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GON4L_MOUSE
ID   GON4L_MOUSE             Reviewed;        2260 AA.
AC   Q9DB00; E9Q5N3; Q80TB4; Q91YI9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=GON-4-like protein;
DE   AltName: Full=GON-4 homolog;
GN   Name=Gon4l; Synonyms=Gon4, Kiaa1606;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-168.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-2260.
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1531-2260.
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=20530203; DOI=10.1084/jem.20100147;
RA   Lu P., Hankel I.L., Knisz J., Marquardt A., Chiang M.Y., Grosse J.,
RA   Constien R., Meyer T., Schroeder A., Zeitlmann L., Al-Alem U.,
RA   Friedman A.D., Elliott E.I., Meyerholz D.K., Waldschmidt T.J.,
RA   Rothman P.B., Colgan J.D.;
RT   "The Justy mutation identifies Gon4-like as a gene that is essential for B
RT   lymphopoiesis.";
RL   J. Exp. Med. 207:1359-1367(2010).
RN   [7]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH YY1; SIN3A AND HDAC1, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=21454521; DOI=10.1074/jbc.m110.133603;
RA   Lu P., Hankel I.L., Hostager B.S., Swartzendruber J.A., Friedman A.D.,
RA   Brenton J.L., Rothman P.B., Colgan J.D.;
RT   "The developmental regulator protein Gon4l associates with protein YY1, co-
RT   repressor Sin3a, and histone deacetylase 1 and mediates transcriptional
RT   repression.";
RL   J. Biol. Chem. 286:18311-18319(2011).
RN   [8]
RP   STRUCTURE BY NMR OF 2148-2230.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of mouse hypothetical gene (2610100B20Rik) product
RT   homologous to Myb DNA-binding domain.";
RL   Submitted (JUN-2004) to the PDB data bank.
CC   -!- FUNCTION: Has transcriptional repressor activity, probably as part of a
CC       complex with YY1, SIN3A AND HDAC1 (PubMed:21454521). Required for B
CC       cell lymphopoiesis (PubMed:20530203). {ECO:0000269|PubMed:20530203,
CC       ECO:0000269|PubMed:21454521}.
CC   -!- SUBUNIT: Found in a complex with YY1, SIN3A and HDAC1.
CC       {ECO:0000269|PubMed:21454521}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810,
CC       ECO:0000269|PubMed:21454521}.
CC   -!- TISSUE SPECIFICITY: Expressed in thymus. Specifically expressed in B
CC       cells and their precursors (at protein level). Also detected in brain,
CC       heart, spleen and bone marrow. {ECO:0000269|PubMed:20530203}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB23992.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC       Sequence=BAC65813.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC127377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK005385; BAB23992.1; ALT_TERM; mRNA.
DR   EMBL; AK122531; BAC65813.1; ALT_INIT; mRNA.
DR   EMBL; BC016616; AAH16616.1; ALT_INIT; mRNA.
DR   RefSeq; XP_017175282.1; XM_017319793.1.
DR   PDB; 1UG2; NMR; -; A=2148-2228.
DR   PDBsum; 1UG2; -.
DR   AlphaFoldDB; Q9DB00; -.
DR   SMR; Q9DB00; -.
DR   BioGRID; 217912; 4.
DR   CORUM; Q9DB00; -.
DR   STRING; 10090.ENSMUSP00000088461; -.
DR   iPTMnet; Q9DB00; -.
DR   PhosphoSitePlus; Q9DB00; -.
DR   EPD; Q9DB00; -.
DR   jPOST; Q9DB00; -.
DR   MaxQB; Q9DB00; -.
DR   PaxDb; Q9DB00; -.
DR   PRIDE; Q9DB00; -.
DR   ProteomicsDB; 271251; -.
DR   Ensembl; ENSMUST00000081695; ENSMUSP00000080397; ENSMUSG00000054199.
DR   GeneID; 76022; -.
DR   UCSC; uc008pxb.1; mouse.
DR   CTD; 54856; -.
DR   MGI; MGI:1917579; Gon4l.
DR   eggNOG; ENOG502QT2W; Eukaryota.
DR   GeneTree; ENSGT00390000016256; -.
DR   InParanoid; Q9DB00; -.
DR   OrthoDB; 49443at2759; -.
DR   BioGRID-ORCS; 76022; 10 hits in 73 CRISPR screens.
DR   ChiTaRS; Gon4l; mouse.
DR   EvolutionaryTrace; Q9DB00; -.
DR   PRO; PR:Q9DB00; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9DB00; protein.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.20.1160.11; -; 1.
DR   InterPro; IPR033277; GON-4-like.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR003822; PAH.
DR   InterPro; IPR036600; PAH_sf.
DR   InterPro; IPR001005; SANT/Myb.
DR   PANTHER; PTHR16088:SF11; PTHR16088:SF11; 2.
DR   Pfam; PF02671; PAH; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF47762; SSF47762; 2.
DR   PROSITE; PS50090; MYB_LIKE; 1.
DR   PROSITE; PS51477; PAH; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..2260
FT                   /note="GON-4-like protein"
FT                   /id="PRO_0000197110"
FT   DOMAIN          1648..1720
FT                   /note="PAH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT   DOMAIN          1730..1801
FT                   /note="PAH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT   DOMAIN          2167..2220
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..1364
FT                   /note="Required for interaction with YY1, SIN3A AND HDAC1,
FT                   and transcriptional repression activity"
FT                   /evidence="ECO:0000269|PubMed:21454521"
FT   REGION          613..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          946..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1367..1625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1835..1935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1949..1974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2026..2088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2134..2162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2227..2260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..392
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..572
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..967
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1368..1383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1384..1407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1419..1444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1477..1502
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1536..1560
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1837..1870
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1896..1910
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T8J9"
FT   MOD_RES         784
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1925
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T8J9"
FT   MOD_RES         1998
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T8J9"
FT   CONFLICT        259
FT                   /note="P -> L (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        734
FT                   /note="I -> V (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1080
FT                   /note="A -> S (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1341
FT                   /note="S -> P (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1354
FT                   /note="Q -> E (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1364
FT                   /note="F -> L (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1392
FT                   /note="S -> R (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1407
FT                   /note="M -> T (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1438
FT                   /note="L -> P (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1458
FT                   /note="A -> V (in Ref. 3; BAC65813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2069
FT                   /note="S -> P (in Ref. 3; BAC65813 and 4; AAH16616)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2173..2175
FT                   /evidence="ECO:0007829|PDB:1UG2"
FT   HELIX           2177..2189
FT                   /evidence="ECO:0007829|PDB:1UG2"
FT   TURN            2194..2196
FT                   /evidence="ECO:0007829|PDB:1UG2"
FT   HELIX           2197..2204
FT                   /evidence="ECO:0007829|PDB:1UG2"
FT   HELIX           2209..2225
FT                   /evidence="ECO:0007829|PDB:1UG2"
FT   STRAND          2227..2229
FT                   /evidence="ECO:0007829|PDB:1UG2"
SQ   SEQUENCE   2260 AA;  248742 MW;  BB0F605666D642C6 CRC64;
     MLPCKKRRLS VTESSQQQDD QEGDDLDLEA AVKPDTDQLP DSASESLSWG QSQDSAVCPE
     GLSMQDGDDQ LRAEGLSLNS KMLAQHVNLA VLEAVDVAVS QEIPLPSLES SHSLPVHVDK
     GRLQVSASKK GKRVVFTPGQ VTREDRGDHP VPEEPPSGEP AEEAKTEGGE LELRSDGEVP
     LLSSSSQSAK PGAQPRKSVQ PDGSAFPQDK PLGPLVRQAE EEMEDGGLFI PTEEQDSEES
     DKKKKTKKGT KRKRDGKGPE QGTMVYDPKL DDMLDRTLED GAKQHNLTAV NVRNILHEVI
     TNEHVVAMMK AAISETEDMP LFEPKMTRSK LKEVVEKGVV IPTWNISPIK KASEIKQPPQ
     FVDIHLEEDD SSDEEYSPDE EEEDETAEES LLESDVESTA SSPRGVKRSR LRLSSEVAET
     DEESGMLSEV EKAATPALRH ISAEVVPMGP PPPPKPKQSR DSVFMEKLDA VDEELASSPV
     CMDSFQPMED SLIAFRTRSK MPLKDVPLGQ LEAELQAPDI TPDMYDPNTA DDEDWKQWLG
     GLINDDVENE DEADDDDDPE YNFLEDLDEP DTEDFRTDRA VRITKKEVNG LMEELFETVQ
     SVVPSKFQDE MGFSNMEDDG PEEEERATES RPSFNTPQAL RFEEPLANLL NERHRTVKEL
     LEQLKMKKPS VRQQPEVEKL KPQEEAAHQT LVLDPAQRSR LQQQMQQHVQ LLTQIYLLTT
     SNPNLSSEAS TTRIFLKELG TFAENSIALH QQFNPRFQTL FQPCNWMGAM RLIEDFTQVS
     IDCSPHKTAK KTASEFPCLP KQVAWILATN KVFMYPELLP ICSLKANNPR DKTIFTKAED
     NLLALGLKHF EGTEFPKPLI SKYLVTCKTA HQLTVRIKNL NLNRAPNNVI KFYKKTKQLP
     VLVRCCEEIQ PHQWKPPFEK EEHRLPFWLK ASLQSIQDEL RNISEGATEG GSVTTATESS
     TDQHLQKASP ALGDEPQYPL LLPKGVVLKL KPGSKRFSRK AWRQKRPLVQ KPLLIQPSPS
     VQPVFNPGKM ATWPTQSEVP PSNTVVQIPH LIQPAAVLQT LPGFPSVGVR GEDGFESPTA
     LPAMPCGSEA RTTFPLSETQ SAPPSCSAPK LMLPSLAPSK FRKPYVRRKP TRRKGAKVSP
     CVKPAPIIHP TPVIFTVPAT TVKVVSIGGG CNMIQPVSAA VAPSPQTIPI TTLLVNPTTF
     PCSLNQPLVA SSISPLIVSS NPLTLPVTSI PEDKAQVKLD VAEGKNAPQN PESKLKPQEL
     TPLCTTVFSK EEPKSWHSSA DTGSQEAFSE SSACSWAVVK TESQEGSSEK SACGWTVVKT
     EDGGHAVEPL PQNLQDSLSS SSKDLLNMVK MEAQDCMVEI SSNFPKQDIG EEVKEECSME
     LDSESPQEKP SSASEMSKQT VLQREDMQAA KSPSVPQDAA AEGRTSSHAS RGLPKSTLSS
     MGQGGGLSGP PGKLEDSANA DGQSVGTPAG PDTGGEKDGP EEEEEEDFDD LTQDEEDELS
     SASEESVLSV PELQETMEKL TWLASERRMS QEGESEEENS QEENSEPEEE EEEEAEGMET
     LQKEDEVNDE AVGDAAKKPP STLASPQTAP EIETSIAPAG ESIKAAGKGR SSHRARNKRG
     SRARASKDTS KLLLLYDEDI LDRDPLREQK DLAFAQAYLT RVREALQHTP GKYEDFLQII
     YEFESSTQMH SAVDLFKSLQ TLLQDWPQLL KDFAAFLLPE QALSCGLFEE QQAFEKSRKF
     LRQLEICFAE NPSHHQKIIK VLQGCADCLP QDIAELKTQM WQLLRGHDHL QDEFSIFFDH
     LRPAASRMGD FEEINWTEEK EYEFDGFEEV ILPDVEEDEE PAKVSTASKS KRRKEIGVQH
     QDKDTEWPEA AKDCSCSCHE GGPESKLKKS KRRNCHCSSK VCDSKPYKSK EPPELVGSGP
     LHEASTVPGS KEAGQGKDML EEEILEEQEN MEVTQSKTAR TTRKGEAPAP GSTIGSTLLC
     PAEVTPMELL LEGPALCSAE TPRLPPQTGA VVCSVRRNQA GPEVVSCLST SSLPPEEGED
     QRAAANSETI APHREASETE RLPETVEHSA PLPSPVSTRT RDTGRRHICG KAGSQSWLIE
     SRAEAEAAHV AAPICEKSSG ARASEAAPKT AREVLAEDSG TQGMGPEGAL PKASEATVCA
     NNSKVSSTGE KVVLWTREAD RVILTMCQEQ GAQPHTFSVI SQQLGNKTPV EVSHRFRELM
     QLFHTACEAS SEDEDDATST SNADQLSDHG DLLSEEELDE
 
 
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