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Q7Z7M9

- GALT5_HUMAN

UniProt

Q7Z7M9 - GALT5_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

GALNT5

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 activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (By similarity).By similarity

Catalytic activityi

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

Cofactori

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei536 – 5361SubstrateBy similarity
Binding sitei565 – 5651SubstrateBy similarity
Metal bindingi588 – 5881ManganeseBy similarity
Binding sitei589 – 5891SubstrateBy similarity
Metal bindingi590 – 5901ManganeseBy similarity
Binding sitei695 – 6951SubstrateBy similarity
Metal bindingi723 – 7231ManganeseBy similarity
Binding sitei726 – 7261SubstrateBy similarity
Binding sitei731 – 7311SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. glycosaminoglycan biosynthetic process Source: UniProtKB
  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

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 5 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 5
Short name:
GalNAc-T5
Short name:
pp-GaNTase 5
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
Gene namesi
Name:GALNT5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4127. GALNT5.

Subcellular locationi

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28540.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 940940Polypeptide N-acetylgalactosaminyltransferase 5PRO_0000059110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi486 ↔ 718PROSITE-ProRule annotation
Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi709 ↔ 789PROSITE-ProRule annotation
Glycosylationi776 – 7761N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi822 ↔ 835PROSITE-ProRule annotation
Glycosylationi827 – 8271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi845 – 8451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi858 ↔ 873PROSITE-ProRule annotation
Disulfide bondi908 ↔ 923PROSITE-ProRule annotation
Glycosylationi912 – 9121N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ7Z7M9.
PaxDbiQ7Z7M9.
PRIDEiQ7Z7M9.

PTM databases

PhosphoSiteiQ7Z7M9.

Expressioni

Gene expression databases

BgeeiQ7Z7M9.
CleanExiHS_GALNT5.
ExpressionAtlasiQ7Z7M9. baseline and differential.
GenevestigatoriQ7Z7M9.

Organism-specific databases

HPAiHPA008963.
HPA009035.

Interactioni

Subunit structurei

Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3.1 Publication

Protein-protein interaction databases

BioGridi116394. 2 interactions.
STRINGi9606.ENSP00000259056.

Structurei

3D structure databases

ProteinModelPortaliQ7Z7M9.
SMRiQ7Z7M9. Positions 439-935.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini36 – 940905LumenalSequence 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
Domaini804 – 935132Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni495 – 604110Catalytic subdomain AAdd
BLAST
Regioni664 – 72663Catalytic 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 binds to GalNAc and contributes to the glycopeptide specificity.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG307550.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000231869.
HOVERGENiHBG051698.
InParanoidiQ7Z7M9.
KOiK00710.
OMAiSHVVIIT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ7Z7M9.
TreeFamiTF313267.

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]

Sequencei

Sequence statusi: Complete.

Q7Z7M9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNRIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVIKEDIV
60 70 80 90 100
RRERIGFRVQ PDQGKIFYSS IKEMKPPLRG HGKGAWGKEN VRKTEESVLK
110 120 130 140 150
VEVDLDQTQR ERKMQNALGR GKVVPLWHPA HLQTLPVTPN KQKTDGRGTK
160 170 180 190 200
PEASSHQGTP KQTTAQGAPK TSFIAAKGTQ VVKISVHMGR VSLKQEPRKS
210 220 230 240 250
HSPSSDTSKL AAERDLNVTI SLSTDRPKQR SQAVANERAH PASTAVPKSG
260 270 280 290 300
EAMALNKTKT QSKEVNANKH KANTSLPFPK FTVNSNRLRK QSINETPLGS
310 320 330 340 350
LSKDDGARGA HGKKLNFSES HLVIITKEEE QKADPKEVSN SKTKTIFPKV
360 370 380 390 400
LGKSQSKHIS RNRSEMSSSS LAPHRVPLSQ TNHALTGGLE PAKINITAKA
410 420 430 440 450
PSTEYNQSHI KALLPEDSGT HQVLRIDVTL SPRDPKAPGQ FGRPVVVPHG
460 470 480 490 500
KEKEAERRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNNLPTTSV
510 520 530 540 550
IMCFVDEVWS TLLRSVHSVI NRSPPHLIKE ILLVDDFSTK DYLKDNLDKY
560 570 580 590 600
MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP
610 620 630 640 650
LLERVYLSRK KVACPVIEVI NDKDMSYMTV DNFQRGIFVW PMNFGWRTIP
660 670 680 690 700
PDVIAKNRIK ETDTIRCPVM AGGLFSIDKS YFFELGTYDP GLDVWGGENM
710 720 730 740 750
ELSFKVWMCG GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE
760 770 780 790 800
VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK SFKWYLENVF
810 820 830 840 850
PDLRAPIVRA SGVLINVALG KCISIENTTV ILEDCDGSKE LQQFNYTWLR
860 870 880 890 900
LIKCGEWCIA PIPDKGAVRL HPCDNRNKGL KWLHKSTSVF HPELVNHIVF
910 920 930 940
ENNQQLLCLE GNFSQKILKV AACDPVKPYQ KWKFEKYYEA
Length:940
Mass (Da):106,266
Last modified:October 1, 2003 - v1
Checksum:iDB2DFACDCACD0F6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2753NTS → AEG1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771P → L.
Corresponds to variant rs3739112 [ dbSNP | Ensembl ].
VAR_019578
Natural varianti489 – 4891Q → H.
Corresponds to variant rs6759356 [ dbSNP | Ensembl ].
VAR_019579
Natural varianti507 – 5071E → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_035991
Natural varianti692 – 6921L → F in a breast cancer sample; somatic mutation. 1 Publication
VAR_035992

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY277591 mRNA. Translation: AAP34404.1.
AK292154 mRNA. Translation: BAF84843.1.
CH471058 Genomic DNA. Translation: EAX11449.1.
BC142676 mRNA. Translation: AAI42677.1.
AJ245539 mRNA. Translation: CAB65104.1.
AF154107 mRNA. Translation: AAF15313.1.
CCDSiCCDS2203.1.
RefSeqiNP_055383.1. NM_014568.1.
UniGeneiHs.269027.

Genome annotation databases

EnsembliENST00000259056; ENSP00000259056; ENSG00000136542.
GeneIDi11227.
KEGGihsa:11227.
UCSCiuc002tzg.3. human.

Polymorphism databases

DMDMi51315940.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY277591 mRNA. Translation: AAP34404.1 .
AK292154 mRNA. Translation: BAF84843.1 .
CH471058 Genomic DNA. Translation: EAX11449.1 .
BC142676 mRNA. Translation: AAI42677.1 .
AJ245539 mRNA. Translation: CAB65104.1 .
AF154107 mRNA. Translation: AAF15313.1 .
CCDSi CCDS2203.1.
RefSeqi NP_055383.1. NM_014568.1.
UniGenei Hs.269027.

3D structure databases

ProteinModelPortali Q7Z7M9.
SMRi Q7Z7M9. Positions 439-935.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116394. 2 interactions.
STRINGi 9606.ENSP00000259056.

Protein family/group databases

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

PTM databases

PhosphoSitei Q7Z7M9.

Polymorphism databases

DMDMi 51315940.

Proteomic databases

MaxQBi Q7Z7M9.
PaxDbi Q7Z7M9.
PRIDEi Q7Z7M9.

Protocols and materials databases

DNASUi 11227.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259056 ; ENSP00000259056 ; ENSG00000136542 .
GeneIDi 11227.
KEGGi hsa:11227.
UCSCi uc002tzg.3. human.

Organism-specific databases

CTDi 11227.
GeneCardsi GC02P158079.
HGNCi HGNC:4127. GALNT5.
HPAi HPA008963.
HPA009035.
neXtProti NX_Q7Z7M9.
PharmGKBi PA28540.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307550.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000231869.
HOVERGENi HBG051698.
InParanoidi Q7Z7M9.
KOi K00710.
OMAi SHVVIIT.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q7Z7M9.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSi GALNT5. human.
GenomeRNAii 11227.
NextBioi 42730.
PROi Q7Z7M9.

Gene expression databases

Bgeei Q7Z7M9.
CleanExi HS_GALNT5.
ExpressionAtlasi Q7Z7M9. baseline and differential.
Genevestigatori Q7Z7M9.

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. Huang C.Q., Wu S.L., Cheng Z.
    Submitted (APR-2003) 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].
    Tissue: Synovium.
  3. 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].
  5. Bennett E.P.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 273-940.
  6. "A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses."
    Simmons A.D., Musy M.M., Lopes C.S., Hwang L.-Y., Yang Y.-P., Lovett M.
    Hum. Mol. Genet. 8:2155-2164(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 331-940, INTERACTION WITH EXT2.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-507 AND PHE-692.

Entry informationi

Entry nameiGALT5_HUMAN
AccessioniPrimary (citable) accession number: Q7Z7M9
Secondary accession number(s): A5PKZ1, Q9UGK7, Q9UHL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 98 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 2
    Human chromosome 2: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3