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Q16394

- EXT1_HUMAN

UniProt

Q16394 - EXT1_HUMAN

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Protein

Exostosin-1

Gene

EXT1

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

Functioni

Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor.1 Publication

Catalytic activityi

UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan = UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan.
UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan.

Cofactori

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei518 – 5181SubstrateBy similarity
Metal bindingi567 – 5671Manganese; catalyticBy similarity
Binding sitei595 – 5951SubstrateBy similarity
Active sitei654 – 6541By similarity

GO - Molecular functioni

  1. acetylglucosaminyltransferase activity Source: BHF-UCL
  2. glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Source: UniProtKB
  3. glucuronosyltransferase activity Source: BHF-UCL
  4. heparan sulfate N-acetylglucosaminyltransferase activity Source: BHF-UCL
  5. N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Source: UniProtKB
  6. protein heterodimerization activity Source: BHF-UCL
  7. protein homodimerization activity Source: BHF-UCL
  8. transferase activity, transferring glycosyl groups Source: BHF-UCL

GO - Biological processi

  1. axon guidance Source: Ensembl
  2. carbohydrate metabolic process Source: Reactome
  3. cellular polysaccharide biosynthetic process Source: BHF-UCL
  4. embryonic skeletal joint development Source: Ensembl
  5. endoderm development Source: Ensembl
  6. gastrulation Source: Ensembl
  7. glycosaminoglycan biosynthetic process Source: BHF-UCL
  8. glycosaminoglycan metabolic process Source: Reactome
  9. heparan sulfate proteoglycan biosynthetic process Source: UniProtKB
  10. heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Source: BHF-UCL
  11. mesoderm development Source: Ensembl
  12. olfactory bulb development Source: Ensembl
  13. ossification Source: BHF-UCL
  14. protein glycosylation Source: UniProtKB-UniPathway
  15. signal transduction Source: ProtInc
  16. skeletal system development Source: ProtInc
  17. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00012-MONOMER.
ReactomeiREACT_121248. HS-GAG biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

Names & Taxonomyi

Protein namesi
Recommended name:
Exostosin-1 (EC:2.4.1.224, EC:2.4.1.225)
Alternative name(s):
Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
Multiple exostoses protein 1
Putative tumor suppressor protein EXT1
Gene namesi
Name:EXT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3512. EXT1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Note: The EXT1/EXT2 complex is localized in the Golgi apparatus.

GO - Cellular componenti

  1. endoplasmic reticulum Source: BHF-UCL
  2. endoplasmic reticulum membrane Source: BHF-UCL
  3. Golgi apparatus Source: BHF-UCL
  4. Golgi membrane Source: BHF-UCL
  5. integral component of endoplasmic reticulum membrane Source: UniProtKB
  6. integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Hereditary multiple exostoses 1 (EXT1) [MIM:133700]: EXT is a genetically heterogeneous bone disorder caused by genes segregating on human chromosomes 8, 11, and 19 and designated EXT1, EXT2 and EXT3 respectively. EXT is a dominantly inherited skeletal disorder primarily affecting endochondral bone during growth. The disease is characterized by formation of numerous cartilage-capped, benign bone tumors (osteocartilaginous exostoses or osteochondromas) that are often accompanied by skeletal deformities and short stature. In a small percentage of cases exostoses have exhibited malignant transformation resulting in an osteosarcoma or chondrosarcoma. Osteochondromas development can also occur as a sporadic event.8 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271Q → K in EXT1; no loss of activity.
VAR_012815
Natural varianti164 – 1641D → H in EXT1; loss of activity. 1 Publication
VAR_012816
Natural varianti215 – 2217Missing in EXT1.
VAR_012817
Natural varianti280 – 2801R → G in EXT1; loss of activity. 3 Publications
VAR_002370
Natural varianti280 – 2801R → S in EXT1; loss of activity. 1 Publication
VAR_002371
Natural varianti339 – 3391G → D in EXT1; loss of activity. 1 Publication
VAR_002372
Natural varianti340 – 3401R → C in EXT1; loss of activity; still able to form an oligomeric complex. 1 Publication
VAR_002373
Natural varianti340 – 3401R → H in EXT1; loss of activity. 2 Publications
VAR_002374
Natural varianti340 – 3401R → L in EXT1; loss of activity. 1 Publication
VAR_002375
Natural varianti340 – 3401R → S in EXT1; loss of activity. 1 Publication
VAR_002376
Natural varianti486 – 4861A → V in EXT1; no loss of activity. 1 Publication
Corresponds to variant rs188859975 [ dbSNP | Ensembl ].
VAR_012821
Natural varianti496 – 4961P → L in EXT1; no loss of activity. 1 Publication
VAR_012822
Natural varianti627 – 6271Missing in EXT1; loss of activity. 1 Publication
VAR_002377
Tricho-rhino-phalangeal syndrome 2 (TRPS2) [MIM:150230]: A syndrome that combines the clinical features of tricho-rhino-phalangeal syndrome type 1 and multiple exostoses type 1. Affected individuals manifest multiple dysmorphic facial features including large, laterally protruding ears, a bulbous nose, an elongated upper lip, as well as sparse scalp hair, winged scapulae, multiple cartilaginous exostoses, redundant skin, and mental retardation.
Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration resulting in the loss of functional copies of TRPS1 and EXT1 has been found in TRPS2 patients.
Chondrosarcoma (CHDSA) [MIM:215300]: A malignant neoplasm derived from cartilage cells. Chondrosarcomas range from slow-growing non-metastasizing lesions to highly aggressive metastasizing sarcomas.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271Q → A or P: No effect on heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi27 – 271Missing: No effect on heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi164 – 1641D → E: Abolishes heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi164 – 1641Missing: Abolishes heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi316 – 3161N → A: No effect on heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi316 – 3161Missing: No effect on heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi486 – 4861A → H: No effect on heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi486 – 4861Missing: No effect on heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi496 – 4961P → H: No effect on heparan-sulfate biosynthesis. 1 Publication
Mutagenesisi496 – 4961Missing: No effect on heparan-sulfate biosynthesis. 1 Publication

Keywords - Diseasei

Disease mutation, Hereditary multiple exostoses, Tumor suppressor

Organism-specific databases

MIMi133700. phenotype.
150230. phenotype.
215300. phenotype.
Orphaneti55880. Chondrosarcoma.
502. Langer-Giedion syndrome.
321. Multiple osteochondromas.
PharmGKBiPA27924.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 746746Exostosin-1PRO_0000149648Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi652 ↔ 704By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ16394.
PaxDbiQ16394.
PRIDEiQ16394.

PTM databases

PhosphoSiteiQ16394.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ16394.
CleanExiHS_EXT1.
ExpressionAtlasiQ16394. baseline and differential.
GenevestigatoriQ16394.

Organism-specific databases

HPAiHPA044394.

Interactioni

Subunit structurei

Forms a homo/hetero-oligomeric complex with EXT2.1 Publication

Protein-protein interaction databases

BioGridi108432. 11 interactions.
IntActiQ16394. 1 interaction.
MINTiMINT-120274.
STRINGi9606.ENSP00000367446.

Structurei

3D structure databases

ProteinModelPortaliQ16394.
SMRiQ16394. Positions 512-724.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence Analysis
Topological domaini29 – 746718LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni544 – 5496Substrate bindingBy similarity
Regioni565 – 5673Substrate bindingBy similarity
Regioni650 – 6545Substrate bindingBy similarity
Regioni688 – 70114Substrate bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG272619.
GeneTreeiENSGT00550000074496.
HOGENOMiHOG000266990.
HOVERGENiHBG003459.
InParanoidiQ16394.
KOiK02366.
OMAiVTTCKHG.
OrthoDBiEOG7RBZ7Z.
PhylomeDBiQ16394.
TreeFamiTF314231.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004263. Exostosin.
IPR027670. Exostosin-1.
IPR015338. HexNAc_Trfase_a.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11062. PTHR11062. 1 hit.
PTHR11062:SF45. PTHR11062:SF45. 1 hit.
PfamiPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q16394-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQAKKRYFIL LSAGSCLALL FYFGGLQFRA SRSHSRREEH SGRNGLHHPS
60 70 80 90 100
PDHFWPRFPD ALRPFVPWDQ LENEDSSVHI SPRQKRDANS SIYKGKKCRM
110 120 130 140 150
ESCFDFTLCK KNGFKVYVYP QQKGEKIAES YQNILAAIEG SRFYTSDPSQ
160 170 180 190 200
ACLFVLSLDT LDRDQLSPQY VHNLRSKVQS LHLWNNGRNH LIFNLYSGTW
210 220 230 240 250
PDYTEDVGFD IGQAMLAKAS ISTENFRPNF DVSIPLFSKD HPRTGGERGF
260 270 280 290 300
LKFNTIPPLR KYMLVFKGKR YLTGIGSDTR NALYHVHNGE DVVLLTTCKH
310 320 330 340 350
GKDWQKHKDS RCDRDNTEYE KYDYREMLHN ATFCLVPRGR RLGSFRFLEA
360 370 380 390 400
LQAACVPVML SNGWELPFSE VINWNQAAVI GDERLLLQIP STIRSIHQDK
410 420 430 440 450
ILALRQQTQF LWEAYFSSVE KIVLTTLEII QDRIFKHISR NSLIWNKHPG
460 470 480 490 500
GLFVLPQYSS YLGDFPYYYA NLGLKPPSKF TAVIHAVTPL VSQSQPVLKL
510 520 530 540 550
LVAAAKSQYC AQIIVLWNCD KPLPAKHRWP ATAVPVVVIE GESKVMSSRF
560 570 580 590 600
LPYDNIITDA VLSLDEDTVL STTEVDFAFT VWQSFPERIV GYPARSHFWD
610 620 630 640 650
NSKERWGYTS KWTNDYSMVL TGAAIYHKYY HYLYSHYLPA SLKNMVDQLA
660 670 680 690 700
NCEDILMNFL VSAVTKLPPI KVTQKKQYKE TMMGQTSRAS RWADPDHFAQ
710 720 730 740
RQSCMNTFAS WFGYMPLIHS QMRLDPVLFK DQVSILRKKY RDIERL
Length:746
Mass (Da):86,255
Last modified:March 27, 2002 - v2
Checksum:i842CD7E6C1312C1A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 612DA → EP(PubMed:7550340)Curated
Sequence conflicti60 – 612DA → EP1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271Q → K in EXT1; no loss of activity.
VAR_012815
Natural varianti164 – 1641D → H in EXT1; loss of activity. 1 Publication
VAR_012816
Natural varianti215 – 2228MLAKASIS → I in isolated osteochondroma; somatic mutation. 1 Publication
VAR_012818
Natural varianti215 – 2217Missing in EXT1.
VAR_012817
Natural varianti235 – 2395Missing in multiple osteochondromas. 1 Publication
VAR_012819
Natural varianti280 – 2801R → G in EXT1; loss of activity. 3 Publications
VAR_002370
Natural varianti280 – 2801R → S in EXT1; loss of activity. 1 Publication
VAR_002371
Natural varianti316 – 3161N → S in chondrosarcoma; no loss of activity. 1 Publication
VAR_012820
Natural varianti339 – 3391G → D in EXT1; loss of activity. 1 Publication
VAR_002372
Natural varianti340 – 3401R → C in EXT1; loss of activity; still able to form an oligomeric complex. 1 Publication
VAR_002373
Natural varianti340 – 3401R → H in EXT1; loss of activity. 2 Publications
VAR_002374
Natural varianti340 – 3401R → L in EXT1; loss of activity. 1 Publication
VAR_002375
Natural varianti340 – 3401R → S in EXT1; loss of activity. 1 Publication
VAR_002376
Natural varianti486 – 4861A → V in EXT1; no loss of activity. 1 Publication
Corresponds to variant rs188859975 [ dbSNP | Ensembl ].
VAR_012821
Natural varianti496 – 4961P → L in EXT1; no loss of activity. 1 Publication
VAR_012822
Natural varianti627 – 6271Missing in EXT1; loss of activity. 1 Publication
VAR_002377

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S79639 mRNA. Translation: AAB62283.1.
AK313129 mRNA. Translation: BAG35949.1.
CH471060 Genomic DNA. Translation: EAW91972.1.
BC001174 mRNA. Translation: AAH01174.1.
U70539 Genomic DNA. Translation: AAC51154.1.
CCDSiCCDS6324.1.
RefSeqiNP_000118.2. NM_000127.2.
UniGeneiHs.492618.

Genome annotation databases

EnsembliENST00000378204; ENSP00000367446; ENSG00000182197.
GeneIDi2131.
KEGGihsa:2131.
UCSCiuc003yok.1. human.

Polymorphism databases

DMDMi20141422.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S79639 mRNA. Translation: AAB62283.1 .
AK313129 mRNA. Translation: BAG35949.1 .
CH471060 Genomic DNA. Translation: EAW91972.1 .
BC001174 mRNA. Translation: AAH01174.1 .
U70539 Genomic DNA. Translation: AAC51154.1 .
CCDSi CCDS6324.1.
RefSeqi NP_000118.2. NM_000127.2.
UniGenei Hs.492618.

3D structure databases

ProteinModelPortali Q16394.
SMRi Q16394. Positions 512-724.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108432. 11 interactions.
IntActi Q16394. 1 interaction.
MINTi MINT-120274.
STRINGi 9606.ENSP00000367446.

Protein family/group databases

CAZyi GT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

PTM databases

PhosphoSitei Q16394.

Polymorphism databases

DMDMi 20141422.

Proteomic databases

MaxQBi Q16394.
PaxDbi Q16394.
PRIDEi Q16394.

Protocols and materials databases

DNASUi 2131.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378204 ; ENSP00000367446 ; ENSG00000182197 .
GeneIDi 2131.
KEGGi hsa:2131.
UCSCi uc003yok.1. human.

Organism-specific databases

CTDi 2131.
GeneCardsi GC08M118880.
GeneReviewsi EXT1.
HGNCi HGNC:3512. EXT1.
HPAi HPA044394.
MIMi 133700. phenotype.
150230. phenotype.
215300. phenotype.
608177. gene.
neXtProti NX_Q16394.
Orphaneti 55880. Chondrosarcoma.
502. Langer-Giedion syndrome.
321. Multiple osteochondromas.
PharmGKBi PA27924.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG272619.
GeneTreei ENSGT00550000074496.
HOGENOMi HOG000266990.
HOVERGENi HBG003459.
InParanoidi Q16394.
KOi K02366.
OMAi VTTCKHG.
OrthoDBi EOG7RBZ7Z.
PhylomeDBi Q16394.
TreeFami TF314231.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci MetaCyc:HS00012-MONOMER.
Reactomei REACT_121248. HS-GAG biosynthesis.

Miscellaneous databases

ChiTaRSi EXT1. human.
GeneWikii EXT1.
GenomeRNAii 2131.
NextBioi 8611.
PROi Q16394.
SOURCEi Search...

Gene expression databases

Bgeei Q16394.
CleanExi HS_EXT1.
ExpressionAtlasi Q16394. baseline and differential.
Genevestigatori Q16394.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR004263. Exostosin.
IPR027670. Exostosin-1.
IPR015338. HexNAc_Trfase_a.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR11062. PTHR11062. 1 hit.
PTHR11062:SF45. PTHR11062:SF45. 1 hit.
Pfami PF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the putative tumour suppressor gene for hereditary multiple exostoses (EXT1)."
    Ahn J., Luedecke H.-J., Lindow S., Horton W.A., Lee B., Wagner M.J., Horsthemke B., Wells D.E.
    Nat. Genet. 11:137-143(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "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].
    Tissue: Tongue.
  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: Brain.
  5. "Genomic organization and promoter structure of the human EXT1 gene."
    Luedecke H.-J., Ahn J., Lin X., Hill A., Wagner M.J., Schomburg L., Horsthemke B., Wells D.E.
    Genomics 40:351-354(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-320.
    Tissue: Lung.
  6. "Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus."
    Kobayashi S., Morimoto K., Shimizu T., Takahashi M., Kurosawa H., Shirasawa T.
    Biochem. Biophys. Res. Commun. 268:860-867(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  7. "The link between heparan sulfate and hereditary bone disease: finding a function for the EXT family of putative tumor suppressor proteins."
    Duncan G., McCormick C., Tufaro F.
    J. Clin. Invest. 108:511-516(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes."
    Wuyts W., Van Hul W.
    Hum. Mutat. 15:220-227(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  9. "Spectrum of EXT1 mutations in hereditary multiple exostoses."
    Raskind W.H., Matsushita M., Conrad E.U. III, Wells D.E., Sandell L.J., Wagner M.J., Houck J.
    Am. J. Hum. Genet. 59:A280-A280(1996)
    Cited for: VARIANTS EXT1 GLY-280 AND HIS-340.
  10. "Hereditary multiple exostoses (EXT): mutational studies of familial EXT1 cases and EXT-associated malignancies."
    Hecht J.T., Hogue D.A., Wang Y., Blanton S.H., Wagner M.J., Strong L.C., Raskind W.H., Hansen M.F., Wells D.E.
    Am. J. Hum. Genet. 60:80-86(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EXT1 LEU-340.
  11. "Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses."
    Philippe C., Porter D.E., Emerton M.E., Wells D.E., Simpson A.H.R.W., Monaco A.P.
    Am. J. Hum. Genet. 61:520-528(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EXT1 ASP-339 AND CYS-340.
  12. Cited for: VARIANTS EXT1 GLY-280 AND SER-340.
  13. "Evaluation of locus heterogeneity and EXT1 mutations in 34 families with hereditary multiple exostoses."
    Raskind W.H., Conrad E.U. III, Matsushita M., Wijsman E.M., Wells D.E., Chapman N., Sandell L.J., Wagner M.J., Houck J.
    Hum. Mutat. 11:231-239(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EXT1 GLY-280; SER-280; HIS-340 AND HIS-627 DEL.
  14. "EXT-mutation analysis and loss of heterozygosity in sporadic and hereditary osteochondromas and secondary chondrosarcomas."
    Bovee J.V.M.G., Cleton-Jansen A.-M., Wuyts W., Caethoven G., Taminiau A.H.M., Bakker E., van Hul W., Cornelisse C.J., Hogendoorn P.C.W.
    Am. J. Hum. Genet. 65:689-698(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EXT1 HIS-164; 235-PRO--LYS-239 DEL AND SER-316.
  15. "Mutation analysis of hereditary multiple exostoses in the Chinese."
    Xu L., Xia J., Jiang H., Zhou J., Li H., Wang D., Pan Q., Long Z., Fan C., Deng H.-X.
    Hum. Genet. 105:45-50(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EXT1 VAL-486 AND LEU-496.
  16. "Diminished levels of the putative tumor suppressor proteins EXT1 and EXT2 in exostosis chondrocytes."
    Bernard M.A., Hall C.E., Hogue D.A., Cole W.G., Scott A., Snuggs M.B., Clines G.A., Luedecke H.-J., Lovett M., Van Winkle W.B., Hecht J.T.
    Cell Motil. Cytoskeleton 48:149-162(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EXT1 215-MET--SER-221 DEL, VARIANT OSTEOCHONDROMA 215-MET--SER-222 DELINS ILE.
  17. "Etiological point mutations in the hereditary multiple exostoses gene EXT1: a functional analysis of heparan sulfate polymerase activity."
    Cheung P.K., McCormick C., Crawford B.E., Esko J.D., Tufaro F., Duncan G.
    Am. J. Hum. Genet. 69:55-66(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS, MUTAGENESIS OF GLN-27; ASP-164; ASN-316; ALA-486 AND PRO-496.

Entry informationi

Entry nameiEXT1_HUMAN
AccessioniPrimary (citable) accession number: Q16394
Secondary accession number(s): B2R7V2, Q9BVI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 27, 2002
Last modified: October 29, 2014
This is version 151 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 8
    Human chromosome 8: 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

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