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P08121

- CO3A1_MOUSE

UniProt

P08121 - CO3A1_MOUSE

Protein

Collagen alpha-1(III) chain

Gene

Col3a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of Gpr56 in the developing brain and binding to Gpr56 inhibits neuronal migration and activates the RhoA pathway by coupling Gpr56 to Gna13 and possibly Gna12.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1278 – 12781CalciumBy similarity
    Metal bindingi1280 – 12801CalciumBy similarity
    Metal bindingi1281 – 12811Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1283 – 12831Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1286 – 12861CalciumBy similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: Ensembl
    2. metal ion binding Source: UniProtKB-KW
    3. SMAD binding Source: MGI

    GO - Biological processi

    1. aging Source: Ensembl
    2. aorta smooth muscle tissue morphogenesis Source: BHF-UCL
    3. blood vessel development Source: MGI
    4. cell-matrix adhesion Source: Ensembl
    5. cellular response to amino acid stimulus Source: MGI
    6. cerebral cortex development Source: UniProtKB
    7. collagen biosynthetic process Source: Ensembl
    8. collagen fibril organization Source: MGI
    9. digestive tract development Source: MGI
    10. extracellular fibril organization Source: Ensembl
    11. heart development Source: Ensembl
    12. integrin-mediated signaling pathway Source: Ensembl
    13. negative regulation of immune response Source: Ensembl
    14. negative regulation of neuron migration Source: UniProtKB
    15. peptide cross-linking Source: Ensembl
    16. positive regulation of Rho protein signal transduction Source: UniProtKB
    17. response to cytokine Source: Ensembl
    18. response to mechanical stimulus Source: Ensembl
    19. response to radiation Source: Ensembl
    20. skeletal system development Source: Ensembl
    21. skin development Source: Ensembl
    22. transforming growth factor beta receptor signaling pathway Source: Ensembl
    23. wound healing Source: Ensembl

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196581. Scavenging by Class A Receptors.
    REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_196644. Syndecan interactions.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.
    REACT_206066. Extracellular matrix organization.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(III) chain
    Gene namesi
    Name:Col3a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:88453. Col3a1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen trimer Source: MGI
    2. collagen type III trimer Source: MGI
    3. extracellular matrix Source: MGI
    4. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Neuronal ectopias and abnormal cortical lamination.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323By similarityAdd
    BLAST
    Propeptidei24 – 154131N-terminal propeptidePRO_0000005743Add
    BLAST
    Chaini155 – 12191065Collagen alpha-1(III) chainPRO_0000005744Add
    BLAST
    Propeptidei1220 – 1464245C-terminal propeptidePRO_0000005745Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei262 – 26215-hydroxylysine; alternateBy similarity
    Glycosylationi262 – 2621O-linked (Gal...); alternateBy similarity
    Modified residuei283 – 28315-hydroxylysineBy similarity
    Modified residuei859 – 85915-hydroxylysineBy similarity
    Modified residuei976 – 97615-hydroxylysineBy similarity
    Modified residuei1093 – 109315-hydroxylysineBy similarity
    Modified residuei1105 – 110515-hydroxylysineBy similarity
    Disulfide bondi1195 – 1195InterchainPROSITE-ProRule annotation
    Disulfide bondi1196 – 1196InterchainPROSITE-ProRule annotation
    Disulfide bondi1260 ↔ 1292PROSITE-ProRule annotation
    Disulfide bondi1266 – 1266Interchain (with C-1283)PROSITE-ProRule annotation
    Disulfide bondi1283 – 1283Interchain (with C-1266)PROSITE-ProRule annotation
    Disulfide bondi1300 ↔ 1462PROSITE-ProRule annotation
    Disulfide bondi1370 ↔ 1415PROSITE-ProRule annotation

    Post-translational modificationi

    Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
    O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiP08121.
    PaxDbiP08121.
    PRIDEiP08121.

    PTM databases

    PhosphoSiteiP08121.

    Expressioni

    Tissue specificityi

    Expressed in embryonic brain, specifically in the meninges, pial basement membrane and blood vessels (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP08121.
    BgeeiP08121.
    CleanExiMM_COL3A1.
    GenevestigatoriP08121.

    Interactioni

    Subunit structurei

    Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines.

    Protein-protein interaction databases

    BioGridi198815. 5 interactions.
    IntActiP08121. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP08121.
    SMRiP08121. Positions 1247-1464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 9060VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1230 – 1464235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni155 – 16915Nonhelical region (N-terminal)Add
    BLAST
    Regioni170 – 11951026Triple-helical regionAdd
    BLAST

    Domaini

    The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.By similarity

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
    Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG004933.
    InParanoidiP08121.
    KOiK06236.
    OMAiPGPSGHQ.
    OrthoDBiEOG7TJ3HH.
    TreeFamiTF344135.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 7 hits.
    PF00093. VWC. 1 hit.
    [Graphical view]
    ProDomiPD002078. Fib_collagen_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00038. COLFI. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    PROSITEiPS51461. NC1_FIB. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08121-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMSFVQSGTW FLLTLLHPTL ILAQQSNVDE LGCSHLGQSY ESRDVWKPEP     50
    CQICVCDSGS VLCDDIICDE EPLDCPNPEI PFGECCAICP QPSTPAPVLP 100
    DGHGPQGPKG DPGPPGIPGR NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ 150
    NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP PGPPGSSGHP GSPGSPGYQG 200
    PPGEPGQAGP AGPPGPPGAL GPAGPAGKDG ESGRPGRPGE RGLPGPPGIK 250
    GPAGMPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP 300
    RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG 350
    EVGPAGSPGS NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA 400
    GIPGAPGLIG ARGPPGPAGT NGIPGTRGPS GEPGKNGAKG EPGARGERGE 450
    AGSPGIPGPK GEDGKDGSPG EPGANGLPGA AGERGPSGFR GPAGPNGIPG 500
    EKGPPGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS PGGPGNDGKP 550
    GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG 600
    PGLPGPAGKN GETGPQGPPG PTGPAGDKGD SGPPGPQGLQ GIPGTGGPPG 650
    ENGKPGEPGP KGEVGAPGAP GGKGDSGAPG ERGPPGTAGI PGARGGAGPP 700
    GPEGGKGPAG PPGPPGASGS PGLQGMPGER GGPGSPGPKG EKGEPGGAGA 750
    DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE GGSPGLPGIA GPRGGPGERG 800
    EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGP AGPTGSSGPA 850
    GPPGPQGVKG ERGSPGGPGT AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK 900
    DGPPGPAGNS GSPGNPGIAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG 950
    LTGARGLAGP PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP 1000
    GQPGTAGEPG RDGNPGSDGQ PGRDGSPGGK GDRGENGSPG APGAPGHPGP 1050
    PGPVGPSGKS GDRGETGPAG PSGAPGPAGA RGAPGPQGPR GDKGETGERG 1100
    SNGIKGHRGF PGNPGPPGSP GAAGHQGAIG SPGPAGPRGP VGPHGPPGKD 1150
    GTSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA 1200
    AAIAGVGGEK SGGFSPYYGD DPMDFKINTE EIMSSLKSVN GQIESLISPD 1250
    GSRKNPARNC RDLKFCHPEL KSGEYWVDPN QGCKMDAIKV FCNMETGETC 1300
    INASPMTVPR KHWWTDSGAE KKHVWFGESM NGGFQFSYGP PDLPEDVVDV 1350
    QLAFLRLLSS RASQNITYHC KNSIAYMDQA SGNVKKSLKL MGSNEGEFKA 1400
    EGNSKFTYTV LEDGCTKHTG EWSKTVFEYQ TRKAMRLPII DIAPYDIGGP 1450
    DQEFGVDIGP VCFL 1464
    Length:1,464
    Mass (Da):138,943
    Last modified:July 15, 1999 - v4
    Checksum:i2104EC27A886090B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52046 Genomic DNA. Translation: CAA36279.1.
    BC043089 mRNA. Translation: AAH43089.1.
    BC058724 mRNA. Translation: AAH58724.1.
    M18933 mRNA. Translation: AAA37338.1.
    K03037 Genomic DNA. No translation available.
    AK019448 mRNA. Translation: BAB31724.1.
    X57983 Genomic DNA. Translation: CAA41048.1.
    CCDSiCCDS35554.1.
    PIRiA27353.
    S59856.
    RefSeqiNP_034060.2. NM_009930.2.
    UniGeneiMm.249555.

    Genome annotation databases

    EnsembliENSMUST00000087883; ENSMUSP00000085192; ENSMUSG00000026043.
    GeneIDi12825.
    KEGGimmu:12825.
    UCSCiuc007awq.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52046 Genomic DNA. Translation: CAA36279.1 .
    BC043089 mRNA. Translation: AAH43089.1 .
    BC058724 mRNA. Translation: AAH58724.1 .
    M18933 mRNA. Translation: AAA37338.1 .
    K03037 Genomic DNA. No translation available.
    AK019448 mRNA. Translation: BAB31724.1 .
    X57983 Genomic DNA. Translation: CAA41048.1 .
    CCDSi CCDS35554.1.
    PIRi A27353.
    S59856.
    RefSeqi NP_034060.2. NM_009930.2.
    UniGenei Mm.249555.

    3D structure databases

    ProteinModelPortali P08121.
    SMRi P08121. Positions 1247-1464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198815. 5 interactions.
    IntActi P08121. 2 interactions.

    PTM databases

    PhosphoSitei P08121.

    Proteomic databases

    MaxQBi P08121.
    PaxDbi P08121.
    PRIDEi P08121.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000087883 ; ENSMUSP00000085192 ; ENSMUSG00000026043 .
    GeneIDi 12825.
    KEGGi mmu:12825.
    UCSCi uc007awq.2. mouse.

    Organism-specific databases

    CTDi 1281.
    MGIi MGI:88453. Col3a1.

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG004933.
    InParanoidi P08121.
    KOi K06236.
    OMAi PGPSGHQ.
    OrthoDBi EOG7TJ3HH.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_196581. Scavenging by Class A Receptors.
    REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_196644. Syndecan interactions.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.
    REACT_206066. Extracellular matrix organization.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi COL3A1. mouse.
    NextBioi 282310.
    PROi P08121.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08121.
    Bgeei P08121.
    CleanExi MM_COL3A1.
    Genevestigatori P08121.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 7 hits.
    PF00093. VWC. 1 hit.
    [Graphical view ]
    ProDomi PD002078. Fib_collagen_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00038. COLFI. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view ]
    PROSITEi PS51461. NC1_FIB. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mouse type-III procollagen-encoding gene: genomic cloning and complete DNA sequence."
      Toman D., de Crombrugghe B.
      Gene 147:161-168(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/6 X DBA.
      Tissue: Embryo.
    2. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Complete nucleotide sequence of the N-terminal domains of the murine alpha-1 type-III collagen chain."
      Wood L., Theriault N., Vogeli G.
      Gene 61:225-230(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-488.
    4. "Identification of the promoter and first exon of the mouse alpha 1 (III) collagen gene."
      Liau G., Mudryj M., de Crombrugghe B.
      J. Biol. Chem. 260:3773-3777(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
    5. "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.
      , 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] OF 810-1464.
      Strain: C57BL/6J.
      Tissue: Embryonic head.
    6. "Specific hybridization probes for mouse type I, II, III and IX collagen mRNAs."
      Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.
      Biochim. Biophys. Acta 1089:241-243(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1442-1464.
      Strain: C57BL/6.
    7. "G protein-coupled receptor 56 and collagen III, a receptor-ligand pair, regulates cortical development and lamination."
      Luo R., Jeong S.J., Jin Z., Strokes N., Li S., Piao X.
      Proc. Natl. Acad. Sci. U.S.A. 108:12925-12930(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RECEPTOR-BINDING, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCO3A1_MOUSE
    AccessioniPrimary (citable) accession number: P08121
    Secondary accession number(s): Q61429, Q9CRN7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 142 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3