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O00505

- IMA4_HUMAN

UniProt

O00505 - IMA4_HUMAN

Protein

Importin subunit alpha-4

Gene

KPNA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9.

    GO - Molecular functioni

    1. nuclear localization sequence binding Source: ProtInc
    2. protein binding Source: IntAct
    3. protein transporter activity Source: InterPro

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. NLS-bearing protein import into nucleus Source: ProtInc
    3. protein complex assembly Source: ProtInc
    4. viral entry into host cell Source: UniProtKB-KW
    5. viral penetration into host nucleus Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Protein transport, Transport, Viral penetration into host nucleus, Virus entry into host cell

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    SignaLinkiO00505.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Importin subunit alpha-4
    Alternative name(s):
    Importin alpha Q2
    Short name:
    Qip2
    Karyopherin subunit alpha-3
    SRP1-gamma
    Gene namesi
    Name:KPNA3
    Synonyms:QIP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:6396. KPNA3.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nuclear pore Source: ProtInc
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30187.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 521520Importin subunit alpha-4PRO_0000120724Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei56 – 561Phosphoserine2 Publications
    Modified residuei60 – 601Phosphoserine5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00505.
    PaxDbiO00505.
    PeptideAtlasiO00505.
    PRIDEiO00505.

    PTM databases

    PhosphoSiteiO00505.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest levels in heart and skeletal muscle.

    Gene expression databases

    BgeeiO00505.
    CleanExiHS_KPNA3.
    GenevestigatoriO00505.

    Organism-specific databases

    HPAiHPA046852.

    Interactioni

    Subunit structurei

    Forms a complex with importin subunit beta-1. Interacts with HIV-1 integrase; this interaction might play a role in nuclear import of HIV pre-integration complex. Interacts with influenza virus nucleoprotein; this interaction might play a role in nuclear import of viral genome.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDKN1BP465274EBI-358297,EBI-519280
    Mkl1Q8K4J69EBI-358297,EBI-8291665From a different organism.

    Protein-protein interaction databases

    BioGridi110037. 32 interactions.
    DIPiDIP-27586N.
    IntActiO00505. 33 interactions.
    MINTiMINT-88920.
    STRINGi9606.ENSP00000261667.

    Structurei

    3D structure databases

    ProteinModelPortaliO00505.
    SMRiO00505. Positions 11-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 5857IBBPROSITE-ProRule annotationAdd
    BLAST
    Repeati66 – 10641ARM 1; truncatedAdd
    BLAST
    Repeati107 – 14943ARM 2Add
    BLAST
    Repeati150 – 19445ARM 3Add
    BLAST
    Repeati195 – 23339ARM 4Add
    BLAST
    Repeati234 – 27845ARM 5Add
    BLAST
    Repeati279 – 31840ARM 6Add
    BLAST
    Repeati319 – 36042ARM 7Add
    BLAST
    Repeati361 – 40040ARM 8Add
    BLAST
    Repeati401 – 44343ARM 9Add
    BLAST
    Repeati447 – 48539ARM 10; atypicalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni137 – 22993NLS binding site (major)By similarityAdd
    BLAST
    Regioni306 – 39489NLS binding site (minor)By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi43 – 5210Nuclear localization signalBy similarity

    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 By similarity.By similarity
    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 By similarity.By similarity

    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.
    InParanoidiO00505.
    OMAiNCDVLSY.
    OrthoDBiEOG7VHSWV.
    PhylomeDBiO00505.
    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. 3 hits.
    PS51214. IBB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O00505-1 [UniParc]FASTAAdd to Basket

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    MAENPSLENH RIKSFKNKGR DVETMRRHRN EVTVELRKNK RDEHLLKKRN    50
    VPQEESLEDS DVDADFKAQN VTLEAILQNA TSDNPVVQLS AVQAARKLLS 100
    SDRNPPIDDL IKSGILPILV KCLERDDNPS LQFEAAWALT NIASGTSAQT 150
    QAVVQSNAVP LFLRLLRSPH QNVCEQAVWA LGNIIGDGPQ CRDYVISLGV 200
    VKPLLSFISP SIPITFLRNV TWVIVNLCRN KDPPPPMETV QEILPALCVL 250
    IYHTDINILV DTVWALSYLT DGGNEQIQMV IDSGVVPFLV PLLSHQEVKV 300
    QTAALRAVGN IVTGTDEQTQ VVLNCDVLSH FPNLLSHPKE KINKEAVWFL 350
    SNITAGNQQQ VQAVIDAGLI PMIIHQLAKG DFGTQKEAAW AISNLTISGR 400
    KDQVEYLVQQ NVIPPFCNLL SVKDSQVVQV VLDGLKNILI MAGDEASTIA 450
    EIIEECGGLE KIEVLQQHEN EDIYKLAFEI IDQYFSGDDI DEDPCLIPEA 500
    TQGGTYNFDP TANLQTKEFN F 521
    Length:521
    Mass (Da):57,811
    Last modified:January 23, 2002 - v2
    Checksum:iC4FF132C3F346B7F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341V → M in CAA73026. (PubMed:9395085)Curated
    Sequence conflicti103 – 1031R → Q in BAA20378. (PubMed:9154134)Curated
    Sequence conflicti154 – 1541V → G in AAB87693. (PubMed:9435235)Curated
    Sequence conflicti236 – 2361P → T in AAB87693. (PubMed:9435235)Curated
    Sequence conflicti237 – 2371M → L in CAA73026. (PubMed:9395085)Curated
    Sequence conflicti256 – 2561I → V in CAA73026. (PubMed:9395085)Curated
    Sequence conflicti259 – 2591L → V in CAA73026. (PubMed:9395085)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti291 – 2911P → S.
    Corresponds to variant rs1043015 [ dbSNP | Ensembl ].
    VAR_014454

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89618 mRNA. Translation: BAA20378.1.
    Y12394 mRNA. Translation: CAA73026.1.
    AF034756 mRNA. Translation: AAB87693.1.
    AF005263 mRNA. Translation: AAQ13404.1.
    AK290528 mRNA. Translation: BAF83217.1.
    AK291000 mRNA. Translation: BAF83689.1.
    AL136301, AL135901 Genomic DNA. Translation: CAH71145.1.
    AL135901, AL136301 Genomic DNA. Translation: CAI40716.1.
    CH471075 Genomic DNA. Translation: EAX08837.1.
    BC017355 mRNA. Translation: AAH17355.1.
    BC024202 mRNA. Translation: AAH24202.1.
    CCDSiCCDS9421.1.
    RefSeqiNP_002258.2. NM_002267.3.
    UniGeneiHs.527919.

    Genome annotation databases

    EnsembliENST00000261667; ENSP00000261667; ENSG00000102753.
    GeneIDi3839.
    KEGGihsa:3839.
    UCSCiuc001vdj.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89618 mRNA. Translation: BAA20378.1 .
    Y12394 mRNA. Translation: CAA73026.1 .
    AF034756 mRNA. Translation: AAB87693.1 .
    AF005263 mRNA. Translation: AAQ13404.1 .
    AK290528 mRNA. Translation: BAF83217.1 .
    AK291000 mRNA. Translation: BAF83689.1 .
    AL136301 , AL135901 Genomic DNA. Translation: CAH71145.1 .
    AL135901 , AL136301 Genomic DNA. Translation: CAI40716.1 .
    CH471075 Genomic DNA. Translation: EAX08837.1 .
    BC017355 mRNA. Translation: AAH17355.1 .
    BC024202 mRNA. Translation: AAH24202.1 .
    CCDSi CCDS9421.1.
    RefSeqi NP_002258.2. NM_002267.3.
    UniGenei Hs.527919.

    3D structure databases

    ProteinModelPortali O00505.
    SMRi O00505. Positions 11-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110037. 32 interactions.
    DIPi DIP-27586N.
    IntActi O00505. 33 interactions.
    MINTi MINT-88920.
    STRINGi 9606.ENSP00000261667.

    PTM databases

    PhosphoSitei O00505.

    Proteomic databases

    MaxQBi O00505.
    PaxDbi O00505.
    PeptideAtlasi O00505.
    PRIDEi O00505.

    Protocols and materials databases

    DNASUi 3839.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261667 ; ENSP00000261667 ; ENSG00000102753 .
    GeneIDi 3839.
    KEGGi hsa:3839.
    UCSCi uc001vdj.2. human.

    Organism-specific databases

    CTDi 3839.
    GeneCardsi GC13M050273.
    HGNCi HGNC:6396. KPNA3.
    HPAi HPA046852.
    MIMi 601892. gene.
    neXtProti NX_O00505.
    PharmGKBi PA30187.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5064.
    HOGENOMi HOG000167616.
    HOVERGENi HBG001846.
    InParanoidi O00505.
    OMAi NCDVLSY.
    OrthoDBi EOG7VHSWV.
    PhylomeDBi O00505.
    TreeFami TF101178.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    SignaLinki O00505.

    Miscellaneous databases

    ChiTaRSi KPNA3. human.
    GeneWikii KPNA3.
    GenomeRNAii 3839.
    NextBioi 15107.
    PROi O00505.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00505.
    CleanExi HS_KPNA3.
    Genevestigatori O00505.

    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. 3 hits.
    PS51214. IBB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and mapping of karyopherin alpha 3 (KPNA3), a human gene that is highly homologous to genes encoding Xenopus importin, yeast SRP1 and human RCH1."
      Takeda S., Fujiwara T., Shimizu F., Kawai A., Shinomiya K., Okuno S., Ozaki K., Katagiri T., Shimada Y., Nagata M., Watanabe T., Takaichi A., Kuga Y., Suzuki M., Hishigaki H., Takahashi E., Shin S., Nakamura Y., Hirai Y.
      Cytogenet. Cell Genet. 76:87-93(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    2. "Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family."
      Koehler M., Ansieau S., Prehn S., Leutz A., Haller H., Hartmann E.
      FEBS Lett. 417:104-108(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    3. "Cloning and characterization of hSRP1 gamma, a tissue-specific nuclear transport factor."
      Nachury M.V., Ryder U.W., Lamond A.I., Weis K.
      Proc. Natl. Acad. Sci. U.S.A. 95:582-587(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Importin alpha-3, a novel variant of the small importin subunit evolutionarily conserved from hydrozoa to man."
      Fischer R.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Muscle.
    9. "Importin alpha nuclear localization signal binding sites for STAT1, STAT2, and influenza A virus nucleoprotein."
      Melen K., Fagerlund R., Franke J., Koehler M., Kinnunen L., Julkunen I.
      J. Biol. Chem. 278:28193-28200(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INFLUENZA VIRUS NP.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Importin alpha3 interacts with HIV-1 integrase and contributes to HIV-1 nuclear import and replication."
      Ao Z., Danappa Jayappa K., Wang B., Zheng Y., Kung S., Rassart E., Depping R., Kohler M., Cohen E.A., Yao X.
      J. Virol. 84:8650-8663(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 INTEGRASE.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIMA4_HUMAN
    AccessioniPrimary (citable) accession number: O00505
    Secondary accession number(s): O00191
    , O43195, Q5JVM9, Q96AA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Was termed importin alpha-4.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3