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DHX32_HUMAN
ID   DHX32_HUMAN             Reviewed;         743 AA.
AC   Q7L7V1; A8MSV2; D3DRF9; Q49AG5; Q5T3L0; Q5T3L5; Q96NY1; Q9BUN0; Q9H769;
AC   Q9NSL5; Q9NV74; Q9NVJ7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD/H box 32;
DE   AltName: Full=DEAD/H helicase-like protein 1;
DE            Short=DHLP1;
DE   AltName: Full=DEAH box protein 32;
DE   AltName: Full=HuDDX32;
GN   Name=DHX32; Synonyms=DDX32;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   230-414 (ISOFORM 2), INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Myeloid leukemia cell;
RX   PubMed=12163057; DOI=10.1016/s0145-2126(02)00040-1;
RA   Abdelhaleem M.;
RT   "The novel helicase homologue DDX32 is down-regulated in acute
RT   lymphoblastic leukemia.";
RL   Leuk. Res. 26:945-954(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=12527204; DOI=10.1016/s0378-1119(02)01098-3;
RA   Meng X., Liu J., Shen Z.;
RT   "Genomic structure of the human BCCIP gene and its expression in cancer.";
RL   Gene 302:139-146(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, Kidney, and Placenta;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-743 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   INDUCTION.
RX   PubMed=16414036; DOI=10.1016/j.cellimm.2005.12.003;
RA   Alli Z., Nam E.H., Beimnet K., Abdelhaleem M.;
RT   "The activation-induced expression of DHX32 in Jurkat T cells is specific
RT   and involves calcium and nuclear factor of activated T cells.";
RL   Cell. Immunol. 237:141-146(2005).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=16181624; DOI=10.1016/j.yexmp.2005.07.002;
RA   Alli Z., Ho M., Abdelhaleem M.;
RT   "Expression of DHX32 in lymphoid tissues.";
RL   Exp. Mol. Pathol. 79:219-223(2005).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16959245; DOI=10.1016/j.yexmp.2006.07.005;
RA   Alli Z., Ackerley C., Chen Y., Al-Saud B., Abdelhaleem M.;
RT   "Nuclear and mitochondrial localization of the putative RNA helicase
RT   DHX32.";
RL   Exp. Mol. Pathol. 81:245-248(2006).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] ARG-209.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- INTERACTION:
CC       Q7L7V1; Q3B820: FAM161A; NbExp=9; IntAct=EBI-2807297, EBI-719941;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16959245}.
CC       Mitochondrion {ECO:0000269|PubMed:16959245}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7L7V1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7L7V1-2; Sequence=VSP_026427;
CC   -!- TISSUE SPECIFICITY: Expressed in lymphoid tissues (at protein level).
CC       Expressed in brain, heart, skeletal muscle, colon, thymus, spleen,
CC       kidney, liver, small intestine, placenta, lung, lymphoid tissues and
CC       blood leukocytes. {ECO:0000269|PubMed:12163057,
CC       ECO:0000269|PubMed:16181624}.
CC   -!- INDUCTION: Up-regulated by ionomycin in T-lymphocytes. Down-regulated
CC       in acute lymphoblastic leukemia. {ECO:0000269|PubMed:12163057,
CC       ECO:0000269|PubMed:16414036}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37925.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB15029.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF427340; AAL26550.1; -; mRNA.
DR   EMBL; AF427341; AAL26551.1; -; mRNA.
DR   EMBL; AY064247; AAL55437.1; -; Genomic_DNA.
DR   EMBL; AY064250; AAL55441.1; -; mRNA.
DR   EMBL; AK001556; BAA91754.1; -; mRNA.
DR   EMBL; AK001751; BAA91882.1; -; mRNA.
DR   EMBL; AK024869; BAB15029.1; ALT_INIT; mRNA.
DR   EMBL; AL360176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW49216.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49217.1; -; Genomic_DNA.
DR   EMBL; BC002473; AAH02473.3; -; mRNA.
DR   EMBL; BC037925; AAH37925.1; ALT_FRAME; mRNA.
DR   EMBL; BC068471; AAH68471.1; -; mRNA.
DR   EMBL; AL162051; CAB82394.1; -; mRNA.
DR   CCDS; CCDS7652.1; -. [Q7L7V1-1]
DR   PIR; T47184; T47184.
DR   RefSeq; NP_060650.2; NM_018180.2. [Q7L7V1-1]
DR   RefSeq; XP_016871893.1; XM_017016404.1.
DR   RefSeq; XP_016871894.1; XM_017016405.1.
DR   AlphaFoldDB; Q7L7V1; -.
DR   SMR; Q7L7V1; -.
DR   BioGRID; 120878; 50.
DR   IntAct; Q7L7V1; 13.
DR   MINT; Q7L7V1; -.
DR   STRING; 9606.ENSP00000284690; -.
DR   iPTMnet; Q7L7V1; -.
DR   PhosphoSitePlus; Q7L7V1; -.
DR   BioMuta; DHX32; -.
DR   DMDM; 74759011; -.
DR   EPD; Q7L7V1; -.
DR   jPOST; Q7L7V1; -.
DR   MassIVE; Q7L7V1; -.
DR   MaxQB; Q7L7V1; -.
DR   PaxDb; Q7L7V1; -.
DR   PeptideAtlas; Q7L7V1; -.
DR   PRIDE; Q7L7V1; -.
DR   ProteomicsDB; 68827; -. [Q7L7V1-1]
DR   ProteomicsDB; 68828; -. [Q7L7V1-2]
DR   Antibodypedia; 32435; 164 antibodies from 23 providers.
DR   DNASU; 55760; -.
DR   Ensembl; ENST00000284690.4; ENSP00000284690.3; ENSG00000089876.12. [Q7L7V1-1]
DR   GeneID; 55760; -.
DR   KEGG; hsa:55760; -.
DR   MANE-Select; ENST00000284690.4; ENSP00000284690.3; NM_018180.3; NP_060650.2.
DR   UCSC; uc001ljf.1; human. [Q7L7V1-1]
DR   CTD; 55760; -.
DR   DisGeNET; 55760; -.
DR   GeneCards; DHX32; -.
DR   HGNC; HGNC:16717; DHX32.
DR   HPA; ENSG00000089876; Low tissue specificity.
DR   MIM; 607960; gene.
DR   neXtProt; NX_Q7L7V1; -.
DR   OpenTargets; ENSG00000089876; -.
DR   PharmGKB; PA27219; -.
DR   VEuPathDB; HostDB:ENSG00000089876; -.
DR   eggNOG; KOG0925; Eukaryota.
DR   GeneTree; ENSGT00940000157227; -.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; Q7L7V1; -.
DR   OMA; NKEQKMC; -.
DR   OrthoDB; 354219at2759; -.
DR   PhylomeDB; Q7L7V1; -.
DR   TreeFam; TF105735; -.
DR   PathwayCommons; Q7L7V1; -.
DR   SignaLink; Q7L7V1; -.
DR   BioGRID-ORCS; 55760; 5 hits in 1084 CRISPR screens.
DR   ChiTaRS; DHX32; human.
DR   GeneWiki; DHX32; -.
DR   GenomeRNAi; 55760; -.
DR   Pharos; Q7L7V1; Tbio.
DR   PRO; PR:Q7L7V1; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q7L7V1; protein.
DR   Bgee; ENSG00000089876; Expressed in nasal cavity epithelium and 208 other tissues.
DR   ExpressionAtlas; Q7L7V1; baseline and differential.
DR   Genevisible; Q7L7V1; HS.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00847; HA2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Helicase; Hydrolase;
KW   Mitochondrion; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..743
FT                   /note="Putative pre-mRNA-splicing factor ATP-dependent RNA
FT                   helicase DHX32"
FT                   /id="PRO_0000292663"
FT   DOMAIN          72..238
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           185..188
FT                   /note="DEAH box"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   VAR_SEQ         284..364
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12163057"
FT                   /id="VSP_026427"
FT   VARIANT         209
FT                   /note="P -> R (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035843"
FT   VARIANT         271
FT                   /note="E -> D (in dbSNP:rs11244674)"
FT                   /id="VAR_052181"
FT   VARIANT         301
FT                   /note="D -> A (in dbSNP:rs35772239)"
FT                   /id="VAR_052182"
FT   VARIANT         430
FT                   /note="V -> L (in dbSNP:rs17153669)"
FT                   /id="VAR_052183"
FT   CONFLICT        26
FT                   /note="D -> G (in Ref. 3; BAA91754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="V -> M (in Ref. 3; BAA91882)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="M -> V (in Ref. 3; BAA91754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="N -> F (in Ref. 1; AAL26551)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="L -> S (in Ref. 3; BAA91882)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        496
FT                   /note="A -> G (in Ref. 3; BAA91882)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        499
FT                   /note="E -> G (in Ref. 6; AAH37925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        567
FT                   /note="V -> A (in Ref. 3; BAB15029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590
FT                   /note="E -> G (in Ref. 6; AAH37925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        686
FT                   /note="P -> L (in Ref. 3; BAA91882)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   743 AA;  84419 MW;  D6D5C570561C468A CRC64;
     MEEEGLECPN SSSEKRYFPE SLDSSDGDEE EVLACEDLEL NPFDGLPYSS RYYKLLKERE
     DLPIWKEKYS FMENLLQNQI VIVSGDAKCG KSAQVPQWCA EYCLSIHYQH GGVICTQVHK
     QTVVQLALRV ADEMDVNIGH EVGYVIPFEN CCTNETILRY CTDDMLQREM MSNPFLGSYG
     VIILDDIHER SIATDVLLGL LKDVLLARPE LKLIINSSPH LISKLNSYYG NVPVIEVKNK
     HPVEVVYLSE AQKDSFESIL RLIFEIHHSG EKGDIVVFLA CEQDIEKVCE TVYQGSNLNP
     DLGELVVVPL YPKEKCSLFK PLDETEKRCQ VYQRRVVLTT SSGEFLIWSN SVRFVIDVGV
     ERRKVYNPRI RANSLVMQPI SQSQAEIRKQ ILGSSSSGKF FCLYTEEFAS KDMTPLKPAE
     MQEANLTSMV LFMKRIDIAG LGHCDFMNRP APESLMQALE DLDYLAALDN DGNLSEFGII
     MSEFPLDPQL SKSILASCEF DCVDEVLTIA AMVTAPNCFS HVPHGAEEAA LTCWKTFLHP
     EGDHFTLISI YKAYQDTTLN SSSEYCVEKW CRDYFLNCSA LRMADVIRAE LLEIIKRIEL
     PYAEPAFGSK ENTLNIKKAL LSGYFMQIAR DVDGSGNYLM LTHKQVAQLH PLSGYSITKK
     MPEWVLFHKF SISENNYIRI TSEISPELFM QLVPQYYFSN LPPSESKDIL QQVVDHLSPV
     STMNKEQQMC ETCPETEQRC TLQ
 
 
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