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Q86SR1

- GLT10_HUMAN

UniProt

Q86SR1 - GLT10_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 10

Gene

GALNT10

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 Muc5Ac and EA2 peptide substrates.

Catalytic activityi

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

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei154 – 1541Substrate
Binding sitei156 – 1561Substrate
Binding sitei185 – 1851Substrate
Binding sitei214 – 2141Substrate
Metal bindingi237 – 2371Manganese
Binding sitei238 – 2381Substrate
Metal bindingi239 – 2391Manganese
Binding sitei342 – 3421Substrate
Metal bindingi370 – 3701Manganese
Binding sitei373 – 3731Substrate
Binding sitei378 – 3781Substrate

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. O-glycan processing Source: Reactome
  3. 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 10 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 10
Short name:
GalNAc-T10
Short name:
pp-GaNTase 10
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene namesi
Name:GALNT10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:19873. GALNT10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 603572LumenalSequence AnalysisAdd
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

PharmGKBiPA134870832.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603Polypeptide N-acetylgalactosaminyltransferase 10PRO_0000059122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi124 – 1241N-linked (GlcNAc...)1 Publication
Disulfide bondi135 ↔ 3651 PublicationPROSITE-ProRule annotation
Glycosylationi146 – 1461N-linked (GlcNAc...)1 Publication
Disulfide bondi356 ↔ 4321 PublicationPROSITE-ProRule annotation
Disulfide bondi471 ↔ 4881 PublicationPROSITE-ProRule annotation
Disulfide bondi523 ↔ 5381 PublicationPROSITE-ProRule annotation
Disulfide bondi563 ↔ 5781 PublicationPROSITE-ProRule annotation
Glycosylationi593 – 5931N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ86SR1.
PaxDbiQ86SR1.
PRIDEiQ86SR1.

PTM databases

PhosphoSiteiQ86SR1.

Expressioni

Tissue specificityi

Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues.1 Publication

Gene expression databases

BgeeiQ86SR1.
ExpressionAtlasiQ86SR1. baseline and differential.
GenevestigatoriQ86SR1.

Organism-specific databases

HPAiHPA007525.

Interactioni

Protein-protein interaction databases

BioGridi120723. 2 interactions.
IntActiQ86SR1. 1 interaction.
MINTiMINT-2808648.

Structurei

Secondary structure

1
603
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi77 – 848Combined sources
Helixi91 – 933Combined sources
Turni100 – 1034Combined sources
Helixi106 – 1094Combined sources
Helixi115 – 1195Combined sources
Helixi133 – 1364Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi147 – 1559Combined sources
Helixi158 – 17114Combined sources
Helixi174 – 1763Combined sources
Beta strandi177 – 1848Combined sources
Helixi190 – 1923Combined sources
Helixi194 – 2007Combined sources
Beta strandi206 – 2105Combined sources
Helixi217 – 22711Combined sources
Beta strandi230 – 2356Combined sources
Beta strandi238 – 2425Combined sources
Helixi248 – 2569Combined sources
Beta strandi260 – 26910Combined sources
Turni271 – 2733Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi294 – 2974Combined sources
Turni301 – 3033Combined sources
Beta strandi319 – 3257Combined sources
Helixi326 – 3316Combined sources
Beta strandi341 – 3444Combined sources
Helixi345 – 35511Combined sources
Beta strandi359 – 37012Combined sources
Helixi386 – 39712Combined sources
Helixi399 – 4013Combined sources
Helixi402 – 4065Combined sources
Helixi410 – 4123Combined sources
Helixi421 – 43010Combined sources
Helixi435 – 4417Combined sources
Helixi446 – 4494Combined sources
Beta strandi458 – 4658Combined sources
Turni466 – 4683Combined sources
Turni478 – 4803Combined sources
Helixi495 – 4973Combined sources
Beta strandi503 – 5053Combined sources
Turni507 – 5093Combined sources
Beta strandi511 – 5144Combined sources
Beta strandi521 – 5255Combined sources
Beta strandi528 – 5325Combined sources
Beta strandi534 – 5374Combined sources
Beta strandi540 – 5434Combined sources
Beta strandi548 – 5503Combined sources
Turni551 – 5533Combined sources
Beta strandi554 – 5563Combined sources
Turni558 – 5603Combined sources
Beta strandi563 – 5664Combined sources
Turni568 – 5703Combined sources
Beta strandi573 – 5764Combined sources
Beta strandi587 – 5915Combined sources
Helixi594 – 5974Combined sources
Turni598 – 6014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D7IX-ray2.50A40-603[»]
2D7RX-ray2.80A40-603[»]
ProteinModelPortaliQ86SR1.
SMRiQ86SR1. Positions 68-603.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86SR1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 590133Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 253110Catalytic subdomain AAdd
BLAST
Regioni311 – 37363Catalytic subdomain BAdd
BLAST
Regioni373 – 38412Flexible loopAdd
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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ86SR1.
KOiK00710.
OMAiHSRQKKT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ86SR1.
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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86SR1-1) [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
MRRKEKRLLQ AVALVLAALV LLPNVGLWAL YRERQPDGTP GGSGAAVAPA
60 70 80 90 100
AGQGSHSRQK KTFFLGDGQK LKDWHDKEAI RRDAQRVGNG EQGRPYPMTD
110 120 130 140 150
AERVDQAYRE NGFNIYVSDK ISLNRSLPDI RHPNCNSKRY LETLPNTSII
160 170 180 190 200
IPFHNEGWSS LLRTVHSVLN RSPPELVAEI VLVDDFSDRE HLKKPLEDYM
210 220 230 240 250
ALFPSVRILR TKKREGLIRT RMLGASVATG DVITFLDSHC EANVNWLPPL
260 270 280 290 300
LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP
310 320 330 340 350
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS
360 370 380 390 400
FKVWMCGGRM EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE
410 420 430 440 450
YAEYIYQRRP EYRHLSAGDV AVQKKLRSSL NCKSFKWFMT KIAWDLPKFY
460 470 480 490 500
PPVEPPAAAW GEIRNVGTGL CADTKHGALG SPLRLEGCVR GRGEAAWNNM
510 520 530 540 550
QVFTFTWRED IRPGDPQHTK KFCFDAISHT SPVTLYDCHS MKGNQLWKYR
560 570 580 590 600
KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLEKF

NRN
Length:603
Mass (Da):68,992
Last modified:August 16, 2004 - v2
Checksum:iEE176F6139B92573
GO
Isoform 2 (identifier: Q86SR1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     190-251: Missing.

Note: No experimental confirmation available.

Show »
Length:541
Mass (Da):61,947
Checksum:i4216612D314EA82B
GO
Isoform 3 (identifier: Q86SR1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     354-366: WMCGGRMEDIPCS → SQLSRRPVLGTAS
     367-603: Missing.

Note: No experimental confirmation available.

Show »
Length:366
Mass (Da):41,452
Checksum:i52AB23ABC6F797FE
GO
Isoform 4 (identifier: Q86SR1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-329: Missing.
     330-352: WELGGYDPGLEIWGGEQYEISFK → MLAWRDGELEAETSSSLFLLAMQ
     389-389: N → VRT

Note: No experimental confirmation available.

Show »
Length:276
Mass (Da):31,833
Checksum:iF357AFF828E57DC7
GO

Sequence cautioni

The sequence BAB14676.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti518 – 5181H → Y in BAC56890. (PubMed:12417297)Curated
Sequence conflicti518 – 5181H → Y in BAB14676. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 329329Missing in isoform 4. 1 PublicationVSP_011207Add
BLAST
Alternative sequencei190 – 25162Missing in isoform 2. 1 PublicationVSP_011209Add
BLAST
Alternative sequencei330 – 35223WELGG…EISFK → MLAWRDGELEAETSSSLFLL AMQ in isoform 4. 1 PublicationVSP_011208Add
BLAST
Alternative sequencei354 – 36613WMCGG…DIPCS → SQLSRRPVLGTAS in isoform 3. 1 PublicationVSP_011212Add
BLAST
Alternative sequencei367 – 603237Missing in isoform 3. 1 PublicationVSP_011213Add
BLAST
Alternative sequencei389 – 3891N → VRT in isoform 4. 1 PublicationVSP_011214

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB078145 mRNA. Translation: BAC56890.1.
AJ505950 mRNA. Translation: CAD44532.1.
AK023782 mRNA. Translation: BAB14676.1. Different initiation.
AK127135 mRNA. Translation: BAG54441.1.
AL096739 mRNA. Translation: CAB46378.1.
AK074132 mRNA. Translation: BAB84958.1.
BC007224 mRNA. Translation: AAH07224.2.
BC072450 mRNA. Translation: AAH72450.1.
CCDSiCCDS4325.1. [Q86SR1-1]
PIRiT12552.
RefSeqiNP_938080.1. NM_198321.3. [Q86SR1-1]
UniGeneiHs.631797.

Genome annotation databases

EnsembliENST00000297107; ENSP00000297107; ENSG00000164574. [Q86SR1-1]
ENST00000377661; ENSP00000366889; ENSG00000164574. [Q86SR1-2]
ENST00000425427; ENSP00000415210; ENSG00000164574. [Q86SR1-3]
GeneIDi55568.
KEGGihsa:55568.
UCSCiuc003lvg.1. human. [Q86SR1-3]
uc003lvh.3. human. [Q86SR1-1]
uc010jid.3. human. [Q86SR1-2]

Polymorphism databases

DMDMi51315962.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB078145 mRNA. Translation: BAC56890.1 .
AJ505950 mRNA. Translation: CAD44532.1 .
AK023782 mRNA. Translation: BAB14676.1 . Different initiation.
AK127135 mRNA. Translation: BAG54441.1 .
AL096739 mRNA. Translation: CAB46378.1 .
AK074132 mRNA. Translation: BAB84958.1 .
BC007224 mRNA. Translation: AAH07224.2 .
BC072450 mRNA. Translation: AAH72450.1 .
CCDSi CCDS4325.1. [Q86SR1-1 ]
PIRi T12552.
RefSeqi NP_938080.1. NM_198321.3. [Q86SR1-1 ]
UniGenei Hs.631797.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D7I X-ray 2.50 A 40-603 [» ]
2D7R X-ray 2.80 A 40-603 [» ]
ProteinModelPortali Q86SR1.
SMRi Q86SR1. Positions 68-603.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120723. 2 interactions.
IntActi Q86SR1. 1 interaction.
MINTi MINT-2808648.

Protein family/group databases

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

PTM databases

PhosphoSitei Q86SR1.

Polymorphism databases

DMDMi 51315962.

Proteomic databases

MaxQBi Q86SR1.
PaxDbi Q86SR1.
PRIDEi Q86SR1.

Protocols and materials databases

DNASUi 55568.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297107 ; ENSP00000297107 ; ENSG00000164574 . [Q86SR1-1 ]
ENST00000377661 ; ENSP00000366889 ; ENSG00000164574 . [Q86SR1-2 ]
ENST00000425427 ; ENSP00000415210 ; ENSG00000164574 . [Q86SR1-3 ]
GeneIDi 55568.
KEGGi hsa:55568.
UCSCi uc003lvg.1. human. [Q86SR1-3 ]
uc003lvh.3. human. [Q86SR1-1 ]
uc010jid.3. human. [Q86SR1-2 ]

Organism-specific databases

CTDi 55568.
GeneCardsi GC05P153550.
HGNCi HGNC:19873. GALNT10.
HPAi HPA007525.
MIMi 608043. gene.
neXtProti NX_Q86SR1.
PharmGKBi PA134870832.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOVERGENi HBG051699.
InParanoidi Q86SR1.
KOi K00710.
OMAi HSRQKKT.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q86SR1.
TreeFami TF313267.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi GALNT10. human.
EvolutionaryTracei Q86SR1.
GenomeRNAii 55568.
NextBioi 60056.
PROi Q86SR1.
SOURCEi Search...

Gene expression databases

Bgeei Q86SR1.
ExpressionAtlasi Q86SR1. baseline and differential.
Genevestigatori Q86SR1.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Colon cancer.
  2. Bennett E.P.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-603 (ISOFORM 2).
    Tissue: Brain and Placenta.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Uterus.
  5. "Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
    Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
    DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-366 (ISOFORM 3).
    Tissue: Spleen.
  6. "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] OF 191-603 (ISOFORM 1).
    Tissue: Kidney and Skin.
  7. "Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)."
    Kubota T., Shiba T., Sugioka S., Furukawa S., Sawaki H., Kato R., Wakatsuki S., Narimatsu H.
    J. Mol. Biol. 359:708-727(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-603 IN COMPLEX WITH UDP-GALNAC AND GALNAC-SERINE, DISULFIDE BOND, MANGANESE-BINDING SITES, GLYCOSYLATION AT ASN-124; ASN-146 AND ASN-593.

Entry informationi

Entry nameiGLT10_HUMAN
AccessioniPrimary (citable) accession number: Q86SR1
Secondary accession number(s): B3KXC9
, Q6IN56, Q86VP8, Q8IXJ2, Q8TEJ2, Q96IV2, Q9H8E1, Q9Y4M4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 26, 2014
This is version 116 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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