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Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

POFUT1

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

Functioni

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs).2 Publications

Catalytic activityi

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.

Kineticsi

  1. KM=6 µM for F7 EGF domain1 Publication
  2. KM=4 µM for GDP-fucose1 Publication

Vmax=3 µmol/min/mg enzyme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei335 – 3351SubstrateBy similarity

GO - Molecular functioni

  1. fucosyltransferase activity Source: UniProtKB
  2. peptide-O-fucosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. embryo development Source: UniProtKB
  3. fucose metabolic process Source: UniProtKB-KW
  4. heart development Source: Ensembl
  5. nervous system development Source: Ensembl
  6. Notch signaling pathway Source: UniProtKB
  7. O-glycan processing Source: UniProtKB
  8. protein O-linked fucosylation Source: UniProtKB
  9. protein O-linked glycosylation Source: UniProtKB
  10. regulation of transcription, DNA-templated Source: UniProtKB
  11. somitogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

Keywords - Ligandi

Manganese

Enzyme and pathway databases

ReactomeiREACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
SignaLinkiQ9H488.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT65. Glycosyltransferase Family 65.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-fucose protein O-fucosyltransferase 1 (EC:2.4.1.221)
Alternative name(s):
Peptide-O-fucosyltransferase 1
Short name:
O-FucT-1
Gene namesi
Name:POFUT1
Synonyms:FUT12, KIAA0180
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:14988. POFUT1.

Subcellular locationi

Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Dowling-Degos disease 21 Publication

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

Disease descriptionAn autosomal dominant genodermatosis. Affected individuals develop a postpubertal reticulate hyperpigmentation that is progressive and disfiguring, and small hyperkeratotic dark brown papules that affect mainly the flexures and great skin folds. Patients usually show no abnormalities of the hair or nails.

See also OMIM:615327

Organism-specific databases

MIMi615327. phenotype.
Orphaneti79145. Dowling-Degos disease.
PharmGKBiPA33495.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 388362GDP-fucose protein O-fucosyltransferase 1PRO_0000012148Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 40By similarity
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi126 ↔ 140By similarity
Glycosylationi160 – 1601N-linked (GlcNAc...)1 Publication
Disulfide bondi249 ↔ 283By similarity
Disulfide bondi267 ↔ 354By similarity

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9H488.
PaxDbiQ9H488.
PeptideAtlasiQ9H488.
PRIDEiQ9H488.

PTM databases

PhosphoSiteiQ9H488.

Expressioni

Tissue specificityi

Highly expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

BgeeiQ9H488.
CleanExiHS_POFUT1.
ExpressionAtlasiQ9H488. baseline and differential.
GenevestigatoriQ9H488.

Organism-specific databases

HPAiHPA054519.

Interactioni

Protein-protein interaction databases

BioGridi117056. 6 interactions.
IntActiQ9H488. 2 interactions.
STRINGi9606.ENSP00000364902.

Structurei

3D structure databases

ProteinModelPortaliQ9H488.
SMRiQ9H488. Positions 30-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 463Substrate bindingBy similarity
Regioni238 – 2403Substrate bindingBy similarity
Regioni356 – 3572Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi385 – 3884Prevents secretion from ERSequence Analysis

Sequence similaritiesi

Belongs to the glycosyltransferase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG250895.
GeneTreeiENSGT00390000015634.
HOGENOMiHOG000231651.
HOVERGENiHBG059976.
InParanoidiQ9H488.
KOiK03691.
OMAiRNGIDWV.
PhylomeDBiQ9H488.
TreeFamiTF314805.

Family and domain databases

InterProiIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamiPF10250. O-FucT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H488-1) [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
MGAAAWARPL SVSFLLLLLP LPGMPAGSWD PAGYLLYCPC MGRFGNQADH
60 70 80 90 100
FLGSLAFAKL LNRTLAVPPW IEYQHHKPPF TNLHVSYQKY FKLEPLQAYH
110 120 130 140 150
RVISLEDFME KLAPTHWPPE KRVAYCFEVA AQRSPDKKTC PMKEGNPFGP
160 170 180 190 200
FWDQFHVSFN KSELFTGISF SASYREQWSQ RFSPKEHPVL ALPGAPAQFP
210 220 230 240 250
VLEEHRPLQK YMVWSDEMVK TGEAQIHAHL VRPYVGIHLR IGSDWKNACA
260 270 280 290 300
MLKDGTAGSH FMASPQCVGY SRSTAAPLTM TMCLPDLKEI QRAVKLWVRS
310 320 330 340 350
LDAQSVYVAT DSESYVPELQ QLFKGKVKVV SLKPEVAQVD LYILGQADHF
360 370 380
IGNCVSSFTA FVKRERDLQG RPSSFFGMDR PPKLRDEF
Length:388
Mass (Da):43,956
Last modified:March 1, 2001 - v1
Checksum:i3FACCCA434D02415
GO
Isoform 2 (identifier: Q9H488-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     182-388: FSPKEHPVLA...DRPPKLRDEF → RENHSCVTLLFPR

Note: No experimental confirmation available.

Show »
Length:194
Mass (Da):22,338
Checksum:i5ADE77CE45147644
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti322 – 3221L → F.
Corresponds to variant rs17268666 [ dbSNP | Ensembl ].
VAR_049231
Natural varianti348 – 3481D → N.
Corresponds to variant rs35259534 [ dbSNP | Ensembl ].
VAR_049232

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei182 – 388207FSPKE…LRDEF → RENHSCVTLLFPR in isoform 2. 1 PublicationVSP_001809Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF375884 mRNA. Translation: AAL09576.1.
D80002 mRNA. Translation: BAA11497.2.
AL121897 Genomic DNA. Translation: CAC16424.1.
AL121897 Genomic DNA. Translation: CAH73300.1.
AK291033 mRNA. Translation: BAF83722.1.
CH471077 Genomic DNA. Translation: EAW76383.1.
CH471077 Genomic DNA. Translation: EAW76384.1.
CH471077 Genomic DNA. Translation: EAW76385.1.
BC000582 mRNA. Translation: AAH00582.1.
CCDSiCCDS13198.1. [Q9H488-1]
CCDS13199.1. [Q9H488-2]
RefSeqiNP_056167.1. NM_015352.1. [Q9H488-1]
NP_758436.1. NM_172236.1. [Q9H488-2]
UniGeneiHs.472409.

Genome annotation databases

EnsembliENST00000375730; ENSP00000364882; ENSG00000101346. [Q9H488-2]
ENST00000375749; ENSP00000364902; ENSG00000101346. [Q9H488-1]
GeneIDi23509.
KEGGihsa:23509.
UCSCiuc002wxo.3. human. [Q9H488-2]
uc002wxp.3. human. [Q9H488-1]

Polymorphism databases

DMDMi23396787.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF375884 mRNA. Translation: AAL09576.1.
D80002 mRNA. Translation: BAA11497.2.
AL121897 Genomic DNA. Translation: CAC16424.1.
AL121897 Genomic DNA. Translation: CAH73300.1.
AK291033 mRNA. Translation: BAF83722.1.
CH471077 Genomic DNA. Translation: EAW76383.1.
CH471077 Genomic DNA. Translation: EAW76384.1.
CH471077 Genomic DNA. Translation: EAW76385.1.
BC000582 mRNA. Translation: AAH00582.1.
CCDSiCCDS13198.1. [Q9H488-1]
CCDS13199.1. [Q9H488-2]
RefSeqiNP_056167.1. NM_015352.1. [Q9H488-1]
NP_758436.1. NM_172236.1. [Q9H488-2]
UniGeneiHs.472409.

3D structure databases

ProteinModelPortaliQ9H488.
SMRiQ9H488. Positions 30-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117056. 6 interactions.
IntActiQ9H488. 2 interactions.
STRINGi9606.ENSP00000364902.

Protein family/group databases

CAZyiGT65. Glycosyltransferase Family 65.

PTM databases

PhosphoSiteiQ9H488.

Polymorphism databases

DMDMi23396787.

Proteomic databases

MaxQBiQ9H488.
PaxDbiQ9H488.
PeptideAtlasiQ9H488.
PRIDEiQ9H488.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375730; ENSP00000364882; ENSG00000101346. [Q9H488-2]
ENST00000375749; ENSP00000364902; ENSG00000101346. [Q9H488-1]
GeneIDi23509.
KEGGihsa:23509.
UCSCiuc002wxo.3. human. [Q9H488-2]
uc002wxp.3. human. [Q9H488-1]

Organism-specific databases

CTDi23509.
GeneCardsiGC20P030795.
HGNCiHGNC:14988. POFUT1.
HPAiHPA054519.
MIMi607491. gene.
615327. phenotype.
neXtProtiNX_Q9H488.
Orphaneti79145. Dowling-Degos disease.
PharmGKBiPA33495.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250895.
GeneTreeiENSGT00390000015634.
HOGENOMiHOG000231651.
HOVERGENiHBG059976.
InParanoidiQ9H488.
KOiK03691.
OMAiRNGIDWV.
PhylomeDBiQ9H488.
TreeFamiTF314805.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
SignaLinkiQ9H488.

Miscellaneous databases

ChiTaRSiPOFUT1. human.
GenomeRNAii23509.
NextBioi45915.
PROiQ9H488.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H488.
CleanExiHS_POFUT1.
ExpressionAtlasiQ9H488. baseline and differential.
GenevestigatoriQ9H488.

Family and domain databases

InterProiIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamiPF10250. O-FucT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Modification of epidermal growth factor-like repeats with O-fucose: molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase."
    Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., Haltiwanger R.S.
    J. Biol. Chem. 276:40338-40345(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Heart.
  2. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
    DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "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 1).
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Brain.
  8. "O-linked fucose and other post-translational modifications unique to EGF modules."
    Harris R.J., Spellman M.W.
    Glycobiology 3:219-224(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160.
    Tissue: Liver.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Mutations in POFUT1, encoding protein O-fucosyltransferase 1, cause generalized Dowling-Degos disease."
    Li M., Cheng R., Liang J., Yan H., Zhang H., Yang L., Li C., Jiao Q., Lu Z., He J., Ji J., Shen Z., Li C., Hao F., Yu H., Yao Z.
    Am. J. Hum. Genet. 92:895-903(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DDD2.

Entry informationi

Entry nameiOFUT1_HUMAN
AccessioniPrimary (citable) accession number: Q9H488
Secondary accession number(s): A8K4R8
, E1P5M4, Q14685, Q5W185, Q9BW76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 125 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.