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P52293

- IMA1_MOUSE

UniProt

P52293 - IMA1_MOUSE

Protein

Importin subunit alpha-1

Gene

Kpna2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein transporter activity Source: InterPro

    GO - Biological processi

    1. protein import into nucleus Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Importin subunit alpha-1
    Alternative name(s):
    Importin alpha P1
    Karyopherin subunit alpha-2
    Pendulin
    Pore targeting complex 58 kDa subunit
    Short name:
    PTAC58
    RAG cohort protein 1
    SRP1-alpha
    Gene namesi
    Name:Kpna2
    Synonyms:Rch1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:103561. Kpna2.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 529528Importin subunit alpha-1PRO_0000120723Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei62 – 621PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP52293.
    PaxDbiP52293.
    PRIDEiP52293.

    PTM databases

    PhosphoSiteiP52293.

    Expressioni

    Tissue specificityi

    Slightly detected in brain but not in cerebellum and skeletal muscle, highly expressed in testis and spleen.

    Gene expression databases

    BgeeiP52293.
    CleanExiMM_KPNA2.
    GenevestigatoriP52293.

    Interactioni

    Subunit structurei

    Heterodimer; with KPNB1 By similarity. Component of a complex containing CSE1L, RAN and KPNA2. Interacts directly with CSE1L. Interacts with PLAG1. Interacts with APEX1 (via N-terminus). Interacts with FRG1 (via N-terminus) By similarity. Interacts with ARL4A, CTNNBL1 and NBN By similarity. Interacts with ANP32E. Interacts with SNAI1 (via zinc fingers). Interacts with SNAI2 (via zinc fingers) By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P030703EBI-3043908,EBI-617698From a different organism.
    IfngP015805EBI-3043908,EBI-7892102
    S100A2P290342EBI-3043908,EBI-752230From a different organism.
    TNPO1Q3SYU73EBI-3043908,EBI-8469003From a different organism.

    Protein-protein interaction databases

    BioGridi201007. 12 interactions.
    IntActiP52293. 9 interactions.

    Structurei

    Secondary structure

    1
    529
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi71 – 733
    Helixi78 – 858
    Beta strandi86 – 883
    Helixi90 – 10415
    Beta strandi106 – 1083
    Helixi112 – 1176
    Helixi120 – 1289
    Helixi131 – 1333
    Helixi134 – 14815
    Helixi152 – 1609
    Helixi163 – 1708
    Helixi176 – 19015
    Helixi194 – 2029
    Helixi206 – 2127
    Helixi218 – 2203
    Helixi223 – 23715
    Helixi246 – 25914
    Helixi265 – 27814
    Beta strandi280 – 2823
    Helixi283 – 2908
    Turni291 – 2933
    Helixi295 – 3028
    Helixi307 – 32014
    Helixi325 – 3339
    Helixi336 – 3394
    Helixi340 – 3434
    Helixi349 – 36214
    Helixi367 – 3759
    Helixi378 – 38710
    Helixi391 – 40717
    Helixi410 – 4189
    Helixi422 – 4276
    Helixi428 – 4303
    Helixi434 – 45421
    Helixi457 – 46610
    Helixi469 – 4768
    Beta strandi479 – 4813
    Helixi482 – 49514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EJLX-ray2.80I70-529[»]
    1EJYX-ray2.90I70-529[»]
    1IALX-ray2.50A44-496[»]
    1IQ1X-ray2.80A/B44-54[»]
    C70-529[»]
    1PJMX-ray2.50B70-529[»]
    1PJNX-ray2.50B70-529[»]
    1Q1SX-ray2.30C70-529[»]
    1Q1TX-ray2.50C70-529[»]
    1Y2AX-ray2.20C70-497[»]
    2C1MX-ray2.20A75-498[»]
    2YNRX-ray2.30A72-496[»]
    3BTRX-ray2.60C70-496[»]
    3KNDX-ray2.15A70-529[»]
    3L3QX-ray2.30A71-497[»]
    3OQSX-ray2.00A70-529[»]
    3Q5UX-ray2.50A70-529[»]
    3RZ9X-ray2.29A70-529[»]
    3RZXX-ray2.61A70-529[»]
    3TPMX-ray2.10A75-496[»]
    3TPOX-ray2.10A1-529[»]
    3UKWX-ray2.10B70-529[»]
    3UKXX-ray2.20B70-529[»]
    3UKYX-ray2.35B70-529[»]
    3UKZX-ray2.30B70-529[»]
    3UL0X-ray2.00B70-529[»]
    3UL1X-ray1.90B70-529[»]
    3UVUX-ray2.38A70-529[»]
    3VE6X-ray2.83A71-496[»]
    3ZINX-ray2.00A72-496[»]
    3ZIOX-ray2.10A72-496[»]
    3ZIPX-ray2.40A72-497[»]
    3ZIQX-ray2.10A72-497[»]
    3ZIRX-ray2.30A72-497[»]
    4BA3X-ray2.10A70-529[»]
    4HTVX-ray3.00A70-528[»]
    4MZ5X-ray2.10E70-528[»]
    4MZ6X-ray1.88E70-528[»]
    4OIHX-ray2.10A70-529[»]
    ProteinModelPortaliP52293.
    SMRiP52293. Positions 11-497.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52293.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 6059IBBPROSITE-ProRule annotationAdd
    BLAST
    Repeati71 – 11141ARM 1; truncatedAdd
    BLAST
    Repeati112 – 15140ARM 2Add
    BLAST
    Repeati152 – 19342ARM 3Add
    BLAST
    Repeati200 – 24445ARM 4Add
    BLAST
    Repeati246 – 28237ARM 5Add
    BLAST
    Repeati283 – 32240ARM 6Add
    BLAST
    Repeati325 – 36440ARM 7Add
    BLAST
    Repeati367 – 40943ARM 8Add
    BLAST
    Repeati410 – 45647ARM 9Add
    BLAST
    Repeati457 – 49640ARM 10; atypicalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni142 – 23897NLS binding site (major)Add
    BLAST
    Regioni315 – 40389NLS binding site (minor)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi45 – 5410Nuclear localization signal2 Publications

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi28 – 314Poly-Arg
    Compositional biasi499 – 5024Poly-Glu

    Domaini

    Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.
    The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins.
    The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding.

    Sequence similaritiesi

    Belongs to the importin alpha family.Curated
    Contains 10 ARM repeats.PROSITE-ProRule annotation
    Contains 1 IBB domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5064.
    HOGENOMiHOG000167616.
    HOVERGENiHBG001846.
    InParanoidiP52293.
    KOiK15043.
    OMAiNETEKLC.
    OrthoDBiEOG7VHSWV.
    PhylomeDBiP52293.
    TreeFamiTF101178.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR002652. Importin-a_IBB.
    IPR024931. Importing_su_alpha.
    [Graphical view]
    PfamiPF00514. Arm. 8 hits.
    PF01749. IBB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005673. Importin_alpha. 1 hit.
    SMARTiSM00185. ARM. 8 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50176. ARM_REPEAT. 6 hits.
    PS51214. IBB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P52293-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNENANLP AARLNRFKNK GKDSTEMRRR RIEVNVELRK AKKDEQMLKR    50
    RNVSSFPDDA TSPLQENRNN QGTVNWSVED IVKGINSNNL ESQLQATQAA 100
    RKLLSREKQP PIDNIIRAGL IPKFVSFLGK TDCSPIQFES AWALTNIASG 150
    TSEQTKAVVD GGAIPAFISL LASPHAHISE QAVWALGNIA GDGSAFRDLV 200
    IKHGAIDPLL ALLAVPDLST LACGYLRNLT WTLSNLCRNK NPAPPLDAVE 250
    QILPTLVRLL HHNDPEVLAD SCWAISYLTD GPNERIEMVV KKGVVPQLVK 300
    LLGATELPIV TPALRAIGNI VTGTDEQTQK VIDAGALAVF PSLLTNPKTN 350
    IQKEATWTMS NITAGRQDQI QQVVNHGLVP FLVGVLSKAD FKTQKEAAWA 400
    ITNYTSGGTV EQIVYLVHCG IIEPLMNLLS AKDTKIIQVI LDAISNIFQA 450
    AEKLGETEKL SIMIEECGGL DKIEALQRHE NESVYKASLN LIEKYFSVEE 500
    EEDQNVVPET TSEGFAFQVQ DGAPGTFNF 529
    Length:529
    Mass (Da):57,928
    Last modified:November 1, 1997 - v2
    Checksum:i19E64AA3E9C3C7B5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti242 – 2421P → S in AAA85281. (PubMed:7565597)Curated
    Sequence conflicti418 – 4181H → P in AAA85281. (PubMed:7565597)Curated
    Sequence conflicti420 – 4201G → R in AAA85281. (PubMed:7565597)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D55720 mRNA. Translation: BAA09536.1.
    U12270 mRNA. Translation: AAA85281.1.
    U34229 mRNA. Translation: AAC52451.1.
    BC003274 mRNA. Translation: AAH03274.1.
    BC006720 mRNA. Translation: AAH06720.1.
    CCDSiCCDS25565.1.
    PIRiS57345.
    S57873.
    S62116.
    RefSeqiNP_034785.1. NM_010655.3.
    UniGeneiMm.12508.
    Mm.391577.
    Mm.423000.

    Genome annotation databases

    EnsembliENSMUST00000018506; ENSMUSP00000018506; ENSMUSG00000018362.
    ENSMUST00000086423; ENSMUSP00000137310; ENSMUSG00000066878.
    ENSMUST00000091289; ENSMUSP00000137080; ENSMUSG00000069083.
    GeneIDi16647.
    KEGGimmu:16647.
    UCSCiuc007lzz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D55720 mRNA. Translation: BAA09536.1 .
    U12270 mRNA. Translation: AAA85281.1 .
    U34229 mRNA. Translation: AAC52451.1 .
    BC003274 mRNA. Translation: AAH03274.1 .
    BC006720 mRNA. Translation: AAH06720.1 .
    CCDSi CCDS25565.1.
    PIRi S57345.
    S57873.
    S62116.
    RefSeqi NP_034785.1. NM_010655.3.
    UniGenei Mm.12508.
    Mm.391577.
    Mm.423000.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EJL X-ray 2.80 I 70-529 [» ]
    1EJY X-ray 2.90 I 70-529 [» ]
    1IAL X-ray 2.50 A 44-496 [» ]
    1IQ1 X-ray 2.80 A/B 44-54 [» ]
    C 70-529 [» ]
    1PJM X-ray 2.50 B 70-529 [» ]
    1PJN X-ray 2.50 B 70-529 [» ]
    1Q1S X-ray 2.30 C 70-529 [» ]
    1Q1T X-ray 2.50 C 70-529 [» ]
    1Y2A X-ray 2.20 C 70-497 [» ]
    2C1M X-ray 2.20 A 75-498 [» ]
    2YNR X-ray 2.30 A 72-496 [» ]
    3BTR X-ray 2.60 C 70-496 [» ]
    3KND X-ray 2.15 A 70-529 [» ]
    3L3Q X-ray 2.30 A 71-497 [» ]
    3OQS X-ray 2.00 A 70-529 [» ]
    3Q5U X-ray 2.50 A 70-529 [» ]
    3RZ9 X-ray 2.29 A 70-529 [» ]
    3RZX X-ray 2.61 A 70-529 [» ]
    3TPM X-ray 2.10 A 75-496 [» ]
    3TPO X-ray 2.10 A 1-529 [» ]
    3UKW X-ray 2.10 B 70-529 [» ]
    3UKX X-ray 2.20 B 70-529 [» ]
    3UKY X-ray 2.35 B 70-529 [» ]
    3UKZ X-ray 2.30 B 70-529 [» ]
    3UL0 X-ray 2.00 B 70-529 [» ]
    3UL1 X-ray 1.90 B 70-529 [» ]
    3UVU X-ray 2.38 A 70-529 [» ]
    3VE6 X-ray 2.83 A 71-496 [» ]
    3ZIN X-ray 2.00 A 72-496 [» ]
    3ZIO X-ray 2.10 A 72-496 [» ]
    3ZIP X-ray 2.40 A 72-497 [» ]
    3ZIQ X-ray 2.10 A 72-497 [» ]
    3ZIR X-ray 2.30 A 72-497 [» ]
    4BA3 X-ray 2.10 A 70-529 [» ]
    4HTV X-ray 3.00 A 70-528 [» ]
    4MZ5 X-ray 2.10 E 70-528 [» ]
    4MZ6 X-ray 1.88 E 70-528 [» ]
    4OIH X-ray 2.10 A 70-529 [» ]
    ProteinModelPortali P52293.
    SMRi P52293. Positions 11-497.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201007. 12 interactions.
    IntActi P52293. 9 interactions.

    PTM databases

    PhosphoSitei P52293.

    Proteomic databases

    MaxQBi P52293.
    PaxDbi P52293.
    PRIDEi P52293.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018506 ; ENSMUSP00000018506 ; ENSMUSG00000018362 .
    ENSMUST00000086423 ; ENSMUSP00000137310 ; ENSMUSG00000066878 .
    ENSMUST00000091289 ; ENSMUSP00000137080 ; ENSMUSG00000069083 .
    GeneIDi 16647.
    KEGGi mmu:16647.
    UCSCi uc007lzz.1. mouse.

    Organism-specific databases

    CTDi 3838.
    MGIi MGI:103561. Kpna2.

    Phylogenomic databases

    eggNOGi COG5064.
    HOGENOMi HOG000167616.
    HOVERGENi HBG001846.
    InParanoidi P52293.
    KOi K15043.
    OMAi NETEKLC.
    OrthoDBi EOG7VHSWV.
    PhylomeDBi P52293.
    TreeFami TF101178.

    Miscellaneous databases

    EvolutionaryTracei P52293.
    NextBioi 290325.
    PROi P52293.
    SOURCEi Search...

    Gene expression databases

    Bgeei P52293.
    CleanExi MM_KPNA2.
    Genevestigatori P52293.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR002652. Importin-a_IBB.
    IPR024931. Importing_su_alpha.
    [Graphical view ]
    Pfami PF00514. Arm. 8 hits.
    PF01749. IBB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005673. Importin_alpha. 1 hit.
    SMARTi SM00185. ARM. 8 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50176. ARM_REPEAT. 6 hits.
    PS51214. IBB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "In vivo evidence for involvement of a 58 kDa component of nuclear pore-targeting complex in nuclear protein import."
      Imamoto N., Shimamoto T., Takao T., Tachibana T., Kose S., Matsubae M., Sekimoto T., Shimonishi Y., Yoneda Y.
      EMBO J. 14:3617-3626(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis."
      Kuessel P., Frasch M.
      Mol. Gen. Genet. 248:351-363(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryo.
    3. "The nuclear localization signal of lymphoid enhancer factor-1 is recognized by two differentially expressed Srp1-nuclear localization sequence receptor proteins."
      Prieve M.G., Guttridge K.L., Waterman M.L.
      J. Biol. Chem. 271:7654-7658(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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. "Characterization of the nuclear transport of a novel leucine-rich acidic nuclear protein-like protein."
      Matsubae M., Kurihara T., Tachibana T., Imamoto N., Yoneda Y.
      FEBS Lett. 468:171-175(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANP32E.
    6. "Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha."
      Fontes M.R., Teh T., Kobe B.
      J. Mol. Biol. 297:1183-1194(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 72-497, NUCLEAR LOCALIZATION SIGNAL RECOGNITION.
    7. "Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha."
      Kobe B.
      Nat. Struct. Biol. 6:388-397(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 44-496, NUCLEAR LOCALIZATION SIGNAL, AUTOINHIBITION.
    8. "Biophysical characterization of interactions involving importin-alpha during nuclear import."
      Catimel B., Teh T., Fontes M.R., Jennings I.G., Jans D.A., Howlett G.J., Nice E.C., Kobe B.
      J. Biol. Chem. 276:34189-34198(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 47-54, AUTOINHIBITION.
    9. "Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling."
      Matsuura Y., Stewart M.
      EMBO J. 24:3681-3689(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 75-498 IN COMPLEX WITH NUP50.
    10. "Importin alpha protein acts as a negative regulator for Snail protein nuclear import."
      Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.
      J. Biol. Chem. 286:15126-15131(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTS WITH SNAI1.

    Entry informationi

    Entry nameiIMA1_MOUSE
    AccessioniPrimary (citable) accession number: P52293
    Secondary accession number(s): Q64292
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 141 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

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3