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Q96P70

- IPO9_HUMAN

UniProt

Q96P70 - IPO9_HUMAN

Protein

Importin-9

Gene

IPO9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin 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 the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. 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 By similarity. Mediates the nuclear import of H2B histone By similarity, RPS7 and RPL18A. Prevents the cytoplasmic aggregation of RPS7 and RPL18A by shielding exposed basic domains. May also import H2A, H3, H4 histones By similarity, RPL4 and RPL6.By similarity1 Publication

    GO - Molecular functioni

    1. histone binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein transporter activity Source: UniProtKB

    GO - Biological processi

    1. protein import into nucleus Source: UniProtKB

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Importin-9
    Short name:
    Imp9
    Alternative name(s):
    Ran-binding protein 9
    Short name:
    RanBP9
    Gene namesi
    Name:IPO9
    Synonyms:IMP9, KIAA1192, RANBP9
    ORF Names:HSPC273
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19425. IPO9.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134930111.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 10411040Importin-9PRO_0000120754Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96P70.
    PaxDbiQ96P70.
    PeptideAtlasiQ96P70.
    PRIDEiQ96P70.

    PTM databases

    PhosphoSiteiQ96P70.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96P70.
    BgeeiQ96P70.
    CleanExiHS_IPO9.
    HS_RANBP9.
    GenevestigatoriQ96P70.

    Organism-specific databases

    HPAiHPA054894.
    HPA059540.

    Interactioni

    Subunit structurei

    Binds with high affinity to RPS7 and RPL18A. The binding is coupled to RanGTP cycles. May bind H2A, H3, H4 histones By similarity, RPL4 and RPL6 with low affinity. Interacts with PPP2R1A and PPP2R1B.2 Publications

    Protein-protein interaction databases

    BioGridi120830. 30 interactions.
    IntActiQ96P70. 8 interactions.
    MINTiMINT-1153224.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96P70.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 11977Importin N-terminalPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the importin beta family.Curated
    Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5657.
    HOVERGENiHBG049054.
    InParanoidiQ96P70.
    OMAiMPDGPTS.
    OrthoDBiEOG722J7R.
    PhylomeDBiQ96P70.
    TreeFamiTF323706.

    Family and domain databases

    Gene3Di1.25.10.10. 3 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR001494. Importin-beta_N.
    [Graphical view]
    PfamiPF03810. IBN_N. 1 hit.
    [Graphical view]
    SMARTiSM00913. IBN_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.
    PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q96P70-1 [UniParc]FASTAAdd to Basket

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    MAAAAAAGAA SGLPGPVAQG LKEALVDTLT GILSPVQEVR AAAEEQIKVL     50
    EVTEEFGVHL AELTVDPQGA LAIRQLASVI LKQYVETHWC AQSEKFRPPE 100
    TTERAKIVIR ELLPNGLRES ISKVRSSVAY AVSAIAHWDW PEAWPQLFNL 150
    LMEMLVSGDL NAVHGAMRVL TEFTREVTDT QMPLVAPVIL PEMYKIFTMA 200
    EVYGIRTRSR AVEIFTTCAH MICNMEELEK GAAKVLIFPV VQQFTEAFVQ 250
    ALQIPDGPTS DSGFKMEVLK AVTALVKNFP KHMVSSMQQI LPIVWNTLTE 300
    SAAFYVRTEV NYTEEVEDPV DSDGEVLGFE NLVFSIFEFV HALLENSKFK 350
    STVKKALPEL IYYIILYMQI TEEQIKVWTA NPQQFVEDED DDTFSYTVRI 400
    AAQDLLLAVA TDFQNESAAA LAAAATRHLQ EAEQTKNSGT EHWWKIHEAC 450
    MLALGSVKAI ITDSVKNGRI HFDMHGFLTN VILADLNLSV SPFLLGRALW 500
    AASRFTVAMS PELIQQFLQA TVSGLHETQP PSVRISAVRA IWGYCDQLKV 550
    SESTHVLQPF LPSILDGLIH LAAQFSSEVL NLVMETLCIV CTVDPEFTAS 600
    MESKICPFTI AIFLKYSNDP VVASLAQDIF KELSQIEACQ GPMQMRLIPT 650
    LVSIMQAPAD KIPAGLCATA IDILTTVVRN TKPPLSQLLI CQAFPAVAQC 700
    TLHTDDNATM QNGGECLRAY VSVTLEQVAQ WHDEQGHNGL WYVMQVVSQL 750
    LDPRTSEFTA AFVGRLVSTL ISKAGRELGE NLDQILRAIL SKMQQAETLS 800
    VMQSLIMVFA HLVHTQLEPL LEFLCSLPGP TGKPALEFVM AEWTSRQHLF 850
    YGQYEGKVSS VALCKLLQHG INADDKRLQD IRVKGEEIYS MDEGIRTRSK 900
    SAKNPERWTN IPLLVKILKL IINELSNVME ANAARQATPA EWSQDDSNDM 950
    WEDQEEEEEE EEDGLAGQLL SDILATSKYE EDYYEDDEED DPDALKDPLY 1000
    QIDLQAYLTD FLCQFAQQPC YIMFSGHLND NERRVLQTIG I 1041
    Length:1,041
    Mass (Da):115,963
    Last modified:January 23, 2007 - v3
    Checksum:iA1842C357AEDFD90
    GO

    Sequence cautioni

    The sequence AAF28951.1 differs from that shown. Reason: Frameshift at position 982.
    The sequence BAA86506.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA91588.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB55181.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAC11173.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti632 – 6321E → G in BAC11173. (PubMed:14702039)Curated
    Sequence conflicti916 – 9161K → R in BAC11173. (PubMed:14702039)Curated
    Sequence conflicti935 – 9351R → P in BAB55181. (PubMed:14702039)Curated
    Sequence conflicti960 – 9601E → G in BAC11173. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF410465 mRNA. Translation: AAL01416.1.
    AL645504 Genomic DNA. Translation: CAI17015.1.
    AK001264 mRNA. Translation: BAA91588.1. Different initiation.
    AK027532 mRNA. Translation: BAB55181.1. Different initiation.
    AK074740 mRNA. Translation: BAC11173.1. Different initiation.
    AK094603 mRNA. Translation: BAC04383.1. Sequence problems.
    CH471067 Genomic DNA. Translation: EAW91376.1.
    BC003604 mRNA. Translation: AAH03604.2.
    AF161391 mRNA. Translation: AAF28951.1. Frameshift.
    AL834323 mRNA. Translation: CAD38991.1.
    AB033018 mRNA. Translation: BAA86506.1. Different initiation.
    CCDSiCCDS1415.1.
    RefSeqiNP_060555.2. NM_018085.4.
    UniGeneiHs.596014.

    Genome annotation databases

    EnsembliENST00000361565; ENSP00000354742; ENSG00000198700.
    GeneIDi55705.
    KEGGihsa:55705.
    UCSCiuc001gwz.3. human.

    Polymorphism databases

    DMDMi41688593.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF410465 mRNA. Translation: AAL01416.1 .
    AL645504 Genomic DNA. Translation: CAI17015.1 .
    AK001264 mRNA. Translation: BAA91588.1 . Different initiation.
    AK027532 mRNA. Translation: BAB55181.1 . Different initiation.
    AK074740 mRNA. Translation: BAC11173.1 . Different initiation.
    AK094603 mRNA. Translation: BAC04383.1 . Sequence problems.
    CH471067 Genomic DNA. Translation: EAW91376.1 .
    BC003604 mRNA. Translation: AAH03604.2 .
    AF161391 mRNA. Translation: AAF28951.1 . Frameshift.
    AL834323 mRNA. Translation: CAD38991.1 .
    AB033018 mRNA. Translation: BAA86506.1 . Different initiation.
    CCDSi CCDS1415.1.
    RefSeqi NP_060555.2. NM_018085.4.
    UniGenei Hs.596014.

    3D structure databases

    ProteinModelPortali Q96P70.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120830. 30 interactions.
    IntActi Q96P70. 8 interactions.
    MINTi MINT-1153224.

    PTM databases

    PhosphoSitei Q96P70.

    Polymorphism databases

    DMDMi 41688593.

    Proteomic databases

    MaxQBi Q96P70.
    PaxDbi Q96P70.
    PeptideAtlasi Q96P70.
    PRIDEi Q96P70.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361565 ; ENSP00000354742 ; ENSG00000198700 .
    GeneIDi 55705.
    KEGGi hsa:55705.
    UCSCi uc001gwz.3. human.

    Organism-specific databases

    CTDi 55705.
    GeneCardsi GC01P201798.
    HGNCi HGNC:19425. IPO9.
    HPAi HPA054894.
    HPA059540.
    neXtProti NX_Q96P70.
    PharmGKBi PA134930111.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5657.
    HOVERGENi HBG049054.
    InParanoidi Q96P70.
    OMAi MPDGPTS.
    OrthoDBi EOG722J7R.
    PhylomeDBi Q96P70.
    TreeFami TF323706.

    Miscellaneous databases

    ChiTaRSi IPO9. human.
    GeneWikii IPO9.
    GenomeRNAii 55705.
    NextBioi 60559.
    PROi Q96P70.

    Gene expression databases

    ArrayExpressi Q96P70.
    Bgeei Q96P70.
    CleanExi HS_IPO9.
    HS_RANBP9.
    Genevestigatori Q96P70.

    Family and domain databases

    Gene3Di 1.25.10.10. 3 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR001494. Importin-beta_N.
    [Graphical view ]
    Pfami PF03810. IBN_N. 1 hit.
    [Graphical view ]
    SMARTi SM00913. IBN_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    PROSITEi PS50166. IMPORTIN_B_NT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains."
      Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.
      EMBO J. 21:377-386(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RPS7; RPL18A; RPL4 AND RPL6.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] OF 1-276 AND 358-1041.
      Tissue: Amygdala.
    5. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-22; 400-427 AND 908-916, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    6. "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] OF 406-1041.
      Tissue: Placenta.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 632-1041.
      Tissue: Amygdala.
    8. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 767-1041.
      Tissue: Umbilical cord blood.
    9. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
      Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
      DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 780-1041.
      Tissue: Brain.
    10. "Interaction between protein phosphatase 2A and members of the importin beta superfamily."
      Lubert E.J., Sarge K.D.
      Biochem. Biophys. Res. Commun. 303:908-913(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP2R1A AND PPP2R1B.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIPO9_HUMAN
    AccessioniPrimary (citable) accession number: Q96P70
    Secondary accession number(s): B1ASV5
    , Q8N1Y1, Q8N3I2, Q8NCG9, Q96SU6, Q9NW01, Q9P0A8, Q9ULM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 2, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3