Full text data of KPNA4
KPNA4
(QIP1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Importin subunit alpha-3 (Importin alpha Q1; Qip1; Karyopherin subunit alpha-4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Importin subunit alpha-3 (Importin alpha Q1; Qip1; Karyopherin subunit alpha-4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O00629
ID IMA3_HUMAN Reviewed; 521 AA.
AC O00629; A8K4S6; D3DNM2; O00190;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Importin subunit alpha-3;
DE AltName: Full=Importin alpha Q1;
DE Short=Qip1;
DE AltName: Full=Karyopherin subunit alpha-4;
GN Name=KPNA4; Synonyms=QIP1;
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].
RX PubMed=9168958; DOI=10.1006/bbrc.1997.6535;
RA Seki T., Tada S., Katada T., Enomoto T.;
RT "Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1:
RT discrimination of Qip1 and Rch1 from hSrp1 by their ability to
RT interact with DNA helicase Q1/RecQL.";
RL Biochem. Biophys. Res. Commun. 234:48-53(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=9395085; DOI=10.1016/S0014-5793(97)01265-9;
RA Koehler M., Ansieau S., Prehn S., Leutz A., Haller H., Hartmann E.;
RT "Cloning of two novel human importin-alpha subunits and analysis of
RT the expression pattern of the importin-alpha protein family.";
RL FEBS Lett. 417:104-108(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [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].
RC TISSUE=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 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP INTERACTION WITH SNAI1.
RX PubMed=21454664; DOI=10.1074/jbc.M110.213579;
RA Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.;
RT "Importin alpha protein acts as a negative regulator for Snail protein
RT nuclear import.";
RL J. Biol. Chem. 286:15126-15131(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 an adapter
CC protein for nuclear receptor KPNB1. Binds specifically and
CC directly to substrates containing either a simple or bipartite NLS
CC motif. Docking of the importin/substrate complex to the nuclear
CC pore complex (NPC) is mediated by KPNB1 through binding to
CC nucleoporin FxFG repeats 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 importin-beta and the three components separate and
CC importin-alpha and -beta are re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran from importin. 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
CC between the cytoplasm and nucleus. In vitro, mediates the nuclear
CC import of human cytomegalovirus UL84 by recognizing a non-
CC classical NLS. In vitro, mediates the nuclear import of human
CC cytomegalovirus UL84 by recognizing a non-classical NLS.
CC -!- SUBUNIT: Forms a complex with importin subunit beta-1. Interacts
CC with SNAI1.
CC -!- INTERACTION:
CC P46063:RECQL; NbExp=2; IntAct=EBI-396343, EBI-2823728;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, small
CC intestine, heart, skeletal muscle, lung and pancreas, but barely
CC detectable in kidney, thymus, colon and peripheral blood
CC leukocytes.
CC -!- DOMAIN: Consists of an N-terminal hydrophilic region, a
CC hydrophobic central region composed of 10 repeats, and a short
CC hydrophilic C-terminus. The N-terminal hydrophilic region contains
CC the importin beta binding domain (IBB domain), which is sufficient
CC for binding importin beta and essential for nuclear protein
CC import.
CC -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC autoregulatory sequence by interacting with the internal
CC autoinhibitory NLS. Binding of KPNB1 probably overlaps the
CC internal NLS and contributes to a high affinity for cytoplasmic
CC NLS-containing cargo substrates. After dissociation of the
CC importin/substrate complex in the nucleus the internal
CC autohibitory NLS contributes to a low affinity for nuclear NLS-
CC containing proteins (By similarity).
CC -!- DOMAIN: The major and minor NLS binding sites are mainly involved
CC in recognition of simple or bipartite NLS motifs. Structurally
CC located within in a helical surface groove they contain several
CC conserved Trp and Asn residues of the corresponding third helices
CC (H3) of ARM repeats which mainly contribute to binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the importin alpha family.
CC -!- SIMILARITY: Contains 10 ARM repeats.
CC -!- SIMILARITY: Contains 1 IBB domain.
CC -!- CAUTION: Was termed (PubMed:9395085) importin alpha-3.
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DR EMBL; AB002533; BAA19546.1; -; mRNA.
DR EMBL; AK291041; BAF83730.1; -; mRNA.
DR EMBL; CH471052; EAW78632.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78633.1; -; Genomic_DNA.
DR EMBL; U93240; AAC25605.1; -; mRNA.
DR EMBL; Y12393; CAA73025.1; -; mRNA.
DR EMBL; BC028691; AAH28691.1; -; mRNA.
DR EMBL; BC034493; AAH34493.1; -; mRNA.
DR PIR; JC5505; JC5505.
DR RefSeq; NP_002259.1; NM_002268.4.
DR UniGene; Hs.467866; -.
DR ProteinModelPortal; O00629; -.
DR SMR; O00629; 11-486.
DR DIP; DIP-32982N; -.
DR IntAct; O00629; 18.
DR MINT; MINT-5003750; -.
DR STRING; 9606.ENSP00000334373; -.
DR PhosphoSite; O00629; -.
DR PaxDb; O00629; -.
DR PeptideAtlas; O00629; -.
DR PRIDE; O00629; -.
DR DNASU; 3840; -.
DR Ensembl; ENST00000334256; ENSP00000334373; ENSG00000186432.
DR GeneID; 3840; -.
DR KEGG; hsa:3840; -.
DR UCSC; uc003fdn.3; human.
DR CTD; 3840; -.
DR GeneCards; GC03M160212; -.
DR HGNC; HGNC:6397; KPNA4.
DR HPA; HPA043154; -.
DR MIM; 602970; gene.
DR neXtProt; NX_O00629; -.
DR PharmGKB; PA30188; -.
DR eggNOG; COG5064; -.
DR HOGENOM; HOG000167616; -.
DR HOVERGEN; HBG001846; -.
DR InParanoid; O00629; -.
DR OMA; TMRRQRT; -.
DR OrthoDB; EOG7VHSWV; -.
DR PhylomeDB; O00629; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; O00629; -.
DR ChiTaRS; KPNA4; human.
DR GeneWiki; KPNA4; -.
DR GenomeRNAi; 3840; -.
DR NextBio; 15111; -.
DR PMAP-CutDB; O00629; -.
DR PRO; PR:O00629; -.
DR ArrayExpress; O00629; -.
DR Bgee; O00629; -.
DR CleanEx; HS_KPNA4; -.
DR Genevestigator; O00629; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR024931; Importing_su_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 521 Importin subunit alpha-3.
FT /FTId=PRO_0000120726.
FT DOMAIN 2 58 IBB.
FT REPEAT 66 106 ARM 1; truncated.
FT REPEAT 107 149 ARM 2.
FT REPEAT 150 194 ARM 3.
FT REPEAT 195 233 ARM 4.
FT REPEAT 234 278 ARM 5.
FT REPEAT 279 318 ARM 6.
FT REPEAT 319 360 ARM 7.
FT REPEAT 361 400 ARM 8.
FT REPEAT 401 443 ARM 9.
FT REPEAT 447 485 ARM 10; atypical.
FT REGION 137 229 NLS binding site (major) (By similarity).
FT REGION 306 394 NLS binding site (minor) (By similarity).
FT MOTIF 43 52 Nuclear localization signal (By
FT similarity).
FT COMPBIAS 233 236 Poly-Pro.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 60 60 Phosphoserine.
FT CONFLICT 241 241 Q -> T (in Ref. 2; CAA73025).
SQ SEQUENCE 521 AA; 57887 MW; D98BC45002C9F57E CRC64;
MADNEKLDNQ RLKNFKNKGR DLETMRRQRN EVVVELRKNK RDEHLLKRRN VPHEDICEDS
DIDGDYRVQN TSLEAIVQNA SSDNQGIQLS AVQAARKLLS SDRNPPIDDL IKSGILPILV
HCLERDDNPS LQFEAAWALT NIASGTSEQT QAVVQSNAVP LFLRLLHSPH QNVCEQAVWA
LGNIIGDGPQ CRDYVISLGV VKPLLSFISP SIPITFLRNV TWVMVNLCRH KDPPPPMETI
QEILPALCVL IHHTDVNILV DTVWALSYLT DAGNEQIQMV IDSGIVPHLV PLLSHQEVKV
QTAALRAVGN IVTGTDEQTQ VVLNCDALSH FPALLTHPKE KINKEAVWFL SNITAGNQQQ
VQAVIDANLV PMIIHLLDKG DFGTQKEAAW AISNLTISGR KDQVAYLIQQ NVIPPFCNLL
TVKDAQVVQV VLDGLSNILK MAEDEAETIG NLIEECGGLE KIEQLQNHEN EDIYKLAYEI
IDQFFSSDDI DEDPSLVPEA IQGGTFGFNS SANVPTEGFQ F
//
ID IMA3_HUMAN Reviewed; 521 AA.
AC O00629; A8K4S6; D3DNM2; O00190;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Importin subunit alpha-3;
DE AltName: Full=Importin alpha Q1;
DE Short=Qip1;
DE AltName: Full=Karyopherin subunit alpha-4;
GN Name=KPNA4; Synonyms=QIP1;
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].
RX PubMed=9168958; DOI=10.1006/bbrc.1997.6535;
RA Seki T., Tada S., Katada T., Enomoto T.;
RT "Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1:
RT discrimination of Qip1 and Rch1 from hSrp1 by their ability to
RT interact with DNA helicase Q1/RecQL.";
RL Biochem. Biophys. Res. Commun. 234:48-53(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=9395085; DOI=10.1016/S0014-5793(97)01265-9;
RA Koehler M., Ansieau S., Prehn S., Leutz A., Haller H., Hartmann E.;
RT "Cloning of two novel human importin-alpha subunits and analysis of
RT the expression pattern of the importin-alpha protein family.";
RL FEBS Lett. 417:104-108(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [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].
RC TISSUE=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 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP INTERACTION WITH SNAI1.
RX PubMed=21454664; DOI=10.1074/jbc.M110.213579;
RA Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.;
RT "Importin alpha protein acts as a negative regulator for Snail protein
RT nuclear import.";
RL J. Biol. Chem. 286:15126-15131(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 an adapter
CC protein for nuclear receptor KPNB1. Binds specifically and
CC directly to substrates containing either a simple or bipartite NLS
CC motif. Docking of the importin/substrate complex to the nuclear
CC pore complex (NPC) is mediated by KPNB1 through binding to
CC nucleoporin FxFG repeats 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 importin-beta and the three components separate and
CC importin-alpha and -beta are re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran from importin. 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
CC between the cytoplasm and nucleus. In vitro, mediates the nuclear
CC import of human cytomegalovirus UL84 by recognizing a non-
CC classical NLS. In vitro, mediates the nuclear import of human
CC cytomegalovirus UL84 by recognizing a non-classical NLS.
CC -!- SUBUNIT: Forms a complex with importin subunit beta-1. Interacts
CC with SNAI1.
CC -!- INTERACTION:
CC P46063:RECQL; NbExp=2; IntAct=EBI-396343, EBI-2823728;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, small
CC intestine, heart, skeletal muscle, lung and pancreas, but barely
CC detectable in kidney, thymus, colon and peripheral blood
CC leukocytes.
CC -!- DOMAIN: Consists of an N-terminal hydrophilic region, a
CC hydrophobic central region composed of 10 repeats, and a short
CC hydrophilic C-terminus. The N-terminal hydrophilic region contains
CC the importin beta binding domain (IBB domain), which is sufficient
CC for binding importin beta and essential for nuclear protein
CC import.
CC -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC autoregulatory sequence by interacting with the internal
CC autoinhibitory NLS. Binding of KPNB1 probably overlaps the
CC internal NLS and contributes to a high affinity for cytoplasmic
CC NLS-containing cargo substrates. After dissociation of the
CC importin/substrate complex in the nucleus the internal
CC autohibitory NLS contributes to a low affinity for nuclear NLS-
CC containing proteins (By similarity).
CC -!- DOMAIN: The major and minor NLS binding sites are mainly involved
CC in recognition of simple or bipartite NLS motifs. Structurally
CC located within in a helical surface groove they contain several
CC conserved Trp and Asn residues of the corresponding third helices
CC (H3) of ARM repeats which mainly contribute to binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the importin alpha family.
CC -!- SIMILARITY: Contains 10 ARM repeats.
CC -!- SIMILARITY: Contains 1 IBB domain.
CC -!- CAUTION: Was termed (PubMed:9395085) importin alpha-3.
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DR EMBL; AB002533; BAA19546.1; -; mRNA.
DR EMBL; AK291041; BAF83730.1; -; mRNA.
DR EMBL; CH471052; EAW78632.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78633.1; -; Genomic_DNA.
DR EMBL; U93240; AAC25605.1; -; mRNA.
DR EMBL; Y12393; CAA73025.1; -; mRNA.
DR EMBL; BC028691; AAH28691.1; -; mRNA.
DR EMBL; BC034493; AAH34493.1; -; mRNA.
DR PIR; JC5505; JC5505.
DR RefSeq; NP_002259.1; NM_002268.4.
DR UniGene; Hs.467866; -.
DR ProteinModelPortal; O00629; -.
DR SMR; O00629; 11-486.
DR DIP; DIP-32982N; -.
DR IntAct; O00629; 18.
DR MINT; MINT-5003750; -.
DR STRING; 9606.ENSP00000334373; -.
DR PhosphoSite; O00629; -.
DR PaxDb; O00629; -.
DR PeptideAtlas; O00629; -.
DR PRIDE; O00629; -.
DR DNASU; 3840; -.
DR Ensembl; ENST00000334256; ENSP00000334373; ENSG00000186432.
DR GeneID; 3840; -.
DR KEGG; hsa:3840; -.
DR UCSC; uc003fdn.3; human.
DR CTD; 3840; -.
DR GeneCards; GC03M160212; -.
DR HGNC; HGNC:6397; KPNA4.
DR HPA; HPA043154; -.
DR MIM; 602970; gene.
DR neXtProt; NX_O00629; -.
DR PharmGKB; PA30188; -.
DR eggNOG; COG5064; -.
DR HOGENOM; HOG000167616; -.
DR HOVERGEN; HBG001846; -.
DR InParanoid; O00629; -.
DR OMA; TMRRQRT; -.
DR OrthoDB; EOG7VHSWV; -.
DR PhylomeDB; O00629; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; O00629; -.
DR ChiTaRS; KPNA4; human.
DR GeneWiki; KPNA4; -.
DR GenomeRNAi; 3840; -.
DR NextBio; 15111; -.
DR PMAP-CutDB; O00629; -.
DR PRO; PR:O00629; -.
DR ArrayExpress; O00629; -.
DR Bgee; O00629; -.
DR CleanEx; HS_KPNA4; -.
DR Genevestigator; O00629; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR024931; Importing_su_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 521 Importin subunit alpha-3.
FT /FTId=PRO_0000120726.
FT DOMAIN 2 58 IBB.
FT REPEAT 66 106 ARM 1; truncated.
FT REPEAT 107 149 ARM 2.
FT REPEAT 150 194 ARM 3.
FT REPEAT 195 233 ARM 4.
FT REPEAT 234 278 ARM 5.
FT REPEAT 279 318 ARM 6.
FT REPEAT 319 360 ARM 7.
FT REPEAT 361 400 ARM 8.
FT REPEAT 401 443 ARM 9.
FT REPEAT 447 485 ARM 10; atypical.
FT REGION 137 229 NLS binding site (major) (By similarity).
FT REGION 306 394 NLS binding site (minor) (By similarity).
FT MOTIF 43 52 Nuclear localization signal (By
FT similarity).
FT COMPBIAS 233 236 Poly-Pro.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 60 60 Phosphoserine.
FT CONFLICT 241 241 Q -> T (in Ref. 2; CAA73025).
SQ SEQUENCE 521 AA; 57887 MW; D98BC45002C9F57E CRC64;
MADNEKLDNQ RLKNFKNKGR DLETMRRQRN EVVVELRKNK RDEHLLKRRN VPHEDICEDS
DIDGDYRVQN TSLEAIVQNA SSDNQGIQLS AVQAARKLLS SDRNPPIDDL IKSGILPILV
HCLERDDNPS LQFEAAWALT NIASGTSEQT QAVVQSNAVP LFLRLLHSPH QNVCEQAVWA
LGNIIGDGPQ CRDYVISLGV VKPLLSFISP SIPITFLRNV TWVMVNLCRH KDPPPPMETI
QEILPALCVL IHHTDVNILV DTVWALSYLT DAGNEQIQMV IDSGIVPHLV PLLSHQEVKV
QTAALRAVGN IVTGTDEQTQ VVLNCDALSH FPALLTHPKE KINKEAVWFL SNITAGNQQQ
VQAVIDANLV PMIIHLLDKG DFGTQKEAAW AISNLTISGR KDQVAYLIQQ NVIPPFCNLL
TVKDAQVVQV VLDGLSNILK MAEDEAETIG NLIEECGGLE KIEQLQNHEN EDIYKLAYEI
IDQFFSSDDI DEDPSLVPEA IQGGTFGFNS SANVPTEGFQ F
//
MIM
602970
*RECORD*
*FIELD* NO
602970
*FIELD* TI
*602970 KARYOPHERIN ALPHA-4; KPNA4
;;IMPORTIN ALPHA-3;;
QIP1
*FIELD* TX
DESCRIPTION
read more
The nuclear import of karyophilic proteins is directed by short amino
acid sequences termed nuclear localization signals (NLSs). Karyopherins,
or importins, such as KPNA4, are cytoplasmic proteins that recognize
NLSs and dock NLS-containing proteins to the nuclear pore complex
(summary by Seki et al., 1997).
CLONING
Using a yeast 2-hybrid system to identify proteins that interact with
the DNA helicase Q1 (RECQL; 600537), Seki et al. (1997) isolated HeLa
cell cDNAs encoding QIP1. The predicted 521-amino acid QIP1 protein
contains the conserved N-terminal binding site for karyopherin-beta (see
KPNB1; 602738) and a series of 7 degenerate 'armadillo' repeats, which
are 42-amino acid motifs implicated in protein-protein interactions.
Human QIP1 has 50% amino acid identity with human KPNA2 (600685), 49%
with Xenopus importin-alpha, 47% with human KPNA1 (600686), and 46% with
S. cerevisiae Srp1.
Kohler et al. (1997) isolated a human KPNA4 cDNA. The predicted KPNA4
protein contains an N-terminal importin-beta-binding (IBB) domain, 8
armadillo repeats, and a C-terminal acidic region, all of which are
characteristics of importin-alphas. Of the known human importin-alphas,
KPNA4 shares the highest sequence identity with KPNA3 (601892). Northern
blot analysis detected a 4.4-kb KPNA4 transcript in all tissues tested.
However, expression levels varied considerably among tissues, with the
highest expression in testis, ovary, small intestine, and pancreas, and
the lowest expression in kidney, thymus, colon, and peripheral blood
leukocytes.
GENE FUNCTION
Seki et al. (1997) demonstrated that QIP1 interacted with the NLSs of
DNA helicase Q1 and SV40 T antigen.
Using an in vitro import assay based on permeabilized HeLa cells to
study the import substrate specificity of all ubiquitously expressed
importins, including KPNA4, Kohler et al. (1999) found that all
importins tested were able to transport HNRNPK (600712) and PCAF
(602303), in addition to the standard test substrates, but only KPNA4
showed a strong preference for the import of GDP/GTP exchange factor
RCC1 (179710), which is exclusively located inside the nucleus. When
HNRNPK, PCAF, and RCC1 were offered with a competing substrate
nucleoplasmin (164040), they found that substrate binding was diminished
or abolished in some importins and retained in others.
MAPPING
By fluorescence in situ hybridization, Ayala-Madrigal et al. (2000)
mapped the KPNA4 gene to chromosome 11q22. However, Gross (2011) mapped
the KPNA4 gene to chromosome 3q25.33 based on an alignment of the KPNA4
sequence (GenBank GENBANK AB002533) with the genomic sequence (GRCh37).
*FIELD* RF
1. Ayala-Madrigal, M. L.; Doerr, S.; Ramirez-Duenas, M. L.; Hansmann,
I.: Assignment of KPNA4 and KPNB1 encoding karyopherin alpha 4 and
beta 1 to human chromosome bands 11q22 and 17q21 respectively, by
in situ hybridization. Cytogenet. Cell Genet. 89: 258-259, 2000.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 2/25/2011.
3. Kohler, M.; Ansieau, S.; Prehn, S.; Leutz, A.; Haller, H.; Hartmann,
E.: Cloning of two novel human importin-alpha subunits and analysis
of the expression pattern of the importin-alpha protein family. FEBS
Lett. 417: 104-108, 1997.
4. Kohler, M.; Speck, C.; Christiansen, M.; Bischoff, F. R.; Prehn,
S.; Haller, H.; Gorlich, D.; Hartmann, E.: Evidence for distinct
substrate specificities of importin alpha family members in nuclear
protein import. Molec. Cell. Biol. 19: 7782-7791, 1999.
5. Seki, T.; Tada, S.; Katada, T.; Enomoto, T.: Cloning of a cDNA
encoding a novel importin-alpha homologue, Qip1: discrimination of
Qip1 and Rch1 from hSrp1 by their ability to interact with DNA helicase
Q1/RecQL. Biochem. Biophys. Res. Commun. 234: 48-53, 1997.
*FIELD* CN
Matthew B. Gross - updated: 02/25/2011
Patricia A. Hartz - updated: 11/14/2006
Carol A. Bocchini - updated: 1/16/2001
Patti M. Sherman - updated: 2/14/2000
*FIELD* CD
Patti M. Sherman: 8/14/1998
*FIELD* ED
mgross: 02/25/2011
wwang: 11/14/2006
carol: 1/16/2001
mgross: 2/15/2000
psherman: 2/14/2000
alopez: 8/25/1998
*RECORD*
*FIELD* NO
602970
*FIELD* TI
*602970 KARYOPHERIN ALPHA-4; KPNA4
;;IMPORTIN ALPHA-3;;
QIP1
*FIELD* TX
DESCRIPTION
read more
The nuclear import of karyophilic proteins is directed by short amino
acid sequences termed nuclear localization signals (NLSs). Karyopherins,
or importins, such as KPNA4, are cytoplasmic proteins that recognize
NLSs and dock NLS-containing proteins to the nuclear pore complex
(summary by Seki et al., 1997).
CLONING
Using a yeast 2-hybrid system to identify proteins that interact with
the DNA helicase Q1 (RECQL; 600537), Seki et al. (1997) isolated HeLa
cell cDNAs encoding QIP1. The predicted 521-amino acid QIP1 protein
contains the conserved N-terminal binding site for karyopherin-beta (see
KPNB1; 602738) and a series of 7 degenerate 'armadillo' repeats, which
are 42-amino acid motifs implicated in protein-protein interactions.
Human QIP1 has 50% amino acid identity with human KPNA2 (600685), 49%
with Xenopus importin-alpha, 47% with human KPNA1 (600686), and 46% with
S. cerevisiae Srp1.
Kohler et al. (1997) isolated a human KPNA4 cDNA. The predicted KPNA4
protein contains an N-terminal importin-beta-binding (IBB) domain, 8
armadillo repeats, and a C-terminal acidic region, all of which are
characteristics of importin-alphas. Of the known human importin-alphas,
KPNA4 shares the highest sequence identity with KPNA3 (601892). Northern
blot analysis detected a 4.4-kb KPNA4 transcript in all tissues tested.
However, expression levels varied considerably among tissues, with the
highest expression in testis, ovary, small intestine, and pancreas, and
the lowest expression in kidney, thymus, colon, and peripheral blood
leukocytes.
GENE FUNCTION
Seki et al. (1997) demonstrated that QIP1 interacted with the NLSs of
DNA helicase Q1 and SV40 T antigen.
Using an in vitro import assay based on permeabilized HeLa cells to
study the import substrate specificity of all ubiquitously expressed
importins, including KPNA4, Kohler et al. (1999) found that all
importins tested were able to transport HNRNPK (600712) and PCAF
(602303), in addition to the standard test substrates, but only KPNA4
showed a strong preference for the import of GDP/GTP exchange factor
RCC1 (179710), which is exclusively located inside the nucleus. When
HNRNPK, PCAF, and RCC1 were offered with a competing substrate
nucleoplasmin (164040), they found that substrate binding was diminished
or abolished in some importins and retained in others.
MAPPING
By fluorescence in situ hybridization, Ayala-Madrigal et al. (2000)
mapped the KPNA4 gene to chromosome 11q22. However, Gross (2011) mapped
the KPNA4 gene to chromosome 3q25.33 based on an alignment of the KPNA4
sequence (GenBank GENBANK AB002533) with the genomic sequence (GRCh37).
*FIELD* RF
1. Ayala-Madrigal, M. L.; Doerr, S.; Ramirez-Duenas, M. L.; Hansmann,
I.: Assignment of KPNA4 and KPNB1 encoding karyopherin alpha 4 and
beta 1 to human chromosome bands 11q22 and 17q21 respectively, by
in situ hybridization. Cytogenet. Cell Genet. 89: 258-259, 2000.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 2/25/2011.
3. Kohler, M.; Ansieau, S.; Prehn, S.; Leutz, A.; Haller, H.; Hartmann,
E.: Cloning of two novel human importin-alpha subunits and analysis
of the expression pattern of the importin-alpha protein family. FEBS
Lett. 417: 104-108, 1997.
4. Kohler, M.; Speck, C.; Christiansen, M.; Bischoff, F. R.; Prehn,
S.; Haller, H.; Gorlich, D.; Hartmann, E.: Evidence for distinct
substrate specificities of importin alpha family members in nuclear
protein import. Molec. Cell. Biol. 19: 7782-7791, 1999.
5. Seki, T.; Tada, S.; Katada, T.; Enomoto, T.: Cloning of a cDNA
encoding a novel importin-alpha homologue, Qip1: discrimination of
Qip1 and Rch1 from hSrp1 by their ability to interact with DNA helicase
Q1/RecQL. Biochem. Biophys. Res. Commun. 234: 48-53, 1997.
*FIELD* CN
Matthew B. Gross - updated: 02/25/2011
Patricia A. Hartz - updated: 11/14/2006
Carol A. Bocchini - updated: 1/16/2001
Patti M. Sherman - updated: 2/14/2000
*FIELD* CD
Patti M. Sherman: 8/14/1998
*FIELD* ED
mgross: 02/25/2011
wwang: 11/14/2006
carol: 1/16/2001
mgross: 2/15/2000
psherman: 2/14/2000
alopez: 8/25/1998