Full text data of XPO4
XPO4
(KIAA1721)
[Confidence: low (only semi-automatic identification from reviews)]
Exportin-4; Exp4
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Exportin-4; Exp4
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9C0E2
ID XPO4_HUMAN Reviewed; 1151 AA.
AC Q9C0E2; Q5VUZ5; Q8N3V6; Q9H934;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-NOV-2001, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Exportin-4;
DE Short=Exp4;
GN Name=XPO4; Synonyms=KIAA1721;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1151.
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 MRNA] OF 888-1151.
RC TISSUE=Skeletal muscle;
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 [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION IN NUCLEAR PROTEIN EXPORT, AND
RP IDENTIFICATION IN A COMPLEX WITH RAN AND EIF5A.
RX PubMed=10944119; DOI=10.1093/emboj/19.16.4362;
RA Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S.,
RA Hartmann E., Kutay U., Goerlich D.;
RT "Exportin 4: a mediator of a novel nuclear export pathway in higher
RT eukaryotes.";
RL EMBO J. 19:4362-4371(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION IN NUCLEAR PROTEIN EXPORT, IDENTIFICATION IN A COMPLEX WITH
RP RAN AND SMAD3, INTERACTION WITH SMAD3, AND SUBCELLULAR LOCATION.
RX PubMed=16449645; DOI=10.1128/MCB.26.4.1318-1332.2006;
RA Kurisaki A., Kurisaki K., Kowanetz M., Sugino H., Yoneda Y.,
RA Heldin C.-H., Moustakas A.;
RT "The mechanism of nuclear export of Smad3 involves exportin 4 and
RT Ran.";
RL Mol. Cell. Biol. 26:1318-1332(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-521, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP SPECTROMETRY.
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Mediates the nuclear export of proteins (cargos) with
CC broad substrate specificity. In the nucleus binds cooperatively to
CC its cargo and to the GTPase Ran in its active GTP-bound form.
CC Docking of this trimeric complex to the nuclear pore complex (NPC)
CC is mediated through binding to nucleoporins. Upon transit of a
CC nuclear export complex into the cytoplasm, disassembling of the
CC complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1
CC and RANGAP1, respectively) cause release of the cargo from the
CC export receptor. XPO4 then return to the nuclear compartment and
CC mediate another round of transport. The directionality of nuclear
CC export 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.
CC -!- SUBUNIT: Found in a complex with XPO4, Ran and EIF5A. Found in a
CC complex with XPO4, Ran and SMAD3. Interacts with SMAD3. Interacts
CC with Ran and cargo proteins in a GTP-dependent manner.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC the nucleus and the cytoplasm.
CC -!- SIMILARITY: Belongs to the exportin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14409.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB051508; BAB21812.1; -; mRNA.
DR EMBL; AL512652; CAH71795.1; -; Genomic_DNA.
DR EMBL; AL356285; CAH71795.1; JOINED; Genomic_DNA.
DR EMBL; AL356285; CAI15862.1; -; Genomic_DNA.
DR EMBL; AL512652; CAI15862.1; JOINED; Genomic_DNA.
DR EMBL; AK023108; BAB14409.1; ALT_INIT; mRNA.
DR EMBL; AL831819; CAD38533.2; -; mRNA.
DR RefSeq; NP_071904.4; NM_022459.4.
DR UniGene; Hs.507452; -.
DR ProteinModelPortal; Q9C0E2; -.
DR IntAct; Q9C0E2; 1.
DR STRING; 9606.ENSP00000255305; -.
DR PhosphoSite; Q9C0E2; -.
DR DMDM; 17368720; -.
DR PaxDb; Q9C0E2; -.
DR PRIDE; Q9C0E2; -.
DR Ensembl; ENST00000255305; ENSP00000255305; ENSG00000132953.
DR GeneID; 64328; -.
DR KEGG; hsa:64328; -.
DR UCSC; uc001unq.4; human.
DR CTD; 64328; -.
DR GeneCards; GC13M021351; -.
DR H-InvDB; HIX0011162; -.
DR HGNC; HGNC:17796; XPO4.
DR MIM; 611449; gene.
DR neXtProt; NX_Q9C0E2; -.
DR PharmGKB; PA134866468; -.
DR eggNOG; NOG273883; -.
DR HOGENOM; HOG000154878; -.
DR HOVERGEN; HBG023214; -.
DR OrthoDB; EOG7FJGZW; -.
DR GeneWiki; XPO4; -.
DR GenomeRNAi; 64328; -.
DR NextBio; 66257; -.
DR PRO; PR:Q9C0E2; -.
DR ArrayExpress; Q9C0E2; -.
DR Bgee; Q9C0E2; -.
DR CleanEx; HS_XPO4; -.
DR Genevestigator; Q9C0E2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014877; CRM1_C_dom.
DR Pfam; PF08767; CRM1_C; 1.
DR SUPFAM; SSF48371; SSF48371; 5.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 1151 Exportin-4.
FT /FTId=PRO_0000204711.
FT MOD_RES 464 464 Phosphoserine.
FT MOD_RES 521 521 Phosphoserine.
FT VARIANT 149 149 N -> S (in dbSNP:rs17320607).
FT /FTId=VAR_048958.
FT VARIANT 451 451 T -> A (in dbSNP:rs9552285).
FT /FTId=VAR_048959.
FT CONFLICT 511 511 L -> S (in Ref. 3; BAB14409).
SQ SEQUENCE 1151 AA; 130139 MW; 38E7EEFC938B07C5 CRC64;
MMAAALGPPE VIAQLENAAK VLMAPPSMVN NEQRQHAEHI FLSFRKSKSP FAVCKHILET
SKVDYVLFQA ATAIMEAVVR EWILLEKGSI ESLRTFLLTY VLQRPNLQKY VREQILLAVA
VIVKRGSLDK SIDCKSIFHE VSQLISSGNP TVQTLACSIL TALLSEFSSS SKTSNIGLSM
EFHGNCKRVF QEEDLRQIFM LTVEVLQEFS RRENLNAQMS SVFQRYLALA NQVLSWNFLP
PNLGRHYIAM FESSQNVLLK PTESWRETLL DSRVMELFFT VHRKIREDSD MAQDSLQCLA
QLASLHGPIF PDEGSQVDYL AHFIEGLLNT INGIEIEDSE AVGISSIISN LITVFPRNVL
TAIPSELFSS FVNCLTHLTC SFGRSAALEE VLDKDDMVYM EAYDKLLESW LTLVQDDKHF
HKGFFTQHAV QVFNSYIQCH LAAPDGTRNL TANGVASREE EEISELQEDD RDQFSDQLAS
VGMLGRIAAE HCIPLLTSLL EERVTRLHGQ LQRHQQQLLA SPGSSTVDNK MLDDLYEDIH
WLILVTGYLL ADDTQGETPL IPPEIMEYSI KHSSEVDINT TLQILGSPGE KASSIPGYNR
TDSVIRLLSA ILRVSEVESR AIRADLTHLL SPQMGKDIVW FLKRWAKTYL LVDEKLYDQI
SLPFSTAFGA DTEGSQWIIG YLLQKVISNL SVWSSEQDLA NDTVQLLVTL VERRERANLV
IQCENWWNLA KQFASRSPPL NFLSSPVQRT LMKALVLGGF AHMDTETKQQ YWTEVLQPLQ
QRFLRVINQE NFQQMCQQEE VKQEITATLE ALCGIAEATQ IDNVAILFNF LMDFLTNCIG
LMEVYKNTPE TVNLIIEVFV EVAHKQICYL GESKAMNLYE ACLTLLQVYS KNNLGRQRID
VTAEEEQYQD LLLIMELLTN LLSKEFIDFS DTDEVFRGHE PGQAANRSVS AADVVLYGVN
LILPLMSQDL LKFPTLCNQY YKLITFICEI FPEKIPQLPE DLFKSLMYSL ELGMTSMSSE
VCQLCLEALT PLAEQCAKAQ ETDSPLFLAT RHFLKLVFDM LVLQKHNTEM TTAAGEAFYT
LVCLHQAEYS ELVETLLSSQ QDPVIYQRLA DAFNKLTASS TPPTLDRKQK MAFLKSLEEF
MANVGGLLCV K
//
ID XPO4_HUMAN Reviewed; 1151 AA.
AC Q9C0E2; Q5VUZ5; Q8N3V6; Q9H934;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-NOV-2001, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Exportin-4;
DE Short=Exp4;
GN Name=XPO4; Synonyms=KIAA1721;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1151.
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 MRNA] OF 888-1151.
RC TISSUE=Skeletal muscle;
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 [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION IN NUCLEAR PROTEIN EXPORT, AND
RP IDENTIFICATION IN A COMPLEX WITH RAN AND EIF5A.
RX PubMed=10944119; DOI=10.1093/emboj/19.16.4362;
RA Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S.,
RA Hartmann E., Kutay U., Goerlich D.;
RT "Exportin 4: a mediator of a novel nuclear export pathway in higher
RT eukaryotes.";
RL EMBO J. 19:4362-4371(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION IN NUCLEAR PROTEIN EXPORT, IDENTIFICATION IN A COMPLEX WITH
RP RAN AND SMAD3, INTERACTION WITH SMAD3, AND SUBCELLULAR LOCATION.
RX PubMed=16449645; DOI=10.1128/MCB.26.4.1318-1332.2006;
RA Kurisaki A., Kurisaki K., Kowanetz M., Sugino H., Yoneda Y.,
RA Heldin C.-H., Moustakas A.;
RT "The mechanism of nuclear export of Smad3 involves exportin 4 and
RT Ran.";
RL Mol. Cell. Biol. 26:1318-1332(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-521, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP SPECTROMETRY.
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Mediates the nuclear export of proteins (cargos) with
CC broad substrate specificity. In the nucleus binds cooperatively to
CC its cargo and to the GTPase Ran in its active GTP-bound form.
CC Docking of this trimeric complex to the nuclear pore complex (NPC)
CC is mediated through binding to nucleoporins. Upon transit of a
CC nuclear export complex into the cytoplasm, disassembling of the
CC complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1
CC and RANGAP1, respectively) cause release of the cargo from the
CC export receptor. XPO4 then return to the nuclear compartment and
CC mediate another round of transport. The directionality of nuclear
CC export 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.
CC -!- SUBUNIT: Found in a complex with XPO4, Ran and EIF5A. Found in a
CC complex with XPO4, Ran and SMAD3. Interacts with SMAD3. Interacts
CC with Ran and cargo proteins in a GTP-dependent manner.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC the nucleus and the cytoplasm.
CC -!- SIMILARITY: Belongs to the exportin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14409.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB051508; BAB21812.1; -; mRNA.
DR EMBL; AL512652; CAH71795.1; -; Genomic_DNA.
DR EMBL; AL356285; CAH71795.1; JOINED; Genomic_DNA.
DR EMBL; AL356285; CAI15862.1; -; Genomic_DNA.
DR EMBL; AL512652; CAI15862.1; JOINED; Genomic_DNA.
DR EMBL; AK023108; BAB14409.1; ALT_INIT; mRNA.
DR EMBL; AL831819; CAD38533.2; -; mRNA.
DR RefSeq; NP_071904.4; NM_022459.4.
DR UniGene; Hs.507452; -.
DR ProteinModelPortal; Q9C0E2; -.
DR IntAct; Q9C0E2; 1.
DR STRING; 9606.ENSP00000255305; -.
DR PhosphoSite; Q9C0E2; -.
DR DMDM; 17368720; -.
DR PaxDb; Q9C0E2; -.
DR PRIDE; Q9C0E2; -.
DR Ensembl; ENST00000255305; ENSP00000255305; ENSG00000132953.
DR GeneID; 64328; -.
DR KEGG; hsa:64328; -.
DR UCSC; uc001unq.4; human.
DR CTD; 64328; -.
DR GeneCards; GC13M021351; -.
DR H-InvDB; HIX0011162; -.
DR HGNC; HGNC:17796; XPO4.
DR MIM; 611449; gene.
DR neXtProt; NX_Q9C0E2; -.
DR PharmGKB; PA134866468; -.
DR eggNOG; NOG273883; -.
DR HOGENOM; HOG000154878; -.
DR HOVERGEN; HBG023214; -.
DR OrthoDB; EOG7FJGZW; -.
DR GeneWiki; XPO4; -.
DR GenomeRNAi; 64328; -.
DR NextBio; 66257; -.
DR PRO; PR:Q9C0E2; -.
DR ArrayExpress; Q9C0E2; -.
DR Bgee; Q9C0E2; -.
DR CleanEx; HS_XPO4; -.
DR Genevestigator; Q9C0E2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014877; CRM1_C_dom.
DR Pfam; PF08767; CRM1_C; 1.
DR SUPFAM; SSF48371; SSF48371; 5.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 1151 Exportin-4.
FT /FTId=PRO_0000204711.
FT MOD_RES 464 464 Phosphoserine.
FT MOD_RES 521 521 Phosphoserine.
FT VARIANT 149 149 N -> S (in dbSNP:rs17320607).
FT /FTId=VAR_048958.
FT VARIANT 451 451 T -> A (in dbSNP:rs9552285).
FT /FTId=VAR_048959.
FT CONFLICT 511 511 L -> S (in Ref. 3; BAB14409).
SQ SEQUENCE 1151 AA; 130139 MW; 38E7EEFC938B07C5 CRC64;
MMAAALGPPE VIAQLENAAK VLMAPPSMVN NEQRQHAEHI FLSFRKSKSP FAVCKHILET
SKVDYVLFQA ATAIMEAVVR EWILLEKGSI ESLRTFLLTY VLQRPNLQKY VREQILLAVA
VIVKRGSLDK SIDCKSIFHE VSQLISSGNP TVQTLACSIL TALLSEFSSS SKTSNIGLSM
EFHGNCKRVF QEEDLRQIFM LTVEVLQEFS RRENLNAQMS SVFQRYLALA NQVLSWNFLP
PNLGRHYIAM FESSQNVLLK PTESWRETLL DSRVMELFFT VHRKIREDSD MAQDSLQCLA
QLASLHGPIF PDEGSQVDYL AHFIEGLLNT INGIEIEDSE AVGISSIISN LITVFPRNVL
TAIPSELFSS FVNCLTHLTC SFGRSAALEE VLDKDDMVYM EAYDKLLESW LTLVQDDKHF
HKGFFTQHAV QVFNSYIQCH LAAPDGTRNL TANGVASREE EEISELQEDD RDQFSDQLAS
VGMLGRIAAE HCIPLLTSLL EERVTRLHGQ LQRHQQQLLA SPGSSTVDNK MLDDLYEDIH
WLILVTGYLL ADDTQGETPL IPPEIMEYSI KHSSEVDINT TLQILGSPGE KASSIPGYNR
TDSVIRLLSA ILRVSEVESR AIRADLTHLL SPQMGKDIVW FLKRWAKTYL LVDEKLYDQI
SLPFSTAFGA DTEGSQWIIG YLLQKVISNL SVWSSEQDLA NDTVQLLVTL VERRERANLV
IQCENWWNLA KQFASRSPPL NFLSSPVQRT LMKALVLGGF AHMDTETKQQ YWTEVLQPLQ
QRFLRVINQE NFQQMCQQEE VKQEITATLE ALCGIAEATQ IDNVAILFNF LMDFLTNCIG
LMEVYKNTPE TVNLIIEVFV EVAHKQICYL GESKAMNLYE ACLTLLQVYS KNNLGRQRID
VTAEEEQYQD LLLIMELLTN LLSKEFIDFS DTDEVFRGHE PGQAANRSVS AADVVLYGVN
LILPLMSQDL LKFPTLCNQY YKLITFICEI FPEKIPQLPE DLFKSLMYSL ELGMTSMSSE
VCQLCLEALT PLAEQCAKAQ ETDSPLFLAT RHFLKLVFDM LVLQKHNTEM TTAAGEAFYT
LVCLHQAEYS ELVETLLSSQ QDPVIYQRLA DAFNKLTASS TPPTLDRKQK MAFLKSLEEF
MANVGGLLCV K
//
MIM
611449
*RECORD*
*FIELD* NO
611449
*FIELD* TI
*611449 EXPORTIN 4; XPO4
EXP4;;
KIAA1721
*FIELD* TX
DESCRIPTION
XPO4 belongs to a large family of karyopherins (see 602738) that mediate
read morethe transport of proteins and other cargo between the nuclear and
cytoplasmic compartments (Lipowsky et al., 2000).
CLONING
By sequencing clones obtained from a size-fractionated human adult
hippocampus cDNA library, Nagase et al. (2000) cloned XPO4, which they
designated KIAA1721. The 3-prime UTR contains a repetitive sequence, and
the 1,150-amino acid protein shares 99% amino acid identity with mouse
Xpo4. RT-PCR ELISA detected high to moderate expression in all human
tissues and specific brain regions examined.
Using affinity chromatography on immobilized RanGTP (see RANGAP1;
602362) to identify novel RanGTP-binding proteins in HeLa cell extract,
followed by database analysis and 3-prime and 5-prime RACE, Lipowsky et
al. (2000) cloned mouse Xpo4, which they called Exp4. The deduced
1,170-amino acid mouse protein has a calculated molecular mass of 129.9
kD. Xpo4 shares similarity over the N-terminal RanGTP-binding motif with
importin-beta family members, with highest similarity to exportin-1
(XPO1; 602559) and tRNA export receptor exportin-t (XPOT; 603180).
GENE FUNCTION
Using recombinant Xpo4 expressed in E. coli and HeLa cell extract
components, Lipowsky et al. (2000) showed that RanGTP-bound Xpo4 bound
EIF5A (600187) and thymidylate synthase (TYMS; 188350). Immunoblotting
assay of recombinant EIF5A and bound Xpo4 showed that EIF5A forms a
EIF5A-Xpo4-RanGTP complex with Xpo4 specifically and that the Xpo4-EIF5A
interaction was enhanced in the presence of RanGTP. Nuclear export
assays in permeabilized cells demonstrated that Xpo4 mediates specific
nuclear export of EIF5A. By mutation and posttranslational modification
analyses, Lipowsky et al. (2000) concluded that Xpo4-EIF5A interaction
is complex and requires large parts of the EIF5A molecule and hypusine
modification of EIF5A.
Using a protein-protein interaction screen, Kurisaki et al. (2006)
showed that human XPO4 interacted with Smad3 (603109) via the Smad3 MH2
domain. RNAi knockdown of XPO4 blocked Smad3 export, as did addition of
competing short peptides representing the Smad3-XPO4 interaction domain.
In vivo and in vitro assays showed that XPO4 mediated nuclear export of
Smad3 in a RanGTPase-dependent manner.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the XPO4
gene to chromosome 13 (TMAP RH91537).
*FIELD* RF
1. Kurisaki, A.; Kurisaki, K.; Kowanetz, M.; Sugino, H.; Yoneda, Y.;
Heldin, C.-H.; Moustakas, A.: The mechanism of nuclear export of
Smad3 involves exportin 4 and Ran. Molec. Cell. Biol. 26: 1318-1332,
2006.
2. Lipowsky, G.; Bischoff, F. R.; Schwarzmaier, P.; Kraft, R.; Kostka,
S.; Hartmann, E.; Kutay, U.; Gorlich, D.: Exportin 4: a mediator
of a novel nuclear export pathway in higher eukaryotes. EMBO J. 19:
4362-4371, 2000.
3. Nagase, T.; Kikuno, R.; Hattori, A.; Kondo, Y.; Okumura, K.; Ohara,
O.: Prediction of the coding sequences of unidentified human genes.
XIX. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro. DNA Res. 7: 347-355, 2000.
*FIELD* CD
Dorothy S. Reilly: 9/19/2007
*FIELD* ED
wwang: 09/19/2007
*RECORD*
*FIELD* NO
611449
*FIELD* TI
*611449 EXPORTIN 4; XPO4
EXP4;;
KIAA1721
*FIELD* TX
DESCRIPTION
XPO4 belongs to a large family of karyopherins (see 602738) that mediate
read morethe transport of proteins and other cargo between the nuclear and
cytoplasmic compartments (Lipowsky et al., 2000).
CLONING
By sequencing clones obtained from a size-fractionated human adult
hippocampus cDNA library, Nagase et al. (2000) cloned XPO4, which they
designated KIAA1721. The 3-prime UTR contains a repetitive sequence, and
the 1,150-amino acid protein shares 99% amino acid identity with mouse
Xpo4. RT-PCR ELISA detected high to moderate expression in all human
tissues and specific brain regions examined.
Using affinity chromatography on immobilized RanGTP (see RANGAP1;
602362) to identify novel RanGTP-binding proteins in HeLa cell extract,
followed by database analysis and 3-prime and 5-prime RACE, Lipowsky et
al. (2000) cloned mouse Xpo4, which they called Exp4. The deduced
1,170-amino acid mouse protein has a calculated molecular mass of 129.9
kD. Xpo4 shares similarity over the N-terminal RanGTP-binding motif with
importin-beta family members, with highest similarity to exportin-1
(XPO1; 602559) and tRNA export receptor exportin-t (XPOT; 603180).
GENE FUNCTION
Using recombinant Xpo4 expressed in E. coli and HeLa cell extract
components, Lipowsky et al. (2000) showed that RanGTP-bound Xpo4 bound
EIF5A (600187) and thymidylate synthase (TYMS; 188350). Immunoblotting
assay of recombinant EIF5A and bound Xpo4 showed that EIF5A forms a
EIF5A-Xpo4-RanGTP complex with Xpo4 specifically and that the Xpo4-EIF5A
interaction was enhanced in the presence of RanGTP. Nuclear export
assays in permeabilized cells demonstrated that Xpo4 mediates specific
nuclear export of EIF5A. By mutation and posttranslational modification
analyses, Lipowsky et al. (2000) concluded that Xpo4-EIF5A interaction
is complex and requires large parts of the EIF5A molecule and hypusine
modification of EIF5A.
Using a protein-protein interaction screen, Kurisaki et al. (2006)
showed that human XPO4 interacted with Smad3 (603109) via the Smad3 MH2
domain. RNAi knockdown of XPO4 blocked Smad3 export, as did addition of
competing short peptides representing the Smad3-XPO4 interaction domain.
In vivo and in vitro assays showed that XPO4 mediated nuclear export of
Smad3 in a RanGTPase-dependent manner.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the XPO4
gene to chromosome 13 (TMAP RH91537).
*FIELD* RF
1. Kurisaki, A.; Kurisaki, K.; Kowanetz, M.; Sugino, H.; Yoneda, Y.;
Heldin, C.-H.; Moustakas, A.: The mechanism of nuclear export of
Smad3 involves exportin 4 and Ran. Molec. Cell. Biol. 26: 1318-1332,
2006.
2. Lipowsky, G.; Bischoff, F. R.; Schwarzmaier, P.; Kraft, R.; Kostka,
S.; Hartmann, E.; Kutay, U.; Gorlich, D.: Exportin 4: a mediator
of a novel nuclear export pathway in higher eukaryotes. EMBO J. 19:
4362-4371, 2000.
3. Nagase, T.; Kikuno, R.; Hattori, A.; Kondo, Y.; Okumura, K.; Ohara,
O.: Prediction of the coding sequences of unidentified human genes.
XIX. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro. DNA Res. 7: 347-355, 2000.
*FIELD* CD
Dorothy S. Reilly: 9/19/2007
*FIELD* ED
wwang: 09/19/2007