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Q11206 (SIA4C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4

Short name=Alpha 2,3-ST 4
Short name=Beta-galactoside alpha-2,3-sialyltransferase 4
EC=2.4.99.-
Alternative name(s):
Alpha 2,3-sialyltransferase IV
Gal-NAc6S
Gal-beta-1,4-GalNAc-alpha-2,3-sialyltransferase
SAT-3
ST-4
ST3Gal IV
Short name=ST3GalIV
ST3GalA.2
STZ
Sialyltransferase 4C
Short name=SIAT4-C
Gene names
Name:ST3GAL4
Synonyms:CGS23, NANTA3, SIAT4C, STZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

It may catalyze the formation of the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc-sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. It may be involved in the biosynthesis of the sialyl Lewis X determinant. Also acts on the corresponding 1,3-galactosyl derivative. Ref.8

Catalytic activity

CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.

Tissue specificity

Highly expressed in adult placenta, ovary and testes.

Post-translational modification

The soluble form derives from the membrane form by proteolytic processing.

Sequence similarities

Belongs to the glycosyltransferase 29 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processO-glycan processing

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

keratan sulfate biosynthetic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

sialylation

Traceable author statement Ref.1. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of Golgi membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-galactoside (CMP) alpha-2,3-sialyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

monosialoganglioside sialyltransferase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q11206-1)

Also known as: B1;

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.
Isoform 2 (identifier: Q11206-2)

Also known as: A1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MVSKSR → MCPAG
Isoform 3 (identifier: Q11206-3)

Also known as: A2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.
Isoform 4 (identifier: Q11206-4)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: N → KLSPLCS
Isoform 5 (identifier: Q11206-5)

The sequence of this isoform differs from the canonical sequence as follows:
     30-34: RYIEL → S
Isoform 6 (identifier: Q11206-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MVSKSR → MCPAG
     30-34: RYIEL → S
Isoform 7 (identifier: Q11206-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.
     30-34: RYIEL → S

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
PRO_0000149262

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2618Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 333307Lumenal Potential

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Disulfide bond120 ↔ 273 By similarity

Natural variations

Alternative sequence1 – 1111Missing in isoform 3 and isoform 7.
VSP_001785
Alternative sequence1 – 66MVSKSR → MCPAG in isoform 2 and isoform 6.
VSP_001784
Alternative sequence30 – 345RYIEL → S in isoform 5, isoform 6 and isoform 7.
VSP_021104
Alternative sequence611N → KLSPLCS in isoform 4.
VSP_001786

Experimental info

Sequence conflict182 – 1832NP → KG in AAC14162. Ref.8
Sequence conflict2001I → T in AAC14162. Ref.8
Sequence conflict3041M → I in AAC14162. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (B1) [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 15E4BCE1F4F5B3C3

FASTA33338,045
        10         20         30         40         50         60 
MVSKSRWKLL AMLALVLVVM VWYSISREDR YIELFYFPIP EKKEPCLQGE AESKASKLFG 

        70         80         90        100        110        120 
NYSRDQPIFL RLEDYFWVKT PSAYELPYGT KGSEDLLLRV LAITSSSIPK NIQSLRCRRC 

       130        140        150        160        170        180 
VVVGNGHRLR NSSLGDAINK YDVVIRLNNA PVAGYEGDVG SKTTMRLFYP ESAHFDPKVE 

       190        200        210        220        230        240 
NNPDTLLVLV AFKAMDFHWI ETILSDKKRV RKGFWKQPPL IWDVNPKQIR ILNPFFMEIA 

       250        260        270        280        290        300 
ADKLLSLPMQ QPRKIKQKPT TGLLAITLAL HLCDLVHIAG FGYPDAYNKK QTIHYYEQIT 

       310        320        330 
LKSMAGSGHN VSQEALAIKR MLEMGAIKNL TSF 

« Hide

Isoform 2 (A1) [UniParc].

Checksum: 3FF1B2BBAF273A03
Show »

FASTA33237,816
Isoform 3 (A2) [UniParc].

Checksum: 3AA7031A765DF2BD
Show »

FASTA32236,745
Isoform 4 (C) [UniParc].

Checksum: F48917FF5E9CAF87
Show »

FASTA33938,660
Isoform 5 [UniParc].

Checksum: 3A1C52816B5BE9E8
Show »

FASTA32937,458
Isoform 6 [UniParc].

Checksum: 11CEDB415E141CDD
Show »

FASTA32837,228
Isoform 7 [UniParc].

Checksum: B8B413FF58A693F8
Show »

FASTA31836,157

References

« Hide 'large scale' references
[1]"Genomic organization and chromosomal mapping of the Gal beta 1,3GalNAc/Gal beta 1,4GlcNAc alpha 2,3-sialyltransferase."
Kitagawa H., Mattei M.-G., Paulson J.C.
J. Biol. Chem. 271:931-938(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups."
Kitagawa H., Paulson J.C.
J. Biol. Chem. 269:1394-1401(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[3]"Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection."
Sasaki K., Watanabe E., Kawashima K., Sekine S., Dohi T., Oshima M., Hanai N., Nishi T., Hasegawa M.
J. Biol. Chem. 268:22782-22787(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[4]"Identification of nine alternatively spliced alpha2,3-sialyltransferase, ST3Gal IV, transcripts and analysis of their expression by RT-PCR and laser-induced fluorescent capillary electrophoresis (LIF-CE) in twenty-one human tissues."
Grahn A., Larson G.
Glycoconj. J. 18:759-767(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 7), ALTERNATIVE SPLICING.
Tissue: Peripheral blood leukocyte.
[5]"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. expand/collapse author list , 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] (ISOFORM 4).
Tissue: Placenta.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORM 1).
Tissue: Placenta.
[8]"Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line."
Basu S.S., Basu M., Li Z., Basu S.
Biochemistry 35:5166-5174(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-314, FUNCTION.
Tissue: Colon carcinoma.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L23767 mRNA. Translation: AAA16460.1.
X74570 mRNA. Translation: CAA52662.1.
AF516603 mRNA. Translation: AAM66432.1.
AF516604 mRNA. Translation: AAM66433.1.
AY040826 mRNA. Translation: AAK93790.1.
AK291577 mRNA. Translation: BAF84266.1.
AP000806 Genomic DNA. No translation available.
AP001318 Genomic DNA. No translation available.
BC010645 mRNA. Translation: AAH10645.1.
AF035249 mRNA. Translation: AAC14162.1.
PIRA48715.
A49879.
RefSeqNP_001241686.1. NM_001254757.1.
NP_001241687.1. NM_001254758.1.
NP_001241688.1. NM_001254759.1.
NP_006269.1. NM_006278.2.
XP_005271707.1. XM_005271650.1.
XP_005271708.1. XM_005271651.1.
UniGeneHs.591947.

3D structure databases

ProteinModelPortalQ11206.
SMRQ11206. Positions 42-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112377. 1 interaction.
STRING9606.ENSP00000227495.

Protein family/group databases

CAZyGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteQ11206.

Proteomic databases

PaxDbQ11206.
PRIDEQ11206.

Protocols and materials databases

DNASU6484.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227495; ENSP00000227495; ENSG00000110080. [Q11206-5]
ENST00000356132; ENSP00000348451; ENSG00000110080. [Q11206-4]
ENST00000392669; ENSP00000376437; ENSG00000110080. [Q11206-1]
ENST00000444328; ENSP00000394354; ENSG00000110080. [Q11206-1]
ENST00000449406; ENSP00000399444; ENSG00000110080. [Q11206-3]
ENST00000526727; ENSP00000436047; ENSG00000110080. [Q11206-1]
ENST00000530591; ENSP00000433989; ENSG00000110080. [Q11206-5]
ENST00000532243; ENSP00000434349; ENSG00000110080. [Q11206-2]
ENST00000534083; ENSP00000433318; ENSG00000110080. [Q11206-1]
ENST00000534457; ENSP00000434668; ENSG00000110080. [Q11206-6]
GeneID6484.
KEGGhsa:6484.
UCSCuc001qds.3. human. [Q11206-1]
uc001qdw.3. human. [Q11206-2]

Organism-specific databases

CTD6484.
GeneCardsGC11P126225.
HGNCHGNC:10864. ST3GAL4.
HPAHPA049827.
MIM104240. gene.
neXtProtNX_Q11206.
PharmGKBPA35766.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284110.
HOGENOMHOG000000682.
HOVERGENHBG056676.
KOK03494.
OMAIHYYEQI.
PhylomeDBQ11206.
TreeFamTF354325.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ11206.
BgeeQ11206.
CleanExHS_ST3GAL4.
GenevestigatorQ11206.

Family and domain databases

InterProIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFPIRSF005557. Sialyl_trans. 1 hit.
ProtoNetSearch...

Other

ChiTaRSST3GAL4. human.
GeneWikiST3GAL4.
GenomeRNAi6484.
NextBio25191.
PROQ11206.
SOURCESearch...

Entry information

Entry nameSIA4C_HUMAN
AccessionPrimary (citable) accession number: Q11206
Secondary accession number(s): A8K6B2 expand/collapse secondary AC list , O60497, Q8N6A6, Q8NFG7, Q96QQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM