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Q14435

- GALT3_HUMAN

UniProt

Q14435 - GALT3_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 3

Gene

GALNT3

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 HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis.2 Publications

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 sitei225 – 2251SubstrateBy similarity
Binding sitei254 – 2541SubstrateBy similarity
Metal bindingi277 – 2771ManganeseBy similarity
Metal bindingi279 – 2791ManganeseBy similarity
Binding sitei387 – 3871SubstrateBy similarity
Metal bindingi415 – 4151ManganeseBy similarity
Binding sitei418 – 4181SubstrateBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: BHF-UCL
  2. carbohydrate binding Source: UniProtKB-KW
  3. manganese ion binding Source: BHF-UCL
  4. polypeptide N-acetylgalactosaminyltransferase activity Source: BHF-UCL

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 via serine Source: BHF-UCL
  6. protein O-linked glycosylation via threonine Source: UniProtKB
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 3 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 3
Short name:
GalNAc-T3
Short name:
pp-GaNTase 3
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Gene namesi
Name:GALNT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4125. GALNT3.

Subcellular locationi

Golgi apparatusGolgi stack membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Note: Resides preferentially in the trans and medial parts of the Golgi stack.

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: ProtInc
  3. membrane Source: ProtInc
  4. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Tumoral calcinosis, hyperphosphatemic, familial (HFTC) [MIM:211900]: A severe metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi211900. phenotype.
Orphaneti306661. Familial tumoral calcinosis.
PharmGKBiPA28538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Polypeptide N-acetylgalactosaminyltransferase 3PRO_0000059106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi173 ↔ 410PROSITE-ProRule annotation
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi401 ↔ 482PROSITE-ProRule annotation
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi517 ↔ 535PROSITE-ProRule annotation
Disulfide bondi561 ↔ 574PROSITE-ProRule annotation
Disulfide bondi605 ↔ 618PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ14435.
PaxDbiQ14435.
PRIDEiQ14435.

PTM databases

PhosphoSiteiQ14435.

Expressioni

Tissue specificityi

Expressed in organs that contain secretory epithelial glands. Highly expressed in pancreas, skin, kidney and testis. Weakly expressed in prostate, ovary, intestine and colon. Also expressed in placenta and lung and fetal lung and fetal kidney.2 Publications

Gene expression databases

BgeeiQ14435.
CleanExiHS_GALNT3.
ExpressionAtlasiQ14435. baseline and differential.
GenevestigatoriQ14435.

Organism-specific databases

HPAiHPA007613.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000376465.

Structurei

3D structure databases

ProteinModelPortaliQ14435.
SMRiQ14435. Positions 146-608.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini38 – 633596LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 3718Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini504 – 630127Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 293110Catalytic subdomain AAdd
BLAST
Regioni356 – 41863Catalytic 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.
InParanoidiQ14435.
KOiK00710.
OMAiQYFEYSA.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ14435.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14435-1) [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
MAHLKRLVKL HIKRHYHKKF WKLGAVIFFF IIVLVLMQRE VSVQYSKEES
60 70 80 90 100
RMERNMKNKN KMLDLMLEAV NNIKDAMPKM QIGAPVRQNI DAGERPCLQG
110 120 130 140 150
YYTAAELKPV LDRPPQDSNA PGASGKAFKT TNLSVEEQKE KERGEAKHCF
160 170 180 190 200
NAFASDRISL HRDLGPDTRP PECIEQKFKR CPPLPTTSVI IVFHNEAWST
210 220 230 240 250
LLRTVHSVLY SSPAILLKEI ILVDDASVDE YLHDKLDEYV KQFSIVKIVR
260 270 280 290 300
QRERKGLITA RLLGATVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA
310 320 330 340 350
VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR
360 370 380 390 400
KDETYPIKTP TFAGGLFSIS KEYFEYIGSY DEEMEIWGGE NIEMSFRVWQ
410 420 430 440 450
CGGQLEIMPC SVVGHVFRSK SPHSFPKGTQ VIARNQVRLA EVWMDEYKEI
460 470 480 490 500
FYRRNTDAAK IVKQKAFGDL SKRFEIKHRL QCKNFTWYLN NIYPEVYVPD
510 520 530 540 550
LNPVISGYIK SVGQPLCLDV GENNQGGKPL IMYTCHGLGG NQYFEYSAQH
560 570 580 590 600
EIRHNIQKEL CLHAAQGLVQ LKACTYKGHK TVVTGEQIWE IQKDQLLYNP
610 620 630
FLKMCLSANG EHPSLVSCNP SDPLQKWILS QND
Length:633
Mass (Da):72,610
Last modified:October 14, 2008 - v2
Checksum:i3019B2DCCC19A584
GO
Isoform 2 (identifier: Q14435-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     173-192: CIEQKFKRCPPLPTTSVIIV → YVEEYLLFILYHQALQGREG
     193-633: Missing.

Note: No experimental confirmation available.

Show »
Length:192
Mass (Da):22,212
Checksum:i2EEE40B4D6537601
GO

Sequence cautioni

The sequence AAH56246.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti481 – 4811Q → R in CAA63371. (PubMed:8663203)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei173 – 19220CIEQK…SVIIV → YVEEYLLFILYHQALQGREG in isoform 2. 1 PublicationVSP_011202Add
BLAST
Alternative sequencei193 – 633441Missing in isoform 2. 1 PublicationVSP_011203Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92689 mRNA. Translation: CAA63371.1.
AC009495 Genomic DNA. Translation: AAY14678.1.
CH471058 Genomic DNA. Translation: EAX11324.1.
BC056246 mRNA. Translation: AAH56246.1. Different initiation.
BC113565 mRNA. Translation: AAI13566.1.
BC113567 mRNA. Translation: AAI13568.1.
CCDSiCCDS2226.1. [Q14435-1]
RefSeqiNP_004473.2. NM_004482.3. [Q14435-1]
XP_005246506.1. XM_005246449.1. [Q14435-1]
UniGeneiHs.170986.

Genome annotation databases

EnsembliENST00000392701; ENSP00000376465; ENSG00000115339. [Q14435-1]
GeneIDi2591.
KEGGihsa:2591.
UCSCiuc002udi.2. human. [Q14435-2]
uc010fph.1. human. [Q14435-1]

Polymorphism databases

DMDMi209572629.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 3

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92689 mRNA. Translation: CAA63371.1 .
AC009495 Genomic DNA. Translation: AAY14678.1 .
CH471058 Genomic DNA. Translation: EAX11324.1 .
BC056246 mRNA. Translation: AAH56246.1 . Different initiation.
BC113565 mRNA. Translation: AAI13566.1 .
BC113567 mRNA. Translation: AAI13568.1 .
CCDSi CCDS2226.1. [Q14435-1 ]
RefSeqi NP_004473.2. NM_004482.3. [Q14435-1 ]
XP_005246506.1. XM_005246449.1. [Q14435-1 ]
UniGenei Hs.170986.

3D structure databases

ProteinModelPortali Q14435.
SMRi Q14435. Positions 146-608.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000376465.

Protein family/group databases

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

PTM databases

PhosphoSitei Q14435.

Polymorphism databases

DMDMi 209572629.

Proteomic databases

MaxQBi Q14435.
PaxDbi Q14435.
PRIDEi Q14435.

Protocols and materials databases

DNASUi 2591.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392701 ; ENSP00000376465 ; ENSG00000115339 . [Q14435-1 ]
GeneIDi 2591.
KEGGi hsa:2591.
UCSCi uc002udi.2. human. [Q14435-2 ]
uc010fph.1. human. [Q14435-1 ]

Organism-specific databases

CTDi 2591.
GeneCardsi GC02M166567.
H-InvDB HIX0024214.
HGNCi HGNC:4125. GALNT3.
HPAi HPA007613.
MIMi 211900. phenotype.
601756. gene.
neXtProti NX_Q14435.
Orphaneti 306661. Familial tumoral calcinosis.
PharmGKBi PA28538.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q14435.
KOi K00710.
OMAi QYFEYSA.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q14435.
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 GALNT3. human.
GeneWikii GALNT3.
GenomeRNAii 2591.
NextBioi 10249.
PROi Q14435.
SOURCEi Search...

Gene expression databases

Bgeei Q14435.
CleanExi HS_GALNT3.
ExpressionAtlasi Q14435. baseline and differential.
Genevestigatori Q14435.

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. "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3."
    Bennett E.P., Hassan H., Clausen H.
    J. Biol. Chem. 271:17006-17012(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Salivary gland.
  2. "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].
  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] (ISOFORMS 1 AND 2).
    Tissue: Lung.
  5. "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3."
    Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
    J. Biol. Chem. 272:23503-23514(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus."
    Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.
    J. Cell Sci. 111:45-60(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma."
    Onitsuka K., Shibao K., Nakayama Y., Minagawa N., Hirata K., Izumi H., Matsuo K., Nagata N., Kitazato K., Kohno K., Itoh H.
    Cancer Sci. 94:32-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis."
    Topaz O., Shurman D.L., Bergman R., Indelman M., Ratajczak P., Mizrachi M., Khamaysi Z., Behar D., Petronius D., Friedman V., Zelikovic I., Raimer S., Metzker A., Richard G., Sprecher E.
    Nat. Genet. 36:579-581(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HFTC.
  9. "Identification of a recurrent mutation in GALNT3 demonstrates that hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are allelic disorders."
    Frishberg Y., Topaz O., Bergman R., Behar D., Fisher D., Gordon D., Richard G., Sprecher E.
    J. Mol. Med. 83:33-38(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HFTC.
  10. "Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation."
    Kato K., Jeanneau C., Tarp M.A., Benet-Pages A., Lorenz-Depiereux B., Bennett E.P., Mandel U., Strom T.M., Clausen H.
    J. Biol. Chem. 281:18370-18377(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGALT3_HUMAN
AccessioniPrimary (citable) accession number: Q14435
Secondary accession number(s): Q53TG9, Q7Z476
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 135 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

Miscellaneous

Overexpressed in many differentiated carcinomas, suggesting that it may serve as a marker of tumor differentiation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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