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Type 2 lactosamine alpha-2,3-sialyltransferase (EC 2.4.99.-) (CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI) (ST3Gal VI) (ST3GalVI) (Sialyltransferase 10)

 SIA10_HUMAN             Reviewed;         331 AA.
Q9Y274; B2RCH2; B3KMI1; D3DN39; F8W6U0;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
10-OCT-2018, entry version 136.
RecName: Full=Type 2 lactosamine alpha-2,3-sialyltransferase;
EC=2.4.99.-;
AltName: Full=CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI;
AltName: Full=ST3Gal VI;
Short=ST3GalVI;
AltName: Full=Sialyltransferase 10;
Name=ST3GAL6; Synonyms=SIAT10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=10206952; DOI=10.1074/jbc.274.17.11479;
Okajima T., Fukumoto S., Miyazaki H., Ishida H., Kiso M., Furukawa K.,
Urano T., Furukawa K.;
"Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI)
that sialylates type II lactosamine structures on glycoproteins and
glycolipids.";
J. Biol. Chem. 274:11479-11486(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
Kapitonov D., Yu R.K.;
"Sialyltransferases.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
-!- FUNCTION: 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.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y274-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y274-2; Sequence=VSP_047009, VSP_047010;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=ST3Gal VI;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_627";
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EMBL; AB022918; BAA77609.1; -; mRNA.
EMBL; AF119391; AAD39131.1; -; mRNA.
EMBL; AK315111; BAG37569.1; -; mRNA.
EMBL; AK001922; BAG50993.1; -; mRNA.
EMBL; AC106728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79849.1; -; Genomic_DNA.
EMBL; CH471052; EAW79850.1; -; Genomic_DNA.
EMBL; CH471052; EAW79852.1; -; Genomic_DNA.
EMBL; BC023312; AAH23312.1; -; mRNA.
CCDS; CCDS2933.1; -. [Q9Y274-1]
CCDS; CCDS59452.1; -. [Q9Y274-2]
RefSeq; NP_001258074.1; NM_001271145.1.
RefSeq; NP_001258075.1; NM_001271146.1. [Q9Y274-1]
RefSeq; NP_001258076.1; NM_001271147.1. [Q9Y274-2]
RefSeq; NP_001310281.1; NM_001323352.1. [Q9Y274-1]
RefSeq; NP_001310294.1; NM_001323365.1. [Q9Y274-1]
RefSeq; NP_001310297.1; NM_001323368.1. [Q9Y274-1]
RefSeq; NP_006091.1; NM_006100.3. [Q9Y274-1]
UniGene; Hs.148716; -.
ProteinModelPortal; Q9Y274; -.
SMR; Q9Y274; -.
BioGrid; 115674; 9.
STRING; 9606.ENSP00000377717; -.
CAZy; GT29; Glycosyltransferase Family 29.
GlyConnect; 1868; -.
iPTMnet; Q9Y274; -.
PhosphoSitePlus; Q9Y274; -.
DMDM; 54039605; -.
EPD; Q9Y274; -.
PaxDb; Q9Y274; -.
PeptideAtlas; Q9Y274; -.
PRIDE; Q9Y274; -.
ProteomicsDB; 85676; -.
DNASU; 10402; -.
Ensembl; ENST00000265261; ENSP00000265261; ENSG00000064225. [Q9Y274-2]
Ensembl; ENST00000394162; ENSP00000377717; ENSG00000064225. [Q9Y274-1]
Ensembl; ENST00000483910; ENSP00000417376; ENSG00000064225. [Q9Y274-1]
GeneID; 10402; -.
KEGG; hsa:10402; -.
UCSC; uc003dsz.5; human. [Q9Y274-1]
CTD; 10402; -.
DisGeNET; 10402; -.
EuPathDB; HostDB:ENSG00000064225.12; -.
GeneCards; ST3GAL6; -.
HGNC; HGNC:18080; ST3GAL6.
HPA; HPA018792; -.
MIM; 607156; gene.
neXtProt; NX_Q9Y274; -.
OpenTargets; ENSG00000064225; -.
PharmGKB; PA134958548; -.
eggNOG; KOG2692; Eukaryota.
eggNOG; ENOG410XT8P; LUCA.
GeneTree; ENSGT00760000119095; -.
HOGENOM; HOG000000682; -.
HOVERGEN; HBG056676; -.
InParanoid; Q9Y274; -.
KO; K03792; -.
PhylomeDB; Q9Y274; -.
TreeFam; TF354325; -.
BioCyc; MetaCyc:ENSG00000064225-MONOMER; -.
BRENDA; 2.4.99.10; 2681.
BRENDA; 2.4.99.6; 2681.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
Reactome; R-HSA-4085001; Sialic acid metabolism.
GenomeRNAi; 10402; -.
PRO; PR:Q9Y274; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000064225; Expressed in 215 organ(s), highest expression level in testis.
CleanEx; HS_ST3GAL6; -.
ExpressionAtlas; Q9Y274; baseline and differential.
Genevisible; Q9Y274; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; TAS:Reactome.
GO; GO:0052798; F:beta-galactoside alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
GO; GO:0006464; P:cellular protein modification process; IDA:UniProtKB.
GO; GO:0071354; P:cellular response to interleukin-6; IEP:UniProtKB.
GO; GO:0006664; P:glycolipid metabolic process; IDA:UniProtKB.
GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
GO; GO:0009311; P:oligosaccharide metabolic process; IDA:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
Gene3D; 3.90.1480.20; -; 1.
InterPro; IPR001675; Glyco_trans_29.
InterPro; IPR038578; GT29-like_sf.
InterPro; IPR012163; Sialyl_trans.
Pfam; PF00777; Glyco_transf_29; 1.
PIRSF; PIRSF005557; Sialyl_trans; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Membrane; Polymorphism;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 331 Type 2 lactosamine alpha-2,3-
sialyltransferase.
/FTId=PRO_0000149305.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 25 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 26 331 Lumenal. {ECO:0000255}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 86 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047009.
VAR_SEQ 112 144 NIPCKKCVVVGNGGVLKNKTLGEKIDSYDVIIR -> K
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047010.
VARIANT 311 311 A -> T (in dbSNP:rs28489284).
/FTId=VAR_049227.
CONFLICT 271 271 C -> S (in Ref. 3; BAG50993).
{ECO:0000305}.
SEQUENCE 331 AA; 38214 MW; DD2B3D88D3D0A055 CRC64;
MRGYLVAIFL SAVFLYYVLH CILWGTNVYW VAPVEMKRRN KIQPCLSKPA FASLLRFHQF
HPFLCAADFR KIASLYGSDK FDLPYGMRTS AEYFRLALSK LQSCDLFDEF DNIPCKKCVV
VGNGGVLKNK TLGEKIDSYD VIIRMNNGPV LGHEEEVGRR TTFRLFYPES VFSDPIHNDP
NTTVILTAFK PHDLRWLLEL LMGDKINTNG FWKKPALNLI YKPYQIRILD PFIIRTAAYE
LLHFPKVFPK NQKPKHPTTG IIAITLAFYI CHEVHLAGFK YNFSDLKSPL HYYGNATMSL
MNKNAYHNVT AEQLFLKDII EKNLVINLTQ D


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Genprice Inc, Invoices and accounting
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