Full text data of IPO9
IPO9
(IMP9, KIAA1192, RANBP9)
[Confidence: high (present in two of the MS resources)]
Importin-9; Imp9 (Ran-binding protein 9; RanBP9)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Importin-9; Imp9 (Ran-binding protein 9; RanBP9)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00185146
IPI00185146 Importin 9 Importin 9 membrane and soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a cytoplasmic n/a expected molecular weight found in band membrane
IPI00185146 Importin 9 Importin 9 membrane and soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a cytoplasmic n/a expected molecular weight found in band membrane
UniProt
Q96P70
ID IPO9_HUMAN Reviewed; 1041 AA.
AC Q96P70; B1ASV5; Q8N1Y1; Q8N3I2; Q8NCG9; Q96SU6; Q9NW01; Q9P0A8;
read moreAC Q9ULM8;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Importin-9;
DE Short=Imp9;
DE AltName: Full=Ran-binding protein 9;
DE Short=RanBP9;
GN Name=IPO9; Synonyms=IMP9, KIAA1192, RANBP9; ORFNames=HSPC273;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RPS7;
RP RPL18A; RPL4 AND RPL6.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-276 AND 358-1041.
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-22; 400-427 AND 908-916, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1041.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 632-1041.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 767-1041.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 780-1041.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis
RT from size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [10]
RP INTERACTION WITH PPP2R1A AND PPP2R1B.
RX PubMed=12670497; DOI=10.1016/S0006-291X(03)00434-0;
RA Lubert E.J., Sarge K.D.;
RT "Interaction between protein phosphatase 2A and members of the
RT importin beta superfamily.";
RL Biochem. Biophys. Res. Commun. 303:908-913(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals
CC (NLS) in cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC)
CC through binding to nucleoporin and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to the importin, the importin/substrate complex dissociates
CC and importin is re-exported from the nucleus to the cytoplasm
CC where GTP hydrolysis releases Ran. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (By similarity). Mediates the nuclear import of H2B
CC histone (By similarity), RPS7 and RPL18A. Prevents the cytoplasmic
CC aggregation of RPS7 and RPL18A by shielding exposed basic domains.
CC May also import H2A, H3, H4 histones (By similarity), RPL4 and
CC RPL6.
CC -!- SUBUNIT: Binds with high affinity to RPS7 and RPL18A. The binding
CC is coupled to RanGTP cycles. May bind H2A, H3, H4 histones (By
CC similarity), RPL4 and RPL6 with low affinity. Interacts with
CC PPP2R1A and PPP2R1B.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28951.1; Type=Frameshift; Positions=982;
CC Sequence=BAA86506.1; Type=Erroneous initiation;
CC Sequence=BAA91588.1; Type=Erroneous initiation;
CC Sequence=BAB55181.1; Type=Erroneous initiation;
CC Sequence=BAC11173.1; Type=Erroneous initiation;
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DR EMBL; AF410465; AAL01416.1; -; mRNA.
DR EMBL; AL645504; CAI17015.1; -; Genomic_DNA.
DR EMBL; AK001264; BAA91588.1; ALT_INIT; mRNA.
DR EMBL; AK027532; BAB55181.1; ALT_INIT; mRNA.
DR EMBL; AK074740; BAC11173.1; ALT_INIT; mRNA.
DR EMBL; AK094603; BAC04383.1; ALT_SEQ; mRNA.
DR EMBL; CH471067; EAW91376.1; -; Genomic_DNA.
DR EMBL; BC003604; AAH03604.2; -; mRNA.
DR EMBL; AF161391; AAF28951.1; ALT_FRAME; mRNA.
DR EMBL; AL834323; CAD38991.1; -; mRNA.
DR EMBL; AB033018; BAA86506.1; ALT_INIT; mRNA.
DR RefSeq; NP_060555.2; NM_018085.4.
DR UniGene; Hs.596014; -.
DR ProteinModelPortal; Q96P70; -.
DR IntAct; Q96P70; 8.
DR MINT; MINT-1153224; -.
DR PhosphoSite; Q96P70; -.
DR DMDM; 41688593; -.
DR PaxDb; Q96P70; -.
DR PeptideAtlas; Q96P70; -.
DR PRIDE; Q96P70; -.
DR Ensembl; ENST00000361565; ENSP00000354742; ENSG00000198700.
DR GeneID; 55705; -.
DR KEGG; hsa:55705; -.
DR UCSC; uc001gwz.3; human.
DR CTD; 55705; -.
DR GeneCards; GC01P201798; -.
DR HGNC; HGNC:19425; IPO9.
DR neXtProt; NX_Q96P70; -.
DR PharmGKB; PA134930111; -.
DR eggNOG; COG5657; -.
DR HOVERGEN; HBG049054; -.
DR InParanoid; Q96P70; -.
DR OMA; ALQMPDG; -.
DR OrthoDB; EOG722J7R; -.
DR ChiTaRS; IPO9; human.
DR GeneWiki; IPO9; -.
DR GenomeRNAi; 55705; -.
DR NextBio; 60559; -.
DR PRO; PR:Q96P70; -.
DR ArrayExpress; Q96P70; -.
DR Bgee; Q96P70; -.
DR CleanEx; HS_IPO9; -.
DR CleanEx; HS_RANBP9; -.
DR Genevestigator; Q96P70; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; NAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Nucleus; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1041 Importin-9.
FT /FTId=PRO_0000120754.
FT DOMAIN 43 119 Importin N-terminal.
FT MOD_RES 2 2 N-acetylalanine.
FT CONFLICT 632 632 E -> G (in Ref. 4; BAC11173).
FT CONFLICT 916 916 K -> R (in Ref. 4; BAC11173).
FT CONFLICT 935 935 R -> P (in Ref. 4; BAB55181).
FT CONFLICT 960 960 E -> G (in Ref. 4; BAC11173).
SQ SEQUENCE 1041 AA; 115963 MW; A1842C357AEDFD90 CRC64;
MAAAAAAGAA SGLPGPVAQG LKEALVDTLT GILSPVQEVR AAAEEQIKVL EVTEEFGVHL
AELTVDPQGA LAIRQLASVI LKQYVETHWC AQSEKFRPPE TTERAKIVIR ELLPNGLRES
ISKVRSSVAY AVSAIAHWDW PEAWPQLFNL LMEMLVSGDL NAVHGAMRVL TEFTREVTDT
QMPLVAPVIL PEMYKIFTMA EVYGIRTRSR AVEIFTTCAH MICNMEELEK GAAKVLIFPV
VQQFTEAFVQ ALQIPDGPTS DSGFKMEVLK AVTALVKNFP KHMVSSMQQI LPIVWNTLTE
SAAFYVRTEV NYTEEVEDPV DSDGEVLGFE NLVFSIFEFV HALLENSKFK STVKKALPEL
IYYIILYMQI TEEQIKVWTA NPQQFVEDED DDTFSYTVRI AAQDLLLAVA TDFQNESAAA
LAAAATRHLQ EAEQTKNSGT EHWWKIHEAC MLALGSVKAI ITDSVKNGRI HFDMHGFLTN
VILADLNLSV SPFLLGRALW AASRFTVAMS PELIQQFLQA TVSGLHETQP PSVRISAVRA
IWGYCDQLKV SESTHVLQPF LPSILDGLIH LAAQFSSEVL NLVMETLCIV CTVDPEFTAS
MESKICPFTI AIFLKYSNDP VVASLAQDIF KELSQIEACQ GPMQMRLIPT LVSIMQAPAD
KIPAGLCATA IDILTTVVRN TKPPLSQLLI CQAFPAVAQC TLHTDDNATM QNGGECLRAY
VSVTLEQVAQ WHDEQGHNGL WYVMQVVSQL LDPRTSEFTA AFVGRLVSTL ISKAGRELGE
NLDQILRAIL SKMQQAETLS VMQSLIMVFA HLVHTQLEPL LEFLCSLPGP TGKPALEFVM
AEWTSRQHLF YGQYEGKVSS VALCKLLQHG INADDKRLQD IRVKGEEIYS MDEGIRTRSK
SAKNPERWTN IPLLVKILKL IINELSNVME ANAARQATPA EWSQDDSNDM WEDQEEEEEE
EEDGLAGQLL SDILATSKYE EDYYEDDEED DPDALKDPLY QIDLQAYLTD FLCQFAQQPC
YIMFSGHLND NERRVLQTIG I
//
ID IPO9_HUMAN Reviewed; 1041 AA.
AC Q96P70; B1ASV5; Q8N1Y1; Q8N3I2; Q8NCG9; Q96SU6; Q9NW01; Q9P0A8;
read moreAC Q9ULM8;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Importin-9;
DE Short=Imp9;
DE AltName: Full=Ran-binding protein 9;
DE Short=RanBP9;
GN Name=IPO9; Synonyms=IMP9, KIAA1192, RANBP9; ORFNames=HSPC273;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RPS7;
RP RPL18A; RPL4 AND RPL6.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-276 AND 358-1041.
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-22; 400-427 AND 908-916, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1041.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 632-1041.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 767-1041.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 780-1041.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis
RT from size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [10]
RP INTERACTION WITH PPP2R1A AND PPP2R1B.
RX PubMed=12670497; DOI=10.1016/S0006-291X(03)00434-0;
RA Lubert E.J., Sarge K.D.;
RT "Interaction between protein phosphatase 2A and members of the
RT importin beta superfamily.";
RL Biochem. Biophys. Res. Commun. 303:908-913(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals
CC (NLS) in cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC)
CC through binding to nucleoporin and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to the importin, the importin/substrate complex dissociates
CC and importin is re-exported from the nucleus to the cytoplasm
CC where GTP hydrolysis releases Ran. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (By similarity). Mediates the nuclear import of H2B
CC histone (By similarity), RPS7 and RPL18A. Prevents the cytoplasmic
CC aggregation of RPS7 and RPL18A by shielding exposed basic domains.
CC May also import H2A, H3, H4 histones (By similarity), RPL4 and
CC RPL6.
CC -!- SUBUNIT: Binds with high affinity to RPS7 and RPL18A. The binding
CC is coupled to RanGTP cycles. May bind H2A, H3, H4 histones (By
CC similarity), RPL4 and RPL6 with low affinity. Interacts with
CC PPP2R1A and PPP2R1B.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28951.1; Type=Frameshift; Positions=982;
CC Sequence=BAA86506.1; Type=Erroneous initiation;
CC Sequence=BAA91588.1; Type=Erroneous initiation;
CC Sequence=BAB55181.1; Type=Erroneous initiation;
CC Sequence=BAC11173.1; Type=Erroneous initiation;
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DR EMBL; AF410465; AAL01416.1; -; mRNA.
DR EMBL; AL645504; CAI17015.1; -; Genomic_DNA.
DR EMBL; AK001264; BAA91588.1; ALT_INIT; mRNA.
DR EMBL; AK027532; BAB55181.1; ALT_INIT; mRNA.
DR EMBL; AK074740; BAC11173.1; ALT_INIT; mRNA.
DR EMBL; AK094603; BAC04383.1; ALT_SEQ; mRNA.
DR EMBL; CH471067; EAW91376.1; -; Genomic_DNA.
DR EMBL; BC003604; AAH03604.2; -; mRNA.
DR EMBL; AF161391; AAF28951.1; ALT_FRAME; mRNA.
DR EMBL; AL834323; CAD38991.1; -; mRNA.
DR EMBL; AB033018; BAA86506.1; ALT_INIT; mRNA.
DR RefSeq; NP_060555.2; NM_018085.4.
DR UniGene; Hs.596014; -.
DR ProteinModelPortal; Q96P70; -.
DR IntAct; Q96P70; 8.
DR MINT; MINT-1153224; -.
DR PhosphoSite; Q96P70; -.
DR DMDM; 41688593; -.
DR PaxDb; Q96P70; -.
DR PeptideAtlas; Q96P70; -.
DR PRIDE; Q96P70; -.
DR Ensembl; ENST00000361565; ENSP00000354742; ENSG00000198700.
DR GeneID; 55705; -.
DR KEGG; hsa:55705; -.
DR UCSC; uc001gwz.3; human.
DR CTD; 55705; -.
DR GeneCards; GC01P201798; -.
DR HGNC; HGNC:19425; IPO9.
DR neXtProt; NX_Q96P70; -.
DR PharmGKB; PA134930111; -.
DR eggNOG; COG5657; -.
DR HOVERGEN; HBG049054; -.
DR InParanoid; Q96P70; -.
DR OMA; ALQMPDG; -.
DR OrthoDB; EOG722J7R; -.
DR ChiTaRS; IPO9; human.
DR GeneWiki; IPO9; -.
DR GenomeRNAi; 55705; -.
DR NextBio; 60559; -.
DR PRO; PR:Q96P70; -.
DR ArrayExpress; Q96P70; -.
DR Bgee; Q96P70; -.
DR CleanEx; HS_IPO9; -.
DR CleanEx; HS_RANBP9; -.
DR Genevestigator; Q96P70; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; NAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Nucleus; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1041 Importin-9.
FT /FTId=PRO_0000120754.
FT DOMAIN 43 119 Importin N-terminal.
FT MOD_RES 2 2 N-acetylalanine.
FT CONFLICT 632 632 E -> G (in Ref. 4; BAC11173).
FT CONFLICT 916 916 K -> R (in Ref. 4; BAC11173).
FT CONFLICT 935 935 R -> P (in Ref. 4; BAB55181).
FT CONFLICT 960 960 E -> G (in Ref. 4; BAC11173).
SQ SEQUENCE 1041 AA; 115963 MW; A1842C357AEDFD90 CRC64;
MAAAAAAGAA SGLPGPVAQG LKEALVDTLT GILSPVQEVR AAAEEQIKVL EVTEEFGVHL
AELTVDPQGA LAIRQLASVI LKQYVETHWC AQSEKFRPPE TTERAKIVIR ELLPNGLRES
ISKVRSSVAY AVSAIAHWDW PEAWPQLFNL LMEMLVSGDL NAVHGAMRVL TEFTREVTDT
QMPLVAPVIL PEMYKIFTMA EVYGIRTRSR AVEIFTTCAH MICNMEELEK GAAKVLIFPV
VQQFTEAFVQ ALQIPDGPTS DSGFKMEVLK AVTALVKNFP KHMVSSMQQI LPIVWNTLTE
SAAFYVRTEV NYTEEVEDPV DSDGEVLGFE NLVFSIFEFV HALLENSKFK STVKKALPEL
IYYIILYMQI TEEQIKVWTA NPQQFVEDED DDTFSYTVRI AAQDLLLAVA TDFQNESAAA
LAAAATRHLQ EAEQTKNSGT EHWWKIHEAC MLALGSVKAI ITDSVKNGRI HFDMHGFLTN
VILADLNLSV SPFLLGRALW AASRFTVAMS PELIQQFLQA TVSGLHETQP PSVRISAVRA
IWGYCDQLKV SESTHVLQPF LPSILDGLIH LAAQFSSEVL NLVMETLCIV CTVDPEFTAS
MESKICPFTI AIFLKYSNDP VVASLAQDIF KELSQIEACQ GPMQMRLIPT LVSIMQAPAD
KIPAGLCATA IDILTTVVRN TKPPLSQLLI CQAFPAVAQC TLHTDDNATM QNGGECLRAY
VSVTLEQVAQ WHDEQGHNGL WYVMQVVSQL LDPRTSEFTA AFVGRLVSTL ISKAGRELGE
NLDQILRAIL SKMQQAETLS VMQSLIMVFA HLVHTQLEPL LEFLCSLPGP TGKPALEFVM
AEWTSRQHLF YGQYEGKVSS VALCKLLQHG INADDKRLQD IRVKGEEIYS MDEGIRTRSK
SAKNPERWTN IPLLVKILKL IINELSNVME ANAARQATPA EWSQDDSNDM WEDQEEEEEE
EEDGLAGQLL SDILATSKYE EDYYEDDEED DPDALKDPLY QIDLQAYLTD FLCQFAQQPC
YIMFSGHLND NERRVLQTIG I
//