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Protein

Dematin

Gene

DMTN

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

Functioni

Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Plays also a role as a modulator of actin dynamics in fibroblasts; acts as a negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation.6 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • protein self-association Source: UniProtKB
  • receptor binding Source: UniProtKB
  • spectrin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-5223345. Miscellaneous transport and binding events.

Names & Taxonomyi

Protein namesi
Recommended name:
Dematin
Alternative name(s):
Dematin actin-binding protein
Erythrocyte membrane protein band 4.9
Gene namesi
Name:DMTN
Synonyms:DMT, EPB49
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3382. DMTN.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • actin filament Source: UniProtKB
  • cell projection membrane Source: UniProtKB
  • cortical cytoskeleton Source: Ensembl
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB
  • cytosol Source: UniProtKB
  • endomembrane system Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • platelet dense tubular network membrane Source: UniProtKB
  • spectrin-associated cytoskeleton Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi124 – 1241S → A: Reduces interaction with plasmodium berghei 14-3-3 protein. Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-333 and A-403. 1 Publication
Mutagenesisi333 – 3331S → A: Reduces interaction with plasmodium berghei 14-3-3 protein. Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-124 and A-403. 1 Publication
Mutagenesisi403 – 4031S → A: Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-124 and A-333. 2 Publications
Mutagenesisi403 – 4031S → E: Reduces F-actin bundling but not F-actin binding activity. 2 Publications

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA27815.

Polymorphism and mutation databases

BioMutaiDMTN.
DMDMi22654240.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405DematinPRO_0000218755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei92 – 921PhosphoserineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei110 – 1101PhosphoserineBy similarity
Modified residuei113 – 1131PhosphoserineBy similarity
Modified residuei156 – 1561PhosphoserineCombined sources
Modified residuei226 – 2261PhosphoserineCombined sources
Modified residuei269 – 2691PhosphoserineCombined sources
Modified residuei279 – 2791PhosphoserineCombined sources
Modified residuei289 – 2891PhosphoserineCombined sources
Modified residuei303 – 3031PhosphoserineCombined sources
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei333 – 3331PhosphoserineCombined sources
Modified residuei372 – 3721PhosphoserineCombined sources
Modified residuei383 – 3831PhosphoserineCombined sources
Modified residuei403 – 4031Phosphoserine; by PKA3 Publications

Post-translational modificationi

Phosphorylated. Phosphorylation at Ser-403 by PKA causes the C-terminal headpiece domain to associate with the N-terminal core domain, and leads to the inhibition of its actin bundling activity.4 Publications
The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ08495.
PaxDbiQ08495.
PeptideAtlasiQ08495.
PRIDEiQ08495.

PTM databases

iPTMnetiQ08495.
PhosphoSiteiQ08495.

Expressioni

Tissue specificityi

Expressed in platelets (at protein level). Expressed in heart, brain, lung, skeletal muscle, and kidney.1 Publication

Gene expression databases

BgeeiENSG00000158856.
CleanExiHS_EPB49.
ExpressionAtlasiQ08495. baseline and differential.
GenevisibleiQ08495. HS.

Organism-specific databases

HPAiHPA024290.

Interactioni

Subunit structurei

Monomeric (isoform 2); under reducing conditions. Self-associates. Exists under oxidizing condition as a trimer of two isoforms 2 and isoform 1 linked by disulfide bonds (Probable). Found in a complex with DMTN, F-actin and spectrin. Found in a complex with ADD2, DMTN and SLC2A1. Interacts with F-actin, ITPKB, RASGRF2 and spectrin. Isoform 2 interacts with SLC2A1 (via C-terminus cytoplasmic region). Isoform 1 and isoform 2 interact (phosphorylated form) with plasmodium berghei 14-3-3 protein; the interaction occurs in a PKA-dependent manner.Curated8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGA2Q083793EBI-715275,EBI-618309

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • protein self-association Source: UniProtKB
  • receptor binding Source: UniProtKB
  • spectrin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108353. 18 interactions.
IntActiQ08495. 7 interactions.
MINTiMINT-1390442.
STRINGi9606.ENSP00000265800.

Structurei

Secondary structure

1
405
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni346 – 3483Combined sources
Helixi364 – 3663Combined sources
Helixi368 – 3703Combined sources
Helixi373 – 3797Combined sources
Beta strandi380 – 3823Combined sources
Helixi384 – 3896Combined sources
Helixi392 – 40211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZPNMR-A342-405[»]
1ZV6NMR-A342-405[»]
ProteinModelPortaliQ08495.
SMRiQ08495. Positions 341-405.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08495.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini337 – 40569HPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni224 – 30885Interaction with RASGRF2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi216 – 2227Poly-Glu

Domaini

Both the N-terminal core domain and the C-terminal headpiece domain are sufficient for binding to F-actin and necessary for actin bundling activity.

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1044. Eukaryota.
ENOG410XRPY. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000285997.
HOVERGENiHBG031499.
InParanoidiQ08495.
OMAiWAESRTP.
OrthoDBiEOG091G06PE.
PhylomeDBiQ08495.
TreeFamiTF318042.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
InterProiIPR032402. AbLIM_anchor.
IPR003128. Villin_headpiece.
[Graphical view]
PfamiPF16182. AbLIM_anchor. 2 hits.
PF02209. VHP. 1 hit.
[Graphical view]
SMARTiSM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q08495-1) [UniParc]FASTAAdd to basket
Also known as: Long

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
MERLQKQPLT SPGSVSPSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD
60 70 80 90 100
KAILDIERPD LMIYEPHFTY SLLEHVELPR SRERSLSPKS TSPPPSPEVW
110 120 130 140 150
ADSRSPGIIS QASAPRTTGT PRTSLPHFHH PETSRPDSNI YKKPPIYKQR
160 170 180 190 200
ESVGGSPQTK HLIEDLIIES SKFPAAQPPD PNQPAKIETD YWPCPPSLAV
210 220 230 240 250
VETEWRKRKA SRRGAEEEEE EEDDDSGEEM KALRERQREE LSKVTSNLGK
260 270 280 290 300
MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HQGTSKSSSL PAYGRTTLSR
310 320 330 340 350
LQSTEFSPSG SETGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV
360 370 380 390 400
TNKGRTKLPP GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK

KASLF
Length:405
Mass (Da):45,514
Last modified:August 30, 2002 - v3
Checksum:i77D6372E5B16EFF4
GO
Isoform 2 (identifier: Q08495-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     320-341: Missing.

Show »
Length:383
Mass (Da):43,088
Checksum:i3C46AB7704507B6E
GO
Isoform 3 (identifier: Q08495-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-31: Missing.
     320-341: Missing.

Note: No experimental confirmation available.
Show »
Length:358
Mass (Da):40,680
Checksum:i1F985F9D3643F995
GO
Isoform 4 (identifier: Q08495-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-31: Missing.
     83-97: Missing.

Note: No experimental confirmation available.
Show »
Length:365
Mass (Da):41,558
Checksum:iBD11861605E9B618
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811S → Q in AAA58438 (PubMed:8341682).Curated
Sequence conflicti81 – 811S → Q in AAC50223 (PubMed:7615546).Curated
Sequence conflicti155 – 1551G → A in BAG52385 (PubMed:14702039).Curated
Sequence conflicti292 – 2921A → R in AAA58438 (PubMed:8341682).Curated
Sequence conflicti292 – 2921A → R in AAC50223 (PubMed:7615546).Curated
Sequence conflicti347 – 3471M → V in AAA58438 (PubMed:8341682).Curated
Sequence conflicti380 – 3801F → S in AAA58438 (PubMed:8341682).Curated
Sequence conflicti403 – 4031S → P in BAG52385 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei7 – 3125Missing in isoform 3 and isoform 4. 1 PublicationVSP_044803Add
BLAST
Alternative sequencei83 – 9715Missing in isoform 4. 1 PublicationVSP_057428Add
BLAST
Alternative sequencei320 – 34122Missing in isoform 2 and isoform 3. 3 PublicationsVSP_004189Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19713 mRNA. Translation: AAA58438.1.
U28389 mRNA. Translation: AAC50223.1.
AK055842 mRNA. Translation: BAG51582.1.
AK091581 mRNA. Translation: BAG52385.1.
AK289650 mRNA. Translation: BAF82339.1.
AK295452 mRNA. Translation: BAG58387.1.
BT007396 mRNA. Translation: AAP36060.1.
AC091171 Genomic DNA. No translation available.
BC006318 mRNA. Translation: AAH06318.1.
BC017445 mRNA. Translation: AAH17445.1.
BC052805 mRNA. Translation: AAH52805.1.
CCDSiCCDS47820.1. [Q08495-2]
CCDS47821.1. [Q08495-3]
CCDS6020.1. [Q08495-1]
CCDS78311.1. [Q08495-4]
PIRiA48222.
I39062.
RefSeqiNP_001107607.1. NM_001114135.4. [Q08495-1]
NP_001107608.1. NM_001114136.2. [Q08495-1]
NP_001107609.1. NM_001114137.3. [Q08495-2]
NP_001107610.1. NM_001114138.2. [Q08495-2]
NP_001107611.1. NM_001114139.3. [Q08495-3]
NP_001289745.1. NM_001302816.2. [Q08495-2]
NP_001289746.1. NM_001302817.2. [Q08495-4]
NP_001310307.1. NM_001323378.1. [Q08495-1]
NP_001310309.1. NM_001323380.1. [Q08495-1]
NP_001310310.1. NM_001323381.1. [Q08495-1]
NP_001310311.1. NM_001323382.1. [Q08495-1]
NP_001310312.1. NM_001323383.1. [Q08495-2]
NP_001310313.1. NM_001323384.1. [Q08495-2]
NP_001310314.1. NM_001323385.1. [Q08495-2]
NP_001310316.1. NM_001323387.1. [Q08495-3]
NP_001310317.1. NM_001323388.1. [Q08495-4]
NP_001310318.1. NM_001323389.1.
NP_001310319.1. NM_001323390.1.
NP_001310320.1. NM_001323391.1.
NP_001310321.1. NM_001323392.1.
NP_001310322.1. NM_001323393.1.
NP_001310323.1. NM_001323394.1.
NP_001310324.1. NM_001323395.1.
NP_001310325.1. NM_001323396.1.
NP_001310326.1. NM_001323397.1.
NP_001310327.1. NM_001323398.1.
NP_001310328.1. NM_001323399.1.
NP_001310329.1. NM_001323400.1.
NP_001310330.1. NM_001323401.1.
NP_001969.2. NM_001978.4. [Q08495-1]
XP_005273489.1. XM_005273432.1. [Q08495-1]
XP_005273490.1. XM_005273433.1. [Q08495-1]
UniGeneiHs.106124.

Genome annotation databases

EnsembliENST00000265800; ENSP00000265800; ENSG00000158856. [Q08495-1]
ENST00000358242; ENSP00000350977; ENSG00000158856. [Q08495-1]
ENST00000381470; ENSP00000370879; ENSG00000158856. [Q08495-2]
ENST00000415253; ENSP00000401291; ENSG00000158856. [Q08495-2]
ENST00000432128; ENSP00000416111; ENSG00000158856. [Q08495-1]
ENST00000443491; ENSP00000397904; ENSG00000158856. [Q08495-3]
ENST00000517305; ENSP00000430609; ENSG00000158856. [Q08495-1]
ENST00000517600; ENSP00000430618; ENSG00000158856. [Q08495-4]
ENST00000519907; ENSP00000429377; ENSG00000158856. [Q08495-2]
ENST00000523266; ENSP00000427866; ENSG00000158856. [Q08495-1]
ENST00000523782; ENSP00000429234; ENSG00000158856. [Q08495-3]
GeneIDi2039.
KEGGihsa:2039.
UCSCiuc064kwf.1. human. [Q08495-1]
uc064kwj.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19713 mRNA. Translation: AAA58438.1.
U28389 mRNA. Translation: AAC50223.1.
AK055842 mRNA. Translation: BAG51582.1.
AK091581 mRNA. Translation: BAG52385.1.
AK289650 mRNA. Translation: BAF82339.1.
AK295452 mRNA. Translation: BAG58387.1.
BT007396 mRNA. Translation: AAP36060.1.
AC091171 Genomic DNA. No translation available.
BC006318 mRNA. Translation: AAH06318.1.
BC017445 mRNA. Translation: AAH17445.1.
BC052805 mRNA. Translation: AAH52805.1.
CCDSiCCDS47820.1. [Q08495-2]
CCDS47821.1. [Q08495-3]
CCDS6020.1. [Q08495-1]
CCDS78311.1. [Q08495-4]
PIRiA48222.
I39062.
RefSeqiNP_001107607.1. NM_001114135.4. [Q08495-1]
NP_001107608.1. NM_001114136.2. [Q08495-1]
NP_001107609.1. NM_001114137.3. [Q08495-2]
NP_001107610.1. NM_001114138.2. [Q08495-2]
NP_001107611.1. NM_001114139.3. [Q08495-3]
NP_001289745.1. NM_001302816.2. [Q08495-2]
NP_001289746.1. NM_001302817.2. [Q08495-4]
NP_001310307.1. NM_001323378.1. [Q08495-1]
NP_001310309.1. NM_001323380.1. [Q08495-1]
NP_001310310.1. NM_001323381.1. [Q08495-1]
NP_001310311.1. NM_001323382.1. [Q08495-1]
NP_001310312.1. NM_001323383.1. [Q08495-2]
NP_001310313.1. NM_001323384.1. [Q08495-2]
NP_001310314.1. NM_001323385.1. [Q08495-2]
NP_001310316.1. NM_001323387.1. [Q08495-3]
NP_001310317.1. NM_001323388.1. [Q08495-4]
NP_001310318.1. NM_001323389.1.
NP_001310319.1. NM_001323390.1.
NP_001310320.1. NM_001323391.1.
NP_001310321.1. NM_001323392.1.
NP_001310322.1. NM_001323393.1.
NP_001310323.1. NM_001323394.1.
NP_001310324.1. NM_001323395.1.
NP_001310325.1. NM_001323396.1.
NP_001310326.1. NM_001323397.1.
NP_001310327.1. NM_001323398.1.
NP_001310328.1. NM_001323399.1.
NP_001310329.1. NM_001323400.1.
NP_001310330.1. NM_001323401.1.
NP_001969.2. NM_001978.4. [Q08495-1]
XP_005273489.1. XM_005273432.1. [Q08495-1]
XP_005273490.1. XM_005273433.1. [Q08495-1]
UniGeneiHs.106124.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZPNMR-A342-405[»]
1ZV6NMR-A342-405[»]
ProteinModelPortaliQ08495.
SMRiQ08495. Positions 341-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108353. 18 interactions.
IntActiQ08495. 7 interactions.
MINTiMINT-1390442.
STRINGi9606.ENSP00000265800.

PTM databases

iPTMnetiQ08495.
PhosphoSiteiQ08495.

Polymorphism and mutation databases

BioMutaiDMTN.
DMDMi22654240.

Proteomic databases

MaxQBiQ08495.
PaxDbiQ08495.
PeptideAtlasiQ08495.
PRIDEiQ08495.

Protocols and materials databases

DNASUi2039.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265800; ENSP00000265800; ENSG00000158856. [Q08495-1]
ENST00000358242; ENSP00000350977; ENSG00000158856. [Q08495-1]
ENST00000381470; ENSP00000370879; ENSG00000158856. [Q08495-2]
ENST00000415253; ENSP00000401291; ENSG00000158856. [Q08495-2]
ENST00000432128; ENSP00000416111; ENSG00000158856. [Q08495-1]
ENST00000443491; ENSP00000397904; ENSG00000158856. [Q08495-3]
ENST00000517305; ENSP00000430609; ENSG00000158856. [Q08495-1]
ENST00000517600; ENSP00000430618; ENSG00000158856. [Q08495-4]
ENST00000519907; ENSP00000429377; ENSG00000158856. [Q08495-2]
ENST00000523266; ENSP00000427866; ENSG00000158856. [Q08495-1]
ENST00000523782; ENSP00000429234; ENSG00000158856. [Q08495-3]
GeneIDi2039.
KEGGihsa:2039.
UCSCiuc064kwf.1. human. [Q08495-1]
uc064kwj.1. human.

Organism-specific databases

CTDi2039.
GeneCardsiDMTN.
HGNCiHGNC:3382. DMTN.
HPAiHPA024290.
MIMi125305. gene.
neXtProtiNX_Q08495.
PharmGKBiPA27815.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1044. Eukaryota.
ENOG410XRPY. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000285997.
HOVERGENiHBG031499.
InParanoidiQ08495.
OMAiWAESRTP.
OrthoDBiEOG091G06PE.
PhylomeDBiQ08495.
TreeFamiTF318042.

Enzyme and pathway databases

ReactomeiR-HSA-5223345. Miscellaneous transport and binding events.

Miscellaneous databases

ChiTaRSiDMTN. human.
EvolutionaryTraceiQ08495.
GeneWikiiEPB49.
GenomeRNAii2039.
PROiQ08495.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000158856.
CleanExiHS_EPB49.
ExpressionAtlasiQ08495. baseline and differential.
GenevisibleiQ08495. HS.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
InterProiIPR032402. AbLIM_anchor.
IPR003128. Villin_headpiece.
[Graphical view]
PfamiPF16182. AbLIM_anchor. 2 hits.
PF02209. VHP. 1 hit.
[Graphical view]
SMARTiSM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDEMA_HUMAN
AccessioniPrimary (citable) accession number: Q08495
Secondary accession number(s): A8K0T5
, B3KP70, B3KRH3, B4DI75, E9PEJ0, Q13215, Q9BRE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: August 30, 2002
Last modified: September 7, 2016
This is version 169 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.