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O35598

- ADA10_MOUSE

UniProt

O35598 - ADA10_MOUSE

Protein

Disintegrin and metalloproteinase domain-containing protein 10

Gene

Adam10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface By similarity. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) at '687-Lys-|-Leu-688'. Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling By similarity.By similarity

    Catalytic activityi

    Endopeptidase of broad specificity.

    Cofactori

    Binds 1 zinc ion.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi173 – 1731Zinc; in inhibited formBy similarity
    Metal bindingi384 – 3841Zinc; catalytic
    Active sitei385 – 3851PROSITE-ProRule annotation
    Metal bindingi388 – 3881Zinc; catalytic
    Metal bindingi394 – 3941Zinc; catalytic

    GO - Molecular functioni

    1. endopeptidase activity Source: MGI
    2. metalloendopeptidase activity Source: UniProtKB
    3. metallopeptidase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. SH2 domain binding Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. constitutive protein ectodomain proteolysis Source: Ensembl
    2. in utero embryonic development Source: UniProtKB
    3. membrane protein ectodomain proteolysis Source: UniProtKB
    4. monocyte activation Source: Ensembl
    5. negative regulation of cell adhesion Source: UniProtKB
    6. Notch receptor processing Source: UniProtKB
    7. Notch signaling pathway Source: UniProtKB
    8. nucleocytoplasmic transport Source: UniProtKB
    9. PMA-inducible membrane protein ectodomain proteolysis Source: Ensembl
    10. positive regulation of cell growth Source: Ensembl
    11. positive regulation of cell proliferation Source: Ensembl
    12. positive regulation of T cell chemotaxis Source: Ensembl
    13. protein phosphorylation Source: UniProtKB
    14. response to tumor necrosis factor Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Notch signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_196638. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
    REACT_196643. Constitutive Signaling by NOTCH1 HD Domain Mutants.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.
    REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_199404. Signaling by NOTCH4.
    REACT_199411. NOTCH2 Activation and Transmission of Signal to the Nucleus.
    REACT_199413. Signaling by NOTCH3.

    Protein family/group databases

    MEROPSiM12.210.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 10 (EC:3.4.24.81)
    Short name:
    ADAM 10
    Alternative name(s):
    Kuzbanian protein homolog
    Mammalian disintegrin-metalloprotease
    CD_antigen: CD156c
    Gene namesi
    Name:Adam10
    Synonyms:Kuz, Madm
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:109548. Adam10.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB
    4. Golgi-associated vesicle Source: UniProtKB
    5. integral component of membrane Source: UniProtKB-KW
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: Reactome
    8. postsynaptic density Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Propeptidei20 – 214195By similarityPRO_0000029068Add
    BLAST
    Chaini215 – 749535Disintegrin and metalloproteinase domain-containing protein 10PRO_0000029069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi223 ↔ 314By similarity
    Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi279 – 2791N-linked (GlcNAc...)1 Publication
    Disulfide bondi345 ↔ 452By similarity
    Disulfide bondi400 ↔ 436By similarity
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi485 ↔ 516By similarity
    Disulfide bondi504 ↔ 512By similarity
    Disulfide bondi525 ↔ 544By similarity
    Disulfide bondi531 ↔ 563By similarity
    Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi556 ↔ 568By similarity
    Disulfide bondi573 ↔ 599By similarity
    Disulfide bondi581 ↔ 608By similarity
    Disulfide bondi583 ↔ 598By similarity
    Disulfide bondi595 ↔ 640By similarity
    Disulfide bondi633 ↔ 646By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiO35598.
    PaxDbiO35598.
    PRIDEiO35598.

    PTM databases

    PhosphoSiteiO35598.

    Expressioni

    Developmental stagei

    Widely expressed in the nervous system at 18 dpc, with high expression in the posterior midbrain, which diminished toward the anterior midbrain.

    Gene expression databases

    ArrayExpressiO35598.
    BgeeiO35598.
    CleanExiMM_ADAM10.
    GenevestigatoriO35598.

    Interactioni

    Subunit structurei

    Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function, the cleavage occurs in trans, with ADAM10 and its substrate being on the membranes of opposing cells By similarity. Interacts with EPHA2.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi197960. 2 interactions.
    IntActiO35598. 1 interaction.
    MINTiMINT-4086890.
    STRINGi10090.ENSMUSP00000063839.

    Structurei

    3D structure databases

    ProteinModelPortaliO35598.
    SMRiO35598. Positions 220-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 673654ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini695 – 74955CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei674 – 69421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini221 – 457237Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini458 – 55295DisintegrinPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi171 – 1788Cysteine switchBy similarity
    Motifi709 – 7168SH3-bindingSequence Analysis
    Motifi723 – 7297SH3-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi553 – 673121Cys-richAdd
    BLAST

    Domaini

    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
    The Cys-rich region C-terminal to the disintegrin domain functions as a substrate-recognition module, it recognizes the EFNA5-EPHA3 Complex but not the individual proteins.By similarity

    Sequence similaritiesi

    Contains 1 disintegrin domain.PROSITE-ProRule annotation
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG271989.
    GeneTreeiENSGT00670000097974.
    HOGENOMiHOG000008148.
    HOVERGENiHBG050455.
    InParanoidiO35598.
    KOiK06704.
    OMAiHEDDIKY.
    OrthoDBiEOG7SBNNQ.
    TreeFamiTF352021.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProiIPR027053. ADAM_10.
    IPR001762. Blood-coag_inhib_Disintegrin.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view]
    PANTHERiPTHR11905:SF113. PTHR11905:SF113. 1 hit.
    PfamiPF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    [Graphical view]
    SMARTiSM00050. DISIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF57552. SSF57552. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O35598-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLPTVLILL LSWAAGLGGQ YGNPLNKYIR HYEGLSYNVD SLHQKHQRAK    50
    RAVSHEDQFL LLDFHAHGRQ FNLRMKRDTS LFSDEFKVET SNKVLDYDTS 100
    HIYTGHIYGE EGSFSHGSVI DGRFEGFIKT RGGTFYIEPA ERYIKDRILP 150
    FHSVIYHEDD INYPHKYGPQ GGCADHSVFE RMRKYQMTGV EEGARAHPEK 200
    HAASSGPELL RKKRTTLAER NTCQLYIQTD HLFFKYYGTR EAVIAQISSH 250
    VKAIDTIYQT TDFSGIRNIS FMVKRIRINT TSDEKDPTNP FRFPNIGVEK 300
    FLELNSEQNH DDYCLAYVFT DRDFDDGVLG LAWVGAPSGS SGGICEKSKL 350
    YSDGKKKSLN TGIITVQNYG SHVPPKVSHI TFAHEVGHNF GSPHDSGTEC 400
    TPGESKNLGQ KENGNYIMYA RATSGDKLNN NKFSLCSIRN ISQVLEKKRN 450
    NCFVESGQPI CGNGMVEQGE ECDCGYSDQC KDDCCFDANQ PEGKKCKLKP 500
    GKQCSPSQGP CCTAQCAFKS KSEKCRDDSD CAKEGICNGF TALCPASDPK 550
    PNFTDCNRHT QVCINGQCAG SICEKYDLEE CTCASSDGKD DKELCHVCCM 600
    KKMAPSTCAS TGSLQWSKQF SGRTITLQPG SPCNDFRGYC DVFMRCRLVD 650
    ADGPLARLKK AIFSPQLYEN IAEWIVAHWW AVLLMGIALI MLMAGFIKIC 700
    SVHTPSSNPK LPPPKPLPGT LKRRRPPQPI QQPPRQRPRE SYQMGHMRR 749
    Length:749
    Mass (Da):83,968
    Last modified:July 27, 2011 - v2
    Checksum:i6AA2230B2251ABDA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti591 – 5911D → N in AAC53303. (PubMed:9244301)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011379 mRNA. Translation: AAC53303.1.
    CT025701, AC091263, AC160636 Genomic DNA. Translation: CAX15709.1.
    CH466522 Genomic DNA. Translation: EDL26211.1.
    AK036883 mRNA. Translation: BAC29620.1.
    AK036599 mRNA. Translation: BAC29502.1.
    CCDSiCCDS23323.1.
    RefSeqiNP_031425.2. NM_007399.3.
    UniGeneiMm.3037.

    Genome annotation databases

    EnsembliENSMUST00000067880; ENSMUSP00000063839; ENSMUSG00000054693.
    GeneIDi11487.
    KEGGimmu:11487.
    UCSCiuc009qor.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011379 mRNA. Translation: AAC53303.1 .
    CT025701 , AC091263 , AC160636 Genomic DNA. Translation: CAX15709.1 .
    CH466522 Genomic DNA. Translation: EDL26211.1 .
    AK036883 mRNA. Translation: BAC29620.1 .
    AK036599 mRNA. Translation: BAC29502.1 .
    CCDSi CCDS23323.1.
    RefSeqi NP_031425.2. NM_007399.3.
    UniGenei Mm.3037.

    3D structure databases

    ProteinModelPortali O35598.
    SMRi O35598. Positions 220-647.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197960. 2 interactions.
    IntActi O35598. 1 interaction.
    MINTi MINT-4086890.
    STRINGi 10090.ENSMUSP00000063839.

    Protein family/group databases

    MEROPSi M12.210.

    PTM databases

    PhosphoSitei O35598.

    Proteomic databases

    MaxQBi O35598.
    PaxDbi O35598.
    PRIDEi O35598.

    Protocols and materials databases

    DNASUi 11487.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067880 ; ENSMUSP00000063839 ; ENSMUSG00000054693 .
    GeneIDi 11487.
    KEGGi mmu:11487.
    UCSCi uc009qor.1. mouse.

    Organism-specific databases

    CTDi 102.
    MGIi MGI:109548. Adam10.

    Phylogenomic databases

    eggNOGi NOG271989.
    GeneTreei ENSGT00670000097974.
    HOGENOMi HOG000008148.
    HOVERGENi HBG050455.
    InParanoidi O35598.
    KOi K06704.
    OMAi HEDDIKY.
    OrthoDBi EOG7SBNNQ.
    TreeFami TF352021.

    Enzyme and pathway databases

    Reactomei REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_196638. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
    REACT_196643. Constitutive Signaling by NOTCH1 HD Domain Mutants.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.
    REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_199404. Signaling by NOTCH4.
    REACT_199411. NOTCH2 Activation and Transmission of Signal to the Nucleus.
    REACT_199413. Signaling by NOTCH3.

    Miscellaneous databases

    NextBioi 278848.
    PROi O35598.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35598.
    Bgeei O35598.
    CleanExi MM_ADAM10.
    Genevestigatori O35598.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProi IPR027053. ADAM_10.
    IPR001762. Blood-coag_inhib_Disintegrin.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view ]
    PANTHERi PTHR11905:SF113. PTHR11905:SF113. 1 hit.
    Pfami PF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    [Graphical view ]
    SMARTi SM00050. DISIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57552. SSF57552. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis."
      Pan D., Rubin G.M.
      Cell 90:271-280(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 252-749.
      Strain: C57BL/6J.
      Tissue: Bone and Vagina.
    5. "Regulated cleavage of a contact-mediated axon repellent."
      Hattori M., Osterfield M., Flanagan J.G.
      Science 289:1360-1365(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHA2.
    6. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-279.

    Entry informationi

    Entry nameiADA10_MOUSE
    AccessioniPrimary (citable) accession number: O35598
    Secondary accession number(s): B8JJJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 136 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. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3