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SRBD1_HUMAN
ID   SRBD1_HUMAN             Reviewed;         995 AA.
AC   Q8N5C6; Q53T56; Q96TA4; Q9NW11;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=S1 RNA-binding domain-containing protein 1;
GN   Name=SRBD1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964, AND IDENTIFICATION BY
RP   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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [6]
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., Buerckstuemmer T.,
RA   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861 AND SER-964, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-134; LYS-185 AND LYS-955, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-134 AND LYS-185, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-134; LYS-166; LYS-167;
RP   LYS-183 AND LYS-185, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N5C6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N5C6-2; Sequence=VSP_024461;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY14821.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK001241; BAA91577.1; -; mRNA.
DR   EMBL; AK056536; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC012072; AAY14821.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC008179; AAK52078.1; -; Genomic_DNA.
DR   EMBL; BC032538; AAH32538.1; -; mRNA.
DR   CCDS; CCDS1823.1; -. [Q8N5C6-1]
DR   RefSeq; NP_060549.4; NM_018079.4. [Q8N5C6-1]
DR   AlphaFoldDB; Q8N5C6; -.
DR   SMR; Q8N5C6; -.
DR   BioGRID; 120439; 112.
DR   IntAct; Q8N5C6; 32.
DR   MINT; Q8N5C6; -.
DR   STRING; 9606.ENSP00000263736; -.
DR   iPTMnet; Q8N5C6; -.
DR   PhosphoSitePlus; Q8N5C6; -.
DR   BioMuta; SRBD1; -.
DR   DMDM; 145566960; -.
DR   EPD; Q8N5C6; -.
DR   jPOST; Q8N5C6; -.
DR   MassIVE; Q8N5C6; -.
DR   MaxQB; Q8N5C6; -.
DR   PaxDb; Q8N5C6; -.
DR   PeptideAtlas; Q8N5C6; -.
DR   PRIDE; Q8N5C6; -.
DR   ProteomicsDB; 72030; -. [Q8N5C6-1]
DR   ProteomicsDB; 72031; -. [Q8N5C6-2]
DR   Antibodypedia; 29937; 123 antibodies from 24 providers.
DR   DNASU; 55133; -.
DR   Ensembl; ENST00000263736.5; ENSP00000263736.4; ENSG00000068784.13. [Q8N5C6-1]
DR   GeneID; 55133; -.
DR   KEGG; hsa:55133; -.
DR   MANE-Select; ENST00000263736.5; ENSP00000263736.4; NM_018079.5; NP_060549.4.
DR   UCSC; uc002rus.4; human. [Q8N5C6-1]
DR   CTD; 55133; -.
DR   DisGeNET; 55133; -.
DR   GeneCards; SRBD1; -.
DR   HGNC; HGNC:25521; SRBD1.
DR   HPA; ENSG00000068784; Low tissue specificity.
DR   neXtProt; NX_Q8N5C6; -.
DR   OpenTargets; ENSG00000068784; -.
DR   PharmGKB; PA144596269; -.
DR   VEuPathDB; HostDB:ENSG00000068784; -.
DR   eggNOG; KOG1857; Eukaryota.
DR   GeneTree; ENSGT00510000047850; -.
DR   HOGENOM; CLU_009833_1_0_1; -.
DR   InParanoid; Q8N5C6; -.
DR   OMA; RWAWRTR; -.
DR   OrthoDB; 56990at2759; -.
DR   PhylomeDB; Q8N5C6; -.
DR   TreeFam; TF313600; -.
DR   PathwayCommons; Q8N5C6; -.
DR   SignaLink; Q8N5C6; -.
DR   BioGRID-ORCS; 55133; 743 hits in 1090 CRISPR screens.
DR   ChiTaRS; SRBD1; human.
DR   GenomeRNAi; 55133; -.
DR   Pharos; Q8N5C6; Tbio.
DR   PRO; PR:Q8N5C6; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8N5C6; protein.
DR   Bgee; ENSG00000068784; Expressed in monocyte and 135 other tissues.
DR   Genevisible; Q8N5C6; HS.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd05685; S1_Tex; 1.
DR   Gene3D; 1.10.10.650; -; 1.
DR   Gene3D; 1.10.3500.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.420.140; -; 1.
DR   InterPro; IPR041692; HHH_9.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR044146; S1_Tex.
DR   InterPro; IPR023323; Tex-like_dom_sf.
DR   InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR   InterPro; IPR018974; Tex-like_N.
DR   InterPro; IPR032639; Tex_YqgF.
DR   InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR   InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR   Pfam; PF17674; HHH_9; 1.
DR   Pfam; PF00575; S1; 1.
DR   Pfam; PF09371; Tex_N; 1.
DR   Pfam; PF16921; Tex_YqgF; 1.
DR   SMART; SM00316; S1; 1.
DR   SMART; SM00732; YqgFc; 1.
DR   SUPFAM; SSF47781; SSF47781; 2.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50126; S1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; RNA-binding; Ubl conjugation.
FT   CHAIN           1..995
FT                   /note="S1 RNA-binding domain-containing protein 1"
FT                   /id="PRO_0000284357"
FT   DOMAIN          919..992
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   REGION          23..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          258..288
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        38..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         861
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         964
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        84
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        134
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        166
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        167
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        183
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        185
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        185
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        955
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447"
FT   VAR_SEQ         1..375
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024461"
FT   VARIANT         361
FT                   /note="T -> M (in dbSNP:rs6544834)"
FT                   /id="VAR_056995"
FT   VARIANT         798
FT                   /note="V -> F (in dbSNP:rs3755073)"
FT                   /id="VAR_056996"
FT   VARIANT         811
FT                   /note="K -> R (in dbSNP:rs3755072)"
FT                   /id="VAR_056997"
FT   CONFLICT        597
FT                   /note="N -> S (in Ref. 1; BAA91577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        638
FT                   /note="S -> G (in Ref. 1; AK056536)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        795
FT                   /note="S -> P (in Ref. 1; BAA91577)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   995 AA;  111776 MW;  BB286FB734708C55 CRC64;
     MSSLPRRAKV QVQDVVLKDE FSSFSELSSA SEEDDKEDSA WEPQKKVPRS RKQPPPKESK
     PKRMPRVKKN APQISDGSEV VVVKEELNSS VAIADTALED RKNKLDTVQT LKTAKTKQKC
     AAQPHTVRRT KKLKVEEETS KASNLEGESN SSETPSTSTV WGGTCKKEEN DDDFTFGQSA
     LKKIKTETYP QGQPVKFPAN ANSTKEEVEM NWDMVQVLSE RTNIEPWVCA NIIRLFNDDN
     TIPFIIRYRK ELINNLDADS LREVQQTLEE LRAVAKKVHS TIQKIKKEGK MSECLLKAML
     NCKTFEELEH VSAPYKTGSK GTKAQRARQL GLEGAARALL EKPGELSLLS YIRPDVKGLS
     TLQDIEIGVQ HILADMIAKD KDTLDFIRNL CQKRHVCIQS SLAKVSSKKV NEKDVDKFLL
     YQHFSCNIRN IHHHQILAIN RGENLKVLTV KVNISDGVKD EFCRWCIQNR WRPRSFARPE
     LMKILYNSLN DSFKRLIYPL LCREFRAKLT SDAEKESVMM FGRNLRQLLL TSPVPGRTLM
     GVDPGYKHGC KLAIISPTSQ ILHTDVVYLH CGQGFREAEK IKTLLLNFNC STVVIGNGTA
     CRETEAYFAD LIMKNYFAPL DVVYCIVSEA GASIYSVSPE ANKEMPGLDP NLRSAVSIAR
     RVQDPLAELV KIEPKHIGVG MYQHDVSQTL LKATLDSVVE ECVSFVGVDI NICSEVLLRH
     IAGLNANRAK NIIEWREKNG PFINREQLKK VKGLGPKSFQ QCAGFIRINQ DYIRTFCSQQ
     TETSGQIQGV AVTSSADVEV TNEKQGKKKS KTAVNVLLKP NPLDQTCIHP ESYDIAMRFL
     SSIGGTLYEV GKPEMQQKIN SFLEKEGMEK IAERLQTTVH TLQVIIDGLS QPESFDFRTD
     FDKPDFKRSI VCLEDLQIGT VLTGKVENAT LFGIFVDIGV GKSGLIPIRN VTEAKLSKTK
     KRRSLGLGPG ERVEVQVLNI DIPRSRITLD LIRVL
 
 
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