Skip Header

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

Q86SF2

- GALT7_HUMAN

UniProt

Q86SF2 - GALT7_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

N-acetylgalactosaminyltransferase 7

Gene

GALNT7

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

Functioni

Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei247 – 2471SubstrateBy similarity
Binding sitei277 – 2771SubstrateBy similarity
Metal bindingi301 – 3011ManganeseBy similarity
Metal bindingi303 – 3031ManganeseBy similarity
Binding sitei412 – 4121SubstrateBy similarity
Metal bindingi440 – 4401ManganeseBy similarity
Binding sitei443 – 4431SubstrateBy 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
  5. protein O-linked glycosylation Source: ProtInc
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:
N-acetylgalactosaminyltransferase 7 (EC:2.4.1.-)
Alternative name(s):
Polypeptide GalNAc transferase 7
Short name:
GalNAc-T7
Short name:
pp-GaNTase 7
Protein-UDP acetylgalactosaminyltransferase 7
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
Gene namesi
Name:GALNT7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4129. GALNT7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 657628LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28542.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657N-acetylgalactosaminyltransferase 7PRO_0000059116Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi197 ↔ 435PROSITE-ProRule annotation
Disulfide bondi426 ↔ 507PROSITE-ProRule annotation
Disulfide bondi545 ↔ 562PROSITE-ProRule annotation
Disulfide bondi585 ↔ 600PROSITE-ProRule annotation
Disulfide bondi625 ↔ 640PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ86SF2.
PaxDbiQ86SF2.
PeptideAtlasiQ86SF2.
PRIDEiQ86SF2.

PTM databases

PhosphoSiteiQ86SF2.

Expressioni

Tissue specificityi

Widely expressed. Expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS.1 Publication

Gene expression databases

BgeeiQ86SF2.
CleanExiHS_GALNT7.
ExpressionAtlasiQ86SF2. baseline and differential.
GenevestigatoriQ86SF2.

Interactioni

Protein-protein interaction databases

BioGridi119735. 14 interactions.
IntActiQ86SF2. 2 interactions.
STRINGi9606.ENSP00000265000.

Structurei

3D structure databases

ProteinModelPortaliQ86SF2.
SMRiQ86SF2. Positions 148-656.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini532 – 652121Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni206 – 317112Catalytic subdomain AAdd
BLAST
Regioni381 – 44363Catalytic 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

eggNOGiNOG248127.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ86SF2.
KOiK00710.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ86SF2.
TreeFamiTF352176.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF00535. 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.

Q86SF2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLKIGFILR SLLVVGSFLG LVVLWSSLTP RPDDPSPLSR MREDRDVNDP
60 70 80 90 100
MPNRGGNGLA PGEDRFKPVV PWPHVEGVEV DLESIRRINK AKNEQEHHAG
110 120 130 140 150
GDSQKDIMQR QYLTFKPQTF TYHDPVLRPG ILGNFEPKEP EPPGVVGGPG
160 170 180 190 200
EKAKPLVLGP EFKQAIQASI KEFGFNMVAS DMISLDRSVN DLRQEECKYW
210 220 230 240 250
HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA EIVLIDDFSN
260 270 280 290 300
KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
310 320 330 340 350
DAHCEVAVNW YAPLVAPISK DRTICTVPLI DVINGNTYEI IPQGGGDEDG
360 370 380 390 400
YARGAWDWSM LWKRVPLTPQ EKRLRKTKTE PYRSPAMAGG LFAIEREFFF
410 420 430 440 450
ELGLYDPGLQ IWGGENFEIS YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN
460 470 480 490 500
PPPIYVGSSP TLKNYVRVVE VWWDEYKDYF YASRPESQAL PYGDISELKK
510 520 530 540 550
FREDHNCKSF KWFMEEIAYD ITSHYPLPPK NVDWGEIRGF ETAYCIDSMG
560 570 580 590 600
KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGA DGSKVMITHC
610 620 630 640 650
NLNEFKEWQY FKNLHRFTHI PSGKCLDRSE VLHQVFISNC DSSKTTQKWE

MNNIHSV
Length:657
Mass (Da):75,389
Last modified:June 1, 2003 - v1
Checksum:iD78CB5CBDA4B02FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881S → N in CAB60270. (PubMed:10544240)Curated
Sequence conflicti392 – 3921F → C in CAB60270. (PubMed:10544240)Curated
Sequence conflicti408 – 4081G → S in CAB60270. (PubMed:10544240)Curated
Sequence conflicti508 – 5081K → Q in CAB60270. (PubMed:10544240)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002744 mRNA. Translation: CAB60270.1.
AK075488 mRNA. Translation: BAG52155.1.
CH471056 Genomic DNA. Translation: EAX04761.1.
BC035303 mRNA. Translation: AAH35303.1.
BC046129 mRNA. Translation: AAH46129.1.
BC047468 mRNA. Translation: AAH47468.1.
CCDSiCCDS3815.1.
RefSeqiNP_059119.2. NM_017423.2.
UniGeneiHs.548088.

Genome annotation databases

EnsembliENST00000265000; ENSP00000265000; ENSG00000109586.
GeneIDi51809.
KEGGihsa:51809.
UCSCiuc003isz.4. human.

Polymorphism databases

DMDMi51315961.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

N-acetylgalactosaminyltransferase 7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002744 mRNA. Translation: CAB60270.1 .
AK075488 mRNA. Translation: BAG52155.1 .
CH471056 Genomic DNA. Translation: EAX04761.1 .
BC035303 mRNA. Translation: AAH35303.1 .
BC046129 mRNA. Translation: AAH46129.1 .
BC047468 mRNA. Translation: AAH47468.1 .
CCDSi CCDS3815.1.
RefSeqi NP_059119.2. NM_017423.2.
UniGenei Hs.548088.

3D structure databases

ProteinModelPortali Q86SF2.
SMRi Q86SF2. Positions 148-656.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119735. 14 interactions.
IntActi Q86SF2. 2 interactions.
STRINGi 9606.ENSP00000265000.

Protein family/group databases

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

PTM databases

PhosphoSitei Q86SF2.

Polymorphism databases

DMDMi 51315961.

Proteomic databases

MaxQBi Q86SF2.
PaxDbi Q86SF2.
PeptideAtlasi Q86SF2.
PRIDEi Q86SF2.

Protocols and materials databases

DNASUi 51809.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265000 ; ENSP00000265000 ; ENSG00000109586 .
GeneIDi 51809.
KEGGi hsa:51809.
UCSCi uc003isz.4. human.

Organism-specific databases

CTDi 51809.
GeneCardsi GC04P174089.
H-InvDB HIX0031463.
HGNCi HGNC:4129. GALNT7.
MIMi 605005. gene.
neXtProti NX_Q86SF2.
PharmGKBi PA28542.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG248127.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q86SF2.
KOi K00710.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q86SF2.
TreeFami TF352176.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi GALNT7. human.
GenomeRNAii 51809.
NextBioi 55940.
PROi Q86SF2.
SOURCEi Search...

Gene expression databases

Bgeei Q86SF2.
CleanExi HS_GALNT7.
ExpressionAtlasi Q86SF2. baseline and differential.
Genevestigatori Q86SF2.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF02709. Glyco_transf_7C. 1 hit.
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. "A novel human UDP-N-acetyl-D-galactosamine;polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates."
    Bennett E.P., Hassan H., Hollingsworth M.A., Clausen H.
    FEBS Lett. 460:226-230(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
  2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  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].
    Tissue: Placenta and Testis.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGALT7_HUMAN
AccessioniPrimary (citable) accession number: Q86SF2
Secondary accession number(s): B3KQU3, Q7Z5W7, Q9UJ28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 111 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 4
    Human chromosome 4: 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