Q9Y274 (SIA10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ST3GAL6
Synonyms:	SIAT10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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; Single-pass type II membrane protein Potential.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the glycosyltransferase 29 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Inferred from direct assay Ref.1. Source: UniProtKB cellular response to interleukin-6 Inferred from expression pattern PubMed 17944600. Source: UniProtKB glycolipid metabolic process Inferred from direct assay Ref.1. Source: UniProtKB keratan sulfate biosynthetic process Traceable author statement. Source: Reactome oligosaccharide metabolic process Inferred from direct assay Ref.1. Source: UniProtKB protein glycosylation Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to Golgi membrane Inferred from electronic annotation. Source: InterPro integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	beta-galactoside alpha-2,3-sialyltransferase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 331	331	Type 2 lactosamine alpha-2,3-sialyltransferase		PRO_0000149305
Regions
	Topological domain	1 – 4	4	Cytoplasmic Potential
	Transmembrane	5 – 25	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	26 – 331	306	Lumenal Potential
Amino acid modifications
	Glycosylation	129	1	N-linked (GlcNAc...) Potential
	Glycosylation	181	1	N-linked (GlcNAc...) Potential
	Glycosylation	282	1	N-linked (GlcNAc...) Potential
	Glycosylation	295	1	N-linked (GlcNAc...) Potential
	Glycosylation	308	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	327	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	311	1	A → T. Corresponds to variant rs28489284 [ dbSNP | Ensembl ].		VAR_049227

Sequences

	Sequence		Length	Mass (Da)
	Q9Y274 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: DD2B3D88D3D0A055	FASTA	331	38,214
	10 20 30 40 50 60 MRGYLVAIFL SAVFLYYVLH CILWGTNVYW VAPVEMKRRN KIQPCLSKPA FASLLRFHQF 70 80 90 100 110 120 HPFLCAADFR KIASLYGSDK FDLPYGMRTS AEYFRLALSK LQSCDLFDEF DNIPCKKCVV 130 140 150 160 170 180 VGNGGVLKNK TLGEKIDSYD VIIRMNNGPV LGHEEEVGRR TTFRLFYPES VFSDPIHNDP 190 200 210 220 230 240 NTTVILTAFK PHDLRWLLEL LMGDKINTNG FWKKPALNLI YKPYQIRILD PFIIRTAAYE 250 260 270 280 290 300 LLHFPKVFPK NQKPKHPTTG IIAITLAFYI CHEVHLAGFK YNFSDLKSPL HYYGNATMSL 310 320 330 MNKNAYHNVT AEQLFLKDII EKNLVINLTQ D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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], CHARACTERIZATION. Tissue: Brain.
[2]	"Sialyltransferases." Kapitonov D., Yu R.K. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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].
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Placenta.
[6]	"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, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST3Gal VI

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB022918 mRNA. Translation: BAA77609.1. AF119391 mRNA. Translation: AAD39131.1. AK315111 mRNA. Translation: BAG37569.1. CH471052 Genomic DNA. Translation: EAW79849.1. CH471052 Genomic DNA. Translation: EAW79850.1. CH471052 Genomic DNA. Translation: EAW79852.1. BC023312 mRNA. Translation: AAH23312.1.
IPI	IPI00184851.
RefSeq	NP_001258074.1. NM_001271145.1. NP_001258075.1. NM_001271146.1. NP_006091.1. NM_006100.3.
UniGene	Hs.148716.
3D structure databases
ProteinModelPortal	Q9Y274.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000377717.
Protein family/group databases
CAZy	GT29. Glycosyltransferase Family 29.
Polymorphism databases
DMDM	54039605.
Proteomic databases
PaxDb	Q9Y274.
PRIDE	Q9Y274.
Protocols and materials databases
DNASU	10402.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000394162; ENSP00000377717; ENSG00000064225. ENST00000483910; ENSP00000417376; ENSG00000064225.
GeneID	10402.
KEGG	hsa:10402.
UCSC	uc003dsy.3. human.
Organism-specific databases
CTD	10402.
GeneCards	GC03P098451.
HGNC	HGNC:18080. ST3GAL6.
HPA	HPA018792.
MIM	607156. gene.
neXtProt	NX_Q9Y274.
PharmGKB	PA134958548.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG330728.
HOGENOM	HOG000000682.
HOVERGEN	HBG056676.
InParanoid	Q9Y274.
KO	K03792.
OMA	PCKRCVV.
OrthoDB	EOG4W6NWB.
PhylomeDB	Q9Y274.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	Q9Y274.
Bgee	Q9Y274.
CleanEx	HS_ST3GAL6.
Genevestigator	Q9Y274.
GermOnline	ENSG00000064225. Homo sapiens.
Family and domain databases
InterPro	IPR001675. Glyco_trans_29. IPR012163. Sialyl_trans. [Graphical view]
Pfam	PF00777. Glyco_transf_29. 1 hit. [Graphical view]
PIRSF	PIRSF005557. Sialyl_trans. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10402.
NextBio	39420.
SOURCE	Search...

Entry information

Entry name

SIA10_HUMAN

Accession

Primary (citable) accession number: Q9Y274
Secondary accession number(s): B2RCH2, D3DN39

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.