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P97927

- LAMA4_MOUSE

UniProt

P97927 - LAMA4_MOUSE

Protein

Laminin subunit alpha-4

Gene

Lama4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (13 Dec 2001)
      Previous versions | rss
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    Functioni

    Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.

    GO - Biological processi

    1. blood vessel development Source: MGI
    2. brown fat cell differentiation Source: MGI
    3. cell adhesion Source: UniProtKB-KW
    4. regulation of cell adhesion Source: InterPro
    5. regulation of cell migration Source: InterPro
    6. regulation of embryonic development Source: InterPro

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_202342. Laminin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit alpha-4
    Alternative name(s):
    Laminin-14 subunit alpha
    Laminin-8 subunit alpha
    Laminin-9 subunit alpha
    Gene namesi
    Name:Lama4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:109321. Lama4.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: MGI
    2. basement membrane Source: MGI
    3. extracellular region Source: Reactome
    4. extracellular vesicular exosome Source: Ensembl
    5. laminin-1 complex Source: InterPro

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 18161792Laminin subunit alpha-4PRO_0000017061Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi82 ↔ 91By similarity
    Disulfide bondi84 ↔ 98By similarity
    Disulfide bondi101 ↔ 110By similarity
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi113 ↔ 129By similarity
    Disulfide bondi132 ↔ 146By similarity
    Disulfide bondi134 ↔ 155By similarity
    Disulfide bondi157 ↔ 166By similarity
    Disulfide bondi169 ↔ 184By similarity
    Disulfide bondi187 ↔ 202By similarity
    Disulfide bondi189 ↔ 209By similarity
    Disulfide bondi212 ↔ 221By similarity
    Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi224 ↔ 238By similarity
    Disulfide bondi266 – 266InterchainCurated
    Disulfide bondi269 – 269InterchainCurated
    Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi550 – 5501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi571 – 5711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi639 – 6391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi735 – 7351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi751 – 7511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi754 – 7541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi780 – 7801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi803 – 8031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1000 ↔ 1030By similarity
    Glycosylationi1088 – 10881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1196 ↔ 1222By similarity
    Glycosylationi1283 – 12831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1361 – 13611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1365 ↔ 1397By similarity
    Disulfide bondi1610 ↔ 1633By similarity
    Disulfide bondi1785 ↔ 1813By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP97927.
    PaxDbiP97927.
    PRIDEiP97927.

    PTM databases

    PhosphoSiteiP97927.

    Expressioni

    Tissue specificityi

    Strongly expressed in peripheral nerves, cardiac muscle, fat, dermis, lung stroma, aortic endothelium, endocardium and endothelium of blood vessels in skin and brain.

    Gene expression databases

    ArrayExpressiP97927.
    BgeeiP97927.
    CleanExiMM_LAMA4.
    GenevestigatoriP97927.

    Interactioni

    Subunit structurei

    Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-4 is a subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and laminin-14 (laminin-423).

    Protein-protein interaction databases

    IntActiP97927. 1 interaction.
    MINTiMINT-4100077.

    Structurei

    3D structure databases

    ProteinModelPortaliP97927.
    SMRiP97927. Positions 9-300, 829-1373, 1450-1815.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini82 – 13150Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini132 – 18655Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini187 – 24054Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini241 – 25515Laminin EGF-like 4; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini826 – 1030205Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1042 – 1222181Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1229 – 1397169Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1462 – 1633172Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1640 – 1813174Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni256 – 825570Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili431 – 52393Sequence AnalysisAdd
    BLAST
    Coiled coili556 – 60449Sequence AnalysisAdd
    BLAST
    Coiled coili655 – 71763Sequence AnalysisAdd
    BLAST
    Coiled coili770 – 79930Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi717 – 7193Cell attachment siteSequence Analysis

    Domaini

    The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
    Domain G is globular.

    Sequence similaritiesi

    Contains 4 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 5 laminin G-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Laminin EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG247347.
    GeneTreeiENSGT00750000117549.
    HOGENOMiHOG000113278.
    HOVERGENiHBG052299.
    InParanoidiQ14BF2.
    KOiK06241.
    OMAiPKPVDHR.
    OrthoDBiEOG7VX8V2.
    PhylomeDBiP97927.
    TreeFamiTF335359.

    Family and domain databases

    Gene3Di2.60.120.200. 5 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR002049. EGF_laminin.
    IPR001791. Laminin_G.
    IPR009254. Laminin_I.
    IPR010307. Laminin_II.
    [Graphical view]
    PfamiPF00053. Laminin_EGF. 3 hits.
    PF02210. Laminin_G_2. 5 hits.
    PF06008. Laminin_I. 1 hit.
    PF06009. Laminin_II. 1 hit.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 3 hits.
    SM00282. LamG. 5 hits.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 6 hits.
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01248. EGF_LAM_1. 3 hits.
    PS50027. EGF_LAM_2. 3 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P97927-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGWSTAWCSV LALWLLWCAV CSNAASGDGN AFPFDIEGSA VVGRQDPSET     50
    SDSGVTLGRL PPAAERCDAG FFRTLSGECA PCDCNGNSHE CLDGSGFCLH 100
    CQRNTTGEHC EKCLDGYIGD SIRGTPRFCQ PCPCPLPHLA NFAESCYRKN 150
    GAVRCICKEN YVGPNCERCA PGYYGNPLLI GSTCKKCDCS GNSDPNLIFE 200
    DCDEITGQCR NCLRNTTGFK CERCAPGYYG DARTAKNCAV CNCGGGPCDS 250
    VTGECLEEGF EVPTGCDKCV WDLTDDLRLA ALSIEESKSG LLSVSSGAAA 300
    HRHVTDMNST IHLLRTRLSE RENQYTLRKI QINNSENTLR SLLPDVEGLH 350
    EKGSQASRKG MLVEKESMDT IDQATHLVEQ AHNMRDKIQE INSKMLYYGE 400
    NQELGPEEIA EKLVLAQKML EEIRSRQPFL THRELVDEEA DEAQELLSQA 450
    ENWQRLHNDT RSLFPVVLEQ LDDYNAKLSD LQESINQALD HVRDAEDMNR 500
    AITFKQRDHE KQHERVKEQM EVVGASLSMS ADSLTIPQLT LEELDEIIKN 550
    ASGIYAEIDG AKNELQGKLS NLSNLSHDLV QEATDHAYNL QQEADELSRN 600
    LHSSDMNGLV QKALDASNVY ENIANYVSEA NETAELALNI TDRIYDAVSG 650
    IDTQIIYHKD ESDNLLNQAR ELQAKADSSN DEAVADTSRR VGGALWRKGA 700
    LRDRLNDAVK QLQAAERGDA HQRLGQSKLF IEEANKTTAA VQQVTTPMAN 750
    NLSNWSQNLQ TFDSSAYNTA VDSARDAVRN LTEVVPQLLD QLRTVEQKRP 800
    ASNISASIQR IRELIAQTRS VASKIQVSMM FDGQSAVEVH PKVSVDDLKA 850
    FTSISLYMKP PPKPAEPTGA WVADQFVLYL GSKNAKKEYM GLAIKNDNLV 900
    YVYNLGMKDV EILLDSKPVS SWPAYFSIVK IERVGKHGKV FLTVPSLSST 950
    AEEKFIKKGE FAGDDSLLDL TPEDTVFYVG GVPANFKLPA SLNLPSYSGC 1000
    LELATLNNDV ISLYNFKHIY NMDPSKSVPC ARDKLAFTQS RAASYFFDGS 1050
    SYAVVRDITR RGKFGQVTRF DIEIRTPADN GLVLLMVNGS MFFSLEMRNG 1100
    YLHVFYDFGF SNGPVHLEDT LKKAQINDAK YHEISIIYHN DKKMILVVDR 1150
    RHVKSTDNEK KKIPFTDIYI GGAPQEVLQS RTLRAHLPLD INFRGCMKGF 1200
    QFQKKDFNLL EQTETLGVGY GCPEDSLISR RAYFNGQSFI ASIQKISFFD 1250
    GFEGGFNFRT LQPNGLLFYY TSGSDVFSIS LDNGTVVMDV KGIKVMSTDK 1300
    QYHDGLPHFV VTSISDTRYE LVVDKSRLRG KNPTKGKAEQ TQTTEKKFYF 1350
    GGSPISPQYA NFTGCISNAY FTRLDRDVEV EDFQRYSEKV HTSLYECPIE 1400
    SSPLFLLHKK GKNSSKPKTN KQGEKSKDAP SWDPIGLKFL EQKAPRDSHC 1450
    HLSSSPRAIE HAYQYGGTAN SRQEFEHEQG DFGEKSQFAI RLKTRSSHGM 1500
    IFYVSDQEEN DFMTLFLAHG RLVFMFNVGH KKLKIRSQEK YNDGLWHDVI 1550
    FIREKSSGRL VIDGLRVLEE RLPPSGAAWK IKGPIYLGGV APGRAVKNVQ 1600
    ITSVYSFSGC LGNLQLNGAS ITSASQTFSV TPCFEGPMET GTYFSTEGGY 1650
    VVLDESFNIG LKFEIAFEVR PRSSSGTLVH GHSVNGEYLN VHMRNGQVIV 1700
    KVNNGVRDFS TSVTPKQNLC DGRWHRITVI RDSNVVQLDV DSEVNHVVGP 1750
    LNPKPVDHRE PVFVGGVPES LLTPRLAPSK PFTGCIRHFV IDSRPVSFSK 1800
    AALVSGAVSI NSCPTA 1816
    Length:1,816
    Mass (Da):201,819
    Last modified:December 13, 2001 - v2
    Checksum:iB49C45F3A45999D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81C → S in AAC52982. (PubMed:9049981)Curated
    Sequence conflicti18 – 181C → Y(PubMed:9049981)Curated
    Sequence conflicti248 – 2481C → R in AAC24725. (PubMed:9346933)Curated
    Sequence conflicti297 – 2971G → A in AAC24725. (PubMed:9346933)Curated
    Sequence conflicti431 – 4333THR → HPS in AAC52982. (PubMed:9049981)Curated
    Sequence conflicti679 – 6791S → C in AAC24725. (PubMed:9346933)Curated
    Sequence conflicti703 – 7031D → G in AAC52982. (PubMed:9049981)Curated
    Sequence conflicti706 – 7061N → H in AAC52982. (PubMed:9049981)Curated
    Sequence conflicti728 – 7281K → R(PubMed:9049981)Curated
    Sequence conflicti730 – 7301F → I(PubMed:9049981)Curated
    Sequence conflicti779 – 7791R → G AA sequence (PubMed:9219532)Curated
    Sequence conflicti810 – 8101R → S in AAC24725. (PubMed:9346933)Curated
    Sequence conflicti865 – 8673AEP → QT in AAC52982. (PubMed:9049981)Curated
    Sequence conflicti936 – 9361K → E in AAC24725. (PubMed:9346933)Curated
    Sequence conflicti970 – 9701L → V in AAC24725. (PubMed:9346933)Curated
    Sequence conflicti1132 – 11321H → R in AAC52982. (PubMed:9049981)Curated
    Sequence conflicti1200 – 12001F → I in AAC52982. (PubMed:9049981)Curated
    Sequence conflicti1382 – 13821D → A in AAC52982. (PubMed:9049981)Curated
    Sequence conflicti1413 – 14142NS → EF in CAA70970. (PubMed:9219532)Curated
    Sequence conflicti1489 – 14891A → S in AAC52982. (PubMed:9049981)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58950 mRNA. Translation: AAB41840.1.
    Y09827 mRNA. Translation: CAA70970.1.
    U59865 mRNA. Translation: AAC24725.1.
    BC115942 mRNA. Translation: AAI15943.1.
    U88352 mRNA. Translation: AAC53178.1.
    U69176 mRNA. Translation: AAC52982.1.
    CCDSiCCDS35882.1.
    RefSeqiNP_034811.2. NM_010681.4.
    UniGeneiMm.258065.

    Genome annotation databases

    EnsembliENSMUST00000019992; ENSMUSP00000019992; ENSMUSG00000019846.
    GeneIDi16775.
    KEGGimmu:16775.
    UCSCiuc007evq.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58950 mRNA. Translation: AAB41840.1 .
    Y09827 mRNA. Translation: CAA70970.1 .
    U59865 mRNA. Translation: AAC24725.1 .
    BC115942 mRNA. Translation: AAI15943.1 .
    U88352 mRNA. Translation: AAC53178.1 .
    U69176 mRNA. Translation: AAC52982.1 .
    CCDSi CCDS35882.1.
    RefSeqi NP_034811.2. NM_010681.4.
    UniGenei Mm.258065.

    3D structure databases

    ProteinModelPortali P97927.
    SMRi P97927. Positions 9-300, 829-1373, 1450-1815.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97927. 1 interaction.
    MINTi MINT-4100077.

    PTM databases

    PhosphoSitei P97927.

    Proteomic databases

    MaxQBi P97927.
    PaxDbi P97927.
    PRIDEi P97927.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000019992 ; ENSMUSP00000019992 ; ENSMUSG00000019846 .
    GeneIDi 16775.
    KEGGi mmu:16775.
    UCSCi uc007evq.2. mouse.

    Organism-specific databases

    CTDi 3910.
    MGIi MGI:109321. Lama4.

    Phylogenomic databases

    eggNOGi NOG247347.
    GeneTreei ENSGT00750000117549.
    HOGENOMi HOG000113278.
    HOVERGENi HBG052299.
    InParanoidi Q14BF2.
    KOi K06241.
    OMAi PKPVDHR.
    OrthoDBi EOG7VX8V2.
    PhylomeDBi P97927.
    TreeFami TF335359.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_202342. Laminin interactions.

    Miscellaneous databases

    ChiTaRSi LAMA4. mouse.
    NextBioi 290616.
    PROi P97927.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97927.
    Bgeei P97927.
    CleanExi MM_LAMA4.
    Genevestigatori P97927.

    Family and domain databases

    Gene3Di 2.60.120.200. 5 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR002049. EGF_laminin.
    IPR001791. Laminin_G.
    IPR009254. Laminin_I.
    IPR010307. Laminin_II.
    [Graphical view ]
    Pfami PF00053. Laminin_EGF. 3 hits.
    PF02210. Laminin_G_2. 5 hits.
    PF06008. Laminin_I. 1 hit.
    PF06009. Laminin_II. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 3 hits.
    SM00282. LamG. 5 hits.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 6 hits.
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01248. EGF_LAM_1. 3 hits.
    PS50027. EGF_LAM_2. 3 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium."
      Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R., Sorokin L.M.
      Eur. J. Biochem. 246:727-735(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 462-469; 478-483; 776-782 AND 940-945.
      Strain: BALB/c.
      Tissue: Endothelial cell.
    2. "The complete cDNA coding sequence and tissue-specific expression of the mouse laminin alpha 4 chain."
      Liu J., Mayne R.
      Matrix Biol. 15:433-437(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    3. "Primary structure, developmental expression, and immunolocalization of the murine laminin alpha4 chain."
      Iivanainen A., Kortesmaa J., Sahlberg C., Morita T., Bergmann U., Thesleff I., Tryggvason K.
      J. Biol. Chem. 272:27862-27868(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    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].
    5. "The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform."
      Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D., Jenkins N.A., Copeland N.G., Sanes J.R.
      J. Cell Biol. 137:685-701(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 836-1106.
      Strain: ICR.
      Tissue: Placenta.
    6. "Distribution of the ten known laminin chains in the pathways and targets of developing sensory axons."
      Lentz S.I., Miner J.H., Sanes J.R., Snider W.D.
      J. Comp. Neurol. 378:547-561(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1467-1691.
      Tissue: Placenta.

    Entry informationi

    Entry nameiLAMA4_MOUSE
    AccessioniPrimary (citable) accession number: P97927
    Secondary accession number(s): O88785, P70409, Q14BF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: December 13, 2001
    Last modified: October 1, 2014
    This is version 130 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, Direct protein sequencing, 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