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P15907

- SIAT1_HUMAN

UniProt

P15907 - SIAT1_HUMAN

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Protein

Beta-galactoside alpha-2,6-sialyltransferase 1

Gene
ST6GAL1, SIAT1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 enzyme

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 – 3691Substrate Inferred
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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99Cytoplasmic
Transmembranei10 – 2617Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini27 – 406380Lumenal Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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.

Family & Domainsi

Region

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

Sequence similaritiesi

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.

Sequencei

Sequence statusi: Complete.

P15907-1 [UniParc]FASTAAdd to Basket

« 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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271K → L in CAA38246. 1 Publication
Sequence conflicti72 – 732HR → T in CAA38246. 1 Publication
Sequence conflicti144 – 1441L → P in CAA38246. 1 Publication

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.
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.
GeneIDi6480.
KEGGihsa:6480.
UCSCiuc003frb.3. human.

Polymorphism databases

DMDMi115445.

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 .
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 .
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

« Hide 'large scale' publications
  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].
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    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].
    Tissue: Trachea.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Lymph and Skin.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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, D3DNV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 157 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

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