ID   IPO11_HUMAN             Reviewed;         975 AA.
AC   Q9UI26; A6NGJ5; B4DZ73; D3DW98; Q8N5R2; Q9NSJ6; Q9NVB1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-JAN-2012, entry version 86.
DE   RecName: Full=Importin-11;
DE            Short=Imp11;
DE   AltName: Full=Ran-binding protein 11;
DE            Short=RanBP11;
GN   Name=IPO11; Synonyms=RANBP11;
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] (ISOFORM 1).
RA   Goerlich D., Prehn S., Hartmann E.;
RT   "Human RanBP11.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cervix, and Testis;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 816-975 (ISOFORMS 1/2).
RC   TISSUE=Testis;
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   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION
RP   WITH UBE2E3.
RX   PubMed=11032817; DOI=10.1093/emboj/19.20.5502;
RA   Plafker S.M., Macara I.G.;
RT   "Importin-11, a nuclear import receptor for the ubiquitin-conjugating
RT   enzyme, UbcM2.";
RL   EMBO J. 19:5502-5513(2000).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
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   [9]
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 UBE2E3,
CC       and of RPL12 (By similarity).
CC   -!- SUBUNIT: Interacts with UBE2E3 and RPL12.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UI26-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UI26-2; Sequence=VSP_041420;
CC   -!- SIMILARITY: Belongs to the importin beta family.
CC   -!- SIMILARITY: Contains 15 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 importin N-terminal domain.
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DR   EMBL; AF111109; AAF21936.1; -; mRNA.
DR   EMBL; AK302781; BAG63985.1; -; mRNA.
DR   EMBL; AK001696; BAA91843.1; -; mRNA.
DR   EMBL; AC008859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471137; EAW51379.1; -; Genomic_DNA.
DR   EMBL; CH471137; EAW51380.1; -; Genomic_DNA.
DR   EMBL; BC031694; AAH31694.1; -; mRNA.
DR   EMBL; BC033776; AAH33776.1; -; mRNA.
DR   EMBL; AL162083; CAB82416.1; -; mRNA.
DR   IPI; IPI00301107; -.
DR   IPI; IPI00913938; -.
DR   PIR; T47185; T47185.
DR   RefSeq; NP_001128251.1; NM_001134779.1.
DR   RefSeq; NP_057422.3; NM_016338.4.
DR   UniGene; Hs.482269; -.
DR   ProteinModelPortal; Q9UI26; -.
DR   IntAct; Q9UI26; 2.
DR   MINT; MINT-1460740; -.
DR   STRING; Q9UI26; -.
DR   PhosphoSite; Q9UI26; -.
DR   DMDM; 50401199; -.
DR   PeptideAtlas; Q9UI26; -.
DR   PRIDE; Q9UI26; -.
DR   Ensembl; ENST00000325324; ENSP00000316651; ENSG00000086200.
DR   Ensembl; ENST00000409296; ENSP00000386992; ENSG00000086200.
DR   GeneID; 51194; -.
DR   KEGG; hsa:51194; -.
DR   UCSC; uc003jtc.1; human.
DR   CTD; 51194; -.
DR   GeneCards; GC05P061744; -.
DR   HGNC; HGNC:20628; IPO11.
DR   MIM; 610889; gene.
DR   neXtProt; NX_Q9UI26; -.
DR   PharmGKB; PA134936197; -.
DR   eggNOG; prNOG13372; -.
DR   GeneTree; ENSGT00390000014071; -.
DR   HOVERGEN; HBG061387; -.
DR   InParanoid; Q9UI26; -.
DR   PhylomeDB; Q9UI26; -.
DR   NextBio; 54202; -.
DR   ArrayExpress; Q9UI26; -.
DR   Bgee; Q9UI26; -.
DR   CleanEx; HS_IPO11; -.
DR   Genevestigator; Q9UI26; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001494; Importin-beta_N.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF03810; IBN_N; 1.
DR   SMART; SM00913; IBN_N; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR   PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW   Nucleus; Polymorphism; Protein transport; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN         1    975       Importin-11.
FT                                /FTId=PRO_0000120756.
FT   DOMAIN       28    100       Importin N-terminal.
FT   REPEAT      123    160       HEAT 1.
FT   REPEAT      209    248       HEAT 2.
FT   REPEAT      318    356       HEAT 3.
FT   REPEAT      422    459       HEAT 4.
FT   REPEAT      473    509       HEAT 5.
FT   REPEAT      511    548       HEAT 6.
FT   REPEAT      555    593       HEAT 7.
FT   REPEAT      600    636       HEAT 8.
FT   REPEAT      640    677       HEAT 9.
FT   REPEAT      683    720       HEAT 10.
FT   REPEAT      743    764       HEAT 11.
FT   REPEAT      765    804       HEAT 12.
FT   REPEAT      819    849       HEAT 13.
FT   REPEAT      850    887       HEAT 14.
FT   REPEAT      957    974       HEAT 15.
FT   MOD_RES       1      1       N-acetylmethionine.
FT   VAR_SEQ       1      1       M -> MVQPIIHLGYVVYSLLYLGYKPVQHVTALNTVSSCH
FT                                KMVSM (in isoform 2).
FT                                /FTId=VSP_041420.
FT   VARIANT     260    260       N -> D (in dbSNP:rs35107530).
FT                                /FTId=VAR_050004.
FT   VARIANT     937    937       I -> V (in dbSNP:rs11544795).
FT                                /FTId=VAR_050005.
FT   CONFLICT     53     53       T -> A (in Ref. 2; BAG63985).
FT   CONFLICT    204    204       I -> T (in Ref. 2; BAA91843).
FT   CONFLICT    237    237       G -> V (in Ref. 2; BAG63985).
FT   CONFLICT    332    332       A -> T (in Ref. 2; BAG63985).
FT   CONFLICT    504    504       I -> V (in Ref. 2; BAA91843).
FT   CONFLICT    571    571       V -> A (in Ref. 2; BAA91843).
FT   CONFLICT    722    722       L -> S (in Ref. 2; BAG63985).
SQ   SEQUENCE   975 AA;  112535 MW;  6A9349B2F8F36DF9 CRC64;
     MDLNSASTVV LQVLTQATSQ DTAVLKPAEE QLKQWETQPG FYSVLLNIFT NHTLDINVRW
     LAVLYFKHGI DRYWRRVAPH ALSEEEKTTL RAGLITNFNE PINQIATQIA VLIAKVARLD
     CPRQWPELIP TLIESVKVQD DLRQHRALLT FYHVTKTLAS KRLAADRKLF YDLASGIYNF
     ACSLWNHHTD TFLQEVSSGN EAAILSSLER TLLSLKVLRK LTVNGFVEPH KNMEVMGFLH
     GIFERLKQFL ECSRSIGTDN VCRDRLEKTI ILFTKVLLDF LDQHPFSFTP LIQRSLEFSV
     SYVFTEVGEG VTFERFIVQC MNLIKMIVKN YAYKPSKNFE DSSPETLEAH KIKMAFFTYP
     TLTEICRRLV SHYFLLTEEE LTMWEEDPEG FTVEETGGDS WKYSLRPCTE VLFIDIFHEY
     NQTLTPVLLE MMQTLQGPTN VEDMNALLIK DAVYNAVGLA AYELFDSVDF DQWFKNQLLP
     ELQVIHNRYK PLRRRVIWLI GQWISVKFKS DLRPMLYEAI CNLLQDQDLV VRIETATTLK
     LTVDDFEFRT DQFLPYLETM FTLLFQLLQQ VTECDTKMHV LHVLSCVIER VNMQIRPYVG
     CLVQYLPLLW KQSEEHNMLR CAILTTLIHL VQGLGADSKN LYPFLLPVIQ LSTDVSQPPH
     VYLLEDGLEL WLVTLENSPC ITPELLRIFQ NMSPLLELSS ENLRTCFKII NGYIFLSSTE
     FLQTYAVGLC QSFCELLKEI TTEGQVQVLK VVENALKVNP ILGPQMFQPI LPYVFKGIIE
     GERYPVVMST YLGVMGRVLL QNTSFFSSLL NEMAHKFNQE MDQLLGNMIE MWVDRMDNIT
     QPERRKLSAL ALLSLLPSDN SVIQDKFCGI INISVEGLHD VMTEDPETGT YKDCMLMSHL
     EEPKVTEDEE PPTEQDKRKK MLALKDPVHT VSLQQFIYEK LKAQQEMLGE QGFQSLMETV
     DTEIVTQLQE FLQGF
//