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Protein

Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase

Gene

ST6GALNAC4

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

Functioni

Involved in the biosynthesis of ganglioside GD1A from GM1B. Transfers CMP-NeuAc with an alpha-2,6-linkage to GalNAc residue on NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc of glycoproteins and glycolipids. Prefers glycoproteins to glycolipids (By similarity).By similarity

Catalytic activityi

CMP-N-acetylneuraminate + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosaminyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-(N-acetyl-alpha-neuraminyl-(2->6))-N-acetyl-D-galactosaminyl-R.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.99.7. 2681.
ReactomeiR-HSA-4085001. Sialic acid metabolism.
R-HSA-977068. Termination of O-glycan biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase (EC:2.4.99.7)
Alternative name(s):
NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-alpha-2,6-sialyltransferase
ST6GalNAc IV
Short name:
ST6GalNAcIV
Sialyltransferase 3C
Short name:
SIAT3-C
Sialyltransferase 7D
Short name:
SIAT7-D
Gene namesi
Name:ST6GALNAC4
Synonyms:SIAT3C, SIAT7D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:17846. ST6GALNAC4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini28 – 302275LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38250.

Polymorphism and mutation databases

BioMutaiST6GALNAC4.
DMDMi21759443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferasePRO_0000149278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi76 ↔ 225By similarity
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9H4F1.
MaxQBiQ9H4F1.
PaxDbiQ9H4F1.
PRIDEiQ9H4F1.

PTM databases

iPTMnetiQ9H4F1.
PhosphoSiteiQ9H4F1.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9H4F1.
CleanExiHS_ST6GALNAC4.
ExpressionAtlasiQ9H4F1. baseline and differential.
GenevisibleiQ9H4F1. HS.

Organism-specific databases

HPAiHPA009042.

Interactioni

Protein-protein interaction databases

BioGridi117992. 6 interactions.
IntActiQ9H4F1. 1 interaction.
STRINGi9606.ENSP00000336733.

Structurei

3D structure databases

ProteinModelPortaliQ9H4F1.
SMRiQ9H4F1. Positions 60-254.
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.
GeneTreeiENSGT00550000074444.
HOVERGENiHBG058710.
InParanoidiQ9H4F1.
KOiK03374.
OMAiYLAHEQA.
OrthoDBiEOG78SQJV.
PhylomeDBiQ9H4F1.
TreeFamiTF352818.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H4F1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAPGRLVLI ILCSVVFSAV YILLCCWAGL PLCLATCLDH HFPTGSRPTV
60 70 80 90 100
PGPLHFSGYS SVPDGKPLVR EPCRSCAVVS SSGQMLGSGL GAEIDSAECV
110 120 130 140 150
FRMNQAPTVG FEADVGQRST LRVVSHTSVP LLLRNYSHYF QKARDTLYMV
160 170 180 190 200
WGQGRHMDRV LGGRTYRTLL QLTRMYPGLQ VYTFTERMMA YCDQIFQDET
210 220 230 240 250
GKNRRQSGSF LSTGWFTMIL ALELCEEIVV YGMVSDSYCR EKSHPSVPYH
260 270 280 290 300
YFEKGRLDEC QMYLAHEQAP RSAHRFITEK AVFSRWAKKR PIVFAHPSWR

TE
Length:302
Mass (Da):34,201
Last modified:July 11, 2002 - v2
Checksum:i08A4CDC749A6D783
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1202ST → QA in AAF00102 (Ref. 2) Curated
Sequence conflicti119 – 1191S → T in CAC07404 (PubMed:11062056).Curated
Sequence conflicti140 – 1401F → L in BAA91281 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271734 mRNA. Translation: CAC07404.1.
AF127142 mRNA. Translation: AAF00102.1.
AB035172 mRNA. Translation: BAA87034.1.
AK000600 mRNA. Translation: BAA91281.1.
AL157935 Genomic DNA. Translation: CAI12613.1.
CH471090 Genomic DNA. Translation: EAW87717.1.
BC036705 mRNA. Translation: AAH36705.1.
Y17460 Genomic DNA. Translation: CAB44353.1.
Y17461 Genomic DNA. Translation: CAB44354.1.
CCDSiCCDS6883.1.
RefSeqiNP_778204.1. NM_175039.3.
NP_778205.1. NM_175040.3.
UniGeneiHs.3972.
Hs.709827.

Genome annotation databases

EnsembliENST00000335791; ENSP00000336733; ENSG00000136840.
GeneIDi27090.
KEGGihsa:27090.
UCSCiuc004bss.3. human.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST6GalNAc IV

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271734 mRNA. Translation: CAC07404.1.
AF127142 mRNA. Translation: AAF00102.1.
AB035172 mRNA. Translation: BAA87034.1.
AK000600 mRNA. Translation: BAA91281.1.
AL157935 Genomic DNA. Translation: CAI12613.1.
CH471090 Genomic DNA. Translation: EAW87717.1.
BC036705 mRNA. Translation: AAH36705.1.
Y17460 Genomic DNA. Translation: CAB44353.1.
Y17461 Genomic DNA. Translation: CAB44354.1.
CCDSiCCDS6883.1.
RefSeqiNP_778204.1. NM_175039.3.
NP_778205.1. NM_175040.3.
UniGeneiHs.3972.
Hs.709827.

3D structure databases

ProteinModelPortaliQ9H4F1.
SMRiQ9H4F1. Positions 60-254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117992. 6 interactions.
IntActiQ9H4F1. 1 interaction.
STRINGi9606.ENSP00000336733.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

iPTMnetiQ9H4F1.
PhosphoSiteiQ9H4F1.

Polymorphism and mutation databases

BioMutaiST6GALNAC4.
DMDMi21759443.

Proteomic databases

EPDiQ9H4F1.
MaxQBiQ9H4F1.
PaxDbiQ9H4F1.
PRIDEiQ9H4F1.

Protocols and materials databases

DNASUi27090.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335791; ENSP00000336733; ENSG00000136840.
GeneIDi27090.
KEGGihsa:27090.
UCSCiuc004bss.3. human.

Organism-specific databases

CTDi27090.
GeneCardsiST6GALNAC4.
HGNCiHGNC:17846. ST6GALNAC4.
HPAiHPA009042.
MIMi606378. gene.
neXtProtiNX_Q9H4F1.
PharmGKBiPA38250.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00550000074444.
HOVERGENiHBG058710.
InParanoidiQ9H4F1.
KOiK03374.
OMAiYLAHEQA.
OrthoDBiEOG78SQJV.
PhylomeDBiQ9H4F1.
TreeFamiTF352818.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.99.7. 2681.
ReactomeiR-HSA-4085001. Sialic acid metabolism.
R-HSA-977068. Termination of O-glycan biosynthesis.

Miscellaneous databases

GeneWikiiST6GALNAC4.
GenomeRNAii27090.
NextBioi49709.
PROiQ9H4F1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4F1.
CleanExiHS_ST6GALNAC4.
ExpressionAtlasiQ9H4F1. baseline and differential.
GenevisibleiQ9H4F1. HS.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and gene organization of a human Neu5Ac alpha 2-3Gal beta 1-3GalNAc alpha 2,6-sialyltransferase: hST6GalNAcIV."
    Harduin-Lepers A., Stokes D.C., Steelant W.F.A., Samyn-Petit B., Krzewinski-Recchi M.A., Vallejo-Ruiz V., Zanetta J.P., Auge C., Delannoy P.
    Biochem. J. 352:37-48(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Molecular cloning of NeuAcalpha2,3Galbeta1,3GalNAc alpha2,6-sialyltransferase cDNA from human fetal liver."
    Kim K.-W., Kim K.-S., Do S.-I., Kim C.-H., Lee Y.-C.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal liver.
  3. "N-acetylgalactosaminide alpha2,6-sialyltransferase."
    Yoshida A.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  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].
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [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].
    Tissue: B-cell.
  8. "Extensive gene order differences within regions of conserved synteny between the Fugu and human genomes: implications for chromosomal evolution and the cloning of disease genes."
    Gilley J., Fried M.
    Hum. Mol. Genet. 8:1313-1320(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-302.

Entry informationi

Entry nameiSIA7D_HUMAN
AccessioniPrimary (citable) accession number: Q9H4F1
Secondary accession number(s): Q5T9D0
, Q9NWU6, Q9UKU1, Q9ULB9, Q9Y3G3, Q9Y3G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: March 16, 2016
This is version 135 of the entry and version 2 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 9
    Human chromosome 9: 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. 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.