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Protein

Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5

Gene

ST6GALNAC5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the biosynthesis of ganglioside GD1a from GM1b. It exhibits higher activity with glycolipids than with glycoproteins (By similarity).By similarity

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.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Chemistry

SwissLipidsiSLP:000001365.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 (EC:2.4.99.-)
Alternative name(s):
GD1 alpha synthase
GalNAc alpha-2,6-sialyltransferase V
ST6GalNAc V
Short name:
ST6GalNAcV
Sialyltransferase 7E
Short name:
SIAT7-E
Gene namesi
Name:ST6GALNAC5
Synonyms:SIAT7E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:19342. ST6GALNAC5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 336307LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134924485.

Polymorphism and mutation databases

BioMutaiST6GALNAC5.
DMDMi21759442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5PRO_0000149280Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi96 ↔ 245By similarity
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9BVH7.
PRIDEiQ9BVH7.

PTM databases

iPTMnetiQ9BVH7.
PhosphoSiteiQ9BVH7.

Expressioni

Gene expression databases

BgeeiQ9BVH7.
CleanExiHS_ST6GALNAC5.
ExpressionAtlasiQ9BVH7. baseline and differential.
GenevisibleiQ9BVH7. HS.

Interactioni

Protein-protein interaction databases

BioGridi123600. 3 interactions.
STRINGi9606.ENSP00000417583.

Structurei

3D structure databases

ProteinModelPortaliQ9BVH7.
SMRiQ9BVH7. Positions 89-287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi38 – 4912Poly-GlnAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00550000074444.
HOGENOMiHOG000293316.
HOVERGENiHBG058710.
InParanoidiQ9BVH7.
KOiK03375.
OMAiHKMLQFD.
OrthoDBiEOG78SQJV.
PhylomeDBiQ9BVH7.
TreeFamiTF323961.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9BVH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLMRHGLA VCLALTTMCT SLLLVYSSLG GQKERPPQQQ QQQQQQQQQA
60 70 80 90 100
SATGSSQPAA ESSTQQRPGV PAGPRPLDGY LGVADHKPLK MHCRDCALVT
110 120 130 140 150
SSGHLLHSRQ GSQIDQTECV IRMNDAPTRG YGRDVGNRTS LRVIAHSSIQ
160 170 180 190 200
RILRNRHDLL NVSQGTVFIF WGPSSYMRRD GKGQVYNNLH LLSQVLPRLK
210 220 230 240 250
AFMITRHKML QFDELFKQET GKDRKISNTW LSTGWFTMTI ALELCDRINV
260 270 280 290 300
YGMVPPDFCR DPNHPSVPYH YYEPFGPDEC TMYLSHERGR KGSHHRFITE
310 320 330
KRVFKNWART FNIHFFQPDW KPESLAINHP ENKPVF
Length:336
Mass (Da):38,443
Last modified:June 1, 2001 - v1
Checksum:iF5FDD43D45CA11CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ507292 mRNA. Translation: CAD45372.1.
AK056241 mRNA. Translation: BAB71127.1.
AL035409, AC099060 Genomic DNA. Translation: CAM28274.1.
CH471059 Genomic DNA. Translation: EAX06386.1.
BC001201 mRNA. Translation: AAH01201.1.
CCDSiCCDS673.1.
RefSeqiNP_112227.1. NM_030965.2.
UniGeneiHs.149201.
Hs.303609.

Genome annotation databases

EnsembliENST00000477717; ENSP00000417583; ENSG00000117069.
GeneIDi81849.
KEGGihsa:81849.
UCSCiuc001dhi.4. human.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST6GalNAc V

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ507292 mRNA. Translation: CAD45372.1.
AK056241 mRNA. Translation: BAB71127.1.
AL035409, AC099060 Genomic DNA. Translation: CAM28274.1.
CH471059 Genomic DNA. Translation: EAX06386.1.
BC001201 mRNA. Translation: AAH01201.1.
CCDSiCCDS673.1.
RefSeqiNP_112227.1. NM_030965.2.
UniGeneiHs.149201.
Hs.303609.

3D structure databases

ProteinModelPortaliQ9BVH7.
SMRiQ9BVH7. Positions 89-287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123600. 3 interactions.
STRINGi9606.ENSP00000417583.

Chemistry

SwissLipidsiSLP:000001365.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

iPTMnetiQ9BVH7.
PhosphoSiteiQ9BVH7.

Polymorphism and mutation databases

BioMutaiST6GALNAC5.
DMDMi21759442.

Proteomic databases

PaxDbiQ9BVH7.
PRIDEiQ9BVH7.

Protocols and materials databases

DNASUi81849.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000477717; ENSP00000417583; ENSG00000117069.
GeneIDi81849.
KEGGihsa:81849.
UCSCiuc001dhi.4. human.

Organism-specific databases

CTDi81849.
GeneCardsiST6GALNAC5.
HGNCiHGNC:19342. ST6GALNAC5.
MIMi610134. gene.
neXtProtiNX_Q9BVH7.
PharmGKBiPA134924485.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00550000074444.
HOGENOMiHOG000293316.
HOVERGENiHBG058710.
InParanoidiQ9BVH7.
KOiK03375.
OMAiHKMLQFD.
OrthoDBiEOG78SQJV.
PhylomeDBiQ9BVH7.
TreeFamiTF323961.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.99.7. 2681.
ReactomeiR-HSA-4085001. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSiST6GALNAC5. human.
GenomeRNAii81849.
PROiQ9BVH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BVH7.
CleanExiHS_ST6GALNAC5.
ExpressionAtlasiQ9BVH7. baseline and differential.
GenevisibleiQ9BVH7. 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. "Molecular cloning and expression of human ST6GALNAC V."
    Harduin-Lepers A.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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: Eye.

Entry informationi

Entry nameiSIA7E_HUMAN
AccessioniPrimary (citable) accession number: Q9BVH7
Secondary accession number(s): B1AK82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 124 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 1
    Human chromosome 1: 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.