IPO11_HUMAN
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 03-AUG-2022, entry version 170.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 WITH
RP 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) through
CC binding to nucleoporin and the complex is subsequently translocated
CC through the pore by an energy requiring, Ran-dependent mechanism. At
CC the nucleoplasmic side of the NPC, Ran binds to the importin, the
CC importin/substrate complex dissociates and importin is re-exported from
CC the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus (By similarity). Mediates the nuclear import
CC of UBE2E3, and of RPL12 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11032817}.
CC -!- SUBUNIT: Interacts with UBE2E3 and RPL12.
CC {ECO:0000269|PubMed:11032817}.
CC -!- INTERACTION:
CC Q9UI26; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-748752, EBI-946029;
CC Q9UI26; Q14240: EIF4A2; NbExp=3; IntAct=EBI-748752, EBI-73473;
CC Q9UI26-2; Q01546: KRT76; NbExp=3; IntAct=EBI-12200335, EBI-2952745;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11032817}. Nucleus
CC {ECO:0000269|PubMed:11032817}.
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. {ECO:0000305}.
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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 CCDS; CCDS34167.1; -. [Q9UI26-1]
DR CCDS; CCDS47217.1; -. [Q9UI26-2]
DR PIR; T47185; T47185.
DR RefSeq; NP_001128251.1; NM_001134779.1. [Q9UI26-2]
DR RefSeq; NP_057422.3; NM_016338.4. [Q9UI26-1]
DR AlphaFoldDB; Q9UI26; -.
DR SMR; Q9UI26; -.
DR BioGRID; 119368; 153.
DR IntAct; Q9UI26; 35.
DR MINT; Q9UI26; -.
DR STRING; 9606.ENSP00000386992; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9UI26; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UI26; -.
DR PhosphoSitePlus; Q9UI26; -.
DR BioMuta; IPO11; -.
DR DMDM; 50401199; -.
DR EPD; Q9UI26; -.
DR jPOST; Q9UI26; -.
DR MassIVE; Q9UI26; -.
DR MaxQB; Q9UI26; -.
DR PaxDb; Q9UI26; -.
DR PeptideAtlas; Q9UI26; -.
DR PRIDE; Q9UI26; -.
DR ProteomicsDB; 84457; -. [Q9UI26-1]
DR ProteomicsDB; 84458; -. [Q9UI26-2]
DR Antibodypedia; 23693; 218 antibodies from 26 providers.
DR DNASU; 51194; -.
DR Ensembl; ENST00000325324.11; ENSP00000316651.6; ENSG00000086200.17. [Q9UI26-1]
DR Ensembl; ENST00000409296.7; ENSP00000386992.3; ENSG00000086200.17. [Q9UI26-2]
DR GeneID; 51194; -.
DR KEGG; hsa:51194; -.
DR MANE-Select; ENST00000325324.11; ENSP00000316651.6; NM_016338.5; NP_057422.3.
DR UCSC; uc003jtc.4; human. [Q9UI26-1]
DR CTD; 51194; -.
DR DisGeNET; 51194; -.
DR GeneCards; IPO11; -.
DR HGNC; HGNC:20628; IPO11.
DR HPA; ENSG00000086200; Low tissue specificity.
DR MIM; 610889; gene.
DR neXtProt; NX_Q9UI26; -.
DR OpenTargets; ENSG00000086200; -.
DR PharmGKB; PA134936197; -.
DR VEuPathDB; HostDB:ENSG00000086200; -.
DR eggNOG; KOG1993; Eukaryota.
DR GeneTree; ENSGT00390000014071; -.
DR HOGENOM; CLU_003886_0_0_1; -.
DR InParanoid; Q9UI26; -.
DR OMA; SFHYVFH; -.
DR OrthoDB; 228179at2759; -.
DR PhylomeDB; Q9UI26; -.
DR TreeFam; TF324336; -.
DR PathwayCommons; Q9UI26; -.
DR SignaLink; Q9UI26; -.
DR BioGRID-ORCS; 51194; 686 hits in 1096 CRISPR screens.
DR ChiTaRS; IPO11; human.
DR GeneWiki; IPO11; -.
DR GenomeRNAi; 51194; -.
DR Pharos; Q9UI26; Tbio.
DR PRO; PR:Q9UI26; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UI26; protein.
DR Bgee; ENSG00000086200; Expressed in colonic epithelium and 172 other tissues.
DR ExpressionAtlas; Q9UI26; baseline and differential.
DR Genevisible; Q9UI26; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
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; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..975
FT /note="Importin-11"
FT /id="PRO_0000120756"
FT DOMAIN 28..100
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 123..160
FT /note="HEAT 1"
FT REPEAT 209..248
FT /note="HEAT 2"
FT REPEAT 318..356
FT /note="HEAT 3"
FT REPEAT 422..459
FT /note="HEAT 4"
FT REPEAT 473..509
FT /note="HEAT 5"
FT REPEAT 511..548
FT /note="HEAT 6"
FT REPEAT 555..593
FT /note="HEAT 7"
FT REPEAT 600..636
FT /note="HEAT 8"
FT REPEAT 640..677
FT /note="HEAT 9"
FT REPEAT 683..720
FT /note="HEAT 10"
FT REPEAT 743..764
FT /note="HEAT 11"
FT REPEAT 765..804
FT /note="HEAT 12"
FT REPEAT 819..849
FT /note="HEAT 13"
FT REPEAT 850..887
FT /note="HEAT 14"
FT REPEAT 957..974
FT /note="HEAT 15"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MVQPIIHLGYVVYSLLYLGYKPVQHVTALNTVSSCHKMVSM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041420"
FT VARIANT 260
FT /note="N -> D (in dbSNP:rs35107530)"
FT /id="VAR_050004"
FT VARIANT 937
FT /note="I -> V (in dbSNP:rs11544795)"
FT /id="VAR_050005"
FT CONFLICT 53
FT /note="T -> A (in Ref. 2; BAG63985)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="I -> T (in Ref. 2; BAA91843)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="G -> V (in Ref. 2; BAG63985)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="A -> T (in Ref. 2; BAG63985)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="I -> V (in Ref. 2; BAA91843)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="V -> A (in Ref. 2; BAA91843)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="L -> S (in Ref. 2; BAG63985)"
FT /evidence="ECO:0000305"
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
