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Protein

NF-kappa-B inhibitor alpha

Gene

NFKBIA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.1 Publication

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • NF-kappaB binding Source: UniProtKB
  • nuclear localization sequence binding Source: UniProtKB
  • transcription factor binding Source: ProtInc
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-202424. Downstream TCR signaling.
R-HSA-209560. NF-kB is activated and signals survival.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-5603027. IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
R-HSA-5603029. IkBA variant leads to EDA-ID.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-933542. TRAF6 mediated NF-kB activation.
SABIO-RKP25963.
SignaLinkiP25963.
SIGNORiP25963.

Names & Taxonomyi

Protein namesi
Recommended name:
NF-kappa-B inhibitor alpha
Alternative name(s):
I-kappa-B-alpha
Short name:
IkB-alpha
Short name:
IkappaBalpha
Major histocompatibility complex enhancer-binding protein MAD3
Gene namesi
Name:NFKBIA
Synonyms:IKBA, MAD3, NFKBI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:7797. NFKBIA.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • I-kappaB/NF-kappaB complex Source: BHF-UCL
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia, anhidrotic, with T-cell immunodeficiency autosomal dominant (ADEDAID)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. This form of ectodermal dysplasia is associated with decreased production of pro-inflammatory cytokines and certain interferons, rendering patients susceptible to infection.
See also OMIM:612132
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321S → I in ADEDAID. 1 Publication
Corresponds to variant rs28933100 [ dbSNP | Ensembl ].
VAR_034871

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211K → R: Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-22. 4 Publications
Mutagenesisi22 – 221K → R: Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-21. 4 Publications
Mutagenesisi31 – 311D → A: Loss of phosphorylation; when associated with A-35. 1 Publication
Mutagenesisi32 – 321S → A: Loss of phosphorylation, ubiquitination and degradation; when associated with A-36. 2 Publications
Mutagenesisi32 – 321S → T: Decrease in phosphorylation and degradation; when associated with T-36. 2 Publications
Mutagenesisi35 – 351D → A: Loss in phosphorylation; when associated with A-31. 1 Publication
Mutagenesisi35 – 351D → G: No change neither in phosphorylation, nor on degradation. 1 Publication
Mutagenesisi36 – 361S → A: Loss of phosphorylation, ubiquitination, and degradation; when associated with A-32. 2 Publications
Mutagenesisi36 – 361S → T: Decrease in phosphorylation and degradation; when associated with T-32. 2 Publications
Mutagenesisi38 – 381K → R: No change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-47. 1 Publication
Mutagenesisi42 – 421Y → F: No phosphorylation. 1 Publication
Mutagenesisi45 – 528MVKELQEI → AAKEAQEA: No nuclear export. 1 Publication
Mutagenesisi47 – 471K → R: Little change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-38. 1 Publication
Mutagenesisi115 – 1206LHLAVI → AHAAVA: Greatly reduced nuclear localization. Great reduction in its ability to inhibit DNA binding of RELA. 1 Publication
Mutagenesisi210 – 2101N → A: Almost abolished ability to inhibit NF-kappa-B DNA-binding activity; when associated with A-244. 1 Publication
Mutagenesisi234 – 2341S → A: No inducible ubiquitination nor protein degradation. 1 Publication
Mutagenesisi244 – 2441N → A: Almost abolished ability to inhibit NF-kappa-B DNA-binding activity; when associated with A-210. 1 Publication
Mutagenesisi262 – 2621S → A: No inducible ubiquitination nor protein degradation. 1 Publication
Mutagenesisi263 – 2631T → A: No inducible ubiquitination nor protein degradation. 1 Publication

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia

Organism-specific databases

MalaCardsiNFKBIA.
MIMi612132. phenotype.
Orphaneti251579. Giant cell glioblastoma.
251576. Gliosarcoma.
98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
PharmGKBiPA31601.

Chemistry

ChEMBLiCHEMBL2898.
DrugBankiDB00945. Acetylsalicylic acid.

Polymorphism and mutation databases

BioMutaiNFKBIA.
DMDMi126682.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317NF-kappa-B inhibitor alphaPRO_0000066999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki21 – 21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO or ubiquitin); alternate2 Publications
Cross-linki21 – 21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei32 – 321Phosphoserine; by IKKA and IKKE2 Publications
Modified residuei36 – 361Phosphoserine; by IKKA, IKKB, IKKE and TBK12 Publications
Modified residuei42 – 421Phosphotyrosine; by Tyr-kinases1 Publication
Modified residuei210 – 2101(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei244 – 2441(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei283 – 2831Phosphoserine; by CK22 Publications
Modified residuei288 – 2881Phosphoserine; by CK21 Publication
Modified residuei291 – 2911Phosphothreonine; by CK22 Publications
Modified residuei293 – 2931Phosphoserine; by CK21 Publication
Modified residuei299 – 2991Phosphothreonine; by CK21 Publication

Post-translational modificationi

Phosphorylated; disables inhibition of NF-kappa-B DNA-binding activity. Phosphorylation at positions 32 and 36 is prerequisite to recognition by UBE2D3 leading to polyubiquitination and subsequent degradation.3 Publications
Sumoylated; sumoylation requires the presence of the nuclear import signal. Sumoylation blocks ubiquitination and proteasome-mediated degradation of the protein thereby increasing the protein stability.3 Publications
Monoubiquitinated at Lys-21 and/or Lys-22 by UBE2D3. Ubiquitin chain elongation is then performed by CDC34 in cooperation with the SCF(FBXW11) E3 ligase complex, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. The resulting polyubiquitination leads to protein degradation. Also ubiquitinated by SCF(BTRC) following stimulus-dependent phosphorylation at Ser-32 and Ser-36.5 Publications
Deubiquitinated by porcine reproductive and respiratory syndrome virus Nsp2 protein, which thereby interferes with NFKBIA degradation and impairs subsequent NF-kappa-B activation.

Keywords - PTMi

Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP25963.
MaxQBiP25963.
PaxDbiP25963.
PeptideAtlasiP25963.
PRIDEiP25963.

PTM databases

iPTMnetiP25963.
PhosphoSiteiP25963.

Miscellaneous databases

PMAP-CutDBP25963.

Expressioni

Inductioni

Induced in adherent monocytes.

Gene expression databases

BgeeiENSG00000100906.
CleanExiHS_NFKBIA.
ExpressionAtlasiP25963. baseline and differential.
GenevisibleiP25963. HS.

Organism-specific databases

HPAiCAB003815.
HPA029207.

Interactioni

Subunit structurei

Interacts with RELA; the interaction requires the nuclear import signal. Interacts with NKIRAS1 and NKIRAS2. Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Interacts with HBV protein X. Interacts with isoform 1 and isoform 2 of RWDD3; the interaction enhances sumoylation. Interacts (when phosphorylated at the 2 serine residues in the destruction motif D-S-G-X(2,3,4)-S) with BTRC. Associates with the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC; the association is mediated via interaction with BTRC. Part of a SCF(BTRC)-like complex lacking CUL1, which is associated with RELA; RELA interacts directly with NFKBIA. Interacts with PRMT2. Interacts with PRKACA in platelets; this interaction is disrupted by thrombin and collagen. Interacts with HIF1AN. Interacts with MEFV.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-307386,EBI-307386
P143402EBI-307386,EBI-465733From a different organism.
Q9E7P02EBI-307386,EBI-11361108From a different organism.
CHUKO1511114EBI-307386,EBI-81249
ChukQ60680-22EBI-307386,EBI-646264From a different organism.
COMMD1Q8N6683EBI-307386,EBI-1550112
IKBKBO1492020EBI-307386,EBI-81266
IKBKGQ9Y6K96EBI-307386,EBI-81279
NEDD9Q145113EBI-307386,EBI-2108053
NFKB1P198384EBI-307386,EBI-300010
RELQ048642EBI-307386,EBI-307352
RELAQ0420621EBI-307386,EBI-73886
RPS3P233966EBI-307386,EBI-351193
UBCP0CG483EBI-307386,EBI-3390054
UL54Q9J0X93EBI-307386,EBI-7967856From a different organism.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • NF-kappaB binding Source: UniProtKB
  • transcription factor binding Source: ProtInc
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110859. 138 interactions.
DIPiDIP-139N.
IntActiP25963. 58 interactions.
MINTiMINT-120458.
STRINGi9606.ENSP00000216797.

Chemistry

BindingDBiP25963.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni72 – 743Combined sources
Helixi79 – 835Combined sources
Beta strandi87 – 915Combined sources
Helixi101 – 1044Combined sources
Helixi114 – 1207Combined sources
Helixi124 – 1285Combined sources
Helixi147 – 1548Combined sources
Helixi157 – 1659Combined sources
Turni167 – 1704Combined sources
Beta strandi171 – 1733Combined sources
Helixi175 – 1773Combined sources
Helixi186 – 1927Combined sources
Helixi196 – 20510Combined sources
Turni214 – 2163Combined sources
Helixi220 – 2267Combined sources
Helixi230 – 2378Combined sources
Turni238 – 2403Combined sources
Helixi253 – 2564Combined sources
Helixi263 – 2708Combined sources
Helixi275 – 2773Combined sources
Turni285 – 2873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IKNX-ray2.30D67-302[»]
1NFIX-ray2.70E/F70-282[»]
DisProtiDP00468.
ProteinModelPortaliP25963.
SMRiP25963. Positions 40-281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25963.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati73 – 10331ANK 1Add
BLAST
Repeati110 – 13930ANK 2Add
BLAST
Repeati143 – 17230ANK 3Add
BLAST
Repeati182 – 21130ANK 4Add
BLAST
Repeati216 – 24530ANK 5Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 367Destruction motif
Motifi45 – 5410Nuclear export signal
Motifi110 – 12011Nuclear import signalAdd
BLAST

Sequence similaritiesi

Belongs to the NF-kappa-B inhibitor family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00550000074527.
HOGENOMiHOG000059576.
HOVERGENiHBG018875.
InParanoidiP25963.
KOiK04734.
OMAiHNCLHLA.
OrthoDBiEOG091G0CSV.
PhylomeDBiP25963.
TreeFamiTF320166.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25963-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ
60 70 80 90 100
EIRLEPQEVP RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD
110 120 130 140 150
LAFLNFQNNL QQTPLHLAVI TNQPEIAEAL LGAGCDPELR DFRGNTPLHL
160 170 180 190 200
ACEQGCLASV GVLTQSCTTP HLHSILKATN YNGHTCLHLA SIHGYLGIVE
210 220 230 240 250
LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG ADVNRVTYQG
260 270 280 290 300
YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE
310
DELPYDDCVF GGQRLTL
Length:317
Mass (Da):35,609
Last modified:May 1, 1992 - v1
Checksum:i088B313226786395
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321S → I in ADEDAID. 1 Publication
Corresponds to variant rs28933100 [ dbSNP | Ensembl ].
VAR_034871

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69043 mRNA. Translation: AAA16489.1.
AJ249294
, AJ249295, AJ249283, AJ249284, AJ249285, AJ249286 Genomic DNA. Translation: CAB65556.2.
AY033600 mRNA. Translation: AAK51149.1.
BT007091 mRNA. Translation: AAP35754.1.
AY496422 Genomic DNA. Translation: AAR29599.1.
AK313421 mRNA. Translation: BAG36213.1.
AL133163 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65875.1.
BC002601 mRNA. Translation: AAH02601.1.
BC004983 mRNA. Translation: AAH04983.1.
CCDSiCCDS9656.1.
PIRiA39935.
RefSeqiNP_065390.1. NM_020529.2.
UniGeneiHs.81328.

Genome annotation databases

EnsembliENST00000216797; ENSP00000216797; ENSG00000100906.
GeneIDi4792.
KEGGihsa:4792.
UCSCiuc001wtf.5. human.

Cross-referencesi

Web resourcesi

NFKBIAbase

NFKBIA mutation db

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69043 mRNA. Translation: AAA16489.1.
AJ249294
, AJ249295, AJ249283, AJ249284, AJ249285, AJ249286 Genomic DNA. Translation: CAB65556.2.
AY033600 mRNA. Translation: AAK51149.1.
BT007091 mRNA. Translation: AAP35754.1.
AY496422 Genomic DNA. Translation: AAR29599.1.
AK313421 mRNA. Translation: BAG36213.1.
AL133163 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65875.1.
BC002601 mRNA. Translation: AAH02601.1.
BC004983 mRNA. Translation: AAH04983.1.
CCDSiCCDS9656.1.
PIRiA39935.
RefSeqiNP_065390.1. NM_020529.2.
UniGeneiHs.81328.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IKNX-ray2.30D67-302[»]
1NFIX-ray2.70E/F70-282[»]
DisProtiDP00468.
ProteinModelPortaliP25963.
SMRiP25963. Positions 40-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110859. 138 interactions.
DIPiDIP-139N.
IntActiP25963. 58 interactions.
MINTiMINT-120458.
STRINGi9606.ENSP00000216797.

Chemistry

BindingDBiP25963.
ChEMBLiCHEMBL2898.
DrugBankiDB00945. Acetylsalicylic acid.

PTM databases

iPTMnetiP25963.
PhosphoSiteiP25963.

Polymorphism and mutation databases

BioMutaiNFKBIA.
DMDMi126682.

Proteomic databases

EPDiP25963.
MaxQBiP25963.
PaxDbiP25963.
PeptideAtlasiP25963.
PRIDEiP25963.

Protocols and materials databases

DNASUi4792.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216797; ENSP00000216797; ENSG00000100906.
GeneIDi4792.
KEGGihsa:4792.
UCSCiuc001wtf.5. human.

Organism-specific databases

CTDi4792.
GeneCardsiNFKBIA.
HGNCiHGNC:7797. NFKBIA.
HPAiCAB003815.
HPA029207.
MalaCardsiNFKBIA.
MIMi164008. gene.
612132. phenotype.
neXtProtiNX_P25963.
Orphaneti251579. Giant cell glioblastoma.
251576. Gliosarcoma.
98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
PharmGKBiPA31601.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00550000074527.
HOGENOMiHOG000059576.
HOVERGENiHBG018875.
InParanoidiP25963.
KOiK04734.
OMAiHNCLHLA.
OrthoDBiEOG091G0CSV.
PhylomeDBiP25963.
TreeFamiTF320166.

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-202424. Downstream TCR signaling.
R-HSA-209560. NF-kB is activated and signals survival.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-5603027. IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
R-HSA-5603029. IkBA variant leads to EDA-ID.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-933542. TRAF6 mediated NF-kB activation.
SABIO-RKP25963.
SignaLinkiP25963.
SIGNORiP25963.

Miscellaneous databases

ChiTaRSiNFKBIA. human.
EvolutionaryTraceiP25963.
GeneWikiiI%CE%BAB%CE%B1.
GenomeRNAii4792.
PMAP-CutDBP25963.
PROiP25963.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100906.
CleanExiHS_NFKBIA.
ExpressionAtlasiP25963. baseline and differential.
GenevisibleiP25963. HS.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIKBA_HUMAN
AccessioniPrimary (citable) accession number: P25963
Secondary accession number(s): B2R8L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: September 7, 2016
This is version 188 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.