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Protein

Deleted in malignant brain tumors 1 protein

Gene

DMBT1

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

Functioni

May be considered as a candidate tumor suppressor gene for brain, lung, esophageal, gastric, and colorectal cancers. May play roles in mucosal defense system, cellular immune defense and epithelial differentiation. May play a role as an opsonin receptor for SFTPD and SPAR in macrophage tissues throughout the body, including epithelial cells lining the gastrointestinal tract. May play a role in liver regeneration. May be an important factor in fate decision and differentiation of transit-amplifying ductular (oval) cells within the hepatic lineage. Required for terminal differentiation of columnar epithelial cells during early embryogenesis. May function as a binding protein in saliva for the regulation of taste sensation. Binds to HIV-1 envelope protein and has been shown to both inhibit and facilitate viral transmission. Displays a broad calcium-dependent binding spectrum against both Gram-positive and Gram-negative bacteria, suggesting a role in defense against bacterial pathogens. Binds to a range of poly-sulfated and poly-phosphorylated ligands which may explain its broad bacterial-binding specificity. Inhibits cytoinvasion of S.enterica. Associates with the actin cytoskeleton and is involved in its remodeling during regulated exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner and may act as a Golgi cargo receptor in the regulated secretory pathway of the pancreatic acinar cell.8 Publications

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • scavenger receptor activity Source: UniProtKB
  • signaling pattern recognition receptor activity Source: UniProtKB
  • zymogen binding Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • defense response to virus Source: UniProtKB-KW
  • epithelial cell differentiation Source: UniProtKB
  • induction of bacterial agglutination Source: UniProtKB
  • innate immune response Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • pattern recognition receptor signaling pathway Source: GOC
  • protein transport Source: UniProtKB-KW
  • receptor-mediated endocytosis Source: GOC
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Antiviral defense, Differentiation, Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-5683826. Surfactant metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Deleted in malignant brain tumors 1 protein
Alternative name(s):
Glycoprotein 340
Short name:
Gp-340
Hensin
Salivary agglutinin
Short name:
SAG
Surfactant pulmonary-associated D-binding protein
Gene namesi
Name:DMBT1
Synonyms:GP340
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:2926. DMBT1.

Subcellular locationi

  • Secreted By similarity

  • Note: Some isoforms may be membrane-bound. Localized to the lumenal aspect of crypt cells in the small intestine. In the colon, seen in the lumenal aspect of surface epithelial cells. Formed in the ducts of von Ebner gland, and released into the fluid bathing the taste buds contained in the taste papillae (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
  • phagocytic vesicle membrane Source: UniProtKB
  • zymogen granule membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Glioma (GLM)
The gene represented in this entry is involved in disease pathogenesis. Homozygous deletions may be the predominant mechanism of DMBT1 inactivation playing a role in carcinogenesis. DMBT1 is deleted in medulloblastoma and glioblastoma cell lines; point mutations have also been reported in patients with glioma. A loss or reduction of DMBT1 expression has been seen in esophageal, gastric, lung and colorectal carcinomas as well.
Disease descriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
See also OMIM:137800

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

Organism-specific databases

MIMi137800. phenotype.
PharmGKBiPA27376.

Polymorphism and mutation databases

BioMutaiDMBT1.
DMDMi85687556.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 24132394Deleted in malignant brain tumors 1 proteinPRO_0000045387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi127 ↔ 191By similarity
Disulfide bondi140 ↔ 201By similarity
Disulfide bondi171 ↔ 181By similarity
Disulfide bondi259 ↔ 323By similarity
Disulfide bondi272 ↔ 333By similarity
Disulfide bondi303 ↔ 313By similarity
Disulfide bondi388 ↔ 452By similarity
Disulfide bondi401 ↔ 462By similarity
Disulfide bondi432 ↔ 442By similarity
Disulfide bondi519 ↔ 583By similarity
Disulfide bondi532 ↔ 593By similarity
Disulfide bondi563 ↔ 573By similarity
Glycosylationi566 – 5661N-linked (GlcNAc...)Sequence analysis
Disulfide bondi627 ↔ 691By similarity
Disulfide bondi640 ↔ 701By similarity
Disulfide bondi671 ↔ 681By similarity
Glycosylationi737 – 7371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi758 ↔ 822By similarity
Disulfide bondi771 ↔ 832By similarity
Disulfide bondi802 ↔ 812By similarity
Disulfide bondi887 ↔ 951By similarity
Disulfide bondi900 ↔ 961By similarity
Disulfide bondi931 ↔ 941By similarity
Disulfide bondi1018 ↔ 1082By similarity
Disulfide bondi1031 ↔ 1092By similarity
Disulfide bondi1062 ↔ 1072By similarity
Disulfide bondi1147 ↔ 1211By similarity
Disulfide bondi1160 ↔ 1221By similarity
Disulfide bondi1191 ↔ 1201By similarity
Disulfide bondi1276 ↔ 1340By similarity
Disulfide bondi1289 ↔ 1350By similarity
Disulfide bondi1320 ↔ 1330By similarity
Disulfide bondi1405 ↔ 1469By similarity
Disulfide bondi1418 ↔ 1479By similarity
Disulfide bondi1449 ↔ 1459By similarity
Disulfide bondi1534 ↔ 1598By similarity
Disulfide bondi1547 ↔ 1608By similarity
Disulfide bondi1578 ↔ 1588By similarity
Disulfide bondi1665 ↔ 1729By similarity
Disulfide bondi1678 ↔ 1739By similarity
Disulfide bondi1709 ↔ 1719By similarity
Glycosylationi1712 – 17121N-linked (GlcNAc...)1 Publication
Glycosylationi1745 – 17451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1766 ↔ 1792By similarity
Glycosylationi1818 – 18181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1819 ↔ 1841By similarity
Glycosylationi1832 – 18321N-linked (GlcNAc...)Sequence analysis
Glycosylationi1842 – 18421N-linked (GlcNAc...)Sequence analysis
Glycosylationi1889 – 18891N-linked (GlcNAc...)1 Publication
Disulfide bondi1911 ↔ 1975By similarity
Disulfide bondi1924 ↔ 1985By similarity
Disulfide bondi1955 ↔ 1965By similarity
Glycosylationi1998 – 19981N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2008 ↔ 2034By similarity
Disulfide bondi2059 ↔ 2081By similarity
Glycosylationi2120 – 21201N-linked (GlcNAc...)Sequence analysis
Glycosylationi2188 – 21881N-linked (GlcNAc...)1 Publication
Glycosylationi2233 – 22331N-linked (GlcNAc...)Sequence analysis
Glycosylationi2240 – 22401N-linked (GlcNAc...)Sequence analysis
Glycosylationi2256 – 22561N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2302 ↔ 2360By similarity

Post-translational modificationi

Highly N- and O-glycosylated. The O-glycans are heavily sulfated (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9UGM3.
PaxDbiQ9UGM3.
PRIDEiQ9UGM3.

PTM databases

iPTMnetiQ9UGM3.
PhosphoSiteiQ9UGM3.

Expressioni

Tissue specificityi

Highly expressed in alveolar and macrophage tissues. In some macrophages, expression is seen on the membrane, and in other macrophages, strongly expressed in the phagosome/phagolysosome compartments. Expressed in lung, trachea, salivary gland, small intestine and stomach. In pancreas, expressed in certain cells of the islets of Langerhans. In digestive tract, confined to tissues with large epithelial surfaces. In intestinal tissue, moderately expressed in epithelial cells of the midcrypts and the crypt base. Expression is significantly elevated in intestinal tissue from patients with inflammatory bowel disease (IBD), particularly in surface epithelial and Paneth cells, but not in IBD patients with mutant NOD2. Present in crypt bases of the duodenum, in crypt tops of the colon, and in collecting ducts of the cortical kidney. Expressed in stratified squamous epithelium of vagina and in outer luminar surface and basilar region of columnar epithelial cells in cervix (at protein level). Isoform 1 is secreted to the lumen of the respiratory tract.7 Publications

Developmental stagei

Expressed in fetal lung, intestine and skin. Secreted to the extracellular matrix (ECM) in certain fetal epithelia.2 Publications

Inductioni

Up-regulated in intestinal epithelial cells in response to proinflammatory stimuli including TNF and bacterial lipopolysaccharides (LPS).1 Publication

Gene expression databases

BgeeiQ9UGM3.
GenevisibleiQ9UGM3. HS.

Organism-specific databases

HPAiHPA040778.

Interactioni

Subunit structurei

Interacts with LGALS3 (By similarity). Binds SFTPD and SPAR in a calcium-dependent manner. Binds to HIV-1 glycoprotein 120.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SFTPA1Q8IWL22EBI-1044970,EBI-11316418

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • zymogen binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108095. 12 interactions.
DIPiDIP-50763N.
IntActiQ9UGM3. 6 interactions.
STRINGi9606.ENSP00000357905.

Structurei

3D structure databases

ProteinModelPortaliQ9UGM3.
SMRiQ9UGM3. Positions 102-202, 234-334, 363-463, 494-594, 602-702, 733-833, 862-962, 993-1093, 1122-1222, 1251-1351, 1380-1480, 1509-1609, 1640-1740, 1763-2151, 2252-2365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini102 – 202101SRCR 1PROSITE-ProRule annotationAdd
BLAST
Domaini234 – 334101SRCR 2PROSITE-ProRule annotationAdd
BLAST
Domaini363 – 463101SRCR 3PROSITE-ProRule annotationAdd
BLAST
Domaini494 – 594101SRCR 4PROSITE-ProRule annotationAdd
BLAST
Domaini602 – 702101SRCR 5PROSITE-ProRule annotationAdd
BLAST
Domaini733 – 833101SRCR 6PROSITE-ProRule annotationAdd
BLAST
Domaini862 – 962101SRCR 7PROSITE-ProRule annotationAdd
BLAST
Domaini993 – 1093101SRCR 8PROSITE-ProRule annotationAdd
BLAST
Domaini1122 – 1222101SRCR 9PROSITE-ProRule annotationAdd
BLAST
Domaini1251 – 1351101SRCR 10PROSITE-ProRule annotationAdd
BLAST
Domaini1380 – 1480101SRCR 11PROSITE-ProRule annotationAdd
BLAST
Domaini1509 – 1609101SRCR 12PROSITE-ProRule annotationAdd
BLAST
Domaini1640 – 1740101SRCR 13PROSITE-ProRule annotationAdd
BLAST
Domaini1766 – 1877112CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini1883 – 1986104SRCR 14PROSITE-ProRule annotationAdd
BLAST
Domaini2008 – 2117110CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini2126 – 2381256ZPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1755 – 17595Poly-Thr

Domaini

The SRCR domains mediate binding to bacteria. The minimal bacterial-binding site is an 11-residue repeat of GRVEVLYRGSW where VEVL and W are critical residues.

Sequence similaritiesi

Belongs to the DMBT1 family.Curated
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 14 SRCR domains.PROSITE-ProRule annotation
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IHBC. Eukaryota.
ENOG410XQVR. LUCA.
GeneTreeiENSGT00840000129699.
HOVERGENiHBG060122.
InParanoidiQ9UGM3.
KOiK13912.
OMAiPHNGWLT.
OrthoDBiEOG7RNK07.
PhylomeDBiQ9UGM3.
TreeFamiTF329295.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
3.10.250.10. 14 hits.
InterProiIPR000859. CUB_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00530. SRCR. 14 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00258. SPERACTRCPTR.
SMARTiSM00042. CUB. 2 hits.
SM00202. SR. 14 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF56487. SSF56487. 14 hits.
PROSITEiPS01180. CUB. 2 hits.
PS00420. SRCR_1. 13 hits.
PS50287. SRCR_2. 14 hits.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Note: More isoforms may exist.

Isoform 1 (identifier: Q9UGM3-1) [UniParc]FASTAAdd to basket

Also known as: DMBT1/8kb.2

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
MGISTVILEM CLLWGQVLST GGWIPRTTDY ASLIPSEVPL DPTVAEGSPF
60 70 80 90 100
PSESTLESTV AEGSPISLES TLESTVAEGS LIPSESTLES TVAEGSDSGL
110 120 130 140 150
ALRLVNGDGR CQGRVEILYR GSWGTVCDDS WDTNDANVVC RQLGCGWAMS
160 170 180 190 200
APGNAWFGQG SGPIALDDVR CSGHESYLWS CPHNGWLSHN CGHGEDAGVI
210 220 230 240 250
CSAAQPQSTL RPESWPVRIS PPVPTEGSES SLALRLVNGG DRCRGRVEVL
260 270 280 290 300
YRGSWGTVCD DYWDTNDANV VCRQLGCGWA MSAPGNAQFG QGSGPIVLDD
310 320 330 340 350
VRCSGHESYL WSCPHNGWLT HNCGHSEDAG VICSAPQSRP TPSPDTWPTS
360 370 380 390 400
HASTAGPESS LALRLVNGGD RCQGRVEVLY RGSWGTVCDD SWDTSDANVV
410 420 430 440 450
CRQLGCGWAT SAPGNARFGQ GSGPIVLDDV RCSGYESYLW SCPHNGWLSH
460 470 480 490 500
NCQHSEDAGV ICSAAHSWST PSPDTLPTIT LPASTVGSES SLALRLVNGG
510 520 530 540 550
DRCQGRVEVL YRGSWGTVCD DSWDTNDANV VCRQLGCGWA MLAPGNARFG
560 570 580 590 600
QGSGPIVLDD VRCSGNESYL WSCPHNGWLS HNCGHSEDAG VICSGPESSL
610 620 630 640 650
ALRLVNGGDR CQGRVEVLYR GSWGTVCDDS WDTNDANVVC RQLGCGWATS
660 670 680 690 700
APGNARFGQG SGPIVLDDVR CSGHESYLWS CPNNGWLSHN CGHHEDAGVI
710 720 730 740 750
CSAAQSRSTP RPDTLSTITL PPSTVGSESS LTLRLVNGSD RCQGRVEVLY
760 770 780 790 800
RGSWGTVCDD SWDTNDANVV CRQLGCGWAT SAPGNARFGQ GSGPIVLDDV
810 820 830 840 850
RCSGHESYLW SCPHNGWLSH NCGHHEDAGV ICSVSQSRPT PSPDTWPTSH
860 870 880 890 900
ASTAGPESSL ALRLVNGGDR CQGRVEVLYR GSWGTVCDDS WDTSDANVVC
910 920 930 940 950
RQLGCGWATS APGNARFGQG SGPIVLDDVR CSGYESYLWS CPHNGWLSHN
960 970 980 990 1000
CQHSEDAGVI CSAAHSWSTP SPDTLPTITL PASTVGSESS LALRLVNGGD
1010 1020 1030 1040 1050
RCQGRVEVLY QGSWGTVCDD SWDTNDANVV CRQLGCGWAM SAPGNARFGQ
1060 1070 1080 1090 1100
GSGPIVLDDV RCSGHESYLW SCPHNGWLSH NCGHSEDAGV ICSASQSRPT
1110 1120 1130 1140 1150
PSPDTWPTSH ASTAGSESSL ALRLVNGGDR CQGRVEVLYR GSWGTVCDDY
1160 1170 1180 1190 1200
WDTNDANVVC RQLGCGWAMS APGNARFGQG SGPIVLDDVR CSGHESYLWS
1210 1220 1230 1240 1250
CPHNGWLSHN CGHHEDAGVI CSASQSQPTP SPDTWPTSHA STAGSESSLA
1260 1270 1280 1290 1300
LRLVNGGDRC QGRVEVLYRG SWGTVCDDYW DTNDANVVCR QLGCGWATSA
1310 1320 1330 1340 1350
PGNARFGQGS GPIVLDDVRC SGHESYLWSC PHNGWLSHNC GHHEDAGVIC
1360 1370 1380 1390 1400
SASQSQPTPS PDTWPTSHAS TAGSESSLAL RLVNGGDRCQ GRVEVLYRGS
1410 1420 1430 1440 1450
WGTVCDDYWD TNDANVVCRQ LGCGWATSAP GNARFGQGSG PIVLDDVRCS
1460 1470 1480 1490 1500
GHESYLWSCP HNGWLSHNCG HHEDAGVICS ASQSQPTPSP DTWPTSRAST
1510 1520 1530 1540 1550
AGSESTLALR LVNGGDRCRG RVEVLYQGSW GTVCDDYWDT NDANVVCRQL
1560 1570 1580 1590 1600
GCGWAMSAPG NAQFGQGSGP IVLDDVRCSG HESYLWSCPH NGWLSHNCGH
1610 1620 1630 1640 1650
HEDAGVICSA AQSQSTPRPD TWLTTNLPAL TVGSESSLAL RLVNGGDRCR
1660 1670 1680 1690 1700
GRVEVLYRGS WGTVCDDSWD TNDANVVCRQ LGCGWAMSAP GNARFGQGSG
1710 1720 1730 1740 1750
PIVLDDVRCS GNESYLWSCP HKGWLTHNCG HHEDAGVICS ATQINSTTTD
1760 1770 1780 1790 1800
WWHPTTTTTA RPSSNCGGFL FYASGTFSSP SYPAYYPNNA KCVWEIEVNS
1810 1820 1830 1840 1850
GYRINLGFSN LKLEAHHNCS FDYVEIFDGS LNSSLLLGKI CNDTRQIFTS
1860 1870 1880 1890 1900
SYNRMTIHFR SDISFQNTGF LAWYNSFPSD ATLRLVNLNS SYGLCAGRVE
1910 1920 1930 1940 1950
IYHGGTWGTV CDDSWTIQEA EVVCRQLGCG RAVSALGNAY FGSGSGPITL
1960 1970 1980 1990 2000
DDVECSGTES TLWQCRNRGW FSHNCNHRED AGVICSGNHL STPAPFLNIT
2010 2020 2030 2040 2050
RPNTDYSCGG FLSQPSGDFS SPFYPGNYPN NAKCVWDIEV QNNYRVTVIF
2060 2070 2080 2090 2100
RDVQLEGGCN YDYIEVFDGP YRSSPLIARV CDGARGSFTS SSNFMSIRFI
2110 2120 2130 2140 2150
SDHSITRRGF RAEYYSSPSN DSTNLLCLPN HMQASVSRSY LQSLGFSASD
2160 2170 2180 2190 2200
LVISTWNGYY ECRPQITPNL VIFTIPYSGC GTFKQADNDT IDYSNFLTAA
2210 2220 2230 2240 2250
VSGGIIKRRT DLRIHVSCRM LQNTWVDTMY IANDTIHVAN NTIQVEEVQY
2260 2270 2280 2290 2300
GNFDVNISFY TSSSFLYPVT SRPYYVDLNQ DLYVQAEILH SDAVLTLFVD
2310 2320 2330 2340 2350
TCVASPYSND FTSLTYDLIR SGCVRDDTYG PYSSPSLRIA RFRFRAFHFL
2360 2370 2380 2390 2400
NRFPSVYLRC KMVVCRAYDP SSRCYRGCVL RSKRDVGSYQ EKVDVVLGPI
2410
QLQTPPRREE EPR
Length:2,413
Mass (Da):260,735
Last modified:January 10, 2006 - v2
Checksum:i25363E6263234F15
GO
Isoform 2 (identifier: Q9UGM3-2) [UniParc]FASTAAdd to basket

Also known as: DMBT1/6kb.1

The sequence of this isoform differs from the canonical sequence as follows:
     337-835: Missing.
     1170-1298: Missing.

Show »
Length:1,785
Mass (Da):193,971
Checksum:iA01C68AF13C478BB
GO
Isoform 3 (identifier: Q9UGM3-3) [UniParc]FASTAAdd to basket

Also known as: DMBT1/8kb.1

The sequence of this isoform differs from the canonical sequence as follows:
     464-473: Missing.

Show »
Length:2,403
Mass (Da):259,713
Checksum:iC46A2BD09B2C874D
GO
Isoform 4 (identifier: Q9UGM3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     523-1408: Missing.

Note: No experimental confirmation available.
Show »
Length:1,527
Mass (Da):166,501
Checksum:iED984E0EF2736C69
GO
Isoform 6 (identifier: Q9UGM3-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1169-1169: M → MSAPGNARFG...CRQLGCGWAT

Show »
Length:2,542
Mass (Da):274,465
Checksum:iA6390E0D194E6A22
GO
Isoform 7 (identifier: Q9UGM3-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     464-473: Missing.
     1169-1169: M → MSAPGNARFG...CRQLGCGWAT

Show »
Length:2,532
Mass (Da):273,443
Checksum:i3E96E2D1F87EA45A
GO
Isoform 8 (identifier: Q9UGM3-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     472-478: SPDTLPT → RPGERPR
     479-971: Missing.
     1099-1356: Missing.

Show »
Length:1,662
Mass (Da):180,973
Checksum:iB9655F67233F6AE3
GO
Isoform 5 (identifier: Q9UGM3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1741-1761: ATQINSTTTDWWHPTTTTTAR → G

Note: No experimental confirmation available.
Show »
Length:2,393
Mass (Da):258,420
Checksum:iD2AA22898581A701
GO
Isoform 9 (identifier: Q9UGM3-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     201-332: Missing.
     344-1360: Missing.
     1608-1738: Missing.

Note: No experimental confirmation available.
Show »
Length:1,133
Mass (Da):124,452
Checksum:i59ED2884BD6C86A5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101M → V in CAC44122 (PubMed:11751412).Curated
Sequence conflicti13 – 131L → S in BAH14118 (PubMed:14702039).Curated
Sequence conflicti31 – 311A → T in AAI53300 (PubMed:15489334).Curated
Sequence conflicti42 – 421P → Q in AAD49696 (PubMed:10485905).Curated
Sequence conflicti42 – 421P → Q in AAI53300 (PubMed:15489334).Curated
Sequence conflicti74 – 741S → T in CAB56155 (PubMed:10485905).Curated
Sequence conflicti125 – 1251T → A in CAB56155 (PubMed:10485905).Curated
Sequence conflicti188 – 1881S → T in BAH14118 (PubMed:14702039).Curated
Sequence conflicti194 – 1941G → S in BAH14118 (PubMed:14702039).Curated
Sequence conflicti468 – 4681W → R in CAC44122 (PubMed:11751412).Curated
Sequence conflicti594 – 5941S → SDTLPTTTLPASTV in CAB63941 (PubMed:10597221).Curated
Sequence conflicti603 – 6031R → G in CAB63942 (PubMed:10597221).Curated
Sequence conflicti711 – 7111R → G in CAC44122 (PubMed:11751412).Curated
Sequence conflicti902 – 9021Q → R in CAB63942 (PubMed:10597221).Curated
Sequence conflicti1034 – 10341L → P in CAA04019 (PubMed:9288095).Curated
Sequence conflicti1034 – 10341L → P in AAD49696 (PubMed:10485905).Curated
Sequence conflicti1060 – 10601V → A in CAB56155 (PubMed:10485905).Curated
Sequence conflicti1069 – 10691L → P in CAA04019 (PubMed:9288095).Curated
Sequence conflicti1069 – 10691L → P in AAD49696 (PubMed:10485905).Curated
Sequence conflicti1159 – 11591V → A in CAB56155 (PubMed:10485905).Curated
Sequence conflicti1204 – 12041N → D in CAB63942 (PubMed:10597221).Curated
Sequence conflicti1271 – 12711S → P in CAB63942 (PubMed:10597221).Curated
Sequence conflicti1295 – 12951G → S in CAC44122 (PubMed:11751412).Curated
Sequence conflicti1336 – 13361L → F in CAC44122 (PubMed:11751412).Curated
Sequence conflicti1411 – 14111T → I in AAI53300 (PubMed:15489334).Curated
Sequence conflicti1432 – 14321N → S in CAB63942 (PubMed:10597221).Curated
Sequence conflicti1443 – 14431V → A in CAB63942 (PubMed:10597221).Curated
Sequence conflicti1448 – 14481R → H in AAI53300 (PubMed:15489334).Curated
Sequence conflicti1482 – 14821S → F in CAB56155 (PubMed:10485905).Curated
Sequence conflicti1583 – 15831S → P in CAB56155 (PubMed:10485905).Curated
Sequence conflicti1591 – 15911N → K in BAH14118 (PubMed:14702039).Curated
Sequence conflicti1595 – 15951S → T in BAH14118 (PubMed:14702039).Curated
Sequence conflicti1705 – 17051D → G in CAB56155 (PubMed:10485905).Curated
Sequence conflicti1845 – 18451R → G (PubMed:17974005).Curated
Sequence conflicti1909 – 19091T → A in CAB56155 (PubMed:10485905).Curated
Sequence conflicti2004 – 20052TD → N in CAB56155 (PubMed:10485905).Curated
Sequence conflicti2004 – 20052TD → N in CAI14494 (PubMed:15164054).Curated
Sequence conflicti2196 – 21961F → L in CAB56155 (PubMed:10485905).Curated
Sequence conflicti2380 – 23801L → S in AAI53300 (PubMed:15489334).Curated
Sequence conflicti2405 – 24051P → A in CAC44122 (PubMed:11751412).Curated

Polymorphismi

The number of SRCR and SRCR-interspersed domains is polymorphic in a variety of tumors and may represent the major site of alterations in cancer.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421P → T.6 Publications
Corresponds to variant rs11523871 [ dbSNP | Ensembl ].
VAR_024788
Natural varianti52 – 521S → W.2 Publications
Corresponds to variant rs75209396 [ dbSNP | Ensembl ].
VAR_024789
Natural varianti54 – 541S → L.6 Publications
Corresponds to variant rs3013236 [ dbSNP | Ensembl ].
VAR_024790
Natural varianti60 – 601V → A.4 Publications
VAR_024791
Natural varianti65 – 651P → L.1 Publication
Corresponds to variant rs185045706 [ dbSNP | Ensembl ].
VAR_024792
Natural varianti162 – 1621G → E in a glioma cell line. 1 Publication
VAR_057981
Natural varianti322 – 3221N → D.1 Publication
Corresponds to variant rs1969620 [ dbSNP | Ensembl ].
VAR_044417
Natural varianti337 – 3371Q → L.2 Publications
VAR_024793
Natural varianti357 – 3571P → S.2 Publications
VAR_024794
Natural varianti364 – 3641R → G.1 Publication
VAR_024795
Natural varianti420 – 4201Q → H in a glioma sample; glioblastoma multiforme; somatic mutation.
VAR_024796
Natural varianti546 – 5461N → S in a glioma cell line. 1 Publication
VAR_057982
Natural varianti607 – 6071G → V in a glioma sample; pilocytic astrocytoma.
VAR_024797
Natural varianti649 – 6491T → M.2 Publications
Corresponds to variant rs189478437 [ dbSNP | Ensembl ].
VAR_024798
Natural varianti656 – 6561R → W.
VAR_024799
Natural varianti670 – 6701R → C.
Corresponds to variant rs2277237 [ dbSNP | Ensembl ].
VAR_052994
Natural varianti719 – 7191T → M.
Corresponds to variant rs2277238 [ dbSNP | Ensembl ].
VAR_052995
Natural varianti780 – 7801T → M.2 Publications
VAR_024800
Natural varianti856 – 8561P → S.4 Publications
Corresponds to variant rs2277240 [ dbSNP | Ensembl ].
VAR_024801
Natural varianti1084 – 10841H → Y.1 Publication
Corresponds to variant rs2277244 [ dbSNP | Ensembl ].
VAR_024802
Natural varianti1095 – 10951S → P.1 Publication
VAR_057983
Natural varianti1102 – 11021S → T.1 Publication
VAR_057984
Natural varianti1169 – 11691M → T.1 Publication
Corresponds to variant rs3758437 [ dbSNP | Ensembl ].
VAR_024803
Natural varianti1176 – 11761R → W.1 Publication
VAR_024804
Natural varianti1434 – 14341R → W.1 Publication
VAR_057985
Natural varianti1545 – 15451V → M.1 Publication
Corresponds to variant rs189221852 [ dbSNP | Ensembl ].
VAR_024805
Natural varianti1732 – 17321H → S Requires 2 nucleotide substitutions. 2 Publications
VAR_024806
Natural varianti1860 – 18601R → L.
Corresponds to variant rs7099177 [ dbSNP | Ensembl ].
VAR_044418
Natural varianti1961 – 19611T → P.1 Publication
VAR_024807
Natural varianti2255 – 22551V → M.1 Publication
Corresponds to variant rs183135544 [ dbSNP | Ensembl ].
VAR_057986

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei201 – 332132Missing in isoform 9. 1 PublicationVSP_053979Add
BLAST
Alternative sequencei337 – 835499Missing in isoform 2. 1 PublicationVSP_016846Add
BLAST
Alternative sequencei344 – 13601017Missing in isoform 9. 1 PublicationVSP_053980Add
BLAST
Alternative sequencei464 – 47310Missing in isoform 3 and isoform 7. 1 PublicationVSP_016847
Alternative sequencei472 – 4787SPDTLPT → RPGERPR in isoform 8. 1 PublicationVSP_034653
Alternative sequencei479 – 971493Missing in isoform 8. 1 PublicationVSP_034654Add
BLAST
Alternative sequencei523 – 1408886Missing in isoform 4. 1 PublicationVSP_016848Add
BLAST
Alternative sequencei1099 – 1356258Missing in isoform 8. 1 PublicationVSP_034655Add
BLAST
Alternative sequencei1169 – 11691M → MSAPGNARFGQGSGPIVLDD VRCSGHESYLWSCPHNGWLS HNCGHHEDAGVICSASQSQP TPSPDTWPTSHASTAGSESS LALRLVNGGDRCQGRVEVLY RGSWGTVCDDYWDTNDANVV CRQLGCGWAT in isoform 6 and isoform 7. CuratedVSP_034656
Alternative sequencei1170 – 1298129Missing in isoform 2. 1 PublicationVSP_016849Add
BLAST
Alternative sequencei1608 – 1738131Missing in isoform 9. 1 PublicationVSP_053981Add
BLAST
Alternative sequencei1741 – 176121ATQIN…TTTAR → G in isoform 5. 1 PublicationVSP_016850Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000342 mRNA. Translation: CAA04019.1.
AF159456 mRNA. Translation: AAD49696.1.
AJ243212 mRNA. Translation: CAB56155.1.
AJ243211 Genomic DNA. Translation: CAB63941.1.
AJ243224 mRNA. Translation: CAB63942.1.
AB020851 Genomic DNA. Translation: BAA78577.1.
AJ297935 mRNA. Translation: CAC44122.1.
AK304149 mRNA. Translation: BAH14118.1.
AL603764 Genomic DNA. Translation: CAI14487.1.
AL603764 Genomic DNA. Translation: CAI14488.1.
AL603764 Genomic DNA. Translation: CAI14489.1.
AL603764 Genomic DNA. Translation: CAI14490.1.
AL603764 Genomic DNA. Translation: CAI14491.1.
AL603764 Genomic DNA. Translation: CAI14492.1.
AL603764 Genomic DNA. Translation: CAI14493.1.
AL603764 Genomic DNA. Translation: CAI14494.1.
AL603764 Genomic DNA. Translation: CAI14495.1.
AL603764 Genomic DNA. Translation: CAI14496.1.
BC153299 mRNA. Translation: AAI53300.1.
AB209691 mRNA. Translation: BAD92928.1.
BX640988 mRNA. Translation: CAE45995.1.
CCDSiCCDS44490.1. [Q9UGM3-1]
CCDS44491.1. [Q9UGM3-2]
CCDS44492.1. [Q9UGM3-3]
PIRiA59386.
RefSeqiNP_001307573.1. NM_001320644.1.
NP_004397.2. NM_004406.2. [Q9UGM3-2]
NP_015568.2. NM_007329.2. [Q9UGM3-1]
NP_060049.2. NM_017579.2. [Q9UGM3-3]
XP_011537690.1. XM_011539388.1. [Q9UGM3-6]
XP_011537693.1. XM_011539391.1. [Q9UGM3-7]
XP_011537707.1. XM_011539405.1. [Q9UGM3-1]
UniGeneiHs.279611.

Genome annotation databases

EnsembliENST00000330163; ENSP00000327747; ENSG00000187908. [Q9UGM3-2]
ENST00000338354; ENSP00000342210; ENSG00000187908. [Q9UGM3-1]
ENST00000344338; ENSP00000343175; ENSG00000187908. [Q9UGM3-3]
ENST00000359586; ENSP00000352593; ENSG00000187908. [Q9UGM3-9]
ENST00000368909; ENSP00000357905; ENSG00000187908. [Q9UGM3-1]
ENST00000368955; ENSP00000357951; ENSG00000187908. [Q9UGM3-3]
ENST00000368956; ENSP00000357952; ENSG00000187908. [Q9UGM3-2]
ENST00000619379; ENSP00000484603; ENSG00000187908. [Q9UGM3-1]
GeneIDi1755.
KEGGihsa:1755.
UCSCiuc001lgk.1. human. [Q9UGM3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000342 mRNA. Translation: CAA04019.1.
AF159456 mRNA. Translation: AAD49696.1.
AJ243212 mRNA. Translation: CAB56155.1.
AJ243211 Genomic DNA. Translation: CAB63941.1.
AJ243224 mRNA. Translation: CAB63942.1.
AB020851 Genomic DNA. Translation: BAA78577.1.
AJ297935 mRNA. Translation: CAC44122.1.
AK304149 mRNA. Translation: BAH14118.1.
AL603764 Genomic DNA. Translation: CAI14487.1.
AL603764 Genomic DNA. Translation: CAI14488.1.
AL603764 Genomic DNA. Translation: CAI14489.1.
AL603764 Genomic DNA. Translation: CAI14490.1.
AL603764 Genomic DNA. Translation: CAI14491.1.
AL603764 Genomic DNA. Translation: CAI14492.1.
AL603764 Genomic DNA. Translation: CAI14493.1.
AL603764 Genomic DNA. Translation: CAI14494.1.
AL603764 Genomic DNA. Translation: CAI14495.1.
AL603764 Genomic DNA. Translation: CAI14496.1.
BC153299 mRNA. Translation: AAI53300.1.
AB209691 mRNA. Translation: BAD92928.1.
BX640988 mRNA. Translation: CAE45995.1.
CCDSiCCDS44490.1. [Q9UGM3-1]
CCDS44491.1. [Q9UGM3-2]
CCDS44492.1. [Q9UGM3-3]
PIRiA59386.
RefSeqiNP_001307573.1. NM_001320644.1.
NP_004397.2. NM_004406.2. [Q9UGM3-2]
NP_015568.2. NM_007329.2. [Q9UGM3-1]
NP_060049.2. NM_017579.2. [Q9UGM3-3]
XP_011537690.1. XM_011539388.1. [Q9UGM3-6]
XP_011537693.1. XM_011539391.1. [Q9UGM3-7]
XP_011537707.1. XM_011539405.1. [Q9UGM3-1]
UniGeneiHs.279611.

3D structure databases

ProteinModelPortaliQ9UGM3.
SMRiQ9UGM3. Positions 102-202, 234-334, 363-463, 494-594, 602-702, 733-833, 862-962, 993-1093, 1122-1222, 1251-1351, 1380-1480, 1509-1609, 1640-1740, 1763-2151, 2252-2365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108095. 12 interactions.
DIPiDIP-50763N.
IntActiQ9UGM3. 6 interactions.
STRINGi9606.ENSP00000357905.

PTM databases

iPTMnetiQ9UGM3.
PhosphoSiteiQ9UGM3.

Polymorphism and mutation databases

BioMutaiDMBT1.
DMDMi85687556.

Proteomic databases

MaxQBiQ9UGM3.
PaxDbiQ9UGM3.
PRIDEiQ9UGM3.

Protocols and materials databases

DNASUi1755.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330163; ENSP00000327747; ENSG00000187908. [Q9UGM3-2]
ENST00000338354; ENSP00000342210; ENSG00000187908. [Q9UGM3-1]
ENST00000344338; ENSP00000343175; ENSG00000187908. [Q9UGM3-3]
ENST00000359586; ENSP00000352593; ENSG00000187908. [Q9UGM3-9]
ENST00000368909; ENSP00000357905; ENSG00000187908. [Q9UGM3-1]
ENST00000368955; ENSP00000357951; ENSG00000187908. [Q9UGM3-3]
ENST00000368956; ENSP00000357952; ENSG00000187908. [Q9UGM3-2]
ENST00000619379; ENSP00000484603; ENSG00000187908. [Q9UGM3-1]
GeneIDi1755.
KEGGihsa:1755.
UCSCiuc001lgk.1. human. [Q9UGM3-1]

Organism-specific databases

CTDi1755.
GeneCardsiDMBT1.
H-InvDBHIX0026114.
HGNCiHGNC:2926. DMBT1.
HPAiHPA040778.
MIMi137800. phenotype.
601969. gene.
neXtProtiNX_Q9UGM3.
PharmGKBiPA27376.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHBC. Eukaryota.
ENOG410XQVR. LUCA.
GeneTreeiENSGT00840000129699.
HOVERGENiHBG060122.
InParanoidiQ9UGM3.
KOiK13912.
OMAiPHNGWLT.
OrthoDBiEOG7RNK07.
PhylomeDBiQ9UGM3.
TreeFamiTF329295.

Enzyme and pathway databases

ReactomeiR-HSA-5683826. Surfactant metabolism.

Miscellaneous databases

ChiTaRSiDMBT1. human.
GeneWikiiDMBT1.
GenomeRNAii1755.
NextBioi35480601.
PROiQ9UGM3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UGM3.
GenevisibleiQ9UGM3. HS.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
3.10.250.10. 14 hits.
InterProiIPR000859. CUB_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00530. SRCR. 14 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00258. SPERACTRCPTR.
SMARTiSM00042. CUB. 2 hits.
SM00202. SR. 14 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF56487. SSF56487. 14 hits.
PROSITEiPS01180. CUB. 2 hits.
PS00420. SRCR_1. 13 hits.
PS50287. SRCR_2. 14 hits.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DMBT1, a new member of the SRCR superfamily on chromosome 10q25.3-q26.1 is deleted in malignant brain tumours."
    Mollenhauer J., Wiemann S., Scheurlen W., Korn B., Hayashi Y., Wilgenbus K.K., von Deimling A., Poustka A.
    Nat. Genet. 17:32-39(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION AS A TUMOR SUPPRESSOR, TISSUE SPECIFICITY, VARIANTS THR-42 AND ALA-60.
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN MUCOSAL AND CELLULAR IMMUNE DEFENSE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, VARIANTS THR-42; LEU-54; ALA-60; MET-649; MET-780 AND SER-856.
    Tissue: Trachea.
  3. "The genomic structure of the DMBT1 gene: evidence for a region with susceptibility to genomic instability."
    Mollenhauer J., Holmskov U., Wiemann S., Krebs I., Herbertz S., Madsen J., Kioschis P., Coy J.F., Poustka A.
    Oncogene 18:6233-6240(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, VARIANTS THR-42; LEU-54; ALA-60; LEU-337 AND SER-856.
    Tissue: Lung.
  4. "Expression of the DMBT1 gene is frequently suppressed in human lung cancer."
    Takeshita H., Sato M., Shiwaku H.O., Semba S., Sakurada A., Hoshi M., Hayashi Y., Tagawa Y., Ayabe H., Horii A.
    Jpn. J. Cancer Res. 90:903-908(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN LUNG CARCINOGENESIS, VARIANTS THR-42; LEU-54 AND SER-856.
  5. "Deleted in malignant brain tumors 1 is a versatile mucin-like molecule likely to play a differential role in digestive tract cancer."
    Mollenhauer J., Herbertz S., Helmke B., Kollender G., Krebs I., Madsen J., Holmskov U., Sorger K., Schmitt L., Wiemann S., Otto H.F., Grone H.-J., Poustka A.
    Cancer Res. 61:8880-8886(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN EPITHELIAL DIFFERENTIATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, INVOLVEMENT IN ESOPHAGEAL CARCINOMAS, VARIANT SER-856.
    Tissue: Small intestine.
  6. "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 9).
    Tissue: Trachea.
  7. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 8), VARIANT LEU-54.
  9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1480 (ISOFORM 4).
    Tissue: Brain.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1689-2413 (ISOFORM 5).
    Tissue: Small intestine.
  11. "Human basal tear peptidome characterization by CID, HCD, and ETD followed by in silico and in vitro analyses for antimicrobial peptide identification."
    Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., Suarez T., Elortza F.
    J. Proteome Res. 14:2649-2658(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2385-2413, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Tear.
  12. "Isolation and characterization of a new member of the scavenger receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule."
    Holmskov U., Lawson P., Teisner B., Tornoe I., Willis A.C., Morgan C., Koch C., Reid K.B.
    J. Biol. Chem. 272:13743-13749(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFTPD.
  13. "Glycoprotein-340 binds surfactant protein-A (SP-A) and stimulates alveolar macrophage migration in an SP-A-independent manner."
    Tino M.J., Wright J.R.
    Am. J. Respir. Cell Mol. Biol. 20:759-768(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPAR.
  14. "Lack of DMBT1 expression in oesophageal, gastric and colon cancers."
    Mori M., Shiraishi T., Tanaka S., Yamagata M., Mafune K., Tanaka Y., Ueo H., Barnard G.F., Sugimachi K.
    Br. J. Cancer 79:211-213(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ESOPHAGEAL; GASTRIC AND COLON CANCERS.
  15. "DMBT1 encodes a protein involved in the immune defense and in epithelial differentiation and is highly unstable in cancer."
    Mollenhauer J., Herbertz S., Holmskov U., Tolnay M., Krebs I., Merlo A., Schroder H.D., Maier D., Breitling F., Wiemann S., Groene H.-J., Poustka A.
    Cancer Res. 60:1704-1710(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  16. "Salivary agglutinin, which binds Streptococcus mutans and Helicobacter pylori, is the lung scavenger receptor cysteine-rich protein gp-340."
    Prakobphol A., Xu F., Hoang V.M., Larsson T., Bergstrom J., Johansson I., Fraengsmyr L., Holmskov U., Leffler H., Nilsson C., Boren T., Wright J.R., Stroemberg N., Fisher S.J.
    J. Biol. Chem. 275:39860-39866(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    Tissue: Saliva.
  17. Cited for: BACTERIAL-BINDING DOMAIN.
  18. "The N-terminal SRCR-SID domain of gp-340 interacts with HIV type 1 gp120 sequences and inhibits viral infection."
    Wu Z., Lee S., Abrams W., Weissman D., Malamud D.
    AIDS Res. Hum. Retroviruses 22:508-515(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIV-1 GP120, TISSUE SPECIFICITY.
  19. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
    Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
    J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1712; ASN-1889 AND ASN-2188.
    Tissue: Saliva.
  20. Cited for: TISSUE SPECIFICITY.
  21. "Regulation of DMBT1 via NOD2 and TLR4 in intestinal epithelial cells modulates bacterial recognition and invasion."
    Rosenstiel P., Sina C., End C., Renner M., Lyer S., Till A., Hellmig S., Nikolaus S., Foelsch U.R., Helmke B., Autschbach F., Schirmacher P., Kioschis P., Hafner M., Poustka A., Mollenhauer J., Schreiber S.
    J. Immunol. 178:8203-8211(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  22. "gp340 expressed on human genital epithelia binds HIV-1 envelope protein and facilitates viral transmission."
    Stoddard E., Cannon G., Ni H., Kariko K., Capodici J., Malamud D., Weissman D.
    J. Immunol. 179:3126-3132(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "A common binding motif for various bacteria of the bacteria-binding peptide SRCRP2 of DMBT1/gp-340/salivary agglutinin."
    Leito J.T.D., Ligtenberg A.J.M., Nazmi K., de Blieck-Hogervorst J.M.A., Veerman E.C.I., Nieuw Amerongen A.V.
    Biol. Chem. 389:1193-1200(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: BACTERIAL-BINDING DOMAIN.
  24. Cited for: FUNCTION.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "The SRCR/SID region of DMBT1 defines a complex multi-allele system representing the major basis for its variability in cancer."
    Mollenhauer J., Mueller H., Kollender G., Lyer S., Diedrichs L., Helmke B., Holmskov U., Ligtenberg T., Herbertz S., Krebs I., Madsen J., Bikker F., Schmitt L., Wiemann S., Scheurlen W., Otto H.F., von Deimling A., Poustka A.
    Genes Chromosomes Cancer 35:242-255(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-42; TRP-52; LEU-54; GLU-162; ASP-322; SER-357; SER-546; PRO-1095; THR-1102; TRP-1434; SER-1732 AND MET-2255.
  27. "Rare mutations of the DMBT1 gene in human astrocytic gliomas."
    Mueller W., Mollenhauer J., Stockhammer F., Poustka A., von Deimling A.
    Oncogene 21:5956-5959(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-42; TRP-52; LEU-54; ALA-60; LEU-65; LEU-337; SER-357; GLY-364; MET-649; MET-780; TYR-1084; THR-1169; TRP-1176; MET-1545; SER-1732 AND PRO-1961.

Entry informationi

Entry nameiDMBT1_HUMAN
AccessioniPrimary (citable) accession number: Q9UGM3
Secondary accession number(s): A6NDG4
, A6NDJ5, A8E4R5, B1ARE7, B1ARE8, B1ARE9, B1ARF0, B7Z8Y2, F8WEF7, Q59EX0, Q5JR26, Q6MZN4, Q96DU4, Q9UGM2, Q9UJ57, Q9UKJ4, Q9Y211, Q9Y4V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: May 11, 2016
This is version 143 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.