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P05784

- K1C18_MOUSE

UniProt

P05784 - K1C18_MOUSE

Protein

Keratin, type I cytoskeletal 18

Gene

Krt18

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 5 (29 May 2007)
      Previous versions | rss
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    Functioni

    When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells By similarity. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei231 – 2322Cleavage; by caspase-3, caspase-6 or caspase-7
    Sitei264 – 2641Stutter
    Sitei324 – 3241Stutter

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. extrinsic apoptotic signaling pathway Source: MGI
    2. Golgi to plasma membrane CFTR protein transport Source: Ensembl
    3. hepatocyte apoptotic process Source: MGI
    4. negative regulation of apoptotic process Source: Ensembl
    5. tumor necrosis factor-mediated signaling pathway Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Keratin, type I cytoskeletal 18
    Alternative name(s):
    Cytokeratin endo B
    Short name:
    Keratin D
    Cytokeratin-18
    Short name:
    CK-18
    Keratin-18
    Short name:
    K18
    Gene namesi
    Name:Krt18
    Synonyms:Kerd, Krt1-18
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:96692. Krt18.

    Subcellular locationi

    Nucleus matrix By similarity. Nucleusnucleolus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cell periphery Source: MGI
    2. centriolar satellite Source: Ensembl
    3. intermediate filament Source: MGI
    4. keratin filament Source: MGI
    5. nuclear matrix Source: UniProtKB-SubCell
    6. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Intermediate filament, Keratin, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 423422Keratin, type I cytoskeletal 18PRO_0000063667Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei7 – 71PhosphoserineBy similarity
    Modified residuei11 – 111PhosphoserineBy similarity
    Modified residuei16 – 161PhosphoserineBy similarity
    Modified residuei19 – 191PhosphoserineBy similarity
    Modified residuei31 – 311Phosphoserine; alternate2 Publications
    Glycosylationi31 – 311O-linked (GlcNAc); alternateBy similarity
    Modified residuei32 – 321Phosphoserine; alternate2 Publications
    Glycosylationi32 – 321O-linked (GlcNAc); alternateBy similarity
    Modified residuei35 – 351Phosphoserine2 Publications
    Modified residuei37 – 371PhosphotyrosineBy similarity
    Modified residuei43 – 431PhosphoserineBy similarity
    Glycosylationi50 – 501O-linked (GlcNAc)By similarity
    Modified residuei52 – 521Phosphoserine; by MAPKAPK2 and MAPKAPK32 Publications
    Modified residuei60 – 601PhosphoserineBy similarity
    Modified residuei92 – 921PhosphoserineBy similarity
    Modified residuei124 – 1241N6-acetyllysineBy similarity
    Modified residuei170 – 1701PhosphoserineBy similarity
    Modified residuei295 – 2951PhosphothreonineBy similarity
    Modified residuei316 – 3161Phosphoserine2 Publications
    Modified residuei392 – 3921PhosphoserineBy similarity
    Modified residuei397 – 3971PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation increases by IL-6.3 Publications
    Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspas-6 or caspase-7.1 Publication
    O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP05784.
    PaxDbiP05784.
    PRIDEiP05784.

    2D gel databases

    SWISS-2DPAGEP05784.

    PTM databases

    PhosphoSiteiP05784.

    Expressioni

    Tissue specificityi

    Expressed in endoderm, intestinal epithelial cells and in most extraembryonic tissues.4 Publications

    Developmental stagei

    During embryogenesis, expressed in a complex spatial and temporal pattern in various embryonic epithelia. In 7.5 and 13.5 day old embryo, expressed in most endodermal epithelia, ectodermal and nascent mesodermal tissues. When the neural plate forms, expression begins in the cells of skin ectoderm, head process/notochord, periderm, whisker buds, choroid plexus and the epithelia of auditory duct and inner ear. High expression in the lining endodermal cells when the foregut and hindgut invaginations form. Expression in all three layers of the urothelium starts at day 15 in the embryo and is not visible after day 18. By day 11 and 12, the entire embryonic palatal epithelium shows expression as well as the nasal passages and the roof of the mouth; which disappears progresively from day 13 to 15.3 Publications

    Inductioni

    By retinoic acid and IL-6.2 Publications

    Gene expression databases

    BgeeiP05784.
    CleanExiMM_KRT18.
    GenevestigatoriP05784.

    Interactioni

    Subunit structurei

    Heterotetramer of two type I and two type II keratins. KRT18 associates with KRT8. Interacts with PNN, HCV core protein and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when phosphorylated. Interacts with the thrombin-antithrombin complex. Interacts with DNAJB6, TCHP and TRADD By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201023. 1 interaction.
    IntActiP05784. 4 interactions.
    MINTiMINT-1866927.

    Structurei

    3D structure databases

    ProteinModelPortaliP05784.
    SMRiP05784. Positions 122-221, 290-378.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 7170HeadAdd
    BLAST
    Regioni62 – 366305Necessary for interaction with PNNBy similarityAdd
    BLAST
    Regioni69 – 12153Interaction with TRADDBy similarityAdd
    BLAST
    Regioni72 – 380309RodAdd
    BLAST
    Regioni72 – 10736Coil 1AAdd
    BLAST
    Regioni108 – 12518Linker 1Add
    BLAST
    Regioni126 – 21792Coil 1BAdd
    BLAST
    Regioni218 – 24124Linker 12Add
    BLAST
    Regioni236 – 384149Interaction with DNAJB6By similarityAdd
    BLAST
    Regioni242 – 380139Coil 2Add
    BLAST
    Regioni381 – 42343TailAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG150427.
    GeneTreeiENSGT00740000115001.
    HOGENOMiHOG000230975.
    HOVERGENiHBG013015.
    InParanoidiP05784.
    KOiK07604.
    OMAiRAKYEKM.
    OrthoDBiEOG7V1FR3.
    PhylomeDBiP05784.
    TreeFamiTF332742.

    Family and domain databases

    InterProiIPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR027695. Keratin-18.
    IPR002957. Keratin_I.
    [Graphical view]
    PANTHERiPTHR23239. PTHR23239. 1 hit.
    PTHR23239:SF35. PTHR23239:SF35. 1 hit.
    PfamiPF00038. Filament. 1 hit.
    [Graphical view]
    PRINTSiPR01248. TYPE1KERATIN.
    PROSITEiPS00226. IF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P05784-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFTTRSTTF STNYRSLGSV RTPSQRVRPA SSAASVYAGA GGSGSRISVS    50
    RSVWGGSVGS AGLAGMGGIQ TEKETMQDLN DRLASYLDKV KSLETENRRL 100
    ESKIREHLEK KGPQGVRDWG HYFKIIEDLR AQIFANSVDN ARIVLQIDNA 150
    RLAADDFRVK YETELAMRQS VESDIHGLRK VVDDTNITRL QLETEIEALK 200
    EELLFMKKNH EEEVQGLEAQ IASSGLTVEV DAPKSQDLSK IMADIRAQYE 250
    ALAQKNREEL DKYWSQQIEE STTVVTTKSA EIRDAETTLT ELRRTLQTLE 300
    IDLDSMKNQN INLENSLGDV EARYKAQMEQ LNGVLLHLES ELAQTRAEGQ 350
    RQAQEYEALL NIKVKLEAEI ATYRRLLEDG EDFSLNDALD SSNSMQTVQK 400
    TTTRKIVDGR VVSETNDTRV LRH 423
    Length:423
    Mass (Da):47,538
    Last modified:May 29, 2007 - v5
    Checksum:iA67ACD6814A02118
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341F → L in AAA39390. (PubMed:2416755)Curated
    Sequence conflicti134 – 1341F → L in AAA39373. 1 PublicationCurated
    Sequence conflicti214 – 2141V → A in BAE26424. (PubMed:16141072)Curated
    Sequence conflicti214 – 2141V → A in BAE39378. (PubMed:16141072)Curated
    Sequence conflicti244 – 2441D → N in AAA39373. 1 PublicationCurated
    Sequence conflicti253 – 2531A → G in AAA39373. 1 PublicationCurated
    Sequence conflicti300 – 3001E → G in BAE39725. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11686 mRNA. Translation: AAA39390.1.
    M36376 mRNA. Translation: AAA39373.1.
    M22832 Genomic DNA. Translation: AAA37552.1.
    AK145413 mRNA. Translation: BAE26424.1.
    AK167072 mRNA. Translation: BAE39232.1.
    AK167265 mRNA. Translation: BAE39378.1.
    AK167432 mRNA. Translation: BAE39519.1.
    AK167469 mRNA. Translation: BAE39553.1.
    AK167676 mRNA. Translation: BAE39725.1.
    BC089022 mRNA. Translation: AAH89022.1.
    Y00217 Genomic DNA. Translation: CAA68365.1.
    CCDSiCCDS27869.1.
    PIRiI59463.
    RefSeqiNP_034794.2. NM_010664.2.
    UniGeneiMm.22479.

    Genome annotation databases

    EnsembliENSMUST00000023803; ENSMUSP00000023803; ENSMUSG00000023043.
    GeneIDi16668.
    KEGGimmu:16668.
    UCSCiuc007xuj.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11686 mRNA. Translation: AAA39390.1 .
    M36376 mRNA. Translation: AAA39373.1 .
    M22832 Genomic DNA. Translation: AAA37552.1 .
    AK145413 mRNA. Translation: BAE26424.1 .
    AK167072 mRNA. Translation: BAE39232.1 .
    AK167265 mRNA. Translation: BAE39378.1 .
    AK167432 mRNA. Translation: BAE39519.1 .
    AK167469 mRNA. Translation: BAE39553.1 .
    AK167676 mRNA. Translation: BAE39725.1 .
    BC089022 mRNA. Translation: AAH89022.1 .
    Y00217 Genomic DNA. Translation: CAA68365.1 .
    CCDSi CCDS27869.1.
    PIRi I59463.
    RefSeqi NP_034794.2. NM_010664.2.
    UniGenei Mm.22479.

    3D structure databases

    ProteinModelPortali P05784.
    SMRi P05784. Positions 122-221, 290-378.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201023. 1 interaction.
    IntActi P05784. 4 interactions.
    MINTi MINT-1866927.

    PTM databases

    PhosphoSitei P05784.

    2D gel databases

    SWISS-2DPAGE P05784.

    Proteomic databases

    MaxQBi P05784.
    PaxDbi P05784.
    PRIDEi P05784.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023803 ; ENSMUSP00000023803 ; ENSMUSG00000023043 .
    GeneIDi 16668.
    KEGGi mmu:16668.
    UCSCi uc007xuj.2. mouse.

    Organism-specific databases

    CTDi 3875.
    MGIi MGI:96692. Krt18.

    Phylogenomic databases

    eggNOGi NOG150427.
    GeneTreei ENSGT00740000115001.
    HOGENOMi HOG000230975.
    HOVERGENi HBG013015.
    InParanoidi P05784.
    KOi K07604.
    OMAi RAKYEKM.
    OrthoDBi EOG7V1FR3.
    PhylomeDBi P05784.
    TreeFami TF332742.

    Miscellaneous databases

    ChiTaRSi KRT18. mouse.
    NextBioi 290387.
    PROi P05784.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05784.
    CleanExi MM_KRT18.
    Genevestigatori P05784.

    Family and domain databases

    InterProi IPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR027695. Keratin-18.
    IPR002957. Keratin_I.
    [Graphical view ]
    PANTHERi PTHR23239. PTHR23239. 1 hit.
    PTHR23239:SF35. PTHR23239:SF35. 1 hit.
    Pfami PF00038. Filament. 1 hit.
    [Graphical view ]
    PRINTSi PR01248. TYPE1KERATIN.
    PROSITEi PS00226. IF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the Endo B cytokeratin expressed in preimplantation mouse embryos."
      Singer P.A., Trevor K., Oshima R.G.
      J. Biol. Chem. 261:538-547(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
      Tissue: Endoderm.
    2. "Cloning and characterization of keratin D, a murine endodermal cytoskeletal protein induced during in vitro differentiation of F9 teratocarcinoma cells."
      Alonso A., Weber T., Jorcano J.L.
      Roux's Arch. Dev. Biol. 196:16-21(1987)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Teratocarcinoma.
    3. "Nucleotide sequence and structure of the mouse cytokeratin endoB gene."
      Ichinose Y., Morita T., Zhang F., Srimahasongcram S., Tondella M.L.C., Matsumoto M., Nozaki M., Matsushiro A.
      Gene 70:85-95(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
      Tissue: Liver.
    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].
      Strain: C57BL/6J.
      Tissue: Blastocyst, Embryo and Placenta.
    5. "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: Eye.
    6. "Identification of the gene coding for the Endo B murine cytokeratin and its methylated, stable inactive state in mouse nonepithelial cells."
      Oshima R.G., Trevor K., Shevinsky L.H., Ryder O.A., Cecena G.
      Genes Dev. 2:505-516(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132, TISSUE SPECIFICITY.
    7. "Embryonic expression of human keratin 18 and K18-beta-galactosidase fusion genes in transgenic mice."
      Thorey I.S., Meneses J.J., Neznanov N., Kulesh D.A., Pedersen R.A., Oshima R.G.
      Dev. Biol. 160:519-534(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    8. "Monoclonal antibodies recognising stage and region specific epitopes in embryonic mouse palatal epithelial cells."
      Dixon M.J., Robinson V., White A., Ferguson M.W.
      J. Anat. 183:423-438(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    9. "Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis."
      Caulin C., Salvesen G.S., Oshima R.G.
      J. Cell Biol. 138:1379-1394(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY CASPASES.
    10. "Superficial cell differentiation during embryonic and postnatal development of mouse urothelium."
      Erman A., Veranic P., Psenicnik M., Jezernik K.
      Tissue Cell 38:293-301(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    11. "Interleukin-6 induces keratin expression in intestinal epithelial cells: potential role of keratin-8 in interleukin-6-induced barrier function alterations."
      Wang L., Srinivasan S., Theiss A.L., Merlin D., Sitaraman S.V.
      J. Biol. Chem. 282:8219-8227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INDUCTION.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-32; SER-35 AND SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate epithelial keratins."
      Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O., Seidler U., Omary M.B., Kotlyarov A., Gaestel M.
      J. Biol. Chem. 285:33242-33251(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-52 BY MAPKAPK2 AND MAPKAPK3.

    Entry informationi

    Entry nameiK1C18_MOUSE
    AccessioniPrimary (citable) accession number: P05784
    Secondary accession number(s): Q3TIX1
    , Q3TJH6, Q3TJW7, Q61766
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

    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