Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9H488

- OFUT1_HUMAN

UniProt

Q9H488 - OFUT1_HUMAN

Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

POFUT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Dowling-Degos disease 2 (DDD2) [MIM:615327]: An 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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

    ArrayExpressiQ9H488.
    BgeeiQ9H488.
    CleanExiHS_POFUT1.
    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.
    HOGENOMiHOG000231651.
    HOVERGENiHBG059976.
    InParanoidiQ9H488.
    KOiK03691.
    OMAiSEHPVLA.
    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

    MGAAAWARPL SVSFLLLLLP LPGMPAGSWD PAGYLLYCPC MGRFGNQADH    50
    FLGSLAFAKL LNRTLAVPPW IEYQHHKPPF TNLHVSYQKY FKLEPLQAYH 100
    RVISLEDFME KLAPTHWPPE KRVAYCFEVA AQRSPDKKTC PMKEGNPFGP 150
    FWDQFHVSFN KSELFTGISF SASYREQWSQ RFSPKEHPVL ALPGAPAQFP 200
    VLEEHRPLQK YMVWSDEMVK TGEAQIHAHL VRPYVGIHLR IGSDWKNACA 250
    MLKDGTAGSH FMASPQCVGY SRSTAAPLTM TMCLPDLKEI QRAVKLWVRS 300
    LDAQSVYVAT DSESYVPELQ QLFKGKVKVV SLKPEVAQVD LYILGQADHF 350
    IGNCVSSFTA FVKRERDLQG RPSSFFGMDR PPKLRDEF 388
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13198.1. [Q9H488-1 ]
    CCDS13199.1. [Q9H488-2 ]
    RefSeqi NP_056167.1. NM_015352.1. [Q9H488-1 ]
    NP_758436.1. NM_172236.1. [Q9H488-2 ]
    UniGenei Hs.472409.

    3D structure databases

    ProteinModelPortali Q9H488.
    SMRi Q9H488. Positions 30-378.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117056. 6 interactions.
    IntActi Q9H488. 2 interactions.
    STRINGi 9606.ENSP00000364902.

    Protein family/group databases

    CAZyi GT65. Glycosyltransferase Family 65.

    PTM databases

    PhosphoSitei Q9H488.

    Polymorphism databases

    DMDMi 23396787.

    Proteomic databases

    MaxQBi Q9H488.
    PaxDbi Q9H488.
    PeptideAtlasi Q9H488.
    PRIDEi Q9H488.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375730 ; ENSP00000364882 ; ENSG00000101346 . [Q9H488-2 ]
    ENST00000375749 ; ENSP00000364902 ; ENSG00000101346 . [Q9H488-1 ]
    GeneIDi 23509.
    KEGGi hsa:23509.
    UCSCi uc002wxo.3. human. [Q9H488-2 ]
    uc002wxp.3. human. [Q9H488-1 ]

    Organism-specific databases

    CTDi 23509.
    GeneCardsi GC20P030795.
    HGNCi HGNC:14988. POFUT1.
    HPAi HPA054519.
    MIMi 607491. gene.
    615327. phenotype.
    neXtProti NX_Q9H488.
    Orphaneti 79145. Dowling-Degos disease.
    PharmGKBi PA33495.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250895.
    HOGENOMi HOG000231651.
    HOVERGENi HBG059976.
    InParanoidi Q9H488.
    KOi K03691.
    OMAi SEHPVLA.
    PhylomeDBi Q9H488.
    TreeFami TF314805.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
    SignaLinki Q9H488.

    Miscellaneous databases

    ChiTaRSi POFUT1. human.
    GenomeRNAii 23509.
    NextBioi 45915.
    PROi Q9H488.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H488.
    Bgeei Q9H488.
    CleanExi HS_POFUT1.
    Genevestigatori Q9H488.

    Family and domain databases

    InterProi IPR019378. GDP-Fuc_O-FucTrfase.
    [Graphical view ]
    Pfami PF10250. O-FucT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 123 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