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Q9WV69 (DEMA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dematin
Alternative name(s):
Dematin actin-binding protein
Erythrocyte membrane protein band 4.9
Gene names
Name:Dmtn
Synonyms:Epb4.9, Epb49
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 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. Ref.6 Ref.10 Ref.11

Subunit structure

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 and spectrin. Isoform 2 interacts with SLC2A1 (via C-terminus cytoplasmic region) By similarity. Interacts with RASGRF2. Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity. Cytoplasmcytosol. Cytoplasmperinuclear region. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity. Membrane. Endomembrane system By similarity. Cell projection. Note: Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane By similarity. Ref.10

Tissue specificity

Expressed in platelets. Isoform 1 and isoform 2 are expressed in mature erythrocytes (at protein level). Ref.6 Ref.11

Domain

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.

Post-translational modification

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 By similarity.

Disruption phenotype

Mice are viable and born at the expected Mendelian ratio. Adult mice show compensated anemia and display mild microcytosis and spherocytosis. The erythrocyte plasma membrane association with the spectrin-actin skeleton is fragile and mechanically unstable. Ref.6

Sequence similarities

Belongs to the villin/gelsolin family.

Contains 1 HP (headpiece) domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainRepeat
   LigandActin-binding
   Molecular functionActin capping
   PTMDisulfide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype Ref.6. Source: UniProtKB

actin filament bundle assembly

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

actin filament reorganization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

calcium-mediated signaling using extracellular calcium source

Inferred from mutant phenotype Ref.11. Source: UniProtKB

calcium-mediated signaling using intracellular calcium source

Inferred from mutant phenotype Ref.11. Source: UniProtKB

cellular response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to calcium ion

Inferred from mutant phenotype Ref.11. Source: UniProtKB

erythrocyte development

Inferred from mutant phenotype Ref.6. Source: UniProtKB

negative regulation of cell-substrate adhesion

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of focal adhesion assembly

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of peptidyl-threonine phosphorylation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of protein targeting to membrane

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of substrate adhesion-dependent cell spreading

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of blood coagulation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of fibroblast migration

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of integrin-mediated signaling pathway

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of platelet aggregation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of substrate adhesion-dependent cell spreading

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of wound healing

Inferred from mutant phenotype Ref.10. Source: UniProtKB

protein complex assembly

Inferred from direct assay Ref.6. Source: UniProtKB

protein secretion by platelet

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of filopodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentactin filament

Inferred from sequence or structural similarity. Source: UniProtKB

cell projection membrane

Inferred from direct assay Ref.10. Source: UniProtKB

cortical cytoskeleton

Inferred from direct assay PubMed 18723693. Source: MGI

cytoplasmic membrane-bounded vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay Ref.10. Source: UniProtKB

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 18723693. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

platelet dense tubular network membrane

Inferred from sequence or structural similarity. Source: UniProtKB

spectrin-associated cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionactin binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein self-association

Inferred from direct assay Ref.6. Source: UniProtKB

receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

spectrin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WV69-1)

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.
Isoform 2 (identifier: Q9WV69-2)

The sequence of this isoform differs from the canonical sequence as follows:
     320-341: Missing.
Isoform 3 (identifier: Q9WV69-3)

The sequence of this isoform differs from the canonical sequence as follows:
     7-31: Missing.
Isoform 4 (identifier: Q9WV69-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Dematin
PRO_0000218756

Regions

Domain337 – 40569HP
Region224 – 30885Interaction with RASGRF2 By similarity
Compositional bias216 – 2227Poly-Glu

Amino acid modifications

Modified residue961Phosphoserine By similarity
Modified residue1141Phosphothreonine Ref.9
Modified residue1561Phosphoserine Ref.8
Modified residue2261Phosphoserine Ref.8 Ref.9
Modified residue3331Phosphoserine By similarity
Modified residue3721Phosphoserine Ref.8
Modified residue4031Phosphoserine; by PKA By similarity

Natural variations

Alternative sequence7 – 3125Missing in isoform 3 and isoform 4.
VSP_047491
Alternative sequence320 – 34122Missing in isoform 2 and isoform 4.
VSP_047492

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: AECA552500BDD19A

FASTA40545,468
        10         20         30         40         50         60 
MERLQKQPLT SPGSVSSSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD 

        70         80         90        100        110        120 
LMIYEPHFTY SLLEHVELPR SRECSLSPKS TSPPPSPEVW AESRTLGIIS QASTPRTTGT 

       130        140        150        160        170        180 
PRTSLPHFHH PETTRPDSNI YKKPPIYKQR ESVGGSPQSK HLIEDLIIES SKFPAAQPPD 

       190        200        210        220        230        240 
PNQPAKIETD YWPCPPSLAV VETEWRKRKA SRKGAEEEEE EEDDDSEEEI KAIRERQKEE 

       250        260        270        280        290        300 
LSKVTSNLGK MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HSGTSKSSSL PSYGRTTLSR 

       310        320        330        340        350        360 
LQSTEFSPSG SEAGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV TNKGRTKLPP 

       370        380        390        400 
GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK KASLF 

« Hide

Isoform 2 [UniParc].

Checksum: C8F3299489322DF1
Show »

FASTA38343,042
Isoform 3 [UniParc].

Checksum: 27E8E56877D0B310
Show »

FASTA38043,071
Isoform 4 [UniParc].

Checksum: 6EF6B051450E509C
Show »

FASTA35840,644

References

« Hide 'large scale' references
[1]"cDNA sequence, genomic structure, and expression of the mouse dematin gene (Epb4.9)."
Azim A.C., Kim A.C., Lutchman M., Andrabi S., Peters L.L., Chishti A.H.
Mamm. Genome 10:1026-1029(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Erythrocyte and Spleen.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
Strain: C57BL/6J.
Tissue: Hypothalamus, Spleen and Visual cortex.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
Strain: FVB/N.
Tissue: Eye and Kidney.
[5]"Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways."
Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M., Boukharov A.A., Hanada T., Chishti A.H.
Eur. J. Biochem. 269:638-649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASGRF2.
[6]"Headpiece domain of dematin is required for the stability of the erythrocyte membrane."
Khanna R., Chang S.H., Andrabi S., Azam M., Kim A., Rivera A., Brugnara C., Low P.S., Liu S.C., Chishti A.H.
Proc. Natl. Acad. Sci. U.S.A. 99:6637-6642(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[7]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[8]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-226 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"The headpiece domain of dematin regulates cell shape, motility, and wound healing by modulating RhoA activation."
Mohseni M., Chishti A.H.
Mol. Cell. Biol. 28:4712-4718(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Headpiece domain of dematin regulates calcium mobilization and signaling in platelets."
Wieschhaus A.J., Le Breton G.C., Chishti A.H.
J. Biol. Chem. 287:41218-41231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF079846 mRNA. Translation: AAD34233.1.
AF155547 mRNA. Translation: AAD38412.1.
AK158744 mRNA. Translation: BAE34638.1.
AK162866 mRNA. Translation: BAE37092.1.
AK165294 mRNA. Translation: BAE38123.1.
AC154563 Genomic DNA. No translation available.
BC016897 mRNA. Translation: AAH16897.1.
BC037021 mRNA. Translation: AAH37021.1.
CCDSCCDS27259.1. [Q9WV69-2]
RefSeqNP_001239591.1. NM_001252662.1. [Q9WV69-1]
NP_001239592.1. NM_001252663.1. [Q9WV69-2]
NP_001239593.1. NM_001252664.1. [Q9WV69-3]
NP_001239594.1. NM_001252665.1. [Q9WV69-4]
NP_001239595.1. NM_001252666.1. [Q9WV69-4]
NP_038542.1. NM_013514.4. [Q9WV69-2]
XP_006518593.1. XM_006518530.1. [Q9WV69-1]
XP_006518594.1. XM_006518531.1. [Q9WV69-1]
XP_006518595.1. XM_006518532.1. [Q9WV69-1]
XP_006518601.1. XM_006518538.1. [Q9WV69-3]
XP_006518602.1. XM_006518539.1. [Q9WV69-3]
XP_006518603.1. XM_006518540.1. [Q9WV69-3]
XP_006518604.1. XM_006518541.1. [Q9WV69-3]
XP_006518605.1. XM_006518542.1. [Q9WV69-4]
UniGeneMm.210863.

3D structure databases

ProteinModelPortalQ9WV69.
SMRQ9WV69. Positions 341-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WV69. 2 interactions.
MINTMINT-4093018.
STRING10090.ENSMUSP00000022695.

PTM databases

PhosphoSiteQ9WV69.

Proteomic databases

MaxQBQ9WV69.
PaxDbQ9WV69.
PRIDEQ9WV69.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022694; ENSMUSP00000022694; ENSMUSG00000022099. [Q9WV69-2]
ENSMUST00000022695; ENSMUSP00000022695; ENSMUSG00000022099. [Q9WV69-3]
ENSMUST00000110984; ENSMUSP00000106612; ENSMUSG00000022099. [Q9WV69-2]
GeneID13829.
KEGGmmu:13829.
UCSCuc007uom.2. mouse. [Q9WV69-1]
uc007uon.2. mouse.
uc029sln.1. mouse.

Organism-specific databases

CTD2039.
MGIMGI:99670. Dmtn.

Phylogenomic databases

eggNOGNOG253396.
GeneTreeENSGT00710000106508.
HOGENOMHOG000285997.
HOVERGENHBG031499.
InParanoidQ9WV69.
OMAWAESRTP.
OrthoDBEOG7PK90G.
PhylomeDBQ9WV69.
TreeFamTF318042.

Gene expression databases

CleanExMM_EPB4.9.
GenevestigatorQ9WV69.

Family and domain databases

Gene3D1.10.950.10. 1 hit.
InterProIPR003128. Villin_headpiece.
[Graphical view]
PfamPF02209. VHP. 1 hit.
[Graphical view]
SMARTSM00153. VHP. 1 hit.
[Graphical view]
SUPFAMSSF47050. SSF47050. 1 hit.
PROSITEPS51089. HP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284636.
PROQ9WV69.
SOURCESearch...

Entry information

Entry nameDEMA_MOUSE
AccessionPrimary (citable) accession number: Q9WV69
Secondary accession number(s): F8WIF9 expand/collapse secondary AC list , Q3TYC5, Q8JZV5, Q9WVM2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot