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Protein

Forkhead box protein P3

Gene

FOXP3

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

Functioni

Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2 (PubMed:15790681). Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7 (PubMed:17360565). Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1 (PubMed:17377532). Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development (PubMed:18368049). Inhibits the transcriptional activator activity of RORA (PubMed:18354202). Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (By similarity).By similarity7 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri197 – 222C2H2-typeAdd BLAST26
DNA bindingi337 – 423Fork-headPROSITE-ProRule annotationAdd BLAST87

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • DNA binding transcription factor activity Source: UniProtKB
  • histone acetyltransferase binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • NFAT protein binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II proximal promoter sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • sequence-specific DNA binding Source: UniProtKB
  • transcription corepressor activity Source: Ensembl
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-8877330 RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)
R-HSA-8939256 RUNX1 regulates transcription of genes involved in WNT signaling
SignaLinkiQ9BZS1
SIGNORiQ9BZS1

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein P3
Alternative name(s):
Scurfin
Cleaved into the following 2 chains:
Gene namesi
Name:FOXP3
Synonyms:IPEX
ORF Names:JM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000049768.14
HGNCiHGNC:6106 FOXP3
MIMi300292 gene
neXtProtiNX_Q9BZS1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency polyendocrinopathy, enteropathy, X-linked syndrome (IPEX)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by neonatal onset insulin-dependent diabetes mellitus, infections, secretory diarrhea, thrombocytopenia, anemia and eczema. It is usually lethal in infancy.
See also OMIM:304790
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078971242L → P in IPEX; mild phenotype; no loss of protein expression. 1 Publication1
Natural variantiVAR_011330251Missing in IPEX; significantly reduces dimerization. 2 Publications1
Natural variantiVAR_078972324F → L in IPEX; mild phenotype; no loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs122467173EnsemblClinVar.1
Natural variantiVAR_078973339P → A in IPEX; no loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs886044787EnsemblClinVar.1
Natural variantiVAR_078974347R → H in IPEX; mild phenotype; no loss of protein expression; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with A-373. 2 Publications1
Natural variantiVAR_023569363I → V in IPEX. 1 Publication1
Natural variantiVAR_011331371F → C in IPEX; no effect on dimerization. 2 PublicationsCorresponds to variant dbSNP:rs122467169EnsemblClinVar.1
Natural variantiVAR_078975373F → A in IPEX; requires 2 nucleotide substitutions; no loss of protein expression; disrupts dimerization; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with H-347. 2 PublicationsCorresponds to variant dbSNP:rs122467172EnsemblClinVar.1
Natural variantiVAR_078976374F → C in IPEX; no loss of protein expression. 1 Publication1
Natural variantiVAR_011332384A → T in IPEX; no loss of protein expression. 3 PublicationsCorresponds to variant dbSNP:rs122467170EnsemblClinVar.1
Natural variantiVAR_011333397R → W in IPEX. 1 PublicationCorresponds to variant dbSNP:rs28935477EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi69L → A: Decrease in nuclear export; when associated with A-71, A-74 and A-76. 1 Publication1
Mutagenesisi71L → A: Decrease in nuclear export; when associated with A-69, A-74 and A-76. 1 Publication1
Mutagenesisi74L → A: Decrease in nuclear export; when associated with A-69, A-71 and A-76. 1 Publication1
Mutagenesisi76L → A: Decrease in nuclear export; when associated with A-69, A-71 and A-74. 1 Publication1
Mutagenesisi95 – 96LL → AA: Loss of interaction with RORA. 1 Publication2
Mutagenesisi242L → A: Decrease in nuclear export; when associated with A-246 and A-248. 1 Publication1
Mutagenesisi246L → A: Decrease in nuclear export; when associated with A-242 and A-248. 1 Publication1
Mutagenesisi248L → A: Decrease in nuclear export; when associated with A-242 and A-246. 1 Publication1
Mutagenesisi348W → Q: No loss of DNA-binding. Disrupts dimerization but does not affect DNA-binding; when associated with T-370. Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with T-370 and P-372. 1 Publication1
Mutagenesisi370M → T: Disrupts dimerization but does not affect DNA-binding; when associated with Q-348. Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with Q-348 and P-372. 1 Publication1
Mutagenesisi372A → P: Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with Q-348 and T-370. 1 Publication1
Mutagenesisi415 – 416KK → EE: Loss of nuclear localization. 1 Publication2
Mutagenesisi418S → A: Decrease in phosphorylation, significant decrease in transcriptional repressor activity and reduced interaction with PP1CA, PP1CB and PP1CG. Significant decrease in phosphorylation and transcriptional repressor activity; when associated with A-422. 1 Publication1
Mutagenesisi418S → E: Slight increase in transcriptional repressor activity. 1 Publication1
Mutagenesisi422S → A: Significant decrease in phosphorylation and transcriptional repressor activity; when associated with A-418. 1 Publication1

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNETi50943
GeneReviewsiFOXP3
MalaCardsiFOXP3
MIMi304790 phenotype
OpenTargetsiENSG00000049768
Orphaneti37042 Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome
PharmGKBiPA201094

Polymorphism and mutation databases

BioMutaiFOXP3
DMDMi14548061

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000918861 – 431Forkhead box protein P3Add BLAST431
ChainiPRO_00004324301 – 417Forkhead box protein P3, C-terminally processed1 PublicationAdd BLAST417
ChainiPRO_000043243152 – 417Forkhead box protein P3 41 kDa form1 PublicationAdd BLAST366
PropeptideiPRO_0000432432418 – 4311 PublicationAdd BLAST14

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Phosphoserine; by CDK2By similarity1
Modified residuei31N6-acetyllysine1 Publication1
Cross-linki250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki252Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei263N6-acetyllysine; alternate1 Publication1
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei268N6-acetyllysine; alternate1 Publication1
Cross-linki268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei418Phosphoserine1 Publication1

Post-translational modificationi

Polyubiquitinated, leading to its proteasomal degradation in regulatory T-cells (Treg) which is mediated by STUB1 in a HSPA1A/B-dependent manner. Deubiquitinated by USP7 leading to increase in protein stability.2 Publications
Phosphorylation at Ser-418 regulates its transcriptional repressor activity and consequently, regulatory T-cells (Treg) suppressive function. Dephosphorylated at Ser-418 by protein phosphatase 1 (PP1) in Treg cells derived from patients with rheumatoid arthritis. Phosphorylation by CDK2 negatively regulates its transcriptional activity and protein stability (By similarity).By similarity1 Publication
Acetylation on lysine residues stabilizes FOXP3 and promotes differentiation of T-cells into induced regulatory T-cells (iTregs) associated with suppressive functions. Deacetylated by SIRT1.2 Publications
Undergoes proteolytic cleavage in activated regulatory T-cells (Treg), and can be cleaved at either the N- or C-terminal site, or at both sites.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei51 – 52Cleavage1 Publication2
Sitei417 – 418Cleavage; by PCSK1 or PCSK21 Publication2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9BZS1
PaxDbiQ9BZS1
PeptideAtlasiQ9BZS1
PRIDEiQ9BZS1
ProteomicsDBi79899
79900 [Q9BZS1-2]
79901 [Q9BZS1-3]
TopDownProteomicsiQ9BZS1-3 [Q9BZS1-3]

PTM databases

iPTMnetiQ9BZS1
PhosphoSitePlusiQ9BZS1
SwissPalmiQ9BZS1

Expressioni

Inductioni

Down-regulated in regulatory T-cells (Treg) during inflammation.1 Publication

Gene expression databases

BgeeiENSG00000049768
CleanExiHS_FOXP3
ExpressionAtlasiQ9BZS1 baseline and differential
GenevisibleiQ9BZS1 HS

Organism-specific databases

HPAiCAB026301
HPA045943

Interactioni

Subunit structurei

Homodimer (PubMed:21458306, PubMed:25567984). Dimerization is essential for its transcriptional regulator activity (PubMed:21458306). Interacts with IKZF3. Isoform 1 (via LXXLL motif), but not isoform 2, interacts with isoform 4 of RORA (via AF-2 motif). Interacts with STUB1, HSPA8 and HSPA1A/B. Interacts with PPP1CA, PPP1CB and PPP1CG. Interacts with KAT5 and HDAC7. Interacts with HDAC9 in the absence of T-cell stimulation. Interacts with USP7. Interacts with isoform 2 of ZFP90 and can form a complex with TRIM28 in the presence of isoform 2 of ZFP90. Interacts with RUNX1. Interacts with RORC. Interacts with RELA and NFATC2. Interacts with RUNX2, RUNX3 and IKZF4 (By similarity).By similarity12 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • histone acetyltransferase binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • NFAT protein binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi119170, 70 interactors
DIPiDIP-36584N
IntActiQ9BZS1, 69 interactors
MINTiQ9BZS1
STRINGi9606.ENSP00000365380

Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi342 – 351Combined sources10
Helixi360 – 371Combined sources12
Turni372 – 375Combined sources4
Helixi381 – 391Combined sources11
Beta strandi395 – 398Combined sources4
Beta strandi401 – 403Combined sources3
Beta strandi405 – 408Combined sources4
Helixi410 – 416Combined sources7

3D structure databases

ProteinModelPortaliQ9BZS1
SMRiQ9BZS1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZS1

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 198Interaction with ZFP901 PublicationAdd BLAST93
Regioni106 – 190Essential for transcriptional repressor activity and for interaction with KAT5 and HDAC71 PublicationAdd BLAST85
Regioni149 – 199Interaction with IKZF4By similarityAdd BLAST51
Regioni239 – 260Leucine-zipperAdd BLAST22
Regioni278 – 336Interaction with RUNX11 PublicationAdd BLAST59

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi68 – 76Nuclear export signal1 Publication9
Motifi92 – 96LXXLL motif1 Publication5
Motifi239 – 248Nuclear export signal1 Publication10
Motifi414 – 417Nuclear localization signal1 Publication4

Domaini

The fork-head DNA-binding domain is essential for its dimerization and interaction with NFATC2.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri197 – 222C2H2-typeAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4385 Eukaryota
COG5025 LUCA
GeneTreeiENSGT00920000148947
HOGENOMiHOG000082490
HOVERGENiHBG051656
InParanoidiQ9BZS1
KOiK10163
OMAiSCCIVAT
OrthoDBiEOG091G08HY
PhylomeDBiQ9BZS1
TreeFamiTF326978

Family and domain databases

CDDicd00059 FH, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR001766 Fork_head_dom
IPR032354 FOXP-CC
IPR030456 TF_fork_head_CS_2
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
IPR013087 Znf_C2H2_type
PfamiView protein in Pfam
PF00250 Forkhead, 1 hit
PF16159 FOXP-CC, 1 hit
PRINTSiPR00053 FORKHEAD
SMARTiView protein in SMART
SM00339 FH, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS00658 FORK_HEAD_2, 1 hit
PS50039 FORK_HEAD_3, 1 hit
PS00028 ZINC_FINGER_C2H2_1, 1 hit

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZS1-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MPNPRPGKPS APSLALGPSP GASPSWRAAP KASDLLGARG PGGTFQGRDL
60 70 80 90 100
RGGAHASSSS LNPMPPSQLQ LPTLPLVMVA PSGARLGPLP HLQALLQDRP
110 120 130 140 150
HFMHQLSTVD AHARTPVLQV HPLESPAMIS LTPPTTATGV FSLKARPGLP
160 170 180 190 200
PGINVASLEW VSREPALLCT FPNPSAPRKD STLSAVPQSS YPLLANGVCK
210 220 230 240 250
WPGCEKVFEE PEDFLKHCQA DHLLDEKGRA QCLLQREMVQ SLEQQLVLEK
260 270 280 290 300
EKLSAMQAHL AGKMALTKAS SVASSDKGSC CIVAAGSQGP VVPAWSGPRE
310 320 330 340 350
APDSLFAVRR HLWGSHGNST FPEFLHNMDY FKFHNMRPPF TYATLIRWAI
360 370 380 390 400
LEAPEKQRTL NEIYHWFTRM FAFFRNHPAT WKNAIRHNLS LHKCFVRVES
410 420 430
EKGAVWTVDE LEFRKKRSQR PSRCSNPTPG P
Length:431
Mass (Da):47,244
Last modified:June 1, 2001 - v1
Checksum:i91737C3CEA665A15
GO
Isoform 2 (identifier: Q9BZS1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-106: Missing.

Show »
Length:396
Mass (Da):43,410
Checksum:iBF4DF0DD83D61CD5
GO
Isoform 3 (identifier: Q9BZS1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-106: Missing.
     382-382: K → KVSSSEVAVTGMASSAIAAQSGQAWVWAHRHIGEERDVGCWWWLLASEVDAHLLPVPGLPQ

Note: No experimental confirmation available.
Show »
Length:456
Mass (Da):49,843
Checksum:i39E7483703031335
GO
Isoform 4 (identifier: Q9BZS1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     246-272: Missing.

Show »
Length:404
Mass (Da):44,407
Checksum:i4D164C39EF069DBB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16 – 20LGPSP → MSPIS in CAA06748 (Ref. 7) Curated5

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078971242L → P in IPEX; mild phenotype; no loss of protein expression. 1 Publication1
Natural variantiVAR_011330251Missing in IPEX; significantly reduces dimerization. 2 Publications1
Natural variantiVAR_078972324F → L in IPEX; mild phenotype; no loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs122467173EnsemblClinVar.1
Natural variantiVAR_078973339P → A in IPEX; no loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs886044787EnsemblClinVar.1
Natural variantiVAR_078974347R → H in IPEX; mild phenotype; no loss of protein expression; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with A-373. 2 Publications1
Natural variantiVAR_023569363I → V in IPEX. 1 Publication1
Natural variantiVAR_011331371F → C in IPEX; no effect on dimerization. 2 PublicationsCorresponds to variant dbSNP:rs122467169EnsemblClinVar.1
Natural variantiVAR_078975373F → A in IPEX; requires 2 nucleotide substitutions; no loss of protein expression; disrupts dimerization; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with H-347. 2 PublicationsCorresponds to variant dbSNP:rs122467172EnsemblClinVar.1
Natural variantiVAR_078976374F → C in IPEX; no loss of protein expression. 1 Publication1
Natural variantiVAR_011332384A → T in IPEX; no loss of protein expression. 3 PublicationsCorresponds to variant dbSNP:rs122467170EnsemblClinVar.1
Natural variantiVAR_011333397R → W in IPEX. 1 PublicationCorresponds to variant dbSNP:rs28935477EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01579672 – 106Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST35
Alternative sequenceiVSP_047859246 – 272Missing in isoform 4. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_036418382K → KVSSSEVAVTGMASSAIAAQ SGQAWVWAHRHIGEERDVGC WWWLLASEVDAHLLPVPGLP Q in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF277993 mRNA Translation: AAG53607.1
EF534714 mRNA Translation: ABQ15210.1
EU855812 mRNA Translation: ACJ46653.1
DQ010327 mRNA Translation: AAY27088.1
AF235097 Genomic DNA No translation available.
BC113401 mRNA Translation: AAI13402.1
BC113403 mRNA Translation: AAI13404.1
BC143785 mRNA Translation: AAI43786.1
AJ005891 mRNA Translation: CAA06748.1
CCDSiCCDS14323.1 [Q9BZS1-1]
CCDS48109.1 [Q9BZS1-2]
RefSeqiNP_001107849.1, NM_001114377.1 [Q9BZS1-2]
NP_054728.2, NM_014009.3 [Q9BZS1-1]
UniGeneiHs.247700

Genome annotation databases

EnsembliENST00000376199; ENSP00000365372; ENSG00000049768 [Q9BZS1-2]
ENST00000376207; ENSP00000365380; ENSG00000049768 [Q9BZS1-1]
ENST00000518685; ENSP00000428952; ENSG00000049768 [Q9BZS1-2]
ENST00000557224; ENSP00000451208; ENSG00000049768 [Q9BZS1-3]
GeneIDi50943
KEGGihsa:50943
UCSCiuc004dne.5 human [Q9BZS1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiFOXP3_HUMAN
AccessioniPrimary (citable) accession number: Q9BZS1
Secondary accession number(s): A5HJT1
, B7ZLG0, B9UN80, O60827, Q14DD8, Q4ZH51
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 1, 2001
Last modified: July 18, 2018
This is version 184 of the entry and version 1 of the sequence. See 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 X
    Human chromosome X: 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

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