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Protein

Polypeptide N-acetylgalactosaminyltransferase 13

Gene

GALNT13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. May be responsible for the synthesis of Tn antigen in neuronal cells.

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 sitei155 – 1551SubstrateBy similarity
Binding sitei185 – 1851SubstrateBy similarity
Metal bindingi208 – 2081ManganeseBy similarity
Metal bindingi210 – 2101ManganeseBy similarity
Binding sitei315 – 3151SubstrateBy similarity
Metal bindingi343 – 3431ManganeseBy similarity
Binding sitei346 – 3461SubstrateBy similarity
Binding sitei351 – 3511SubstrateBy similarity

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
  4. protein O-linked glycosylation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 2681.
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 13 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 13
Short name:
GalNAc-T13
Short name:
pp-GaNTase 13
Protein-UDP acetylgalactosaminyltransferase 13
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
Gene namesi
Name:GALNT13
Synonyms:KIAA1918
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:23242. GALNT13.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence Analysis
Transmembranei5 – 2723Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini28 – 556529LumenalSequence 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

PharmGKBiPA134887166.

Polymorphism and mutation databases

BioMutaiGALNT13.
DMDMi116242497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556Polypeptide N-acetylgalactosaminyltransferase 13PRO_0000059130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi105 ↔ 338PROSITE-ProRule annotation
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi329 ↔ 407PROSITE-ProRule annotation
Disulfide bondi441 ↔ 458PROSITE-ProRule annotation
Disulfide bondi481 ↔ 496PROSITE-ProRule annotation
Disulfide bondi522 ↔ 539PROSITE-ProRule annotation
Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8IUC8.
PaxDbiQ8IUC8.
PRIDEiQ8IUC8.

PTM databases

PhosphoSiteiQ8IUC8.

Expressioni

Tissue specificityi

Specifically expressed in neuronal cells. Expressed in fetal brain, whole adult brain, cerebral cortex and cerebellum. Not expressed in other tissues tested.1 Publication

Gene expression databases

BgeeiQ8IUC8.
CleanExiHS_GALNT13.
ExpressionAtlasiQ8IUC8. baseline and differential.
GenevestigatoriQ8IUC8.

Organism-specific databases

HPAiHPA060775.

Interactioni

Protein-protein interaction databases

BioGridi125365. 3 interactions.
STRINGi9606.ENSP00000376570.

Structurei

3D structure databases

ProteinModelPortaliQ8IUC8.
SMRiQ8IUC8. Positions 94-552.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini428 – 550123Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 224111Catalytic subdomain AAdd
BLAST
Regioni284 – 34663Catalytic 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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8IUC8.
KOiK00710.
OMAiENVYPES.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8IUC8.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IUC8-1) [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
MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI
60 70 80 90 100
SRNQEGPGEM GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV
110 120 130 140 150
RLEGCKTKVY PDELPNTSVV IVFHNEAWST LLRTVYSVIN RSPHYLLSEV
160 170 180 190 200
ILVDDASERD FLKLTLENYV KNLEVPVKII RMEERSGLIR ARLRGAAASK
210 220 230 240 250
GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI SDDTFEYMAG
260 270 280 290 300
SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN
310 320 330 340 350
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP
360 370 380 390 400
YTFPGGTGHV INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT
410 420 430 440 450
LRENLKCKPF SWYLENIYPD SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN
460 470 480 490 500
EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL CLDVSRLNGP VIMLKCHHMR
510 520 530 540 550
GNQLWEYDAE RLTLRHVNSN QCLDEPSEED KMVPTMQDCS GSRSQQWLLR

NMTLGT
Length:556
Mass (Da):64,051
Last modified:October 17, 2006 - v2
Checksum:i00F3DCDDC4754D6F
GO
Isoform 2 (identifier: Q8IUC8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     466-486: VFSYTADKEIRTDDLCLDVSR → TQWTCNHVKMPPYERKSVMGI
     487-556: Missing.

Note: No experimental confirmation available.

Show »
Length:486
Mass (Da):55,984
Checksum:iCBD44DBD154E567D
GO
Isoform 3 (identifier: Q8IUC8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     511-556: RLTLRHVNSN...WLLRNMTLGT → SCLSVNKVAD...IFGNSTDYIL

Note: No experimental confirmation available.

Show »
Length:561
Mass (Da):64,624
Checksum:i309A4A1B365D02B8
GO

Sequence cautioni

The sequence AAF19246.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC85542.1 differs from that shown.Chimera. Chimeric at the N-terminus.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41F → S in BAC54545 (PubMed:12407114).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591E → D.
Corresponds to variant rs34086479 [ dbSNP | Ensembl ].
VAR_049242

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei466 – 48621VFSYT…LDVSR → TQWTCNHVKMPPYERKSVMG I in isoform 2. 1 PublicationVSP_011218Add
BLAST
Alternative sequencei487 – 55670Missing in isoform 2. 1 PublicationVSP_011219Add
BLAST
Alternative sequencei511 – 55646RLTLR…MTLGT → SCLSVNKVADGSQHPTVETC NDSTLQKWLLRNYTRMEIFR NIFGNSTDYIL in isoform 3. 1 PublicationVSP_054411Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB078142 mRNA. Translation: BAC54545.1.
KJ534843 mRNA. Translation: AHW56483.1.
AJ505991 mRNA. Translation: CAD44533.2.
AC008166 Genomic DNA. No translation available.
AC009227 Genomic DNA. Translation: AAF19246.1. Different initiation.
AC009297 Genomic DNA. No translation available.
AC092584 Genomic DNA. No translation available.
AC092589 Genomic DNA. No translation available.
AC133107 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11464.1.
CH471058 Genomic DNA. Translation: EAX11465.1.
BC101031 mRNA. Translation: AAI01032.1.
BC101032 mRNA. Translation: AAI01033.1.
BC101033 mRNA. Translation: AAI01034.1.
BC101034 mRNA. Translation: AAI01035.1.
AB067505 mRNA. Translation: BAB67811.1.
AK123152 mRNA. Translation: BAC85542.1. Sequence problems.
CCDSiCCDS2199.1. [Q8IUC8-1]
RefSeqiNP_001288556.1. NM_001301627.1. [Q8IUC8-3]
NP_443149.2. NM_052917.3. [Q8IUC8-1]
UniGeneiHs.470277.

Genome annotation databases

EnsembliENST00000392825; ENSP00000376570; ENSG00000144278. [Q8IUC8-1]
ENST00000409237; ENSP00000387239; ENSG00000144278. [Q8IUC8-3]
GeneIDi114805.
KEGGihsa:114805.
UCSCiuc002tyr.4. human. [Q8IUC8-1]
uc002tyt.4. human.
uc010foc.1. human. [Q8IUC8-2]

Polymorphism and mutation databases

BioMutaiGALNT13.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB078142 mRNA. Translation: BAC54545.1.
KJ534843 mRNA. Translation: AHW56483.1.
AJ505991 mRNA. Translation: CAD44533.2.
AC008166 Genomic DNA. No translation available.
AC009227 Genomic DNA. Translation: AAF19246.1. Different initiation.
AC009297 Genomic DNA. No translation available.
AC092584 Genomic DNA. No translation available.
AC092589 Genomic DNA. No translation available.
AC133107 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11464.1.
CH471058 Genomic DNA. Translation: EAX11465.1.
BC101031 mRNA. Translation: AAI01032.1.
BC101032 mRNA. Translation: AAI01033.1.
BC101033 mRNA. Translation: AAI01034.1.
BC101034 mRNA. Translation: AAI01035.1.
AB067505 mRNA. Translation: BAB67811.1.
AK123152 mRNA. Translation: BAC85542.1. Sequence problems.
CCDSiCCDS2199.1. [Q8IUC8-1]
RefSeqiNP_001288556.1. NM_001301627.1. [Q8IUC8-3]
NP_443149.2. NM_052917.3. [Q8IUC8-1]
UniGeneiHs.470277.

3D structure databases

ProteinModelPortaliQ8IUC8.
SMRiQ8IUC8. Positions 94-552.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125365. 3 interactions.
STRINGi9606.ENSP00000376570.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteiQ8IUC8.

Polymorphism and mutation databases

BioMutaiGALNT13.
DMDMi116242497.

Proteomic databases

MaxQBiQ8IUC8.
PaxDbiQ8IUC8.
PRIDEiQ8IUC8.

Protocols and materials databases

DNASUi114805.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392825; ENSP00000376570; ENSG00000144278. [Q8IUC8-1]
ENST00000409237; ENSP00000387239; ENSG00000144278. [Q8IUC8-3]
GeneIDi114805.
KEGGihsa:114805.
UCSCiuc002tyr.4. human. [Q8IUC8-1]
uc002tyt.4. human.
uc010foc.1. human. [Q8IUC8-2]

Organism-specific databases

CTDi114805.
GeneCardsiGC02P154765.
HGNCiHGNC:23242. GALNT13.
HPAiHPA060775.
MIMi608369. gene.
neXtProtiNX_Q8IUC8.
PharmGKBiPA134887166.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8IUC8.
KOiK00710.
OMAiENVYPES.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8IUC8.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 2681.
ReactomeiREACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGALNT13. human.
GeneWikiiGALNT13.
GenomeRNAii114805.
NextBioi79266.
PROiQ8IUC8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IUC8.
CleanExiHS_GALNT13.
ExpressionAtlasiQ8IUC8. baseline and differential.
GenevestigatoriQ8IUC8.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen."
    Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.
    J. Biol. Chem. 278:573-584(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  3. "polypetide GalNAc-transferase 13, ppGalNAc-T13, GALNT13."
    Bennett E.P.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 3).
  7. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-556 (ISOFORM 1).
    Tissue: Brain.
  8. "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] OF 262-556 (ISOFORM 2).
    Tissue: Cerebellum.

Entry informationi

Entry nameiGLT13_HUMAN
AccessioniPrimary (citable) accession number: Q8IUC8
Secondary accession number(s): Q08ER7
, Q68VI8, Q6ZWG1, Q96PX0, Q9UIE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 17, 2006
Last modified: April 29, 2015
This is version 119 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

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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.