP88771.1 .
AK292654 mRNA. Translation: BAF85343.1 .
AY865619 Genomic DNA. Translation: AAW56071.1 .
AL121928 Genomic DNA. Translation: CAC08399.1 .
CH471066 Genomic DNA. Translation: EAW49700.1 .
CH471066 Genomic DNA. Translation: EAW49701.1 .
CH471066 Genomic DNA. Translation: EAW49702.1 .
CH471066 Genomic DNA. Translation: EAW49704.1 .
CH471066 Genomic DNA. Translation: EAW49706.1 .
BC002844 mRNA. Translation: AAH02844.1 .
U20816 Genomic DNA. Translation: AAA68171.1 .
CCDSi CCDS41564.1. [Q00653-1 ]
CCDS41565.1. [Q00653-4 ]
PIRi A42024.
A57034.
I38609.
S17233.
RefSeqi NP_001070962.1. NM_001077494.3. [Q00653-1 ]
NP_001248332.1. NM_001261403.2. [Q00653-4 ]
NP_001275653.1. NM_001288724.1. [Q00653-4 ]
NP_002493.3. NM_002502.5. [Q00653-4 ]
XP_005269917.1. XM_005269860.1. [Q00653-1 ]
XP_005269918.1. XM_005269861.2. [Q00653-1 ]
UniGenei Hs.73090.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A3Q X-ray 2.10 A/B 37-327 [» ]
2D96 NMR - A 766-859 [» ]
3DO7 X-ray 3.05 B 37-329 [» ]
ProteinModelPortali Q00653.
SMRi Q00653. Positions 37-329, 434-752, 772-859.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110858. 48 interactions.
DIPi DIP-24239N.
DIP-27535N.
IntActi Q00653. 30 interactions.
MINTi MINT-7944680.
STRINGi 9606.ENSP00000189444.

Chemistry

BindingDBi Q00653.
ChEMBLi CHEMBL2094258.

PTM databases

PhosphoSitei Q00653.

Polymorphism databases

DMDMi 116242678.

Proteomic databases

MaxQBi Q00653.
PaxDbi Q00653.
PRIDEi Q00653.

Protocols and materials databases

DNASUi 4791.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000189444 ; ENSP00000189444 ; ENSG00000077150 . [Q00653-4 ]
ENST00000369966 ; ENSP00000358983 ; ENSG00000077150 . [Q00653-1 ]
ENST00000428099 ; ENSP00000410256 ; ENSG00000077150 . [Q00653-4 ]
GeneIDi 4791.
KEGGi hsa:4791.
UCSCi uc001kva.4. human. [Q00653-4 ]
uc001kvb.4. human. [Q00653-1 ]

Organism-specific databases

CTDi 4791.
GeneCardsi GC10P104144.
HGNCi HGNC:7795. NFKB2.
HPAi CAB022098.
HPA008422.
HPA023900.
MIMi 164012. gene.
615577. phenotype.
neXtProti NX_Q00653.
Orphaneti 1572. Common variable immunodeficiency.
PharmGKBi PA31600.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000004822.
HOVERGENi HBG052613.
InParanoidi Q00653.
KOi K04469.
OMAi FRGHTPL.
OrthoDBi EOG7W154S.
PhylomeDBi Q00653.
TreeFami TF325632.

Enzyme and pathway databases

Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_23950. Interleukin-1 processing.
REACT_24969. TRAF6 mediated NF-kB activation.

Miscellaneous databases

ChiTaRSi NFKB2. human.
EvolutionaryTracei Q00653.
GeneWikii NFKB2.
GenomeRNAii 4791.
NextBioi 18458.
PMAP-CutDB Q00653.
PROi Q00653.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q00653.
Bgeei Q00653.
CleanExi HS_NFKB2.
Genevestigatori Q00653.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view ]
Pfami PF00023. Ank. 5 hits.
PF00531. Death. 1 hit.
PF00554. RHD. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
PR00057. NFKBTNSCPFCT.
SMARTi SM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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 4).
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Thymus.
  7. 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.
  8. "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.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Lymph.
  11. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-220.
  12. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 459-470; 580-597 AND 636-647 (ISOFORM 1).
  13. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH BCL3.
  14. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
  15. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P52-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
  16. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBIE.
  17. "The generation of nfkb2 p52: mechanism and efficiency."
    Heusch M., Lin L., Geleziunas R., Greene W.C.
    Oncogene 18:6201-6208(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: COTRANSLATIONAL FOLDING/PROCESSING OF P100, GENERATION OF P52/P100.
  18. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-713; SER-715 AND SER-717, MUTAGENESIS, DIMERIZATION, PROTEOLYTIC PROCESSING OF P100.
  19. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-866 AND SER-870, MUTAGENESIS OF SER-866 AND SER-870, PROTEOLYTIC PROCESSING OF P100.
  20. "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] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH IGHA1.
  21. "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] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL ABERRATIONS, GENERATION OF LB40 AND EB308.
  22. "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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE TWO PROMOTER REGIONS.
  23. "The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation."
    Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J., Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J., Burns A.L.
    Oncogene 20:4917-4925(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEN1.
  24. "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] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-855.
  25. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Germline mutations in NFKB2 implicate the noncanonical NF-kappaB pathway in the pathogenesis of common variable immunodeficiency."
    Chen K., Coonrod E.M., Kumanovics A., Franks Z.F., Durtschi J.D., Margraf R.L., Wu W., Heikal N.M., Augustine N.H., Ridge P.G., Hill H.R., Jorde L.B., Weyrich A.S., Zimmerman G.A., Gundlapalli A.V., Bohnsack J.F., Voelkerding K.V.
    Am. J. Hum. Genet. 93:812-824(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CVID10.
  30. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 37-327.
  31. "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.

Entry informationi

Entry nameiNFKB2_HUMAN
AccessioniPrimary (citable) accession number: Q00653
Secondary accession number(s): A8K9D9
, D3DR83, Q04860, Q9BU75, Q9H471, Q9H472
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 182 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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