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Q8N4A0

- GALT4_HUMAN

UniProt

Q8N4A0 - GALT4_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 4

Gene

GALNT4

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

Functioni

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG.

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

Cofactori

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei175 – 1751SubstrateBy similarity
Binding sitei204 – 2041SubstrateBy similarity
Metal bindingi227 – 2271ManganeseBy similarity
Metal bindingi229 – 2291ManganeseBy similarity
Binding sitei334 – 3341SubstrateBy similarity
Metal bindingi362 – 3621ManganeseBy similarity
Binding sitei370 – 3701SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: ProtInc
  2. cellular protein metabolic process Source: Reactome
  3. O-glycan processing Source: Reactome
  4. post-translational protein modification Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 2681.
ReactomeiREACT_115606. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 4 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 4
Short name:
GalNAc-T4
Short name:
pp-GaNTase 4
Protein-UDP acetylgalactosaminyltransferase 4
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Gene namesi
Name:GALNT4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:4126. GALNT4.

Subcellular locationi

Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. Golgi apparatus Source: ProtInc
  3. Golgi membrane Source: Reactome
  4. integral component of membrane Source: UniProtKB-KW
  5. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi459 – 4591D → H: Affects the glycopeptide specificity and abolishes ability to glycosylate Muc1, Muc2 and Muc5AC. 1 Publication

Organism-specific databases

PharmGKBiPA28539.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 578578Polypeptide N-acetylgalactosaminyltransferase 4PRO_0000059108Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi124 ↔ 357PROSITE-ProRule annotation
Disulfide bondi348 ↔ 421PROSITE-ProRule annotation
Disulfide bondi457 ↔ 477PROSITE-ProRule annotation
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi503 ↔ 518PROSITE-ProRule annotation
Disulfide bondi547 ↔ 565PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8N4A0.
PeptideAtlasiQ8N4A0.
PRIDEiQ8N4A0.

PTM databases

PhosphoSiteiQ8N4A0.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in mucous cells.1 Publication

Gene expression databases

CleanExiHS_GALNT4.
GenevestigatoriQ8N4A0.

Interactioni

Protein-protein interaction databases

BioGridi114240. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8N4A0.
SMRiQ8N4A0. Positions 89-562.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini36 – 578543LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini444 – 577134Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 243110Catalytic subdomain AAdd
BLAST
Regioni303 – 36563Catalytic subdomain BAdd
BLAST

Domaini

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity
The ricin B-type lectin domain directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.1 Publication

Sequence similaritiesi

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ8N4A0.
KOiK00710.
OMAiINAYEET.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8N4A0.
TreeFamiTF352660.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N4A0-1) [UniParc]FASTAAdd to Basket

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
MAVRWTWAGK SCLLLAFLTV AYIFVELLVS TFHASAGAGR ARELGSRRLS
60 70 80 90 100
DLQKNTEDLS RPLYKKPPAD SRALGEWGKA SKLQLNEDEL KQQEELIERY
110 120 130 140 150
AINIYLSDRI SLHRHIEDKR MYECKSQKFN YRTLPTTSVI IAFYNEAWST
160 170 180 190 200
LLRTIHSVLE TSPAVLLKEI ILVDDLSDRV YLKTQLETYI SNLDRVRLIR
210 220 230 240 250
TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNSGWLEPL LERIGRDETA
260 270 280 290 300
VVCPVIDTID WNTFEFYMQI GEPMIGGFDW RLTFQWHSVP KQERDRRISR
310 320 330 340 350
IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG
360 370 380 390 400
KLEIHPCSHV GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP
410 420 430 440 450
ARKEAYGDIS ERKLLRERLR CKSFDWYLKN VFPNLHVPED RPGWHGAIRS
460 470 480 490 500
RGISSECLDY NSPDNNPTGA NLSLFGCHGQ GGNQFFEYTS NKEIRFNSVT
510 520 530 540 550
ELCAEVPEQK NYVGMQNCPK DGFPVPANII WHFKEDGTIF HPHSGLCLSA
560 570
YRTPEGRPDV QMRTCDALDK NQIWSFEK
Length:578
Mass (Da):66,666
Last modified:June 28, 2011 - v2
Checksum:i6EEEF502A40CBD2E
GO
Isoform 2 (identifier: Q8N4A0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: MAVRWTWAGK...SLHRHIEDKR → MAWCVATADP...WTSAPTASNL
     121-292: Missing.

Note: No experimental confirmation available.

Show »
Length:406
Mass (Da):45,702
Checksum:iEB89E46BF360847D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → T in CAA69875. (PubMed:9804815)Curated
Sequence conflicti227 – 2271D → Y in CAA69875. (PubMed:9804815)Curated
Sequence conflicti247 – 2471D → Y in CAA69875. (PubMed:9804815)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511D → G.1 Publication
Corresponds to variant rs17853610 [ dbSNP | Ensembl ].
VAR_065257
Natural varianti270 – 2701I → T.1 Publication
Corresponds to variant rs2230281 [ dbSNP | Ensembl ].
VAR_019576
Natural varianti506 – 5061V → I.2 Publications
Corresponds to variant rs2230283 [ dbSNP | Ensembl ].
VAR_019577

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 120120MAVRW…IEDKR → MAWCVATADPAHTSRPLFTG LAVSRGSAGHAWSAGFDWAA VVVVTGRRCRSGQTVPGAAR SPLLPHPLPSPLRVPPPTGA LGRPLPRWPQPRRTPFWSVI SKATKLRSPPWTSAPTASNL in isoform 2. 1 PublicationVSP_045009Add
BLAST
Alternative sequencei121 – 292172Missing in isoform 2. 1 PublicationVSP_045010Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08564 Genomic DNA. Translation: CAA69875.1.
AK297677 mRNA. Translation: BAG60038.1.
AK312870 mRNA. Translation: BAG35722.1.
AC010201 Genomic DNA. No translation available.
AC025034 Genomic DNA. No translation available.
BC036390 mRNA. Translation: AAH36390.1.
CCDSiCCDS53817.1. [Q8N4A0-1]
RefSeqiNP_001186711.1. NM_001199782.1. [Q8N4A0-2]
NP_003765.2. NM_003774.4. [Q8N4A0-1]
UniGeneiHs.25130.

Genome annotation databases

EnsembliENST00000529983; ENSP00000436604; ENSG00000257594. [Q8N4A0-1]
GeneIDi100528030.
8693.
KEGGihsa:100528030.
hsa:8693.
UCSCiuc001tbd.3. human. [Q8N4A0-1]
uc010suo.2. human.

Polymorphism databases

DMDMi338817878.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 4

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08564 Genomic DNA. Translation: CAA69875.1 .
AK297677 mRNA. Translation: BAG60038.1 .
AK312870 mRNA. Translation: BAG35722.1 .
AC010201 Genomic DNA. No translation available.
AC025034 Genomic DNA. No translation available.
BC036390 mRNA. Translation: AAH36390.1 .
CCDSi CCDS53817.1. [Q8N4A0-1 ]
RefSeqi NP_001186711.1. NM_001199782.1. [Q8N4A0-2 ]
NP_003765.2. NM_003774.4. [Q8N4A0-1 ]
UniGenei Hs.25130.

3D structure databases

ProteinModelPortali Q8N4A0.
SMRi Q8N4A0. Positions 89-562.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114240. 3 interactions.

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSitei Q8N4A0.

Polymorphism databases

DMDMi 338817878.

Proteomic databases

MaxQBi Q8N4A0.
PeptideAtlasi Q8N4A0.
PRIDEi Q8N4A0.

Protocols and materials databases

DNASUi 8693.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000529983 ; ENSP00000436604 ; ENSG00000257594 . [Q8N4A0-1 ]
GeneIDi 100528030.
8693.
KEGGi hsa:100528030.
hsa:8693.
UCSCi uc001tbd.3. human. [Q8N4A0-1 ]
uc010suo.2. human.

Organism-specific databases

CTDi 100528030.
8693.
GeneCardsi GC12M089913.
HGNCi HGNC:4126. GALNT4.
MIMi 603565. gene.
neXtProti NX_Q8N4A0.
PharmGKBi PA28539.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00760000118828.
HOVERGENi HBG051699.
InParanoidi Q8N4A0.
KOi K00710.
OMAi INAYEET.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8N4A0.
TreeFami TF352660.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 2681.
Reactomei REACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi 32603.
PROi Q8N4A0.
SOURCEi Search...

Gene expression databases

CleanExi HS_GALNT4.
Genevestigatori Q8N4A0.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat."
    Bennett E.P., Hassan H., Mandel U., Mirgorodskaya E., Roepstorff P., Burchell J., Taylor-Papadimitriou J., Hollingsworth M.A., Merkx G., van Kessel A.G., Eiberg H., Steffensen R., Clausen H.
    J. Biol. Chem. 273:30472-30481(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ILE-506.
  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] (ISOFORMS 1 AND 2), VARIANTS THR-270 AND ILE-506.
    Tissue: Kidney and Trachea.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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), VARIANT GLY-51.
    Tissue: Brain.
  5. "The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities."
    Hassan H., Reis C.A., Bennett E.P., Mirgorodskaya E., Roepstorff P., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
    J. Biol. Chem. 275:38197-38205(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF ASP-459.

Entry informationi

Entry nameiGALT4_HUMAN
AccessioniPrimary (citable) accession number: Q8N4A0
Secondary accession number(s): B2R775, B4DMX6, O00208
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 28, 2011
Last modified: October 29, 2014
This is version 104 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3