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Q8IUC8

- GLT13_HUMAN

UniProt

Q8IUC8 - GLT13_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 13

Gene
GALNT13, KIAA1918
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Manganese By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551Substrate By similarity
Binding sitei185 – 1851Substrate By similarity
Metal bindingi208 – 2081Manganese By similarity
Metal bindingi210 – 2101Manganese By similarity
Binding sitei315 – 3151Substrate By similarity
Metal bindingi343 – 3431Manganese By similarity
Binding sitei346 – 3461Substrate By similarity
Binding sitei351 – 3511Substrate By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. 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

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: Chromosome 2

Organism-specific databases

HGNCiHGNC:23242. GALNT13.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2723Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini28 – 556529Lumenal Reviewed predictionAdd
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.

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...) Reviewed prediction
Disulfide bondi105 ↔ 338 By similarity
Glycosylationi116 – 1161N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi329 ↔ 407 By similarity
Disulfide bondi441 ↔ 458 By similarity
Disulfide bondi481 ↔ 496 By similarity
Disulfide bondi522 ↔ 539 By similarity
Glycosylationi551 – 5511N-linked (GlcNAc...) Reviewed prediction

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

ArrayExpressiQ8IUC8.
BgeeiQ8IUC8.
CleanExiHS_GALNT13.
GenevestigatoriQ8IUC8.

Organism-specific databases

HPAiHPA060775.

Interactioni

Protein-protein interaction databases

BioGridi125365. 3 interactions.
STRINGi9606.ENSP00000376570.

Structurei

3D structure databases

ProteinModelPortaliQ8IUC8.
SMRiQ8IUC8. Positions 56-552.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini428 – 550123Ricin B-type lectinAdd
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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
KOiK00710.
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. Align

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

MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI    50
SRNQEGPGEM GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV 100
RLEGCKTKVY PDELPNTSVV IVFHNEAWST LLRTVYSVIN RSPHYLLSEV 150
ILVDDASERD FLKLTLENYV KNLEVPVKII RMEERSGLIR ARLRGAAASK 200
GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI SDDTFEYMAG 250
SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN 300
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP 350
YTFPGGTGHV INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT 400
LRENLKCKPF SWYLENIYPD SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN 450
EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL CLDVSRLNGP VIMLKCHHMR 500
GNQLWEYDAE RLTLRHVNSN QCLDEPSEED KMVPTMQDCS GSRSQQWLLR 550
NMTLGT 556
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 BAC85542.1 differs from that shown. Reason: Chimera. Chimeric at the N-terminus.
The sequence AAF19246.1 differs from that shown. Reason: Erroneous initiation.

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. VSP_011218Add
BLAST
Alternative sequencei487 – 55670Missing in isoform 2. VSP_011219Add
BLAST
Alternative sequencei511 – 55646RLTLR…MTLGT → SCLSVNKVADGSQHPTVETC NDSTLQKWLLRNYTRMEIFR NIFGNSTDYIL in isoform 3. VSP_054411Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41F → S in BAC54545. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_443149.2. NM_052917.2. [Q8IUC8-1]
XP_006712293.1. XM_006712230.1. [Q8IUC8-1]
UniGeneiHs.470277.

Genome annotation databases

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

Polymorphism databases

DMDMi116242497.

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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS2199.1. [Q8IUC8-1 ]
RefSeqi NP_443149.2. NM_052917.2. [Q8IUC8-1 ]
XP_006712293.1. XM_006712230.1. [Q8IUC8-1 ]
UniGenei Hs.470277.

3D structure databases

ProteinModelPortali Q8IUC8.
SMRi Q8IUC8. Positions 56-552.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125365. 3 interactions.
STRINGi 9606.ENSP00000376570.

Protein family/group databases

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

PTM databases

PhosphoSitei Q8IUC8.

Polymorphism databases

DMDMi 116242497.

Proteomic databases

MaxQBi Q8IUC8.
PaxDbi Q8IUC8.
PRIDEi Q8IUC8.

Protocols and materials databases

DNASUi 114805.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392825 ; ENSP00000376570 ; ENSG00000144278 . [Q8IUC8-1 ]
ENST00000409237 ; ENSP00000387239 ; ENSG00000144278 .
GeneIDi 114805.
KEGGi hsa:114805.
UCSCi uc002tyr.4. human. [Q8IUC8-1 ]
uc010foc.1. human. [Q8IUC8-2 ]

Organism-specific databases

CTDi 114805.
GeneCardsi GC02P154765.
HGNCi HGNC:23242. GALNT13.
HPAi HPA060775.
MIMi 608369. gene.
neXtProti NX_Q8IUC8.
PharmGKBi PA134887166.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239675.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
KOi K00710.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8IUC8.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 2681.
Reactomei REACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSi GALNT13. human.
GeneWikii GALNT13.
GenomeRNAii 114805.
NextBioi 79266.
PROi Q8IUC8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IUC8.
Bgeei Q8IUC8.
CleanExi HS_GALNT13.
Genevestigatori Q8IUC8.

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. "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. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
    Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
    , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
    Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
    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: September 3, 2014
This is version 113 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