Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9UGM3 (DMBT1_HUMAN)

UniProt

Q9UGM3 - DMBT1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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
  • protein transport Source: UniProtKB-KW
  • 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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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.
PeptideAtlasiQ9UGM3.
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

BgeeiENSG00000187908.
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. 13 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.
OrthoDBiEOG091G0DF7.
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
Corresponds to variant rs200664624 [ dbSNP | Ensembl ].		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
Corresponds to variant rs200713568 [ dbSNP | Ensembl ].		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
Corresponds to variant rs199704744 [ dbSNP | Ensembl ].		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
Corresponds to variant rs200551848 [ dbSNP | Ensembl ].		VAR_057983
Natural varianti1102 – 11021S → T.1 Publication
Corresponds to variant rs566926424 [ dbSNP | Ensembl ].		VAR_057984
Natural varianti1169 – 11691M → T.1 Publication
Corresponds to variant rs3758437 [ dbSNP | Ensembl ].		VAR_024803
Natural varianti1176 – 11761R → W.1 Publication
Corresponds to variant rs761527369 [ dbSNP | Ensembl ].		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_011539388.2. [Q9UGM3-6]
XP_011537693.1. XM_011539391.2. [Q9UGM3-7]
XP_011537707.1. XM_011539405.2. [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_011539388.2. [Q9UGM3-6]
XP_011537693.1. XM_011539391.2. [Q9UGM3-7]
XP_011537707.1. XM_011539405.2. [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. 13 interactions.
DIPiDIP-50763N.
IntActiQ9UGM3. 6 interactions.
STRINGi9606.ENSP00000357905.

PTM databases

iPTMnetiQ9UGM3.
PhosphoSiteiQ9UGM3.

Polymorphism and mutation databases

BioMutaiDMBT1.
DMDMi85687556.

Proteomic databases

MaxQBiQ9UGM3.
PaxDbiQ9UGM3.
PeptideAtlasiQ9UGM3.
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.
OrthoDBiEOG091G0DF7.
PhylomeDBiQ9UGM3.
TreeFamiTF329295.

Enzyme and pathway databases

ReactomeiR-HSA-5683826. Surfactant metabolism.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000187908.
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...

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: September 7, 2016
This is version 146 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.