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Q7Z7M9 (GALT5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GALNT5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length940 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3. Ref.6

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Domain

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 similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 940940Polypeptide N-acetylgalactosaminyltransferase 5
PRO_0000059110

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3523Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 940905Lumenal Potential
Domain804 – 935132Ricin B-type lectin
Region495 – 604110Catalytic subdomain A
Region664 – 72663Catalytic subdomain B

Sites

Metal binding5881Manganese By similarity
Metal binding5901Manganese By similarity
Metal binding7231Manganese By similarity
Binding site5361Substrate By similarity
Binding site5651Substrate By similarity
Binding site5891Substrate By similarity
Binding site6951Substrate By similarity
Binding site7261Substrate By similarity
Binding site7311Substrate By similarity

Amino acid modifications

Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation5781N-linked (GlcNAc...) Potential
Glycosylation7761N-linked (GlcNAc...) Potential
Glycosylation8271N-linked (GlcNAc...) Potential
Glycosylation8451N-linked (GlcNAc...) Potential
Glycosylation9121N-linked (GlcNAc...) Potential
Disulfide bond486 ↔ 718 By similarity
Disulfide bond709 ↔ 789 By similarity
Disulfide bond822 ↔ 835 By similarity
Disulfide bond858 ↔ 873 By similarity
Disulfide bond908 ↔ 923 By similarity

Natural variations

Natural variant771P → L.
Corresponds to variant rs3739112 [ dbSNP | Ensembl ].
VAR_019578
Natural variant4891Q → H.
Corresponds to variant rs6759356 [ dbSNP | Ensembl ].
VAR_019579
Natural variant5071E → D in a breast cancer sample; somatic mutation. Ref.9
VAR_035991
Natural variant6921L → F in a breast cancer sample; somatic mutation. Ref.9
VAR_035992

Experimental info

Sequence conflict273 – 2753NTS → AEG Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q7Z7M9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: DB2DFACDCACD0F6A

FASTA940106,266
        10         20         30         40         50         60 
MNRIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVIKEDIV RRERIGFRVQ 

        70         80         90        100        110        120 
PDQGKIFYSS IKEMKPPLRG HGKGAWGKEN VRKTEESVLK VEVDLDQTQR ERKMQNALGR 

       130        140        150        160        170        180 
GKVVPLWHPA HLQTLPVTPN KQKTDGRGTK PEASSHQGTP KQTTAQGAPK TSFIAAKGTQ 

       190        200        210        220        230        240 
VVKISVHMGR VSLKQEPRKS HSPSSDTSKL AAERDLNVTI SLSTDRPKQR SQAVANERAH 

       250        260        270        280        290        300 
PASTAVPKSG EAMALNKTKT QSKEVNANKH KANTSLPFPK FTVNSNRLRK QSINETPLGS 

       310        320        330        340        350        360 
LSKDDGARGA HGKKLNFSES HLVIITKEEE QKADPKEVSN SKTKTIFPKV LGKSQSKHIS 

       370        380        390        400        410        420 
RNRSEMSSSS LAPHRVPLSQ TNHALTGGLE PAKINITAKA PSTEYNQSHI KALLPEDSGT 

       430        440        450        460        470        480 
HQVLRIDVTL SPRDPKAPGQ FGRPVVVPHG KEKEAERRWK EGNFNVYLSD LIPVDRAIED 

       490        500        510        520        530        540 
TRPAGCAEQL VHNNLPTTSV IMCFVDEVWS TLLRSVHSVI NRSPPHLIKE ILLVDDFSTK 

       550        560        570        580        590        600 
DYLKDNLDKY MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP 

       610        620        630        640        650        660 
LLERVYLSRK KVACPVIEVI NDKDMSYMTV DNFQRGIFVW PMNFGWRTIP PDVIAKNRIK 

       670        680        690        700        710        720 
ETDTIRCPVM AGGLFSIDKS YFFELGTYDP GLDVWGGENM ELSFKVWMCG GEIEIIPCSR 

       730        740        750        760        770        780 
VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ 

       790        800        810        820        830        840 
RELRKKLKCK SFKWYLENVF PDLRAPIVRA SGVLINVALG KCISIENTTV ILEDCDGSKE 

       850        860        870        880        890        900 
LQQFNYTWLR LIKCGEWCIA PIPDKGAVRL HPCDNRNKGL KWLHKSTSVF HPELVNHIVF 

       910        920        930        940 
ENNQQLLCLE GNFSQKILKV AACDPVKPYQ KWKFEKYYEA 

« Hide

References

« Hide 'large scale' references
[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. 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].
Tissue: Synovium.
[3]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-507 AND PHE-692.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2203.1.
RefSeqNP_055383.1. NM_014568.1.
UniGeneHs.269027.

3D structure databases

ProteinModelPortalQ7Z7M9.
SMRQ7Z7M9. Positions 439-935.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116394. 2 interactions.
STRING9606.ENSP00000259056.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ7Z7M9.

Polymorphism databases

DMDM51315940.

Proteomic databases

MaxQBQ7Z7M9.
PaxDbQ7Z7M9.
PRIDEQ7Z7M9.

Protocols and materials databases

DNASU11227.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259056; ENSP00000259056; ENSG00000136542.
GeneID11227.
KEGGhsa:11227.
UCSCuc002tzg.3. human.

Organism-specific databases

CTD11227.
GeneCardsGC02P158079.
HGNCHGNC:4127. GALNT5.
HPAHPA008963.
HPA009035.
neXtProtNX_Q7Z7M9.
PharmGKBPA28540.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307550.
HOGENOMHOG000231869.
HOVERGENHBG051698.
InParanoidQ7Z7M9.
KOK00710.
OMASHVVIIT.
OrthoDBEOG7J9VP2.
PhylomeDBQ7Z7M9.
TreeFamTF313267.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ7Z7M9.
BgeeQ7Z7M9.
CleanExHS_GALNT5.
GenevestigatorQ7Z7M9.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGALNT5. human.
GenomeRNAi11227.
NextBio42730.
PROQ7Z7M9.

Entry information

Entry nameGALT5_HUMAN
AccessionPrimary (citable) accession number: Q7Z7M9
Secondary accession number(s): A5PKZ1, Q9UGK7, Q9UHL6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 95 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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM