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Q14435

- GALT3_HUMAN

UniProt

Q14435 - GALT3_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 3

Gene

GALNT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis.2 Publications

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei225 – 2251SubstrateBy similarity
    Binding sitei254 – 2541SubstrateBy similarity
    Metal bindingi277 – 2771ManganeseBy similarity
    Metal bindingi279 – 2791ManganeseBy similarity
    Binding sitei387 – 3871SubstrateBy similarity
    Metal bindingi415 – 4151ManganeseBy similarity
    Binding sitei418 – 4181SubstrateBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: BHF-UCL
    2. manganese ion binding Source: BHF-UCL
    3. polypeptide N-acetylgalactosaminyltransferase activity Source: BHF-UCL

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. cellular protein metabolic process Source: Reactome
    3. O-glycan processing Source: Reactome
    4. post-translational protein modification Source: Reactome
    5. protein O-linked glycosylation via serine Source: BHF-UCL
    6. protein O-linked glycosylation via threonine Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi2.4.1.41. 2681.
    ReactomeiREACT_115606. O-linked glycosylation of mucins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 3 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 3
    Short name:
    GalNAc-T3
    Short name:
    pp-GaNTase 3
    Protein-UDP acetylgalactosaminyltransferase 3
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
    Gene namesi
    Name:GALNT3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4125. GALNT3.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane 1 Publication; Single-pass type II membrane protein 1 Publication
    Note: Resides preferentially in the trans and medial parts of the Golgi stack.

    GO - Cellular componenti

    1. Golgi cisterna membrane Source: UniProtKB-SubCell
    2. Golgi membrane Source: Reactome
    3. integral component of membrane Source: ProtInc
    4. membrane Source: ProtInc
    5. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Tumoral calcinosis, hyperphosphatemic, familial (HFTC) [MIM:211900]: A severe metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi211900. phenotype.
    Orphaneti306661. Hypercalcemic tumoral calcinosis.
    PharmGKBiPA28538.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 633633Polypeptide N-acetylgalactosaminyltransferase 3PRO_0000059106Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi173 ↔ 410PROSITE-ProRule annotation
    Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi401 ↔ 482PROSITE-ProRule annotation
    Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi517 ↔ 535PROSITE-ProRule annotation
    Disulfide bondi561 ↔ 574PROSITE-ProRule annotation
    Disulfide bondi605 ↔ 618PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ14435.
    PaxDbiQ14435.
    PRIDEiQ14435.

    PTM databases

    PhosphoSiteiQ14435.

    Expressioni

    Tissue specificityi

    Expressed in organs that contain secretory epithelial glands. Highly expressed in pancreas, skin, kidney and testis. Weakly expressed in prostate, ovary, intestine and colon. Also expressed in placenta and lung and fetal lung and fetal kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ14435.
    BgeeiQ14435.
    CleanExiHS_GALNT3.
    GenevestigatoriQ14435.

    Organism-specific databases

    HPAiHPA007613.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000376465.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14435.
    SMRiQ14435. Positions 122-633.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 633596LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei20 – 3718Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini504 – 630127Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 293110Catalytic subdomain AAdd
    BLAST
    Regioni356 – 41863Catalytic subdomain BAdd
    BLAST

    Domaini

    There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity
    The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.By similarity

    Sequence similaritiesi

    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG239675.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    InParanoidiQ14435.
    KOiK00710.
    OMAiQYFEYSA.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ14435.
    TreeFamiTF313267.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14435-1) [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

    MAHLKRLVKL HIKRHYHKKF WKLGAVIFFF IIVLVLMQRE VSVQYSKEES    50
    RMERNMKNKN KMLDLMLEAV NNIKDAMPKM QIGAPVRQNI DAGERPCLQG 100
    YYTAAELKPV LDRPPQDSNA PGASGKAFKT TNLSVEEQKE KERGEAKHCF 150
    NAFASDRISL HRDLGPDTRP PECIEQKFKR CPPLPTTSVI IVFHNEAWST 200
    LLRTVHSVLY SSPAILLKEI ILVDDASVDE YLHDKLDEYV KQFSIVKIVR 250
    QRERKGLITA RLLGATVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA 300
    VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR 350
    KDETYPIKTP TFAGGLFSIS KEYFEYIGSY DEEMEIWGGE NIEMSFRVWQ 400
    CGGQLEIMPC SVVGHVFRSK SPHSFPKGTQ VIARNQVRLA EVWMDEYKEI 450
    FYRRNTDAAK IVKQKAFGDL SKRFEIKHRL QCKNFTWYLN NIYPEVYVPD 500
    LNPVISGYIK SVGQPLCLDV GENNQGGKPL IMYTCHGLGG NQYFEYSAQH 550
    EIRHNIQKEL CLHAAQGLVQ LKACTYKGHK TVVTGEQIWE IQKDQLLYNP 600
    FLKMCLSANG EHPSLVSCNP SDPLQKWILS QND 633
    Length:633
    Mass (Da):72,610
    Last modified:October 14, 2008 - v2
    Checksum:i3019B2DCCC19A584
    GO
    Isoform 2 (identifier: Q14435-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         173-192: CIEQKFKRCPPLPTTSVIIV → YVEEYLLFILYHQALQGREG
         193-633: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:192
    Mass (Da):22,212
    Checksum:i2EEE40B4D6537601
    GO

    Sequence cautioni

    The sequence AAH56246.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti481 – 4811Q → R in CAA63371. (PubMed:8663203)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei173 – 19220CIEQK…SVIIV → YVEEYLLFILYHQALQGREG in isoform 2. 1 PublicationVSP_011202Add
    BLAST
    Alternative sequencei193 – 633441Missing in isoform 2. 1 PublicationVSP_011203Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92689 mRNA. Translation: CAA63371.1.
    AC009495 Genomic DNA. Translation: AAY14678.1.
    CH471058 Genomic DNA. Translation: EAX11324.1.
    BC056246 mRNA. Translation: AAH56246.1. Different initiation.
    BC113565 mRNA. Translation: AAI13566.1.
    BC113567 mRNA. Translation: AAI13568.1.
    CCDSiCCDS2226.1. [Q14435-1]
    RefSeqiNP_004473.2. NM_004482.3. [Q14435-1]
    XP_005246506.1. XM_005246449.1. [Q14435-1]
    UniGeneiHs.170986.

    Genome annotation databases

    EnsembliENST00000392701; ENSP00000376465; ENSG00000115339. [Q14435-1]
    GeneIDi2591.
    KEGGihsa:2591.
    UCSCiuc002udi.2. human. [Q14435-2]
    uc010fph.1. human. [Q14435-1]

    Polymorphism databases

    DMDMi209572629.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 3

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92689 mRNA. Translation: CAA63371.1 .
    AC009495 Genomic DNA. Translation: AAY14678.1 .
    CH471058 Genomic DNA. Translation: EAX11324.1 .
    BC056246 mRNA. Translation: AAH56246.1 . Different initiation.
    BC113565 mRNA. Translation: AAI13566.1 .
    BC113567 mRNA. Translation: AAI13568.1 .
    CCDSi CCDS2226.1. [Q14435-1 ]
    RefSeqi NP_004473.2. NM_004482.3. [Q14435-1 ]
    XP_005246506.1. XM_005246449.1. [Q14435-1 ]
    UniGenei Hs.170986.

    3D structure databases

    ProteinModelPortali Q14435.
    SMRi Q14435. Positions 122-633.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000376465.

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    PTM databases

    PhosphoSitei Q14435.

    Polymorphism databases

    DMDMi 209572629.

    Proteomic databases

    MaxQBi Q14435.
    PaxDbi Q14435.
    PRIDEi Q14435.

    Protocols and materials databases

    DNASUi 2591.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392701 ; ENSP00000376465 ; ENSG00000115339 . [Q14435-1 ]
    GeneIDi 2591.
    KEGGi hsa:2591.
    UCSCi uc002udi.2. human. [Q14435-2 ]
    uc010fph.1. human. [Q14435-1 ]

    Organism-specific databases

    CTDi 2591.
    GeneCardsi GC02M166567.
    H-InvDB HIX0024214.
    HGNCi HGNC:4125. GALNT3.
    HPAi HPA007613.
    MIMi 211900. phenotype.
    601756. gene.
    neXtProti NX_Q14435.
    Orphaneti 306661. Hypercalcemic tumoral calcinosis.
    PharmGKBi PA28538.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239675.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q14435.
    KOi K00710.
    OMAi QYFEYSA.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q14435.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 2681.
    Reactomei REACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    ChiTaRSi GALNT3. human.
    GeneWikii GALNT3.
    GenomeRNAii 2591.
    NextBioi 10249.
    PROi Q14435.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14435.
    Bgeei Q14435.
    CleanExi HS_GALNT3.
    Genevestigatori Q14435.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3."
      Bennett E.P., Hassan H., Clausen H.
      J. Biol. Chem. 271:17006-17012(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Salivary gland.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Lung.
    5. "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3."
      Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
      J. Biol. Chem. 272:23503-23514(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus."
      Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.
      J. Cell Sci. 111:45-60(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma."
      Onitsuka K., Shibao K., Nakayama Y., Minagawa N., Hirata K., Izumi H., Matsuo K., Nagata N., Kitazato K., Kohno K., Itoh H.
      Cancer Sci. 94:32-36(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis."
      Topaz O., Shurman D.L., Bergman R., Indelman M., Ratajczak P., Mizrachi M., Khamaysi Z., Behar D., Petronius D., Friedman V., Zelikovic I., Raimer S., Metzker A., Richard G., Sprecher E.
      Nat. Genet. 36:579-581(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HFTC.
    9. "Identification of a recurrent mutation in GALNT3 demonstrates that hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are allelic disorders."
      Frishberg Y., Topaz O., Bergman R., Behar D., Fisher D., Gordon D., Richard G., Sprecher E.
      J. Mol. Med. 83:33-38(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HFTC.
    10. "Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation."
      Kato K., Jeanneau C., Tarp M.A., Benet-Pages A., Lorenz-Depiereux B., Bennett E.P., Mandel U., Strom T.M., Clausen H.
      J. Biol. Chem. 281:18370-18377(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGALT3_HUMAN
    AccessioniPrimary (citable) accession number: Q14435
    Secondary accession number(s): Q53TG9, Q7Z476
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 134 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

    Miscellaneous

    Overexpressed in many differentiated carcinomas, suggesting that it may serve as a marker of tumor differentiation.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3