SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7Z7M9

- GALT5_HUMAN

UniProt

Q7Z7M9 - GALT5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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.

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 – 5361Substrate By similarity
Binding sitei565 – 5651Substrate By similarity
Metal bindingi588 – 5881Manganese By similarity
Binding sitei589 – 5891Substrate By similarity
Metal bindingi590 – 5901Manganese By similarity
Binding sitei695 – 6951Substrate By similarity
Metal bindingi723 – 7231Manganese By similarity
Binding sitei726 – 7261Substrate By similarity
Binding sitei731 – 7311Substrate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. O-glycan processing Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. glycosaminoglycan biosynthetic process Source: UniProtKB
  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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini36 – 940905Lumenal Reviewed prediction
Add
BLAST

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 5
PRO_0000059110Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ7Z7M9.
PaxDbiQ7Z7M9.
PRIDEiQ7Z7M9.

PTM databases

PhosphoSiteiQ7Z7M9.

Expressioni

Gene expression databases

ArrayExpressiQ7Z7M9.
BgeeiQ7Z7M9.
CleanExiHS_GALNT5.
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini804 – 935132Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni495 – 604110Catalytic subdomain A
Add
BLAST
Regioni664 – 72663Catalytic subdomain B
Add
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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG307550.
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

MNRIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVIKEDIV    50
RRERIGFRVQ PDQGKIFYSS IKEMKPPLRG HGKGAWGKEN VRKTEESVLK 100
VEVDLDQTQR ERKMQNALGR GKVVPLWHPA HLQTLPVTPN KQKTDGRGTK 150
PEASSHQGTP KQTTAQGAPK TSFIAAKGTQ VVKISVHMGR VSLKQEPRKS 200
HSPSSDTSKL AAERDLNVTI SLSTDRPKQR SQAVANERAH PASTAVPKSG 250
EAMALNKTKT QSKEVNANKH KANTSLPFPK FTVNSNRLRK QSINETPLGS 300
LSKDDGARGA HGKKLNFSES HLVIITKEEE QKADPKEVSN SKTKTIFPKV 350
LGKSQSKHIS RNRSEMSSSS LAPHRVPLSQ TNHALTGGLE PAKINITAKA 400
PSTEYNQSHI KALLPEDSGT HQVLRIDVTL SPRDPKAPGQ FGRPVVVPHG 450
KEKEAERRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNNLPTTSV 500
IMCFVDEVWS TLLRSVHSVI NRSPPHLIKE ILLVDDFSTK DYLKDNLDKY 550
MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP 600
LLERVYLSRK KVACPVIEVI NDKDMSYMTV DNFQRGIFVW PMNFGWRTIP 650
PDVIAKNRIK ETDTIRCPVM AGGLFSIDKS YFFELGTYDP GLDVWGGENM 700
ELSFKVWMCG GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE 750
VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK SFKWYLENVF 800
PDLRAPIVRA SGVLINVALG KCISIENTTV ILEDCDGSKE LQQFNYTWLR 850
LIKCGEWCIA PIPDKGAVRL HPCDNRNKGL KWLHKSTSVF HPELVNHIVF 900
ENNQQLLCLE GNFSQKILKV AACDPVKPYQ KWKFEKYYEA 940
Length:940
Mass (Da):106,266
Last modified:October 1, 2003 - v1
Checksum:iDB2DFACDCACD0F6A
GO

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 conflict

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

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.
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

ArrayExpressi Q7Z7M9.
Bgeei Q7Z7M9.
CleanExi HS_GALNT5.
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: September 3, 2014
This is version 96 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

Similar proteinsi