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Q11206

- SIA4C_HUMAN

UniProt

Q11206 - SIA4C_HUMAN

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Protein

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4

Gene

ST3GAL4

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

Functioni

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.1 Publication

Catalytic activityi

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.

Pathwayi

GO - Molecular functioni

  1. beta-galactoside (CMP) alpha-2,3-sialyltransferase activity Source: ProtInc
  2. monosialoganglioside sialyltransferase activity Source: Ensembl

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. cognition Source: UniProt
  4. glycosaminoglycan metabolic process Source: Reactome
  5. keratan sulfate biosynthetic process Source: Reactome
  6. keratan sulfate metabolic process Source: Reactome
  7. O-glycan processing Source: Reactome
  8. post-translational protein modification Source: Reactome
  9. protein N-linked glycosylation via asparagine Source: Reactome
  10. sialylation Source: GOC
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_115835. Termination of O-glycan biosynthesis.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_121120. Keratan sulfate biosynthesis.
REACT_200874. Sialic acid metabolism.
REACT_25085. N-Glycan antennae elongation.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
Recommended name:
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (EC:2.4.99.-)
Short name:
Alpha 2,3-ST 4
Short name:
Beta-galactoside alpha-2,3-sialyltransferase 4
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 namesi
Name:ST3GAL4
Synonyms:CGS23, NANTA3, SIAT4C, STZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:10864. ST3GAL4.

Subcellular locationi

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.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. Golgi membrane Source: Reactome
  3. integral component of Golgi membrane Source: InterPro
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35766.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4PRO_0000149262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi120 ↔ 273By similarity
Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ11206.
PaxDbiQ11206.
PRIDEiQ11206.

PTM databases

PhosphoSiteiQ11206.

Expressioni

Tissue specificityi

Highly expressed in adult placenta, ovary and testes.

Gene expression databases

BgeeiQ11206.
CleanExiHS_ST3GAL4.
ExpressionAtlasiQ11206. baseline and differential.
GenevestigatoriQ11206.

Organism-specific databases

HPAiHPA049827.

Interactioni

Protein-protein interaction databases

BioGridi112377. 17 interactions.
STRINGi9606.ENSP00000227495.

Structurei

3D structure databases

ProteinModelPortaliQ11206.
SMRiQ11206. Positions 118-298.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Topological domaini27 – 333307LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2618Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG284110.
GeneTreeiENSGT00760000119095.
HOGENOMiHOG000000682.
HOVERGENiHBG056676.
InParanoidiQ11206.
KOiK03494.
OMAiIHYYEQI.
PhylomeDBiQ11206.
TreeFamiTF354325.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q11206-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVSKSRWKLL AMLALVLVVM VWYSISREDR YIELFYFPIP EKKEPCLQGE
60 70 80 90 100
AESKASKLFG NYSRDQPIFL RLEDYFWVKT PSAYELPYGT KGSEDLLLRV
110 120 130 140 150
LAITSSSIPK NIQSLRCRRC VVVGNGHRLR NSSLGDAINK YDVVIRLNNA
160 170 180 190 200
PVAGYEGDVG SKTTMRLFYP ESAHFDPKVE NNPDTLLVLV AFKAMDFHWI
210 220 230 240 250
ETILSDKKRV RKGFWKQPPL IWDVNPKQIR ILNPFFMEIA ADKLLSLPMQ
260 270 280 290 300
QPRKIKQKPT TGLLAITLAL HLCDLVHIAG FGYPDAYNKK QTIHYYEQIT
310 320 330
LKSMAGSGHN VSQEALAIKR MLEMGAIKNL TSF
Length:333
Mass (Da):38,045
Last modified:October 1, 1996 - v1
Checksum:i15E4BCE1F4F5B3C3
GO
Isoform 2 (identifier: Q11206-2) [UniParc]FASTAAdd to Basket

Also known as: A1

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MVSKSR → MCPAG

Show »
Length:332
Mass (Da):37,816
Checksum:i3FF1B2BBAF273A03
GO
Isoform 3 (identifier: Q11206-3) [UniParc]FASTAAdd to Basket

Also known as: A2

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.

Show »
Length:322
Mass (Da):36,745
Checksum:i3AA7031A765DF2BD
GO
Isoform 4 (identifier: Q11206-4) [UniParc]FASTAAdd to Basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: N → KLSPLCS

Show »
Length:339
Mass (Da):38,660
Checksum:iF48917FF5E9CAF87
GO
Isoform 5 (identifier: Q11206-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:329
Mass (Da):37,458
Checksum:i3A1C52816B5BE9E8
GO
Isoform 6 (identifier: Q11206-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MVSKSR → MCPAG
     30-34: RYIEL → S

Show »
Length:328
Mass (Da):37,228
Checksum:i11CEDB415E141CDD
GO
Isoform 7 (identifier: Q11206-7) [UniParc]FASTAAdd to Basket

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

Show »
Length:318
Mass (Da):36,157
Checksum:iB8B413FF58A693F8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1832NP → KG in AAC14162. (PubMed:8611500)Curated
Sequence conflicti200 – 2001I → T in AAC14162. (PubMed:8611500)Curated
Sequence conflicti304 – 3041M → I in AAC14162. (PubMed:8611500)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111Missing in isoform 3 and isoform 7. 1 PublicationVSP_001785Add
BLAST
Alternative sequencei1 – 66MVSKSR → MCPAG in isoform 2 and isoform 6. 2 PublicationsVSP_001784
Alternative sequencei30 – 345RYIEL → S in isoform 5, isoform 6 and isoform 7. 2 PublicationsVSP_021104
Alternative sequencei61 – 611N → KLSPLCS in isoform 4. 2 PublicationsVSP_001786

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS58193.1. [Q11206-1]
CCDS58194.1. [Q11206-2]
CCDS8474.1. [Q11206-5]
PIRiA48715.
A49879.
RefSeqiNP_001241686.1. NM_001254757.1. [Q11206-1]
NP_001241687.1. NM_001254758.1. [Q11206-1]
NP_001241688.1. NM_001254759.1. [Q11206-2]
NP_006269.1. NM_006278.2. [Q11206-5]
XP_005271707.1. XM_005271650.1. [Q11206-1]
XP_005271708.1. XM_005271651.1. [Q11206-5]
UniGeneiHs.591947.

Genome annotation databases

EnsembliENST00000227495; 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]
GeneIDi6484.
KEGGihsa:6484.
UCSCiuc001qds.3. human. [Q11206-1]
uc001qdw.3. human. [Q11206-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST3Gal IV

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS58193.1. [Q11206-1 ]
CCDS58194.1. [Q11206-2 ]
CCDS8474.1. [Q11206-5 ]
PIRi A48715.
A49879.
RefSeqi NP_001241686.1. NM_001254757.1. [Q11206-1 ]
NP_001241687.1. NM_001254758.1. [Q11206-1 ]
NP_001241688.1. NM_001254759.1. [Q11206-2 ]
NP_006269.1. NM_006278.2. [Q11206-5 ]
XP_005271707.1. XM_005271650.1. [Q11206-1 ]
XP_005271708.1. XM_005271651.1. [Q11206-5 ]
UniGenei Hs.591947.

3D structure databases

ProteinModelPortali Q11206.
SMRi Q11206. Positions 118-298.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112377. 17 interactions.
STRINGi 9606.ENSP00000227495.

Protein family/group databases

CAZyi GT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSitei Q11206.

Proteomic databases

MaxQBi Q11206.
PaxDbi Q11206.
PRIDEi Q11206.

Protocols and materials databases

DNASUi 6484.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000227495 ; 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 ]
GeneIDi 6484.
KEGGi hsa:6484.
UCSCi uc001qds.3. human. [Q11206-1 ]
uc001qdw.3. human. [Q11206-2 ]

Organism-specific databases

CTDi 6484.
GeneCardsi GC11P126225.
HGNCi HGNC:10864. ST3GAL4.
HPAi HPA049827.
MIMi 104240. gene.
neXtProti NX_Q11206.
PharmGKBi PA35766.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG284110.
GeneTreei ENSGT00760000119095.
HOGENOMi HOG000000682.
HOVERGENi HBG056676.
InParanoidi Q11206.
KOi K03494.
OMAi IHYYEQI.
PhylomeDBi Q11206.
TreeFami TF354325.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_115835. Termination of O-glycan biosynthesis.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_121120. Keratan sulfate biosynthesis.
REACT_200874. Sialic acid metabolism.
REACT_25085. N-Glycan antennae elongation.

Miscellaneous databases

ChiTaRSi ST3GAL4. human.
GeneWikii ST3GAL4.
GenomeRNAii 6484.
NextBioi 25191.
PROi Q11206.
SOURCEi Search...

Gene expression databases

Bgeei Q11206.
CleanExi HS_ST3GAL4.
ExpressionAtlasi Q11206. baseline and differential.
Genevestigatori Q11206.

Family and domain databases

InterProi IPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view ]
Pfami PF00777. Glyco_transf_29. 1 hit.
[Graphical view ]
PIRSFi PIRSF005557. Sialyl_trans. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSIA4C_HUMAN
AccessioniPrimary (citable) accession number: Q11206
Secondary accession number(s): A8K6B2
, O60497, Q8N6A6, Q8NFG7, Q96QQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 130 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 11
    Human chromosome 11: 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

External Data

Dasty 3