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Protein

Type 2 lactosamine alpha-2,3-sialyltransferase

Gene

ST3GAL6

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

Functioni

Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3-sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.99.10. 2681.
2.4.99.6. 2681.
ReactomeiR-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-2022854. Keratan sulfate biosynthesis.
R-HSA-4085001. Sialic acid metabolism.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
Recommended name:
Type 2 lactosamine alpha-2,3-sialyltransferase (EC:2.4.99.-)
Alternative name(s):
CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI
ST3Gal VI
Short name:
ST3GalVI
Sialyltransferase 10
Gene namesi
Name:ST3GAL6
Synonyms:SIAT10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:18080. ST3GAL6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini26 – 331306LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • Golgi membrane Source: Reactome
  • integral component of Golgi membrane Source: InterPro
  • integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134958548.

Polymorphism and mutation databases

DMDMi54039605.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Type 2 lactosamine alpha-2,3-sialyltransferasePRO_0000149305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence analysis
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence analysis
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence analysis
Glycosylationi308 – 3081N-linked (GlcNAc...)1 Publication
Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9Y274.
PRIDEiQ9Y274.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9Y274.
CleanExiHS_ST3GAL6.
ExpressionAtlasiQ9Y274. baseline and differential.
GenevisibleiQ9Y274. HS.

Organism-specific databases

HPAiHPA018792.

Interactioni

Protein-protein interaction databases

BioGridi115674. 6 interactions.
STRINGi9606.ENSP00000377717.

Structurei

3D structure databases

ProteinModelPortaliQ9Y274.
SMRiQ9Y274. Positions 113-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00760000119095.
HOGENOMiHOG000000682.
HOVERGENiHBG056676.
InParanoidiQ9Y274.
OrthoDBiEOG7N37CV.
PhylomeDBiQ9Y274.
TreeFamiTF354325.

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. AlignAdd to basket

Isoform 1 (identifier: Q9Y274-1) [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
MRGYLVAIFL SAVFLYYVLH CILWGTNVYW VAPVEMKRRN KIQPCLSKPA
60 70 80 90 100
FASLLRFHQF HPFLCAADFR KIASLYGSDK FDLPYGMRTS AEYFRLALSK
110 120 130 140 150
LQSCDLFDEF DNIPCKKCVV VGNGGVLKNK TLGEKIDSYD VIIRMNNGPV
160 170 180 190 200
LGHEEEVGRR TTFRLFYPES VFSDPIHNDP NTTVILTAFK PHDLRWLLEL
210 220 230 240 250
LMGDKINTNG FWKKPALNLI YKPYQIRILD PFIIRTAAYE LLHFPKVFPK
260 270 280 290 300
NQKPKHPTTG IIAITLAFYI CHEVHLAGFK YNFSDLKSPL HYYGNATMSL
310 320 330
MNKNAYHNVT AEQLFLKDII EKNLVINLTQ D
Length:331
Mass (Da):38,214
Last modified:November 1, 1999 - v1
Checksum:iDD2B3D88D3D0A055
GO
Isoform 2 (identifier: Q9Y274-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.
     112-144: NIPCKKCVVVGNGGVLKNKTLGEKIDSYDVIIR → K

Show »
Length:213
Mass (Da):24,782
Checksum:i6AC0FDF802B3D8AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711C → S in BAG50993 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti311 – 3111A → T.
Corresponds to variant rs28489284 [ dbSNP | Ensembl ].
VAR_049227

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8686Missing in isoform 2. 1 PublicationVSP_047009Add
BLAST
Alternative sequencei112 – 14433NIPCK…DVIIR → K in isoform 2. 1 PublicationVSP_047010Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022918 mRNA. Translation: BAA77609.1.
AF119391 mRNA. Translation: AAD39131.1.
AK315111 mRNA. Translation: BAG37569.1.
AK001922 mRNA. Translation: BAG50993.1.
AC106728 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79849.1.
CH471052 Genomic DNA. Translation: EAW79850.1.
CH471052 Genomic DNA. Translation: EAW79852.1.
BC023312 mRNA. Translation: AAH23312.1.
CCDSiCCDS2933.1. [Q9Y274-1]
CCDS59452.1. [Q9Y274-2]
RefSeqiNP_001258074.1. NM_001271145.1.
NP_001258075.1. NM_001271146.1. [Q9Y274-1]
NP_001258076.1. NM_001271147.1. [Q9Y274-2]
NP_006091.1. NM_006100.3. [Q9Y274-1]
XP_005247126.1. XM_005247069.1. [Q9Y274-1]
XP_005247127.1. XM_005247070.3. [Q9Y274-1]
UniGeneiHs.148716.

Genome annotation databases

EnsembliENST00000265261; ENSP00000265261; ENSG00000064225. [Q9Y274-2]
ENST00000394162; ENSP00000377717; ENSG00000064225. [Q9Y274-1]
ENST00000483910; ENSP00000417376; ENSG00000064225. [Q9Y274-1]
GeneIDi10402.
UCSCiuc003dsz.5. human. [Q9Y274-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST3Gal VI

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022918 mRNA. Translation: BAA77609.1.
AF119391 mRNA. Translation: AAD39131.1.
AK315111 mRNA. Translation: BAG37569.1.
AK001922 mRNA. Translation: BAG50993.1.
AC106728 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79849.1.
CH471052 Genomic DNA. Translation: EAW79850.1.
CH471052 Genomic DNA. Translation: EAW79852.1.
BC023312 mRNA. Translation: AAH23312.1.
CCDSiCCDS2933.1. [Q9Y274-1]
CCDS59452.1. [Q9Y274-2]
RefSeqiNP_001258074.1. NM_001271145.1.
NP_001258075.1. NM_001271146.1. [Q9Y274-1]
NP_001258076.1. NM_001271147.1. [Q9Y274-2]
NP_006091.1. NM_006100.3. [Q9Y274-1]
XP_005247126.1. XM_005247069.1. [Q9Y274-1]
XP_005247127.1. XM_005247070.3. [Q9Y274-1]
UniGeneiHs.148716.

3D structure databases

ProteinModelPortaliQ9Y274.
SMRiQ9Y274. Positions 113-330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115674. 6 interactions.
STRINGi9606.ENSP00000377717.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Polymorphism and mutation databases

DMDMi54039605.

Proteomic databases

PaxDbiQ9Y274.
PRIDEiQ9Y274.

Protocols and materials databases

DNASUi10402.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265261; ENSP00000265261; ENSG00000064225. [Q9Y274-2]
ENST00000394162; ENSP00000377717; ENSG00000064225. [Q9Y274-1]
ENST00000483910; ENSP00000417376; ENSG00000064225. [Q9Y274-1]
GeneIDi10402.
UCSCiuc003dsz.5. human. [Q9Y274-1]

Organism-specific databases

CTDi10402.
GeneCardsiST3GAL6.
HGNCiHGNC:18080. ST3GAL6.
HPAiHPA018792.
MIMi607156. gene.
neXtProtiNX_Q9Y274.
PharmGKBiPA134958548.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00760000119095.
HOGENOMiHOG000000682.
HOVERGENiHBG056676.
InParanoidiQ9Y274.
OrthoDBiEOG7N37CV.
PhylomeDBiQ9Y274.
TreeFamiTF354325.

Enzyme and pathway databases

BRENDAi2.4.99.10. 2681.
2.4.99.6. 2681.
ReactomeiR-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-2022854. Keratan sulfate biosynthesis.
R-HSA-4085001. Sialic acid metabolism.

Miscellaneous databases

GenomeRNAii10402.
NextBioi35468880.
PROiQ9Y274.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y274.
CleanExiHS_ST3GAL6.
ExpressionAtlasiQ9Y274. baseline and differential.
GenevisibleiQ9Y274. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids."
    Okajima T., Fukumoto S., Miyazaki H., Ishida H., Kiso M., Furukawa K., Urano T., Furukawa K.
    J. Biol. Chem. 274:11479-11486(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Brain.
  2. "Sialyltransferases."
    Kapitonov D., Yu R.K.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  3. "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: Placenta.
  4. "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].
  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] (ISOFORM 1).
    Tissue: Placenta.
  7. "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-308.
    Tissue: Liver.

Entry informationi

Entry nameiSIA10_HUMAN
AccessioniPrimary (citable) accession number: Q9Y274
Secondary accession number(s): B2RCH2
, B3KMI1, D3DN39, F8W6U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: November 1, 1999
Last modified: March 16, 2016
This is version 118 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 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.