Full text data of IPO4
IPO4
(IMP4B, RANBP4)
[Confidence: low (only semi-automatic identification from reviews)]
Importin-4; Imp4 (Importin-4b; Imp4b; Ran-binding protein 4; RanBP4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Importin-4; Imp4 (Importin-4b; Imp4b; Ran-binding protein 4; RanBP4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8TEX9
ID IPO4_HUMAN Reviewed; 1081 AA.
AC Q8TEX9; B2RN95; Q2NL96; Q86TZ9; Q8NCG8; Q96SJ3; Q9BTI4; Q9H5L0;
read moreDT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Importin-4;
DE Short=Imp4;
DE AltName: Full=Importin-4b;
DE Short=Imp4b;
DE AltName: Full=Ran-binding protein 4;
DE Short=RanBP4;
GN Name=IPO4; Synonyms=IMP4B, RANBP4;
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), FUNCTION, INTERACTION WITH
RP RPS3A, AND VARIANTS VAL-513 AND ALA-580.
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 MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Placenta, and Skin;
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 PROTEIN SEQUENCE OF 1-11; 24-33; 55-62; 82-90; 402-411; 528-534;
RP 751-761; 900-916; 941-951 AND 1042-1053, ACETYLATION AT MET-1, AND
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 233-1081 (ISOFORM 1),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1081 (ISOFORM 2), AND
RP VARIANTS VAL-513 AND ALA-580.
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 [8]
RP INTERACTION WITH HCMV UL84.
RX PubMed=12610148; DOI=10.1128/JVI.77.6.3734-3748.2003;
RA Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.;
RT "A nonconventional nuclear localization signal within the UL84 protein
RT of human cytomegalovirus mediates nuclear import via the importin
RT alpha/beta pathway.";
RL J. Virol. 77:3734-3748(2003).
RN [9]
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 [10]
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).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH ASF1A; ASF1B; CDNA1; HISTONES H3.2
RP AND H4.
RX PubMed=22407294; DOI=10.1038/emboj.2012.55;
RA Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.;
RT "Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1
RT function in S-phase histone supply.";
RL EMBO J. 31:2013-2023(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 RPS3A. In
CC vitro, mediates the nuclear import of human cytomegalovirus UL84
CC by recognizing a non-classical NLS.
CC -!- SUBUNIT: Binds with high affinity to RPS3A. The binding is coupled
CC to RanGTP cycles. Binds to human cytomegalovirus UL84. Found in a
CC cytosolic complex with ASF1A, ASF1B, CDAN1 and histones H3.1 and
CC H4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TEX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TEX9-2; Sequence=VSP_009339;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 6 HEAT repeats.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15616.1; Type=Frameshift; Positions=234;
CC Sequence=BAB55421.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC11174.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAD62595.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF411122; AAL78660.1; -; mRNA.
DR EMBL; BX248267; CAD62595.1; ALT_INIT; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66078.1; -; Genomic_DNA.
DR EMBL; BC003690; AAH03690.2; -; mRNA.
DR EMBL; BC110804; AAI10805.1; -; mRNA.
DR EMBL; BC136759; AAI36760.1; -; mRNA.
DR EMBL; AK026991; BAB15616.1; ALT_FRAME; mRNA.
DR EMBL; AK027871; BAB55421.1; ALT_INIT; mRNA.
DR EMBL; AK074743; BAC11174.1; ALT_INIT; mRNA.
DR RefSeq; NP_078934.3; NM_024658.3.
DR UniGene; Hs.411865; -.
DR ProteinModelPortal; Q8TEX9; -.
DR SMR; Q8TEX9; 347-710.
DR DIP; DIP-32944N; -.
DR IntAct; Q8TEX9; 10.
DR MINT; MINT-3045897; -.
DR STRING; 9606.ENSP00000346453; -.
DR PhosphoSite; Q8TEX9; -.
DR DMDM; 126302558; -.
DR PaxDb; Q8TEX9; -.
DR PRIDE; Q8TEX9; -.
DR Ensembl; ENST00000354464; ENSP00000346453; ENSG00000196497.
DR GeneID; 79711; -.
DR KEGG; hsa:79711; -.
DR UCSC; uc001wmu.2; human.
DR CTD; 79711; -.
DR GeneCards; GC14M024649; -.
DR HGNC; HGNC:19426; IPO4.
DR HPA; HPA039043; -.
DR neXtProt; NX_Q8TEX9; -.
DR PharmGKB; PA134968932; -.
DR eggNOG; NOG249123; -.
DR HOVERGEN; HBG049052; -.
DR InParanoid; Q8TEX9; -.
DR OMA; QRETEHS; -.
DR OrthoDB; EOG7C5M7J; -.
DR ChiTaRS; IPO4; human.
DR GeneWiki; IPO4; -.
DR GenomeRNAi; 79711; -.
DR NextBio; 69037; -.
DR PRO; PR:Q8TEX9; -.
DR ArrayExpress; Q8TEX9; -.
DR Bgee; Q8TEX9; -.
DR CleanEx; HS_IPO4; -.
DR Genevestigator; Q8TEX9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
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; PS50077; HEAT_REPEAT; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Polymorphism; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1 1081 Importin-4.
FT /FTId=PRO_0000120748.
FT DOMAIN 24 90 Importin N-terminal.
FT REPEAT 348 385 HEAT 1.
FT REPEAT 390 427 HEAT 2.
FT REPEAT 431 471 HEAT 3.
FT REPEAT 475 513 HEAT 4.
FT REPEAT 895 932 HEAT 5.
FT REPEAT 936 974 HEAT 6.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 1038 1038 P -> PGE (in isoform 2).
FT /FTId=VSP_009339.
FT VARIANT 513 513 A -> V (in dbSNP:rs7146310).
FT /FTId=VAR_030758.
FT VARIANT 580 580 P -> A (in dbSNP:rs11550452).
FT /FTId=VAR_030759.
FT CONFLICT 865 865 K -> R (in Ref. 7; BAB15616).
FT CONFLICT 943 943 G -> E (in Ref. 7; BAB55421).
SQ SEQUENCE 1081 AA; 118715 MW; 36D11AF0D6DA8B1E CRC64;
MESAGLEQLL RELLLPDTER IRRATEQLQI VLRAPAALPA LCDLLASAAD PQIRQFAAVL
TRRRLNTRWR RLAAEQRESL KSLILTALQR ETEHCVSLSL AQLSATIFRK EGLEAWPQLL
QLLQHSTHSP HSPEREMGLL LLSVVVTSRP EAFQPHHREL LRLLNETLGE VGSPGLLFYS
LRTLTTMAPY LSTEDVPLAR MLVPKLIMAM QTLIPIDEAK ACEALEALDE LLESEVPVIT
PYLSEVLTFC LEVARNVALG NAIRIRILCC LTFLVKVKSK ALLKNRLLPP LLHTLFPIVA
AEPPPGQLDP EDQDSEEEEL EIELMGETPK HFAVQVVDML ALHLPPEKLC PQLMPMLEEA
LRSESPYQRK AGLLVLAVLS DGAGDHIRQR LLPPLLQIVC KGLEDPSQVV RNAALFALGQ
FSENLQPHIS SYSREVMPLL LAYLKSVPLG HTHHLAKACY ALENFVENLG PKVQPYLPEL
MECMLQLLRN PSSPRAKELA VSALGAIATA AQASLLPYFP AIMEHLREFL LTGREDLQPV
QIQSLETLGV LARAVGEPMR PLAEECCQLG LGLCDQVDDP DLRRCTYSLF AALSGLMGEG
LAPHLEQITT LMLLSLRSTE GIVPQYDGSS SFLLFDDESD GEEEEELMDE DVEEEDDSEI
SGYSVENAFF DEKEDTCAAV GEISVNTSVA FLPYMESVFE EVFKLLECPH LNVRKAAHEA
LGQFCCALHK ACQSCPSEPN TAALQAALAR VVPSYMQAVN RERERQVVMA VLEALTGVLR
SCGTLTLKPP GRLAELCGVL KAVLQRKTAC QDTDEEEEEE DDDQAEYDAM LLEHAGEAIP
ALAAAAGGDS FAPFFAGFLP LLVCKTKQGC TVAEKSFAVG TLAETIQGLG AASAQFVSRL
LPVLLSTAQE ADPEVRSNAI FGMGVLAEHG GHPAQEHFPK LLGLLFPLLA RERHDRVRDN
ICGALARLLM ASPTRKPEPQ VLAALLHALP LKEDLEEWVT IGRLFSFLYQ SSPDQVIDVA
PELLRICSLI LADNKIPPDT KAALLLLLTF LAKQHTDSFQ AALGSLPVDK AQELQAVLGL
S
//
ID IPO4_HUMAN Reviewed; 1081 AA.
AC Q8TEX9; B2RN95; Q2NL96; Q86TZ9; Q8NCG8; Q96SJ3; Q9BTI4; Q9H5L0;
read moreDT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Importin-4;
DE Short=Imp4;
DE AltName: Full=Importin-4b;
DE Short=Imp4b;
DE AltName: Full=Ran-binding protein 4;
DE Short=RanBP4;
GN Name=IPO4; Synonyms=IMP4B, RANBP4;
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), FUNCTION, INTERACTION WITH
RP RPS3A, AND VARIANTS VAL-513 AND ALA-580.
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 MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Placenta, and Skin;
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 PROTEIN SEQUENCE OF 1-11; 24-33; 55-62; 82-90; 402-411; 528-534;
RP 751-761; 900-916; 941-951 AND 1042-1053, ACETYLATION AT MET-1, AND
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 233-1081 (ISOFORM 1),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1081 (ISOFORM 2), AND
RP VARIANTS VAL-513 AND ALA-580.
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 [8]
RP INTERACTION WITH HCMV UL84.
RX PubMed=12610148; DOI=10.1128/JVI.77.6.3734-3748.2003;
RA Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.;
RT "A nonconventional nuclear localization signal within the UL84 protein
RT of human cytomegalovirus mediates nuclear import via the importin
RT alpha/beta pathway.";
RL J. Virol. 77:3734-3748(2003).
RN [9]
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 [10]
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).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH ASF1A; ASF1B; CDNA1; HISTONES H3.2
RP AND H4.
RX PubMed=22407294; DOI=10.1038/emboj.2012.55;
RA Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.;
RT "Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1
RT function in S-phase histone supply.";
RL EMBO J. 31:2013-2023(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 RPS3A. In
CC vitro, mediates the nuclear import of human cytomegalovirus UL84
CC by recognizing a non-classical NLS.
CC -!- SUBUNIT: Binds with high affinity to RPS3A. The binding is coupled
CC to RanGTP cycles. Binds to human cytomegalovirus UL84. Found in a
CC cytosolic complex with ASF1A, ASF1B, CDAN1 and histones H3.1 and
CC H4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TEX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TEX9-2; Sequence=VSP_009339;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 6 HEAT repeats.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15616.1; Type=Frameshift; Positions=234;
CC Sequence=BAB55421.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC11174.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAD62595.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF411122; AAL78660.1; -; mRNA.
DR EMBL; BX248267; CAD62595.1; ALT_INIT; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66078.1; -; Genomic_DNA.
DR EMBL; BC003690; AAH03690.2; -; mRNA.
DR EMBL; BC110804; AAI10805.1; -; mRNA.
DR EMBL; BC136759; AAI36760.1; -; mRNA.
DR EMBL; AK026991; BAB15616.1; ALT_FRAME; mRNA.
DR EMBL; AK027871; BAB55421.1; ALT_INIT; mRNA.
DR EMBL; AK074743; BAC11174.1; ALT_INIT; mRNA.
DR RefSeq; NP_078934.3; NM_024658.3.
DR UniGene; Hs.411865; -.
DR ProteinModelPortal; Q8TEX9; -.
DR SMR; Q8TEX9; 347-710.
DR DIP; DIP-32944N; -.
DR IntAct; Q8TEX9; 10.
DR MINT; MINT-3045897; -.
DR STRING; 9606.ENSP00000346453; -.
DR PhosphoSite; Q8TEX9; -.
DR DMDM; 126302558; -.
DR PaxDb; Q8TEX9; -.
DR PRIDE; Q8TEX9; -.
DR Ensembl; ENST00000354464; ENSP00000346453; ENSG00000196497.
DR GeneID; 79711; -.
DR KEGG; hsa:79711; -.
DR UCSC; uc001wmu.2; human.
DR CTD; 79711; -.
DR GeneCards; GC14M024649; -.
DR HGNC; HGNC:19426; IPO4.
DR HPA; HPA039043; -.
DR neXtProt; NX_Q8TEX9; -.
DR PharmGKB; PA134968932; -.
DR eggNOG; NOG249123; -.
DR HOVERGEN; HBG049052; -.
DR InParanoid; Q8TEX9; -.
DR OMA; QRETEHS; -.
DR OrthoDB; EOG7C5M7J; -.
DR ChiTaRS; IPO4; human.
DR GeneWiki; IPO4; -.
DR GenomeRNAi; 79711; -.
DR NextBio; 69037; -.
DR PRO; PR:Q8TEX9; -.
DR ArrayExpress; Q8TEX9; -.
DR Bgee; Q8TEX9; -.
DR CleanEx; HS_IPO4; -.
DR Genevestigator; Q8TEX9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
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; PS50077; HEAT_REPEAT; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Polymorphism; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1 1081 Importin-4.
FT /FTId=PRO_0000120748.
FT DOMAIN 24 90 Importin N-terminal.
FT REPEAT 348 385 HEAT 1.
FT REPEAT 390 427 HEAT 2.
FT REPEAT 431 471 HEAT 3.
FT REPEAT 475 513 HEAT 4.
FT REPEAT 895 932 HEAT 5.
FT REPEAT 936 974 HEAT 6.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 1038 1038 P -> PGE (in isoform 2).
FT /FTId=VSP_009339.
FT VARIANT 513 513 A -> V (in dbSNP:rs7146310).
FT /FTId=VAR_030758.
FT VARIANT 580 580 P -> A (in dbSNP:rs11550452).
FT /FTId=VAR_030759.
FT CONFLICT 865 865 K -> R (in Ref. 7; BAB15616).
FT CONFLICT 943 943 G -> E (in Ref. 7; BAB55421).
SQ SEQUENCE 1081 AA; 118715 MW; 36D11AF0D6DA8B1E CRC64;
MESAGLEQLL RELLLPDTER IRRATEQLQI VLRAPAALPA LCDLLASAAD PQIRQFAAVL
TRRRLNTRWR RLAAEQRESL KSLILTALQR ETEHCVSLSL AQLSATIFRK EGLEAWPQLL
QLLQHSTHSP HSPEREMGLL LLSVVVTSRP EAFQPHHREL LRLLNETLGE VGSPGLLFYS
LRTLTTMAPY LSTEDVPLAR MLVPKLIMAM QTLIPIDEAK ACEALEALDE LLESEVPVIT
PYLSEVLTFC LEVARNVALG NAIRIRILCC LTFLVKVKSK ALLKNRLLPP LLHTLFPIVA
AEPPPGQLDP EDQDSEEEEL EIELMGETPK HFAVQVVDML ALHLPPEKLC PQLMPMLEEA
LRSESPYQRK AGLLVLAVLS DGAGDHIRQR LLPPLLQIVC KGLEDPSQVV RNAALFALGQ
FSENLQPHIS SYSREVMPLL LAYLKSVPLG HTHHLAKACY ALENFVENLG PKVQPYLPEL
MECMLQLLRN PSSPRAKELA VSALGAIATA AQASLLPYFP AIMEHLREFL LTGREDLQPV
QIQSLETLGV LARAVGEPMR PLAEECCQLG LGLCDQVDDP DLRRCTYSLF AALSGLMGEG
LAPHLEQITT LMLLSLRSTE GIVPQYDGSS SFLLFDDESD GEEEEELMDE DVEEEDDSEI
SGYSVENAFF DEKEDTCAAV GEISVNTSVA FLPYMESVFE EVFKLLECPH LNVRKAAHEA
LGQFCCALHK ACQSCPSEPN TAALQAALAR VVPSYMQAVN RERERQVVMA VLEALTGVLR
SCGTLTLKPP GRLAELCGVL KAVLQRKTAC QDTDEEEEEE DDDQAEYDAM LLEHAGEAIP
ALAAAAGGDS FAPFFAGFLP LLVCKTKQGC TVAEKSFAVG TLAETIQGLG AASAQFVSRL
LPVLLSTAQE ADPEVRSNAI FGMGVLAEHG GHPAQEHFPK LLGLLFPLLA RERHDRVRDN
ICGALARLLM ASPTRKPEPQ VLAALLHALP LKEDLEEWVT IGRLFSFLYQ SSPDQVIDVA
PELLRICSLI LADNKIPPDT KAALLLLLTF LAKQHTDSFQ AALGSLPVDK AQELQAVLGL
S
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