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RGRF1_HUMAN
ID   RGRF1_HUMAN             Reviewed;        1273 AA.
AC   Q13972; F8VPA5; H0YKF2; J3KQP9; Q16027;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   03-AUG-2022, entry version 203.
DE   RecName: Full=Ras-specific guanine nucleotide-releasing factor 1;
DE            Short=Ras-GRF1;
DE   AltName: Full=Guanine nucleotide-releasing protein;
DE            Short=GNRP;
DE   AltName: Full=Ras-specific nucleotide exchange factor CDC25;
GN   Name=RASGRF1; Synonyms=CDC25, GNRP, GRF1;
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).
RX   PubMed=7828890; DOI=10.1016/0378-1119(94)90671-8;
RA   Wei W., Das B., Park W., Broek D.;
RT   "Cloning and analysis of human cDNAs encoding a 140-kDa brain guanine
RT   nucleotide-exchange factor, Cdc25GEF, which regulates the function of
RT   Ras.";
RL   Gene 151:279-284(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=7684828;
RA   Schweighoffer F., Faure M., Fath I., Chevallier-Multon M.C., Apiou F.,
RA   Dutrillaux B., Sturani E., Jacquet M., Tocque B.;
RT   "Identification of a human guanine nucleotide-releasing factor (H-GRF55)
RT   specific for Ras proteins.";
RL   Oncogene 8:1477-1485(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-1273 (ISOFORM 3).
RC   TISSUE=Brain;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1045-1273 (ISOFORM 1).
RX   PubMed=1379731; DOI=10.1073/pnas.89.15.7100;
RA   Wei W., Mosteller R.D., Sanyal P., Gonzales E., McKinney D., Dasgupta C.,
RA   Li P., Liu B.-X., Broek D.;
RT   "Identification of a mammalian gene structurally and functionally related
RT   to the CDC25 gene of Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7100-7104(1992).
RN   [7]
RP   OLIGOMERIZATION, AND INTERACTION WITH RASGRF2.
RX   PubMed=10373510; DOI=10.1128/mcb.19.7.4611;
RA   Anborgh P.H., Qian X., Papageorge A.G., Vass W.C., DeClue J.E., Lowy D.R.;
RT   "Ras-specific exchange factor GRF: oligomerization through its Dbl homology
RT   domain and calcium-dependent activation of Raf.";
RL   Mol. Cell. Biol. 19:4611-4622(1999).
RN   [8]
RP   PHOSPHORYLATION, AND FUNCTION.
RX   PubMed=11389730; DOI=10.1046/j.1432-1327.2001.02230.x;
RA   Giglione C., Gonfloni S., Parmeggiani A.;
RT   "Differential actions of p60c-Src and Lck kinases on the Ras regulators
RT   p120-GAP and GDP/GTP exchange factor CDC25Mm.";
RL   Eur. J. Biochem. 268:3275-3283(2001).
CC   -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP.
CC       {ECO:0000269|PubMed:11389730}.
CC   -!- SUBUNIT: Homooligomer and heterooligomer with RASGRF2. Interacts with
CC       USP8, thereby regulating its stability (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q13972-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13972-2; Sequence=VSP_012032;
CC       Name=3;
CC         IsoId=Q13972-3; Sequence=VSP_054072, VSP_054073;
CC   -!- DOMAIN: The DH (DBL-homology) domain mediates interaction with RASGRF2.
CC   -!- PTM: Phosphorylated by PLK2, leading to ubiquitination and degradation
CC       by the proteasome. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated and degraded following phosphorylation by PLK2.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by SRC and LCK. Phosphorylation by LCK increases
CC       its capacity to stimulate the GDP/GTP exchange on Ras, whereas its
CC       phosphorylation by SRC seems not to have an effect on stimulation
CC       activity. {ECO:0000269|PubMed:11389730}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/RASGRF1ID43453ch15q25.html";
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DR   EMBL; L26584; AAA58417.1; -; mRNA.
DR   EMBL; S62035; AAB26881.1; -; mRNA.
DR   EMBL; AC011944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471136; EAW99141.1; -; Genomic_DNA.
DR   EMBL; AK226101; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M91815; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS10309.1; -. [Q13972-1]
DR   CCDS; CCDS42065.1; -. [Q13972-2]
DR   CCDS; CCDS45320.1; -. [Q13972-3]
DR   PIR; A38985; A38985.
DR   RefSeq; NP_002882.3; NM_002891.4. [Q13972-1]
DR   RefSeq; NP_722522.1; NM_153815.2. [Q13972-2]
DR   AlphaFoldDB; Q13972; -.
DR   SMR; Q13972; -.
DR   BioGRID; 111858; 13.
DR   IntAct; Q13972; 8.
DR   MINT; Q13972; -.
DR   STRING; 9606.ENSP00000405963; -.
DR   ChEMBL; CHEMBL5468; -.
DR   GlyConnect; 2067; 1 N-Linked glycan (1 site).
DR   GlyGen; Q13972; 1 site, 2 N-linked glycans (1 site).
DR   iPTMnet; Q13972; -.
DR   PhosphoSitePlus; Q13972; -.
DR   BioMuta; RASGRF1; -.
DR   DMDM; 13124259; -.
DR   jPOST; Q13972; -.
DR   MassIVE; Q13972; -.
DR   PaxDb; Q13972; -.
DR   PeptideAtlas; Q13972; -.
DR   PRIDE; Q13972; -.
DR   ProteomicsDB; 28264; -.
DR   ProteomicsDB; 59779; -. [Q13972-1]
DR   ProteomicsDB; 59780; -. [Q13972-2]
DR   Antibodypedia; 4170; 337 antibodies from 33 providers.
DR   DNASU; 5923; -.
DR   Ensembl; ENST00000394745.3; ENSP00000378228.3; ENSG00000058335.16. [Q13972-2]
DR   Ensembl; ENST00000419573.7; ENSP00000405963.3; ENSG00000058335.16. [Q13972-1]
DR   Ensembl; ENST00000558480.7; ENSP00000452781.2; ENSG00000058335.16. [Q13972-3]
DR   GeneID; 5923; -.
DR   KEGG; hsa:5923; -.
DR   MANE-Select; ENST00000558480.7; ENSP00000452781.2; NM_001145648.3; NP_001139120.1. [Q13972-3]
DR   UCSC; uc002beo.4; human. [Q13972-1]
DR   CTD; 5923; -.
DR   DisGeNET; 5923; -.
DR   GeneCards; RASGRF1; -.
DR   HGNC; HGNC:9875; RASGRF1.
DR   HPA; ENSG00000058335; Group enriched (brain, lung, retina).
DR   MIM; 606600; gene.
DR   neXtProt; NX_Q13972; -.
DR   OpenTargets; ENSG00000058335; -.
DR   PharmGKB; PA34238; -.
DR   VEuPathDB; HostDB:ENSG00000058335; -.
DR   eggNOG; KOG3417; Eukaryota.
DR   GeneTree; ENSGT00940000157599; -.
DR   HOGENOM; CLU_003405_0_1_1; -.
DR   InParanoid; Q13972; -.
DR   OMA; HHYFTVN; -.
DR   PhylomeDB; Q13972; -.
DR   TreeFam; TF317296; -.
DR   PathwayCommons; Q13972; -.
DR   Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   SignaLink; Q13972; -.
DR   SIGNOR; Q13972; -.
DR   BioGRID-ORCS; 5923; 9 hits in 1072 CRISPR screens.
DR   ChiTaRS; RASGRF1; human.
DR   GenomeRNAi; 5923; -.
DR   Pharos; Q13972; Tbio.
DR   PRO; PR:Q13972; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q13972; protein.
DR   Bgee; ENSG00000058335; Expressed in C1 segment of cervical spinal cord and 117 other tissues.
DR   Genevisible; Q13972; HS.
DR   GO; GO:0005829; C:cytosol; ISS:HGNC-UCL.
DR   GO; GO:0030426; C:growth cone; ISS:HGNC-UCL.
DR   GO; GO:0043005; C:neuron projection; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0035254; F:glutamate receptor binding; IEA:Ensembl.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:BHF-UCL.
DR   GO; GO:0090630; P:activation of GTPase activity; ISS:HGNC-UCL.
DR   GO; GO:0007616; P:long-term memory; NAS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:HGNC-UCL.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:HGNC-UCL.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
DR   GO; GO:2000310; P:regulation of NMDA receptor activity; IEA:Ensembl.
DR   GO; GO:0035020; P:regulation of Rac protein signal transduction; ISS:HGNC-UCL.
DR   GO; GO:0046578; P:regulation of Ras protein signal transduction; ISS:HGNC-UCL.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.10.840.10; -; 1.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR030745; RasGRF1.
DR   PANTHER; PTHR23113; PTHR23113; 1.
DR   PANTHER; PTHR23113:SF193; PTHR23113:SF193; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; SSF48065; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..1273
FT                   /note="Ras-specific guanine nucleotide-releasing factor 1"
FT                   /id="PRO_0000068880"
FT   DOMAIN          22..129
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          204..229
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          240..426
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          467..584
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          644..761
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT   DOMAIN          1038..1270
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   REGION          724..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..874
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         577
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000250|UniProtKB:P28818"
FT   MOD_RES         626
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000250|UniProtKB:P28818"
FT   MOD_RES         758
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P27671"
FT   MOD_RES         779
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000250|UniProtKB:P28818"
FT   MOD_RES         800
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000250|UniProtKB:P28818"
FT   VAR_SEQ         1..784
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7684828"
FT                   /id="VSP_012032"
FT   VAR_SEQ         610..622
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054072"
FT   VAR_SEQ         705..707
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054073"
FT   CONFLICT        1053
FT                   /note="V -> A (in Ref. 6; M91815)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1111
FT                   /note="E -> G (in Ref. 6; M91815)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1134
FT                   /note="S -> C (in Ref. 6; M91815)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1273 AA;  145234 MW;  B629AEAFDC7E500A CRC64;
     MQKGIRLNDG HVASLGLLAR KDGTRKGYLS KRSSDNTKWQ TKWFALLQNL LFYFESDSSS
     RPSGLYLLEG CVCDRAPSPK PALSAKEPLE KQHYFTVNFS HENQKALELR TEDAKDCDEW
     VAAIAHASYR TLATEHEALM QKYLHLLQIV ETEKTVAKQL RQQIEDGEIE IERLKAEITS
     LLKDNERIQS TQTVAPNDED SDIKKIKKVQ SFLRGWLCRR KWKTIIQDYI RSPHADSMRK
     RNQVVFSMLE AEAEYVQQLH ILVNNFLRPL RMAASSKKPP ITHDDVSSIF LNSETIMFLH
     QIFYQGLKAR ISSWPTLVLA DLFDILLPML NIYQEFVRNH QYSLQILAHC KQNRDFDKLL
     KHYEAKPDCE ERTLETFLTY PMFQIPRYIL TLHELLAHTP HEHVERNSLD YAKSKLEELS
     RIMHDEVSET ENIRKNLAIE RMIIEGCEIL LDTSQTFVRQ GSLIQVPMSE KGKITRGRLG
     SLSLKKEGER QCFLFSKHLI ICTRGSGGKL HLTKNGVISL IDCTLLEEPE STEEEAKGSG
     QDIDHLDFKI GVEPKDSPPF TVILVASSRQ EKAAWTSDIS QCVDNIRCNG LMMNAFEENS
     KVTVPQMIKR TREGTREAEM SRSDASLYCD DVDIRFSKTM NSCKVLQIRY ASVERLLERL
     TDLRFLSIDF LNTFLHSYRV FTTAIVVLDK LITIYKKPIS AIPARWLRSL ELLFASGQNN
     KLLYGEPPKS PRATRKFSSP PPLSITKTSS PSRRRKLSLN IPIITGGKAL DLAALSCNSN
     GYTSMYSAMS PFSKATLDTS KLYVSSSFTN KIPDEGDTTP EKPEDPSALS KQSSEVSMRE
     ESDIDQNQSD DGDTETSPTK SPTTPKSVKN KNSSEFPLFS YNNGVVMTSC RELDNNRSAL
     SAASAFAIAT AGANEGTPNK EKYRRMSLAS AGFPPDQRNG DKEFVIRRAA TNRVLNVLRH
     WVSKHSQDFE TNDELKCKVI GFLEEVMHDP ELLTQERKAA ANIIRTLTQE DPGDNQITLE
     EITQMAEGVK AEPFENHSAL EIAEQLTLLD HLVFKKIPYE EFFGQGWMKL EKNERTPYIM
     KTTKHFNDIS NLIASEIIRN EDINARVSAI EKWVAVADIC RCLHNYNAVL EITSSMNRSA
     IFRLKKTWLK VSKQTKALID KLQKLVSSEG RFKNLREALK NCDPPCVPYL GMYLTDLAFI
     EEGTPNYTED GLVNFSKMRM ISHIIREIRQ FQQTAYKIEH QAKVTQYLLD QSFVMDEESL
     YESSLRIEPK LPT
 
 
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