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P58022

- LOXL2_MOUSE

UniProt

P58022 - LOXL2_MOUSE

Protein

Lysyl oxidase homolog 2

Gene

Loxl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (22 Nov 2005)
      Previous versions | rss
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    Functioni

    Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). When secreted in extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. When nuclear, acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin, probably by mediating deamination of histone H3 By similarity. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.By similarity1 Publication

    Catalytic activityi

    Peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3 + H2O2.

    Cofactori

    Copper.By similarity
    Contains 1 lysine tyrosylquinone.By similarity

    Enzyme regulationi

    Specifically inhibited by a mouse monoclonal antibody AB0023, inhibition occurs in a non-competitive manner.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi628 – 6281CopperSequence Analysis
    Metal bindingi630 – 6301CopperSequence Analysis
    Metal bindingi632 – 6321CopperSequence Analysis

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. copper ion binding Source: InterPro
    3. methylated histone binding Source: UniProtKB
    4. oligosaccharide binding Source: UniProtKB
    5. protein-lysine 6-oxidase activity Source: UniProtKB
    6. scavenger receptor activity Source: InterPro
    7. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: UniProtKB
    2. collagen fibril organization Source: UniProtKB
    3. endothelial cell migration Source: UniProtKB
    4. endothelial cell proliferation Source: UniProtKB
    5. epithelial to mesenchymal transition Source: UniProtKB
    6. histone modification Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. oxidation-reduction process Source: UniProtKB
    9. positive regulation of chondrocyte differentiation Source: UniProtKB
    10. protein deamination Source: UniProtKB
    11. response to copper ion Source: UniProtKB
    12. response to hypoxia Source: UniProtKB
    13. sprouting angiogenesis Source: UniProtKB
    14. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Oxidoreductase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysyl oxidase homolog 2 (EC:1.4.3.13)
    Alternative name(s):
    Lysyl oxidase-like protein 2
    Gene namesi
    Name:Loxl2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:2137913. Loxl2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrixbasement membrane By similarity. Nucleus By similarity. Chromosome By similarity
    Note: Associated with chromatin By similarity. It is unclear how LOXL2 is nuclear: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, different reports confirmed the intracellular location and its key role in transcription regulation.By similarity

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. chromosome Source: UniProtKB-SubCell
    3. extracellular space Source: UniProtKB
    4. membrane Source: InterPro
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Chromosome, Extracellular matrix, Nucleus, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 776751Lysyl oxidase homolog 2PRO_0000042854Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi87 ↔ 151PROSITE-ProRule annotation
    Disulfide bondi100 ↔ 161PROSITE-ProRule annotation
    Disulfide bondi131 ↔ 141PROSITE-ProRule annotation
    Disulfide bondi221 ↔ 294PROSITE-ProRule annotation
    Disulfide bondi234 ↔ 304PROSITE-ProRule annotation
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi268 ↔ 278PROSITE-ProRule annotation
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi354 ↔ 417PROSITE-ProRule annotation
    Disulfide bondi367 ↔ 427PROSITE-ProRule annotation
    Disulfide bondi398 ↔ 408PROSITE-ProRule annotation
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi467 ↔ 532PROSITE-ProRule annotation
    Disulfide bondi480 ↔ 545PROSITE-ProRule annotation
    Disulfide bondi514 ↔ 524PROSITE-ProRule annotation
    Disulfide bondi575 ↔ 581PROSITE-ProRule annotation
    Disulfide bondi627 ↔ 675PROSITE-ProRule annotation
    Glycosylationi646 – 6461N-linked (GlcNAc...)Sequence Analysis
    Cross-linki655 ↔ 691Lysine tyrosylquinone (Lys-Tyr)By similarity
    Disulfide bondi659 ↔ 665PROSITE-ProRule annotation
    Disulfide bondi687 ↔ 697PROSITE-ProRule annotation
    Modified residuei691 – 69112',4',5'-topaquinoneBy similarity
    Disulfide bondi734 ↔ 748PROSITE-ProRule annotation

    Post-translational modificationi

    The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.By similarity
    N-glycosylated. N-glycosylation on Asn-458 and Asn-646 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, LTQ, TPQ

    Proteomic databases

    PRIDEiP58022.

    PTM databases

    PhosphoSiteiP58022.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest expression in skin, lung and thymus. Present in chondrocytes: mainly expressed by chondrocytes in healing fractures and in epiphyseal growth plates (at protein level).1 Publication

    Inductioni

    Strongly induced in hypoxia.1 Publication

    Gene expression databases

    BgeeiP58022.
    CleanExiMM_LOXL2.
    GenevestigatoriP58022.

    Interactioni

    Subunit structurei

    Component of some chromatin repressor complex. Interacts with SNAI1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiP58022. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP58022.
    SMRiP58022. Positions 71-162, 329-428, 438-525.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 162102SRCR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini191 – 305115SRCR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini329 – 428100SRCR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 546109SRCR 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni550 – 753204Lysyl-oxidase likeBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the lysyl oxidase family.Curated
    Contains 4 SRCR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG40770.
    GeneTreeiENSGT00740000115380.
    HOGENOMiHOG000220841.
    HOVERGENiHBG052336.
    InParanoidiP58022.
    KOiK00280.
    OMAiGHEWSEV.
    OrthoDBiEOG7SN8C6.
    PhylomeDBiP58022.
    TreeFamiTF326061.

    Family and domain databases

    Gene3Di3.10.250.10. 4 hits.
    InterProiIPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view]
    PfamiPF01186. Lysyl_oxidase. 1 hit.
    PF00530. SRCR. 4 hits.
    [Graphical view]
    PRINTSiPR00074. LYSYLOXIDASE.
    PR00258. SPERACTRCPTR.
    SMARTiSM00202. SR. 4 hits.
    [Graphical view]
    SUPFAMiSSF56487. SSF56487. 4 hits.
    PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
    PS00420. SRCR_1. 2 hits.
    PS50287. SRCR_2. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P58022-1) [UniParc]FASTAAdd to Basket

    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

    MELHFGSCLS GCLALLVLLP SLSLAQYEGW PYQLQYPEYF QQPAPEHHQR    50
    QVPSDVVKIQ VRLAGQKRKH NEGRVEVYYE GQWGTVCDDD FSIHAAHVVC 100
    RQVGYVEAKS WAASSSYGPG EGPIWLDNIY CTGKESTLAS CSSNGWGVTD 150
    CKHTEDVGVV CSEKRIPGFK FDNSLINQIE SLNIQVEDIR IRPILSAFRH 200
    RKPVTEGYVE VKEGKAWKQI CNKHWTAKNS HVVCGMFGFP AEKTYNPKAY 250
    KTFASRRKLR YWKFSMNCTG TEAHISSCKL GPSVTRDPVK NATCENGQPA 300
    VVSCVPSQIF SPDGPSRFRK AYKPEQPLVR LRGGAQVGEG RVEVLKNGEW 350
    GTICDDKWDL VSASVVCREL GFGTAKEAIT GSRLGQGIGP IHLNEVQCTG 400
    TEKSIIDCKF NTESQGCNHE EDAGVRCNIP IMGFQKKVRL NGGRNPYEGR 450
    VEVLTERNGS LVWGTVCGQN WGIVEAMVVC RQLGLGFASN AFQETWYWHG 500
    NIFANNVVMS GVKCSGTELS LAHCRHDEEV ACPEGGVRFG AGVACSETAP 550
    DLVLNAEIVQ QTAYLEDRPM SLLQCAMEEN CLSASAVHTD PTRGHRRLLR 600
    FSSQIHNNGQ SDFRPKNGRH AWIWHDCHRH YHSMEVFTYY DLLSLNGTKV 650
    AEGHKASFCL EDTECEGDIQ KSYECANFGE QGITMGCWDM YRHDIDCQWI 700
    DITDVPPGDY LFQVVINPNY EVPESDFSNN IMKCRSRYDG YRIWMYNCHV 750
    GGAFSEETEQ KFEHFSGLLN NQLSVQ 776
    Length:776
    Mass (Da):87,003
    Last modified:November 22, 2005 - v2
    Checksum:i9DE55C6F37DE5EEF
    GO
    Isoform 2 (identifier: P58022-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         714-727: VVINPNYEVPESDF → PSNRVLVRAGQTPY
         728-776: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:727
    Mass (Da):81,168
    Checksum:i9A4A912D0BDA9FCC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti320 – 3201K → E in BAC32186. (PubMed:16141072)Curated
    Sequence conflicti558 – 5603IVQ → HEE in AAF29046. (PubMed:10842102)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei714 – 72714VVINP…PESDF → PSNRVLVRAGQTPY in isoform 2. 1 PublicationVSP_016231Add
    BLAST
    Alternative sequencei728 – 77649Missing in isoform 2. 1 PublicationVSP_016232Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK034957 mRNA. Translation: BAC28894.1.
    AK045019 mRNA. Translation: BAC32186.1.
    AK081898 mRNA. Translation: BAC38364.1.
    AK145323 mRNA. Translation: BAE26367.1.
    AK159386 mRNA. Translation: BAE35041.1.
    AF117951 mRNA. Translation: AAF29046.1.
    CCDSiCCDS27241.1. [P58022-1]
    RefSeqiNP_201582.2. NM_033325.2. [P58022-1]
    XP_003688982.2. XM_003688934.3. [P58022-2]
    XP_006519810.1. XM_006519747.1. [P58022-1]
    UniGeneiMm.116714.

    Genome annotation databases

    EnsembliENSMUST00000022660; ENSMUSP00000022660; ENSMUSG00000034205. [P58022-1]
    ENSMUST00000100420; ENSMUSP00000097987; ENSMUSG00000034205. [P58022-1]
    GeneIDi100862072.
    94352.
    KEGGimmu:100862072.
    mmu:94352.
    UCSCiuc007umn.3. mouse. [P58022-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK034957 mRNA. Translation: BAC28894.1 .
    AK045019 mRNA. Translation: BAC32186.1 .
    AK081898 mRNA. Translation: BAC38364.1 .
    AK145323 mRNA. Translation: BAE26367.1 .
    AK159386 mRNA. Translation: BAE35041.1 .
    AF117951 mRNA. Translation: AAF29046.1 .
    CCDSi CCDS27241.1. [P58022-1 ]
    RefSeqi NP_201582.2. NM_033325.2. [P58022-1 ]
    XP_003688982.2. XM_003688934.3. [P58022-2 ]
    XP_006519810.1. XM_006519747.1. [P58022-1 ]
    UniGenei Mm.116714.

    3D structure databases

    ProteinModelPortali P58022.
    SMRi P58022. Positions 71-162, 329-428, 438-525.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P58022. 1 interaction.

    PTM databases

    PhosphoSitei P58022.

    Proteomic databases

    PRIDEi P58022.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022660 ; ENSMUSP00000022660 ; ENSMUSG00000034205 . [P58022-1 ]
    ENSMUST00000100420 ; ENSMUSP00000097987 ; ENSMUSG00000034205 . [P58022-1 ]
    GeneIDi 100862072.
    94352.
    KEGGi mmu:100862072.
    mmu:94352.
    UCSCi uc007umn.3. mouse. [P58022-1 ]

    Organism-specific databases

    CTDi 4017.
    MGIi MGI:2137913. Loxl2.

    Phylogenomic databases

    eggNOGi NOG40770.
    GeneTreei ENSGT00740000115380.
    HOGENOMi HOG000220841.
    HOVERGENi HBG052336.
    InParanoidi P58022.
    KOi K00280.
    OMAi GHEWSEV.
    OrthoDBi EOG7SN8C6.
    PhylomeDBi P58022.
    TreeFami TF326061.

    Miscellaneous databases

    ChiTaRSi LOXL2. mouse.
    NextBioi 352317.
    PROi P58022.
    SOURCEi Search...

    Gene expression databases

    Bgeei P58022.
    CleanExi MM_LOXL2.
    Genevestigatori P58022.

    Family and domain databases

    Gene3Di 3.10.250.10. 4 hits.
    InterProi IPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view ]
    Pfami PF01186. Lysyl_oxidase. 1 hit.
    PF00530. SRCR. 4 hits.
    [Graphical view ]
    PRINTSi PR00074. LYSYLOXIDASE.
    PR00258. SPERACTRCPTR.
    SMARTi SM00202. SR. 4 hits.
    [Graphical view ]
    SUPFAMi SSF56487. SSF56487. 4 hits.
    PROSITEi PS00926. LYSYL_OXIDASE. 1 hit.
    PS00420. SRCR_1. 2 hits.
    PS50287. SRCR_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Embryo and Head.
    2. "The mouse lysyl oxidase-like 2 gene (mLOXL2) maps to chromosome 14 and is highly expressed in skin, lung and thymus."
      Jourdan-Le Saux C., Le Saux O., Gleyzal C., Sommer P., Csiszar K.
      Matrix Biol. 19:179-183(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 558-776 (ISOFORM 1).
    3. "Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and type IV collagen assembly in the endothelial basement membrane."
      Bignon M., Pichol-Thievend C., Hardouin J., Malbouyres M., Brechot N., Nasciutti L., Barret A., Teillon J., Guillon E., Etienne E., Caron M., Joubert-Caron R., Monnot C., Ruggiero F., Muller L., Germain S.
      Blood 118:3979-3989(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    4. "Lysyl oxidase-like-2 (LOXL2) is a major isoform in chondrocytes and is critically required for differentiation."
      Iftikhar M., Hurtado P., Bais M.V., Wigner N., Stephens D.N., Gerstenfeld L.C., Trackman P.C.
      J. Biol. Chem. 286:909-918(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiLOXL2_MOUSE
    AccessioniPrimary (citable) accession number: P58022
    Secondary accession number(s): Q8BRE6
    , Q8BS86, Q8C4K0, Q9JJ39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 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