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)

P15907

- SIAT1_HUMAN

UniProt

P15907 - SIAT1_HUMAN

Protein

Beta-galactoside alpha-2,6-sialyltransferase 1

Gene

ST6GAL1

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 158 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates.2 Publications

    Catalytic activityi

    CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine.2 Publications

    Enzyme regulationi

    Inhibited by CTP.1 Publication

    Kineticsi

    1. KM=530 µM for CMP-NeuAc1 Publication

    Vmax=1.074 pmol/min/µg enzyme1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei189 – 1891Substrate; via amide nitrogen
    Binding sitei212 – 2121Substrate
    Binding sitei233 – 2331Substrate
    Binding sitei353 – 3531Substrate; via carbonyl oxygen
    Binding sitei354 – 3541Substrate
    Binding sitei365 – 3651Substrate
    Binding sitei369 – 3691SubstrateCurated
    Binding sitei370 – 3701Substrate
    Binding sitei376 – 3761Substrate

    GO - Molecular functioni

    1. beta-galactoside alpha-2,6-sialyltransferase activity Source: UniProtKB
    2. sialyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. humoral immune response Source: ProtInc
    3. N-acetylneuraminate metabolic process Source: UniProtKB
    4. O-glycan processing Source: Reactome
    5. post-translational protein modification Source: Reactome
    6. protein N-linked glycosylation via asparagine Source: UniProtKB
    7. sialylation Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01118-MONOMER.
    BRENDAi2.4.99.1. 2681.
    ReactomeiREACT_115835. Termination of O-glycan biosynthesis.
    REACT_200874. Sialic acid metabolism.
    REACT_25085. N-Glycan antennae elongation.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT29. Glycosyltransferase Family 29.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactoside alpha-2,6-sialyltransferase 1 (EC:2.4.99.1)
    Short name:
    Alpha 2,6-ST 1
    Alternative name(s):
    B-cell antigen CD75
    CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1
    ST6Gal I
    Short name:
    ST6GalI
    Sialyltransferase 1
    Gene namesi
    Name:ST6GAL1
    Synonyms:SIAT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:10860. ST6GAL1.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted
    Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. Golgi membrane Source: Reactome
    4. integral component of Golgi membrane Source: InterPro

    Keywords - Cellular componenti

    Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35762.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Beta-galactoside alpha-2,6-sialyltransferase 1PRO_0000149249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi142 ↔ 4061 Publication
    Glycosylationi149 – 1491N-linked (GlcNAc...)2 Publications
    Glycosylationi161 – 1611N-linked (GlcNAc...)1 Publication
    Disulfide bondi184 ↔ 3351 Publication
    Disulfide bondi353 ↔ 3641 Publication
    Modified residuei369 – 3691Phosphotyrosine1 Publication

    Post-translational modificationi

    The soluble form derives from the membrane form by proteolytic processing.
    The HB-6, CDW75, and CD76 differentiation antigens are cell-surface carbohydrate determinants generated by this enzyme.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP15907.
    PaxDbiP15907.
    PRIDEiP15907.

    PTM databases

    PhosphoSiteiP15907.

    Expressioni

    Gene expression databases

    ArrayExpressiP15907.
    BgeeiP15907.
    CleanExiHS_ST6GAL1.
    GenevestigatoriP15907.

    Organism-specific databases

    HPAiCAB015018.
    CAB016122.

    Interactioni

    Protein-protein interaction databases

    BioGridi112374. 2 interactions.
    IntActiP15907. 1 interaction.
    MINTiMINT-5000509.
    STRINGi9606.ENSP00000169298.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi102 – 1043
    Helixi107 – 11812
    Helixi137 – 14711
    Turni158 – 1614
    Helixi163 – 1653
    Turni166 – 1683
    Helixi174 – 1774
    Beta strandi181 – 1877
    Helixi191 – 1933
    Helixi199 – 2024
    Beta strandi205 – 2117
    Helixi220 – 2234
    Beta strandi228 – 2336
    Helixi234 – 2396
    Helixi241 – 2444
    Helixi247 – 2504
    Beta strandi251 – 2577
    Helixi266 – 2716
    Helixi278 – 28710
    Beta strandi293 – 2964
    Helixi299 – 31113
    Beta strandi312 – 3143
    Helixi323 – 33412
    Beta strandi335 – 34410
    Beta strandi354 – 3563
    Helixi363 – 3664
    Beta strandi368 – 3703
    Helixi372 – 38211
    Helixi387 – 3937
    Beta strandi395 – 3995
    Helixi401 – 4033

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JS1X-ray2.09A89-406[»]
    4JS2X-ray2.30A89-406[»]
    ProteinModelPortaliP15907.
    SMRiP15907. Positions 89-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99Cytoplasmic
    Topological domaini27 – 406380LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 2617Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni322 – 3243Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyltransferase 29 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG249416.
    HOGENOMiHOG000013206.
    HOVERGENiHBG052853.
    InParanoidiP15907.
    KOiK00778.
    OMAiQVWNKDS.
    PhylomeDBiP15907.
    TreeFamiTF323961.

    Family and domain databases

    InterProiIPR001675. Glyco_trans_29.
    IPR012163. Sialyl_trans.
    [Graphical view]
    PfamiPF00777. Glyco_transf_29. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005557. Sialyl_trans. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P15907-1) [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

    MIHTNLKKKF SCCVLVFLLF AVICVWKEKK KGSYYDSFKL QTKEFQVLKS    50
    LGKLAMGSDS QSVSSSSTQD PHRGRQTLGS LRGLAKAKPE ASFQVWNKDS 100
    SSKNLIPRLQ KIWKNYLSMN KYKVSYKGPG PGIKFSAEAL RCHLRDHVNV 150
    SMVEVTDFPF NTSEWEGYLP KESIRTKAGP WGRCAVVSSA GSLKSSQLGR 200
    EIDDHDAVLR FNGAPTANFQ QDVGTKTTIR LMNSQLVTTE KRFLKDSLYN 250
    EGILIVWDPS VYHSDIPKWY QNPDYNFFNN YKTYRKLHPN QPFYILKPQM 300
    PWELWDILQE ISPEEIQPNP PSSGMLGIII MMTLCDQVDI YEFLPSKRKT 350
    DVCYYYQKFF DSACTMGAYH PLLYEKNLVK HLNQGTDEDI YLLGKATLPG 400
    FRTIHC 406
    Length:406
    Mass (Da):46,605
    Last modified:April 1, 1990 - v1
    Checksum:iAC1E24A3875CF00F
    GO
    Isoform 2 (identifier: P15907-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-231: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:175
    Mass (Da):20,764
    Checksum:i2A31915E3D582F4B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271K → L in CAA38246. (PubMed:2373995)Curated
    Sequence conflicti72 – 732HR → T in CAA38246. (PubMed:2373995)Curated
    Sequence conflicti144 – 1441L → P in CAA38246. (PubMed:2373995)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 231231Missing in isoform 2. 1 PublicationVSP_056076Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17247 mRNA. Translation: CAA35111.1.
    X54363 mRNA. Translation: CAA38246.1.
    X62822 mRNA. Translation: CAA44634.1.
    AK292879 mRNA. Translation: BAF85568.1.
    AK312023 mRNA. Translation: BAG34960.1.
    AC007488 Genomic DNA. No translation available.
    AC007690 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78160.1.
    CH471052 Genomic DNA. Translation: EAW78161.1.
    CH471052 Genomic DNA. Translation: EAW78162.1.
    CH471052 Genomic DNA. Translation: EAW78164.1.
    BC031476 mRNA. Translation: AAH31476.1.
    BC040009 mRNA. Translation: AAH40009.1.
    CCDSiCCDS3285.1.
    PIRiA41734.
    RefSeqiNP_003023.1. NM_003032.2.
    NP_775323.1. NM_173216.2.
    NP_775324.1. NM_173217.2.
    XP_005247774.1. XM_005247717.1.
    XP_005247776.1. XM_005247719.1.
    XP_005247777.1. XM_005247720.1.
    XP_006713797.1. XM_006713734.1.
    UniGeneiHs.207459.

    Genome annotation databases

    EnsembliENST00000169298; ENSP00000169298; ENSG00000073849.
    ENST00000448044; ENSP00000389337; ENSG00000073849.
    ENST00000457772; ENSP00000412221; ENSG00000073849.
    GeneIDi6480.
    KEGGihsa:6480.
    UCSCiuc003frb.3. human.

    Polymorphism databases

    DMDMi115445.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    ST6Gal I

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17247 mRNA. Translation: CAA35111.1 .
    X54363 mRNA. Translation: CAA38246.1 .
    X62822 mRNA. Translation: CAA44634.1 .
    AK292879 mRNA. Translation: BAF85568.1 .
    AK312023 mRNA. Translation: BAG34960.1 .
    AC007488 Genomic DNA. No translation available.
    AC007690 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78160.1 .
    CH471052 Genomic DNA. Translation: EAW78161.1 .
    CH471052 Genomic DNA. Translation: EAW78162.1 .
    CH471052 Genomic DNA. Translation: EAW78164.1 .
    BC031476 mRNA. Translation: AAH31476.1 .
    BC040009 mRNA. Translation: AAH40009.1 .
    CCDSi CCDS3285.1.
    PIRi A41734.
    RefSeqi NP_003023.1. NM_003032.2.
    NP_775323.1. NM_173216.2.
    NP_775324.1. NM_173217.2.
    XP_005247774.1. XM_005247717.1.
    XP_005247776.1. XM_005247719.1.
    XP_005247777.1. XM_005247720.1.
    XP_006713797.1. XM_006713734.1.
    UniGenei Hs.207459.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JS1 X-ray 2.09 A 89-406 [» ]
    4JS2 X-ray 2.30 A 89-406 [» ]
    ProteinModelPortali P15907.
    SMRi P15907. Positions 89-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112374. 2 interactions.
    IntActi P15907. 1 interaction.
    MINTi MINT-5000509.
    STRINGi 9606.ENSP00000169298.

    Protein family/group databases

    CAZyi GT29. Glycosyltransferase Family 29.

    PTM databases

    PhosphoSitei P15907.

    Polymorphism databases

    DMDMi 115445.

    Proteomic databases

    MaxQBi P15907.
    PaxDbi P15907.
    PRIDEi P15907.

    Protocols and materials databases

    DNASUi 6480.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000169298 ; ENSP00000169298 ; ENSG00000073849 .
    ENST00000448044 ; ENSP00000389337 ; ENSG00000073849 .
    ENST00000457772 ; ENSP00000412221 ; ENSG00000073849 .
    GeneIDi 6480.
    KEGGi hsa:6480.
    UCSCi uc003frb.3. human.

    Organism-specific databases

    CTDi 6480.
    GeneCardsi GC03P186648.
    HGNCi HGNC:10860. ST6GAL1.
    HPAi CAB015018.
    CAB016122.
    MIMi 109675. gene.
    neXtProti NX_P15907.
    PharmGKBi PA35762.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249416.
    HOGENOMi HOG000013206.
    HOVERGENi HBG052853.
    InParanoidi P15907.
    KOi K00778.
    OMAi QVWNKDS.
    PhylomeDBi P15907.
    TreeFami TF323961.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci MetaCyc:HS01118-MONOMER.
    BRENDAi 2.4.99.1. 2681.
    Reactomei REACT_115835. Termination of O-glycan biosynthesis.
    REACT_200874. Sialic acid metabolism.
    REACT_25085. N-Glycan antennae elongation.

    Miscellaneous databases

    ChiTaRSi ST6GAL1. human.
    GeneWikii ST6GAL1.
    GenomeRNAii 6480.
    NextBioi 25171.
    PROi P15907.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15907.
    Bgeei P15907.
    CleanExi HS_ST6GAL1.
    Genevestigatori P15907.

    Family and domain databases

    InterProi IPR001675. Glyco_trans_29.
    IPR012163. Sialyl_trans.
    [Graphical view ]
    Pfami PF00777. Glyco_transf_29. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005557. Sialyl_trans. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete cDNA sequence encoding human beta-galactoside alpha-2,6-sialyltransferase."
      Grundmann U.G., Nerlich C., Rein T., Zettlmeissl G.
      Nucleic Acids Res. 18:667-667(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The HB-6, CDw75, and CD76 differentiation antigens are unique cell-surface carbohydrate determinants generated by the beta-galactoside alpha 2,6-sialyltransferase."
      Bast B.J.E.G., Zhou L.J., Freeman G.J., Colley K.J., Ernst T.J., Munro J.M., Tedder T.F.
      J. Cell Biol. 116:423-435(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Spleen.
    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 2).
      Tissue: Thymus and Trachea.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(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).
      Tissue: Lymph and Skin.
    8. "Isolation and characterization of a partial cDNA for a human sialyltransferase."
      Lance P., Lau K.M., Lau J.T.Y.
      Biochem. Biophys. Res. Commun. 164:225-232(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-406 (ISOFORM 1).
    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-149 AND ASN-161.
      Tissue: Liver.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Universal phosphatase-coupled glycosyltransferase assay."
      Wu Z.L., Ethen C.M., Prather B., Machacek M., Jiang W.
      Glycobiology 21:727-733(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "The structure of human alpha-2,6-sialyltransferase reveals the binding mode of complex glycans."
      Kuhn B., Benz J., Greif M., Engel A.M., Sobek H., Rudolph M.G.
      Acta Crystallogr. D 69:1826-1838(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 89-406 IN COMPLEXES WITH CMP; CYTIDINE AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-149, DISULFIDE BONDS.

    Entry informationi

    Entry nameiSIAT1_HUMAN
    AccessioniPrimary (citable) accession number: P15907
    Secondary accession number(s): A8KA14, B2R513, D3DNV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 158 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3