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Protein

Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe

Gene

LFNG

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

Functioni

Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Decreases the binding of JAGGED1 to NOTCH2 but not that of DELTA1. Essential mediator of somite segmentation and patterning (By similarity).By similarity

Catalytic activityi

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei86 – 872Cleavage; by furin-like proteaseSequence Analysis
Binding sitei129 – 1291SubstrateBy similarity
Binding sitei201 – 2011SubstrateBy similarity
Metal bindingi202 – 2021ManganeseBy similarity
Active sitei290 – 2901By similarity
Metal bindingi314 – 3141ManganeseBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
SignaLinkiQ8NES3.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC:2.4.1.222)
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene namesi
Name:LFNG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:6560. LFNG.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 379350LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • integral component of Golgi membrane Source: InterPro
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Spondylocostal dysostosis 3, autosomal recessive (SCDO3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA condition of variable severity associated with vertebral and rib segmentation defects. The main skeletal malformations include fusion of vertebrae, hemivertebrae, fusion of certain ribs, and other rib malformations. Deformity of the chest and spine (severe scoliosis, kyphoscoliosis and lordosis) is a natural consequence of the malformation and leads to a dwarf-like appearance. As the thorax is small, infants frequently have respiratory insufficiency and repeated respiratory infections resulting in life-threatening complications in the first year of life.

See also OMIM:609813
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti188 – 1881F → L in SCDO3; not localized to the correct compartment of the cell; unable to modulate Notch signaling in a cell-based assay; enzymatically inactive. 1 Publication
VAR_025850

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi609813. phenotype.
Orphaneti2311. Autosomal recessive spondylocostal dysostosis.
PharmGKBiPA30336.

Polymorphism and mutation databases

BioMutaiLFNG.
DMDMi27734417.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Beta-1,3-N-acetylglucosaminyltransferase lunatic fringePRO_0000219176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi168 ↔ 179By similarity
Disulfide bondi197 ↔ 260By similarity
Disulfide bondi364 ↔ 373By similarity

Post-translational modificationi

A soluble form may be derived from the membrane form by proteolytic processing.Curated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8NES3.
PRIDEiQ8NES3.

PTM databases

PhosphoSiteiQ8NES3.

Expressioni

Gene expression databases

BgeeiQ8NES3.
CleanExiHS_LFNG.
ExpressionAtlasiQ8NES3. baseline and differential.
GenevestigatoriQ8NES3.

Organism-specific databases

HPAiHPA057015.
HPA069130.

Interactioni

Protein-protein interaction databases

BioGridi110146. 3 interactions.
STRINGi9606.ENSP00000222725.

Structurei

3D structure databases

ProteinModelPortaliQ8NES3.
SMRiQ8NES3. Positions 114-374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG70217.
GeneTreeiENSGT00390000009913.
HOGENOMiHOG000046678.
HOVERGENiHBG007986.
InParanoidiQ8NES3.
KOiK05948.
OMAiPWASRGH.
OrthoDBiEOG7ZSHTD.
PhylomeDBiQ8NES3.
TreeFamiTF324207.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

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

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q8NES3-1) [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
MLKRCGRRLL LALAGALLAC LLVLTADPPP PPLPAERGRR ALRSLAGPAG
60 70 80 90 100
AAPAPGLGAA AAAPGALVRD VHSLSEYFSL LTRARRDAGP PPGAAPRPAD
110 120 130 140 150
GHPRPLAEPL APRDVFIAVK TTKKFHRARL DLLLETWISR HKEMTFIFTD
160 170 180 190 200
GEDEALARHT GNVVITNCSA AHSRQALSCK MAVEYDRFIE SGRKWFCHVD
210 220 230 240 250
DDNYVNLRAL LRLLASYPHT RDVYVGKPSL DRPIQAMERV SENKVRPVHF
260 270 280 290 300
WFATGGAGFC ISRGLALKMS PWASGGHFMN TAERIRLPDD CTIGYIVEAL
310 320 330 340 350
LGVPLIRSGL FHSHLENLQQ VPTSELHEQV TLSYGMFENK RNAVHVKGPF
360 370
SVEADPSRFR SIHCHLYPDT PWCPRTAIF
Length:379
Mass (Da):41,773
Last modified:January 10, 2003 - v2
Checksum:i4400ECA731B36B45
GO
Isoform 2 (identifier: Q8NES3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-129: Missing.
     130-145: LDLLLETWISRHKEMT → MTPGRCCLAADIQVET

Show »
Length:250
Mass (Da):28,151
Checksum:iE09162F8B0016412
GO
Isoform 3 (identifier: Q8NES3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     359-361: FRS → WGN
     362-379: Missing.

Show »
Length:361
Mass (Da):39,588
Checksum:iAC5CE1662524395B
GO
Isoform 4 (identifier: Q8NES3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MLKRCGRRLL...PGALVRDVHS → MDEQTGRLRL...RSYGGGLSQQ
     74-144: Missing.

Note: No experimental confirmation available.

Show »
Length:308
Mass (Da):35,266
Checksum:i2FE290EDD113DD28
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041R → A in AAF07187 (Ref. 5) Curated
Sequence conflicti212 – 2121R → L in AAC51360 (PubMed:9187150).Curated
Sequence conflicti221 – 2211R → L in AAC51360 (PubMed:9187150).Curated
Sequence conflicti297 – 2971V → M in BAG53248 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381G → R.1 Publication
VAR_046785
Natural varianti188 – 1881F → L in SCDO3; not localized to the correct compartment of the cell; unable to modulate Notch signaling in a cell-based assay; enzymatically inactive. 1 Publication
VAR_025850
Natural varianti346 – 3461V → M.1 Publication
Corresponds to variant rs71647813 [ dbSNP | Ensembl ].
VAR_046786

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 129129Missing in isoform 2. 1 PublicationVSP_001792Add
BLAST
Alternative sequencei1 – 7373MLKRC…RDVHS → MDEQTGRLRLDTYCMSAKQI WAWSKCSGRLWDEHMKWMEG WTDRWTDGWMDGWMDEWSPT PALRSYGGGLSQQ in isoform 4. 1 PublicationVSP_044850Add
BLAST
Alternative sequencei74 – 14471Missing in isoform 4. 1 PublicationVSP_044851Add
BLAST
Alternative sequencei130 – 14516LDLLL…HKEMT → MTPGRCCLAADIQVET in isoform 2. 1 PublicationVSP_001793Add
BLAST
Alternative sequencei359 – 3613FRS → WGN in isoform 3. 2 PublicationsVSP_001794
Alternative sequencei362 – 37918Missing in isoform 3. 2 PublicationsVSP_001795Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096284 mRNA. Translation: BAG53248.1.
AC092488 Genomic DNA. No translation available.
U94354 mRNA. Translation: AAC51360.1.
AY124582 Genomic DNA. Translation: AAM93542.1.
AF193612 mRNA. Translation: AAF07187.1.
BC014851 mRNA. Translation: AAH14851.1.
CCDSiCCDS34586.1. [Q8NES3-3]
CCDS34587.1. [Q8NES3-1]
CCDS55081.1. [Q8NES3-4]
CCDS55082.1. [Q8NES3-2]
RefSeqiNP_001035257.1. NM_001040167.1. [Q8NES3-1]
NP_001035258.1. NM_001040168.1. [Q8NES3-3]
NP_001159827.1. NM_001166355.1. [Q8NES3-4]
NP_002295.1. NM_002304.2. [Q8NES3-2]
UniGeneiHs.159142.

Genome annotation databases

EnsembliENST00000222725; ENSP00000222725; ENSG00000106003. [Q8NES3-1]
ENST00000338732; ENSP00000343095; ENSG00000106003. [Q8NES3-2]
ENST00000359574; ENSP00000352579; ENSG00000106003. [Q8NES3-3]
ENST00000402045; ENSP00000384786; ENSG00000106003. [Q8NES3-2]
ENST00000402506; ENSP00000385764; ENSG00000106003. [Q8NES3-4]
GeneIDi3955.
KEGGihsa:3955.
UCSCiuc003smf.3. human. [Q8NES3-1]
uc003smg.3. human. [Q8NES3-3]
uc021zyx.1. human. [Q8NES3-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096284 mRNA. Translation: BAG53248.1.
AC092488 Genomic DNA. No translation available.
U94354 mRNA. Translation: AAC51360.1.
AY124582 Genomic DNA. Translation: AAM93542.1.
AF193612 mRNA. Translation: AAF07187.1.
BC014851 mRNA. Translation: AAH14851.1.
CCDSiCCDS34586.1. [Q8NES3-3]
CCDS34587.1. [Q8NES3-1]
CCDS55081.1. [Q8NES3-4]
CCDS55082.1. [Q8NES3-2]
RefSeqiNP_001035257.1. NM_001040167.1. [Q8NES3-1]
NP_001035258.1. NM_001040168.1. [Q8NES3-3]
NP_001159827.1. NM_001166355.1. [Q8NES3-4]
NP_002295.1. NM_002304.2. [Q8NES3-2]
UniGeneiHs.159142.

3D structure databases

ProteinModelPortaliQ8NES3.
SMRiQ8NES3. Positions 114-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110146. 3 interactions.
STRINGi9606.ENSP00000222725.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteiQ8NES3.

Polymorphism and mutation databases

BioMutaiLFNG.
DMDMi27734417.

Proteomic databases

PaxDbiQ8NES3.
PRIDEiQ8NES3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222725; ENSP00000222725; ENSG00000106003. [Q8NES3-1]
ENST00000338732; ENSP00000343095; ENSG00000106003. [Q8NES3-2]
ENST00000359574; ENSP00000352579; ENSG00000106003. [Q8NES3-3]
ENST00000402045; ENSP00000384786; ENSG00000106003. [Q8NES3-2]
ENST00000402506; ENSP00000385764; ENSG00000106003. [Q8NES3-4]
GeneIDi3955.
KEGGihsa:3955.
UCSCiuc003smf.3. human. [Q8NES3-1]
uc003smg.3. human. [Q8NES3-3]
uc021zyx.1. human. [Q8NES3-2]

Organism-specific databases

CTDi3955.
GeneCardsiGC07P002552.
GeneReviewsiLFNG.
HGNCiHGNC:6560. LFNG.
HPAiHPA057015.
HPA069130.
MIMi602576. gene.
609813. phenotype.
neXtProtiNX_Q8NES3.
Orphaneti2311. Autosomal recessive spondylocostal dysostosis.
PharmGKBiPA30336.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG70217.
GeneTreeiENSGT00390000009913.
HOGENOMiHOG000046678.
HOVERGENiHBG007986.
InParanoidiQ8NES3.
KOiK05948.
OMAiPWASRGH.
OrthoDBiEOG7ZSHTD.
PhylomeDBiQ8NES3.
TreeFamiTF324207.

Enzyme and pathway databases

ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
SignaLinkiQ8NES3.

Miscellaneous databases

ChiTaRSiLFNG. human.
GeneWikiiLFNG.
GenomeRNAii3955.
NextBioi15517.
PROiQ8NES3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NES3.
CleanExiHS_LFNG.
ExpressionAtlasiQ8NES3. baseline and differential.
GenevestigatoriQ8NES3.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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).
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "A family of mammalian Fringe genes implicated in boundary determination and the Notch pathway."
    Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D., Vogt T.F.
    Development 124:2245-2254(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-361 (ISOFORM 3).
  4. "Clock regulatory elements control cyclic expression of Lunatic fringe during somitogenesis."
    Cole S.E., Levorse J.M., Tilghman S.M., Vogt T.F.
    Dev. Cell 3:75-84(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144 (ISOFORM 1).
  5. "Homo sapiens fringe gene homolog."
    Holloway J., Blumberg H., Jelinek L., Whitmore T., Jaspers S., Gross J., Haldeman B., Taft D., O'Hara P.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 104-361 (ISOFORM 3).
  6. "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 2).
    Tissue: Kidney.
  7. "Manic fringe and lunatic fringe modify different sites of the Notch2 extracellular region, resulting in different signaling modulation."
    Shimizu K., Chiba S., Saito T., Kumano K., Takahashi T., Hirai H.
    J. Biol. Chem. 276:25753-25758(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Mutation of the LUNATIC FRINGE gene in humans causes spondylocostal dysostosis with a severe vertebral phenotype."
    Sparrow D.B., Chapman G., Wouters M.A., Whittock N.V., Ellard S., Fatkin D., Turnpenny P.D., Kusumi K., Sillence D., Dunwoodie S.L.
    Am. J. Hum. Genet. 78:28-37(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCDO3 LEU-188, CHARACTERIZATION OF VARIANT SCDO3 LEU-188.
  9. Cited for: VARIANTS ARG-38 AND MET-346.

Entry informationi

Entry nameiLFNG_HUMAN
AccessioniPrimary (citable) accession number: Q8NES3
Secondary accession number(s): B3KTY6
, B5MCR5, O00589, Q96C39, Q9UJW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: January 10, 2003
Last modified: May 27, 2015
This is version 120 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.