Full text data of IPO11
IPO11
(RANBP11)
[Confidence: low (only semi-automatic identification from reviews)]
Importin-11; Imp11 (Ran-binding protein 11; RanBP11)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Importin-11; Imp11 (Ran-binding protein 11; RanBP11)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UI26
ID IPO11_HUMAN Reviewed; 975 AA.
AC Q9UI26; A6NGJ5; B4DZ73; D3DW98; Q8N5R2; Q9NSJ6; Q9NVB1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 101.
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.
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 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 SMR; Q9UI26; 10-540.
DR IntAct; Q9UI26; 4.
DR MINT; MINT-1460740; -.
DR STRING; 9606.ENSP00000386992; -.
DR PhosphoSite; Q9UI26; -.
DR DMDM; 50401199; -.
DR PaxDb; Q9UI26; -.
DR PeptideAtlas; Q9UI26; -.
DR PRIDE; Q9UI26; -.
DR DNASU; 51194; -.
DR Ensembl; ENST00000325324; ENSP00000316651; ENSG00000086200.
DR Ensembl; ENST00000409296; ENSP00000386992; ENSG00000086200.
DR GeneID; 51194; -.
DR KEGG; hsa:51194; -.
DR UCSC; uc003jtc.3; human.
DR CTD; 51194; -.
DR GeneCards; GC05P061699; -.
DR HGNC; HGNC:20628; IPO11.
DR MIM; 610889; gene.
DR neXtProt; NX_Q9UI26; -.
DR PharmGKB; PA134936197; -.
DR eggNOG; COG5657; -.
DR HOGENOM; HOG000008140; -.
DR HOVERGEN; HBG061387; -.
DR InParanoid; Q9UI26; -.
DR OMA; LDVNVRW; -.
DR ChiTaRS; IPO11; human.
DR GeneWiki; IPO11; -.
DR GenomeRNAi; 51194; -.
DR NextBio; 54202; -.
DR PRO; PR:Q9UI26; -.
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:0008565; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 2.
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; 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
//
ID IPO11_HUMAN Reviewed; 975 AA.
AC Q9UI26; A6NGJ5; B4DZ73; D3DW98; Q8N5R2; Q9NSJ6; Q9NVB1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 101.
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.
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 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 SMR; Q9UI26; 10-540.
DR IntAct; Q9UI26; 4.
DR MINT; MINT-1460740; -.
DR STRING; 9606.ENSP00000386992; -.
DR PhosphoSite; Q9UI26; -.
DR DMDM; 50401199; -.
DR PaxDb; Q9UI26; -.
DR PeptideAtlas; Q9UI26; -.
DR PRIDE; Q9UI26; -.
DR DNASU; 51194; -.
DR Ensembl; ENST00000325324; ENSP00000316651; ENSG00000086200.
DR Ensembl; ENST00000409296; ENSP00000386992; ENSG00000086200.
DR GeneID; 51194; -.
DR KEGG; hsa:51194; -.
DR UCSC; uc003jtc.3; human.
DR CTD; 51194; -.
DR GeneCards; GC05P061699; -.
DR HGNC; HGNC:20628; IPO11.
DR MIM; 610889; gene.
DR neXtProt; NX_Q9UI26; -.
DR PharmGKB; PA134936197; -.
DR eggNOG; COG5657; -.
DR HOGENOM; HOG000008140; -.
DR HOVERGEN; HBG061387; -.
DR InParanoid; Q9UI26; -.
DR OMA; LDVNVRW; -.
DR ChiTaRS; IPO11; human.
DR GeneWiki; IPO11; -.
DR GenomeRNAi; 51194; -.
DR NextBio; 54202; -.
DR PRO; PR:Q9UI26; -.
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:0008565; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 2.
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; 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
//
MIM
610889
*RECORD*
*FIELD* NO
610889
*FIELD* TI
*610889 IMPORTIN 11; IPO11
;;RAN-BINDING PROTEIN 11; RANBP11
SYNLEURIN, INCLUDED; SLRN, INCLUDED
read more*FIELD* TX
DESCRIPTION
Importins, including IPO11, are a members of the
karyopherin/importin-beta family of transport receptors (see KPNB1;
602738) that mediate nucleocytoplasmic transport of protein and RNA
cargoes (Plafker and Macara, 2000).
CLONING
By database analysis using S. cerevisiae Lph2 as probe, followed by
5-prime RACE of a human brain cDNA library, Plafker and Macara (2000)
cloned IPO11. The deduced 975-amino acid protein shares 24% amino acid
identity with S. cerevisiae Lph2 protein. Northern blot analysis
detected a 4.4-kb transcript in all human tissues examined.
Immunofluorescence studies localized IPO11 to the nucleus in baby
hamster kidney (BHK) cells.
Wang et al. (2003) isolated a splice variant of IPO11, which they called
synleurin, by screening for Toll-like receptor homologs in a human cDNA
database. The deduced 623-amino acid variant contains a transmembrane
domain and 12 leucine-rich repeats over the extracellular domain.
Northern blot analysis detected a 2.5-kb transcript in human spleen,
thymus, prostate, testis, small intestine, colon, and peripheral blood
leukocytes, with 2 additional 4.3- and 5.0-kb bands in testis.
GENE FUNCTION
Using yeast 2-hybrid and in vitro immunoprecipitation studies, Plafker
and Macara (2000) showed that IPO11 binds Ran GTPase (RAN; 601179) in
its GTP-bound form. Deletion analysis showed that N-terminal region of
IPO11 contains the RAN-binding domain. Using a heterokaryon shuttling
assay with BHK cells fused with a transformed HeLa cell line, they
demonstrated that IPO11 shuttles between the donor and acceptor nuclei
of the fused cells, suggesting that IPO11 shuttles constitutively
between the nuclear and cytoplasmic compartments. Yeast 2-hybrid and GST
pull-down analysis showed that IPO11 interacts specifically with mouse
E2-type ubiquitin conjugating enzyme UbcM2 (UBE2E3; 604151). The
IPO11-UbcM2 complex was disrupted by GTP-bound Ran, consistent with the
model that transport receptor-cargo complexes form in the cytoplasm and
are dissociated by Ran-GTP in the nucleus.
Using yeast 2-hybrid and GST pull-down studies, Plafker and Macara
(2002) showed that IPO11 binds RPL12 (180475). Competition assay and
microinjection studies in BHK cells showed that RPL12 and UbcM2 interact
with the same or overlapping sites on IPO11, competing with each other
for IPO11 binding. IPO11 increased nuclear accumulation of RPL12 in a
RAN-dependent manner, and overexpression of an IPO11 mutant lacking the
RAN-binding domain did not increase nuclear accumulation of RPL12. In
vitro binding assay showed that IPO11 did not bind RPL23A (602326), and
transient transfection assay showed that importin-beta and IPO5 (RANBP5;
602008) had no effect on nucleocytoplasmic distribution of RPL12,
indicating that IPO11 is a specific nuclear import receptor for RPL12.
Wang et al. (2003) found that synleurin plays a role in potentiation of
cytokine responses by amplifying signal transduction activation of FGF2
(134920), EGF (131530), PDGFB (190040), IGF1 (147440), IGF2 (147470),
and lipopolysaccharide when expressed in HEK293 cells.
MAPPING
By genomic sequence analysis, Wang et al. (2003) mapped the IPO11 gene
to chromosome 5q12.1
*FIELD* RF
1. Plafker, S. M.; Macara, I. G.: Importin-11, a nuclear import receptor
for the ubiquitin-conjugating enzyme, UbcM2. EMBO J. 19: 5502-5513,
2000.
2. Plafker, S. M.; Macara, I. G.: Ribosomal protein L12 uses a distinct
nuclear import pathway mediated by importin 11. Molec. Cell. Biol. 22:
1266-1275, 2002.
3. Wang, W.; Yang, Y.; Li, L.; Shi, Y.: Synleurin, a novel leucine-rich
repeat protein that increases the intensity of pleiotropic cytokine
responses. Biochem. Biophys. Res. Commun. 305: 981-988, 2003.
*FIELD* CD
Dorothy S. Reilly: 3/26/2007
*FIELD* ED
wwang: 03/27/2007
wwang: 3/27/2007
*RECORD*
*FIELD* NO
610889
*FIELD* TI
*610889 IMPORTIN 11; IPO11
;;RAN-BINDING PROTEIN 11; RANBP11
SYNLEURIN, INCLUDED; SLRN, INCLUDED
read more*FIELD* TX
DESCRIPTION
Importins, including IPO11, are a members of the
karyopherin/importin-beta family of transport receptors (see KPNB1;
602738) that mediate nucleocytoplasmic transport of protein and RNA
cargoes (Plafker and Macara, 2000).
CLONING
By database analysis using S. cerevisiae Lph2 as probe, followed by
5-prime RACE of a human brain cDNA library, Plafker and Macara (2000)
cloned IPO11. The deduced 975-amino acid protein shares 24% amino acid
identity with S. cerevisiae Lph2 protein. Northern blot analysis
detected a 4.4-kb transcript in all human tissues examined.
Immunofluorescence studies localized IPO11 to the nucleus in baby
hamster kidney (BHK) cells.
Wang et al. (2003) isolated a splice variant of IPO11, which they called
synleurin, by screening for Toll-like receptor homologs in a human cDNA
database. The deduced 623-amino acid variant contains a transmembrane
domain and 12 leucine-rich repeats over the extracellular domain.
Northern blot analysis detected a 2.5-kb transcript in human spleen,
thymus, prostate, testis, small intestine, colon, and peripheral blood
leukocytes, with 2 additional 4.3- and 5.0-kb bands in testis.
GENE FUNCTION
Using yeast 2-hybrid and in vitro immunoprecipitation studies, Plafker
and Macara (2000) showed that IPO11 binds Ran GTPase (RAN; 601179) in
its GTP-bound form. Deletion analysis showed that N-terminal region of
IPO11 contains the RAN-binding domain. Using a heterokaryon shuttling
assay with BHK cells fused with a transformed HeLa cell line, they
demonstrated that IPO11 shuttles between the donor and acceptor nuclei
of the fused cells, suggesting that IPO11 shuttles constitutively
between the nuclear and cytoplasmic compartments. Yeast 2-hybrid and GST
pull-down analysis showed that IPO11 interacts specifically with mouse
E2-type ubiquitin conjugating enzyme UbcM2 (UBE2E3; 604151). The
IPO11-UbcM2 complex was disrupted by GTP-bound Ran, consistent with the
model that transport receptor-cargo complexes form in the cytoplasm and
are dissociated by Ran-GTP in the nucleus.
Using yeast 2-hybrid and GST pull-down studies, Plafker and Macara
(2002) showed that IPO11 binds RPL12 (180475). Competition assay and
microinjection studies in BHK cells showed that RPL12 and UbcM2 interact
with the same or overlapping sites on IPO11, competing with each other
for IPO11 binding. IPO11 increased nuclear accumulation of RPL12 in a
RAN-dependent manner, and overexpression of an IPO11 mutant lacking the
RAN-binding domain did not increase nuclear accumulation of RPL12. In
vitro binding assay showed that IPO11 did not bind RPL23A (602326), and
transient transfection assay showed that importin-beta and IPO5 (RANBP5;
602008) had no effect on nucleocytoplasmic distribution of RPL12,
indicating that IPO11 is a specific nuclear import receptor for RPL12.
Wang et al. (2003) found that synleurin plays a role in potentiation of
cytokine responses by amplifying signal transduction activation of FGF2
(134920), EGF (131530), PDGFB (190040), IGF1 (147440), IGF2 (147470),
and lipopolysaccharide when expressed in HEK293 cells.
MAPPING
By genomic sequence analysis, Wang et al. (2003) mapped the IPO11 gene
to chromosome 5q12.1
*FIELD* RF
1. Plafker, S. M.; Macara, I. G.: Importin-11, a nuclear import receptor
for the ubiquitin-conjugating enzyme, UbcM2. EMBO J. 19: 5502-5513,
2000.
2. Plafker, S. M.; Macara, I. G.: Ribosomal protein L12 uses a distinct
nuclear import pathway mediated by importin 11. Molec. Cell. Biol. 22:
1266-1275, 2002.
3. Wang, W.; Yang, Y.; Li, L.; Shi, Y.: Synleurin, a novel leucine-rich
repeat protein that increases the intensity of pleiotropic cytokine
responses. Biochem. Biophys. Res. Commun. 305: 981-988, 2003.
*FIELD* CD
Dorothy S. Reilly: 3/26/2007
*FIELD* ED
wwang: 03/27/2007
wwang: 3/27/2007