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Protein

Beta-1,4-galactosyltransferase 2

Gene

B4GALT2

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

Functioni

Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose.

Catalytic activityi

UDP-alpha-D-galactose + D-glucose = UDP + lactose.
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide.
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.

Cofactori

Mn2+By similarity

Kineticsi

  1. KM=71 µM for GlcNAc-B-S-pNP1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi218 – 2181ManganeseBy similarity
    Binding sitei278 – 2781UDP-alpha-D-galactoseBy similarity
    Metal bindingi311 – 3111Manganese; via tele nitrogenBy similarity
    Binding sitei323 – 3231N-acetyl-D-glucosamineBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi2.4.1.38. 2681.
    2.4.1.90. 2681.
    ReactomeiREACT_121120. Keratan sulfate biosynthesis.
    REACT_25085. N-Glycan antennae elongation.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT7. Glycosyltransferase Family 7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-1,4-galactosyltransferase 2 (EC:2.4.1.-)
    Short name:
    Beta-1,4-GalTase 2
    Short name:
    Beta4Gal-T2
    Short name:
    b4Gal-T2
    Alternative name(s):
    UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2
    UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2
    Including the following 4 domains:
    Lactose synthase A protein (EC:2.4.1.22)
    N-acetyllactosamine synthase (EC:2.4.1.90)
    Alternative name(s):
    Nal synthase
    Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC:2.4.1.38)
    Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase (EC:2.4.1.-)
    Gene namesi
    Name:B4GALT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:925. B4GALT2.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei16 – 3621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini37 – 372336LumenalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25224.

    Chemistry

    DrugBankiDB00141. N-Acetyl-D-glucosamine.

    Polymorphism and mutation databases

    BioMutaiB4GALT2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 372372Beta-1,4-galactosyltransferase 2PRO_0000080533Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi97 ↔ 139By similarity
    Disulfide bondi211 ↔ 230By similarity
    Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO60909.
    PaxDbiO60909.
    PRIDEiO60909.

    PTM databases

    PhosphoSiteiO60909.

    Expressioni

    Tissue specificityi

    Weakly expressed in various tissues. Highest expression in prostate, testis, ovary, intestine, muscle, and in fetal brain.

    Gene expression databases

    BgeeiO60909.
    CleanExiHS_B4GALT2.
    GenevestigatoriO60909.

    Organism-specific databases

    HPAiHPA047739.

    Interactioni

    Protein-protein interaction databases

    BioGridi114247. 1 interaction.
    IntActiO60909. 1 interaction.
    STRINGi9606.ENSP00000349293.

    Structurei

    3D structure databases

    ProteinModelPortaliO60909.
    SMRiO60909. Positions 97-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni150 – 1545UDP-alpha-D-galactose bindingBy similarity
    Regioni189 – 1913UDP-alpha-D-galactose bindingBy similarity
    Regioni217 – 2182UDP-alpha-D-galactose bindingBy similarity
    Regioni280 – 2834N-acetyl-D-glucosamine bindingBy similarity
    Regioni311 – 3133UDP-alpha-D-galactose bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyltransferase 7 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG327897.
    GeneTreeiENSGT00760000119140.
    HOGENOMiHOG000231027.
    HOVERGENiHBG058334.
    InParanoidiO60909.
    KOiK07967.
    OMAiEQPRHFA.
    OrthoDBiEOG7060R0.
    PhylomeDBiO60909.
    TreeFamiTF312834.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR003859. Galactosyl_T.
    IPR027791. Galactosyl_T_C.
    IPR027995. Galactosyl_T_N.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR19300. PTHR19300. 1 hit.
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF13733. Glyco_transf_7N. 1 hit.
    [Graphical view]
    PRINTSiPR02050. B14GALTRFASE.
    SUPFAMiSSF53448. SSF53448. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: O60909-1) [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
    MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSARGP
    60 70 80 90 100
    AHALHPAASS SSSSSNCSRP NATASSSGLP EVPSALPGPT APTLPPCPDS
    110 120 130 140 150
    PPGLVGRLLI EFTSPMPLER VQRENPGVLM GGRYTPPDCT PAQTVAVIIP
    160 170 180 190 200
    FRHREHHLRY WLHYLHPILR RQRLRYGVYV INQHGEDTFN RAKLLNVGFL
    210 220 230 240 250
    EALKEDAAYD CFIFSDVDLV PMDDRNLYRC GDQPRHFAIA MDKFGFRLPY
    260 270 280 290 300
    AGYFGGVSGL SKAQFLRING FPNEYWGWGG EDDDIFNRIS LTGMKISRPD
    310 320 330 340 350
    IRIGRYRMIK HDRDKHNEPN PQRFTKIQNT KLTMKRDGIG SVRYQVLEVS
    360 370
    RQPLFTNITV DIGRPPSWPP RG
    Length:372
    Mass (Da):41,972
    Last modified:August 1, 1998 - v1
    Checksum:iA6F7800251AA1E4F
    GO
    Isoform 2 (identifier: O60909-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-118: Missing.
         119-119: E → MPSTQLLAAAAAAATAPGPTPPPLAPGSLRSPVPCPVPRLPRCHPVLTRHLVL

    Note: No experimental confirmation available.

    Show »
    Length:306
    Mass (Da):34,883
    Checksum:iA483868104528A2B
    GO
    Isoform 3 (identifier: O60909-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAVEVQEQWPCLPAAGCPGPLGGPVAACGM

    Note: No experimental confirmation available.

    Show »
    Length:401
    Mass (Da):44,764
    Checksum:i70B4877C779850C1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001S → TS (PubMed:9597550).Curated
    Sequence conflicti136 – 1361P → S in AAC39733 (PubMed:9597550).Curated
    Sequence conflicti177 – 1771G → C in AAC39733 (PubMed:9597550).Curated
    Sequence conflicti315 – 3162KH → ND in AAC39733 (PubMed:9597550).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti122 – 1221Q → H.1 Publication
    Corresponds to variant rs1859728 [ dbSNP | Ensembl ].
    VAR_020487
    Natural varianti338 – 3381G → R.
    Corresponds to variant rs35904809 [ dbSNP | Ensembl ].
    VAR_054021

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 118118Missing in isoform 2. CuratedVSP_014103Add
    BLAST
    Alternative sequencei1 – 11M → MAVEVQEQWPCLPAAGCPGP LGGPVAACGM in isoform 3. 1 PublicationVSP_043010
    Alternative sequencei119 – 1191E → MPSTQLLAAAAAAATAPGPT PPPLAPGSLRSPVPCPVPRL PRCHPVLTRHLVL in isoform 2. CuratedVSP_014104

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y12510 mRNA. Translation: CAA73112.1.
    AF038660 mRNA. Translation: AAC39733.1.
    AB024434 mRNA. Translation: BAA75819.1.
    AK095873 mRNA. Translation: BAG53152.1.
    AK293418 mRNA. Translation: BAG56925.1.
    AL139220, AL357079 Genomic DNA. Translation: CAI19431.1.
    AL139220, AL357079 Genomic DNA. Translation: CAI19432.1.
    AL357079, AL139220 Genomic DNA. Translation: CAI16802.1.
    AL357079, AL139220 Genomic DNA. Translation: CAI16803.1.
    CH471059 Genomic DNA. Translation: EAX07062.1.
    CH471059 Genomic DNA. Translation: EAX07063.1.
    CH471059 Genomic DNA. Translation: EAX07064.1.
    CH471059 Genomic DNA. Translation: EAX07065.1.
    BC096821 mRNA. Translation: AAH96821.1.
    AL137647 mRNA. Translation: CAB70857.1.
    CCDSiCCDS506.1. [O60909-1]
    CCDS55596.1. [O60909-3]
    PIRiT46511.
    RefSeqiNP_001005417.1. NM_001005417.2. [O60909-1]
    NP_003771.1. NM_003780.4. [O60909-1]
    NP_085076.2. NM_030587.2. [O60909-3]
    UniGeneiHs.632403.
    Hs.736507.

    Genome annotation databases

    EnsembliENST00000309519; ENSP00000310696; ENSG00000117411. [O60909-3]
    ENST00000356836; ENSP00000349293; ENSG00000117411. [O60909-1]
    ENST00000372324; ENSP00000361399; ENSG00000117411. [O60909-1]
    ENST00000434555; ENSP00000407468; ENSG00000117411. [O60909-2]
    GeneIDi8704.
    KEGGihsa:8704.
    UCSCiuc001clg.3. human. [O60909-1]
    uc001clh.3. human. [O60909-2]
    uc010okl.2. human. [O60909-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Beta-1,4-galactosyltransferase 2

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y12510 mRNA. Translation: CAA73112.1.
    AF038660 mRNA. Translation: AAC39733.1.
    AB024434 mRNA. Translation: BAA75819.1.
    AK095873 mRNA. Translation: BAG53152.1.
    AK293418 mRNA. Translation: BAG56925.1.
    AL139220, AL357079 Genomic DNA. Translation: CAI19431.1.
    AL139220, AL357079 Genomic DNA. Translation: CAI19432.1.
    AL357079, AL139220 Genomic DNA. Translation: CAI16802.1.
    AL357079, AL139220 Genomic DNA. Translation: CAI16803.1.
    CH471059 Genomic DNA. Translation: EAX07062.1.
    CH471059 Genomic DNA. Translation: EAX07063.1.
    CH471059 Genomic DNA. Translation: EAX07064.1.
    CH471059 Genomic DNA. Translation: EAX07065.1.
    BC096821 mRNA. Translation: AAH96821.1.
    AL137647 mRNA. Translation: CAB70857.1.
    CCDSiCCDS506.1. [O60909-1]
    CCDS55596.1. [O60909-3]
    PIRiT46511.
    RefSeqiNP_001005417.1. NM_001005417.2. [O60909-1]
    NP_003771.1. NM_003780.4. [O60909-1]
    NP_085076.2. NM_030587.2. [O60909-3]
    UniGeneiHs.632403.
    Hs.736507.

    3D structure databases

    ProteinModelPortaliO60909.
    SMRiO60909. Positions 97-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114247. 1 interaction.
    IntActiO60909. 1 interaction.
    STRINGi9606.ENSP00000349293.

    Chemistry

    DrugBankiDB00141. N-Acetyl-D-glucosamine.

    Protein family/group databases

    CAZyiGT7. Glycosyltransferase Family 7.

    PTM databases

    PhosphoSiteiO60909.

    Polymorphism and mutation databases

    BioMutaiB4GALT2.

    Proteomic databases

    MaxQBiO60909.
    PaxDbiO60909.
    PRIDEiO60909.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000309519; ENSP00000310696; ENSG00000117411. [O60909-3]
    ENST00000356836; ENSP00000349293; ENSG00000117411. [O60909-1]
    ENST00000372324; ENSP00000361399; ENSG00000117411. [O60909-1]
    ENST00000434555; ENSP00000407468; ENSG00000117411. [O60909-2]
    GeneIDi8704.
    KEGGihsa:8704.
    UCSCiuc001clg.3. human. [O60909-1]
    uc001clh.3. human. [O60909-2]
    uc010okl.2. human. [O60909-3]

    Organism-specific databases

    CTDi8704.
    GeneCardsiGC01P044444.
    HGNCiHGNC:925. B4GALT2.
    HPAiHPA047739.
    MIMi604013. gene.
    neXtProtiNX_O60909.
    PharmGKBiPA25224.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG327897.
    GeneTreeiENSGT00760000119140.
    HOGENOMiHOG000231027.
    HOVERGENiHBG058334.
    InParanoidiO60909.
    KOiK07967.
    OMAiEQPRHFA.
    OrthoDBiEOG7060R0.
    PhylomeDBiO60909.
    TreeFamiTF312834.

    Enzyme and pathway databases

    UniPathwayiUPA00378.
    BRENDAi2.4.1.38. 2681.
    2.4.1.90. 2681.
    ReactomeiREACT_121120. Keratan sulfate biosynthesis.
    REACT_25085. N-Glycan antennae elongation.

    Miscellaneous databases

    ChiTaRSiB4GALT2. human.
    GeneWikiiB4GALT2.
    GenomeRNAii8704.
    NextBioi32635.
    PROiO60909.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO60909.
    CleanExiHS_B4GALT2.
    GenevestigatoriO60909.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR003859. Galactosyl_T.
    IPR027791. Galactosyl_T_C.
    IPR027995. Galactosyl_T_N.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR19300. PTHR19300. 1 hit.
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF13733. Glyco_transf_7N. 1 hit.
    [Graphical view]
    PRINTSiPR02050. B14GALTRFASE.
    SUPFAMiSSF53448. SSF53448. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3."
      Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G., van Kessel A.G., Rygaard E., Hassan H., Bennett E., Clausen H.
      J. Biol. Chem. 272:31979-31991(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The expanding beta 4-galactosyltransferase gene family: messages from the databanks."
      Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.
      Glycobiology 8:517-526(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells."
      Guo S., Sato T., Shirane K., Furukawa K.
      Glycobiology 11:813-820(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Erythroleukemia.
    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] (ISOFORMS 1 AND 3).
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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 1), VARIANT HIS-122.
      Tissue: Chondrosarcoma.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-372 (ISOFORMS 1/2).
      Tissue: Uterus.
    9. "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions."
      Amado M., Almeida R., Schwientek T., Clausen H.
      Biochim. Biophys. Acta 1473:35-53(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiB4GT2_HUMAN
    AccessioniPrimary (citable) accession number: O60909
    Secondary accession number(s): B3KTP0
    , B4DE14, D3DPY6, D3DPY7, O60511, Q4V9L9, Q5T4X5, Q5T4Y5, Q9BUP6, Q9NSY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: August 1, 1998
    Last modified: May 27, 2015
    This is version 143 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 1
      Human chromosome 1: 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.