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HERC1_HUMAN
ID   HERC1_HUMAN             Reviewed;        4861 AA.
AC   Q15751; Q8IW65;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase HERC1;
DE            EC=2.3.2.26;
DE   AltName: Full=HECT domain and RCC1-like domain-containing protein 1;
DE   AltName: Full=HECT-type E3 ubiquitin transferase HERC1;
DE   AltName: Full=p532;
DE   AltName: Full=p619;
GN   Name=HERC1;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INTERACTION WITH ARF1, AND VARIANTS ALA-1696; VAL-2220 AND
RP   ASP-3722.
RX   PubMed=8861955; DOI=10.1002/j.1460-2075.1996.tb00801.x;
RA   Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M.;
RT   "p619, a giant protein related to the chromosome condensation regulator
RT   RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins.";
RL   EMBO J. 15:4262-4273(1996).
RN   [2]
RP   ERRATUM OF PUBMED:8861955.
RA   Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M.;
RL   EMBO J. 15:5738-5738(1996).
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 MRNA] OF 4211-4861.
RC   TISSUE=Liver;
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   FUNCTION, AND INTERACTION WITH CLTC.
RX   PubMed=9233772; DOI=10.1038/sj.onc.1201170;
RA   Rosa J.L., Barbacid M.;
RT   "A giant protein that stimulates guanine nucleotide exchange on ARF1 and
RT   Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70.";
RL   Oncogene 15:1-6(1997).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PKM.
RX   PubMed=12650930; DOI=10.1016/s0014-5793(03)00205-9;
RA   Garcia-Gonzalo F.R., Cruz C., Munoz P., Mazurek S., Eigenbrodt E.,
RA   Ventura F., Bartrons R., Rosa J.L.;
RT   "Interaction between HERC1 and M2-type pyruvate kinase.";
RL   FEBS Lett. 539:78-84(2003).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14960311; DOI=10.1016/s0014-5793(04)00030-4;
RA   Garcia-Gonzalo F.R., Munoz P., Gonzalez E., Casaroli-Marano R.P.,
RA   Vilaro S., Bartrons R., Ventura F., Rosa J.L.;
RT   "The giant protein HERC1 is recruited to aluminum fluoride-induced actin-
RT   rich surface protrusions in HeLa cells.";
RL   FEBS Lett. 559:77-83(2004).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH ARF6.
RX   PubMed=15642342; DOI=10.1016/j.febslet.2004.11.095;
RA   Garcia-Gonzalo F.R., Bartrons R., Ventura F., Rosa J.L.;
RT   "Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1-mediated
RT   guanine nucleotide release from ARF proteins.";
RL   FEBS Lett. 579:343-348(2005).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   INTERACTION WITH TSC2.
RX   PubMed=16464865; DOI=10.1074/jbc.c500451200;
RA   Chong-Kopera H., Inoki K., Li Y., Zhu T., Garcia-Gonzalo F.R., Rosa J.L.,
RA   Guan K.-L.;
RT   "TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the
RT   HERC1 ubiquitin ligase.";
RL   J. Biol. Chem. 281:8313-8316(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1521, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2701, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1517; SER-1521; THR-2701;
RP   SER-2706 AND SER-2710, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1521 AND THR-2701, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4857, 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   [16]
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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1491, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342; SER-1428; SER-1512;
RP   SER-1521; SER-2422; THR-2701; SER-2720 AND SER-2723, AND IDENTIFICATION BY
RP   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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1406 AND SER-1512, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [20]
RP   INVOLVEMENT IN MDFPMR, AND VARIANT MDFPMR GLU-4520.
RX   PubMed=26138117; DOI=10.1111/cge.12634;
RA   Ortega-Recalde O., Beltran O.I., Galvez J.M., Palma-Montero A.,
RA   Restrepo C.M., Mateus H.E., Laissue P.;
RT   "Biallelic HERC1 mutations in a syndromic form of overgrowth and
RT   intellectual disability.";
RL   Clin. Genet. 88:E1-E3(2015).
RN   [21]
RP   VARIANT ASN-3485.
RX   PubMed=29463886; DOI=10.1038/s41380-018-0020-x;
RA   Eising E., Carrion-Castillo A., Vino A., Strand E.A., Jakielski K.J.,
RA   Scerri T.S., Hildebrand M.S., Webster R., Ma A., Mazoyer B., Francks C.,
RA   Bahlo M., Scheffer I.E., Morgan A.T., Shriberg L.D., Fisher S.E.;
RT   "A set of regulatory genes co-expressed in embryonic human brain is
RT   implicated in disrupted speech development.";
RL   Mol. Psychiatry 24:1065-1078(2019).
CC   -!- FUNCTION: Involved in membrane trafficking via some guanine nucleotide
CC       exchange factor (GEF) activity and its ability to bind clathrin. Acts
CC       as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds
CC       phosphatidylinositol 4,5-bisphosphate, which is required for GEF
CC       activity. May also act as a E3 ubiquitin-protein ligase which accepts
CC       ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a
CC       thioester and then directly transfers the ubiquitin to targeted
CC       substrates. {ECO:0000269|PubMed:15642342, ECO:0000269|PubMed:8861955,
CC       ECO:0000269|PubMed:9233772}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with TSC2; interaction is inhibited by TSC1.
CC       Interacts with PKM, ARF1 and ARF6. Forms a ternary complex with
CC       clathrin heavy chain (CLTC) and HSPA1A. {ECO:0000269|PubMed:12650930,
CC       ECO:0000269|PubMed:15642342, ECO:0000269|PubMed:16464865,
CC       ECO:0000269|PubMed:8861955, ECO:0000269|PubMed:9233772}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm,
CC       cytosol. Golgi apparatus. Note=Recruited onto actin-rich surface
CC       protrusions.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8861955}.
CC   -!- DISEASE: Macrocephaly, dysmorphic facies, and psychomotor retardation
CC       (MDFPMR) [MIM:617011]: An autosomal recessive syndrome characterized by
CC       large head and somatic overgrowth, intellectual disability, and facial
CC       dysmorphism. Seizures, hypotonia and ataxic gait are observed in some
CC       patients. {ECO:0000269|PubMed:26138117}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
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DR   EMBL; U50078; AAD12586.1; -; mRNA.
DR   EMBL; AC073167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC118274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC040929; AAH40929.1; -; mRNA.
DR   CCDS; CCDS45277.1; -.
DR   PIR; S71752; S71752.
DR   RefSeq; NP_003913.3; NM_003922.3.
DR   PDB; 4O2W; X-ray; 2.00 A; A/B/C/D=3975-4360.
DR   PDB; 4QT6; X-ray; 1.64 A; A=2035-2192.
DR   PDBsum; 4O2W; -.
DR   PDBsum; 4QT6; -.
DR   SMR; Q15751; -.
DR   BioGRID; 114439; 158.
DR   CORUM; Q15751; -.
DR   IntAct; Q15751; 44.
DR   MINT; Q15751; -.
DR   STRING; 9606.ENSP00000390158; -.
DR   iPTMnet; Q15751; -.
DR   MetOSite; Q15751; -.
DR   PhosphoSitePlus; Q15751; -.
DR   BioMuta; HERC1; -.
DR   DMDM; 296434522; -.
DR   EPD; Q15751; -.
DR   jPOST; Q15751; -.
DR   MassIVE; Q15751; -.
DR   MaxQB; Q15751; -.
DR   PaxDb; Q15751; -.
DR   PeptideAtlas; Q15751; -.
DR   PRIDE; Q15751; -.
DR   ProteomicsDB; 60743; -.
DR   Antibodypedia; 25716; 57 antibodies from 10 providers.
DR   DNASU; 8925; -.
DR   Ensembl; ENST00000443617.7; ENSP00000390158.2; ENSG00000103657.14.
DR   GeneID; 8925; -.
DR   KEGG; hsa:8925; -.
DR   MANE-Select; ENST00000443617.7; ENSP00000390158.2; NM_003922.4; NP_003913.3.
DR   UCSC; uc002amp.4; human.
DR   CTD; 8925; -.
DR   DisGeNET; 8925; -.
DR   GeneCards; HERC1; -.
DR   HGNC; HGNC:4867; HERC1.
DR   HPA; ENSG00000103657; Low tissue specificity.
DR   MalaCards; HERC1; -.
DR   MIM; 605109; gene.
DR   MIM; 617011; phenotype.
DR   neXtProt; NX_Q15751; -.
DR   OpenTargets; ENSG00000103657; -.
DR   Orphanet; 457359; Megalencephaly-severe kyphoscoliosis-overgrowth syndrome.
DR   PharmGKB; PA29242; -.
DR   VEuPathDB; HostDB:ENSG00000103657; -.
DR   eggNOG; KOG1426; Eukaryota.
DR   GeneTree; ENSGT00940000155907; -.
DR   HOGENOM; CLU_000091_0_0_1; -.
DR   InParanoid; Q15751; -.
DR   OMA; HISKNHD; -.
DR   OrthoDB; 1062377at2759; -.
DR   PhylomeDB; Q15751; -.
DR   TreeFam; TF106426; -.
DR   PathwayCommons; Q15751; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q15751; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 8925; 26 hits in 1120 CRISPR screens.
DR   ChiTaRS; HERC1; human.
DR   GeneWiki; HERC1; -.
DR   GenomeRNAi; 8925; -.
DR   Pharos; Q15751; Tbio.
DR   PRO; PR:Q15751; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q15751; protein.
DR   Bgee; ENSG00000103657; Expressed in cortical plate and 195 other tissues.
DR   ExpressionAtlas; Q15751; baseline and differential.
DR   Genevisible; Q15751; HS.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:ProtInc.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl.
DR   GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd12881; SPRY_HERC1; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.130.10.30; -; 2.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR035768; SPRY_HERC1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00415; RCC1; 10.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF50978; SSF50978; 2.
DR   SUPFAM; SSF50985; SSF50985; 2.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS00626; RCC1_2; 4.
DR   PROSITE; PS50012; RCC1_3; 14.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Disease variant; Golgi apparatus;
KW   Guanine-nucleotide releasing factor; Intellectual disability; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase; Transport;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..4861
FT                   /note="Probable E3 ubiquitin-protein ligase HERC1"
FT                   /id="PRO_0000328871"
FT   REPEAT          371..420
FT                   /note="RCC1 1"
FT   REPEAT          421..475
FT                   /note="RCC1 2"
FT   REPEAT          476..528
FT                   /note="RCC1 3"
FT   REPEAT          529..578
FT                   /note="RCC1 4"
FT   REPEAT          580..631
FT                   /note="RCC1 5"
FT   REPEAT          633..682
FT                   /note="RCC1 6"
FT   REPEAT          683..735
FT                   /note="RCC1 7"
FT   DOMAIN          2002..2193
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REPEAT          3426..3465
FT                   /note="WD 1"
FT   REPEAT          3484..3522
FT                   /note="WD 2"
FT   REPEAT          3524..3572
FT                   /note="WD 3"
FT   REPEAT          3580..3619
FT                   /note="WD 4"
FT   REPEAT          3624..3663
FT                   /note="WD 5"
FT   REPEAT          3667..3713
FT                   /note="WD 6"
FT   REPEAT          3745..3784
FT                   /note="WD 7"
FT   REPEAT          3996..4044
FT                   /note="RCC1 8"
FT   REPEAT          4046..4099
FT                   /note="RCC1 9"
FT   REPEAT          4101..4151
FT                   /note="RCC1 10"
FT   REPEAT          4153..4203
FT                   /note="RCC1 11"
FT   REPEAT          4205..4256
FT                   /note="RCC1 12"
FT   REPEAT          4258..4308
FT                   /note="RCC1 13"
FT   REPEAT          4310..4360
FT                   /note="RCC1 14"
FT   DOMAIN          4501..4848
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          125..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1322..1341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1348..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1397..1432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1503..1529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1864..1886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2257..2286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2406..2497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2617..2675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2692..2752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2798..2876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3236..3255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1348..1364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2406..2436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2439..2479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2480..2497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2622..2669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2692..2743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2855..2871
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        4811
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   MOD_RES         1342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1491
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         1517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         2422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2701
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         2706
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         2710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         2720
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2723
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         4857
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VARIANT         1088
FT                   /note="L -> F (in dbSNP:rs1063423)"
FT                   /id="VAR_042556"
FT   VARIANT         1278
FT                   /note="L -> F (in dbSNP:rs3764187)"
FT                   /id="VAR_042557"
FT   VARIANT         1411
FT                   /note="G -> V (in dbSNP:rs36089909)"
FT                   /id="VAR_042558"
FT   VARIANT         1447
FT                   /note="H -> N (in dbSNP:rs7162519)"
FT                   /id="VAR_042559"
FT   VARIANT         1572
FT                   /note="S -> A (in dbSNP:rs16947363)"
FT                   /id="VAR_042560"
FT   VARIANT         1696
FT                   /note="G -> A (in dbSNP:rs2255243)"
FT                   /evidence="ECO:0000269|PubMed:8861955"
FT                   /id="VAR_042561"
FT   VARIANT         1995
FT                   /note="T -> A (in dbSNP:rs2228512)"
FT                   /id="VAR_042562"
FT   VARIANT         2220
FT                   /note="I -> V (in dbSNP:rs2228510)"
FT                   /evidence="ECO:0000269|PubMed:8861955"
FT                   /id="VAR_042563"
FT   VARIANT         2816
FT                   /note="A -> T (in dbSNP:rs35122568)"
FT                   /id="VAR_042564"
FT   VARIANT         3152
FT                   /note="S -> F (in dbSNP:rs2228513)"
FT                   /id="VAR_042565"
FT   VARIANT         3485
FT                   /note="S -> N (de novo variant found in a patient with
FT                   childhood apraxia of speech; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:29463886"
FT                   /id="VAR_081534"
FT   VARIANT         3517
FT                   /note="G -> R (in dbSNP:rs7182782)"
FT                   /id="VAR_042566"
FT   VARIANT         3722
FT                   /note="E -> D (in dbSNP:rs2229749)"
FT                   /evidence="ECO:0000269|PubMed:8861955"
FT                   /id="VAR_042567"
FT   VARIANT         4394
FT                   /note="I -> V (in dbSNP:rs2228516)"
FT                   /id="VAR_057122"
FT   VARIANT         4520
FT                   /note="G -> E (in MDFPMR; dbSNP:rs769677823)"
FT                   /evidence="ECO:0000269|PubMed:26138117"
FT                   /id="VAR_076995"
FT   CONFLICT        1532
FT                   /note="R -> Q (in Ref. 1; AAD12586)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2035..2046
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   TURN            2047..2049
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2050..2053
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2055..2065
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2069..2080
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2088..2093
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   TURN            2102..2104
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2106..2112
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   TURN            2113..2115
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2117..2127
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2136..2142
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   TURN            2143..2146
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2147..2152
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2158..2161
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2167..2175
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2178..2180
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          2183..2187
FT                   /evidence="ECO:0007829|PDB:4QT6"
FT   STRAND          3999..4004
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4011..4013
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4015..4022
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4024..4026
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4029..4034
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4036..4043
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4048..4052
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4055..4057
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4060..4063
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4067..4072
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4074..4076
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4081..4086
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4093..4098
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4103..4107
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4110..4112
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4116..4118
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4122..4127
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4129..4131
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4136..4141
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4143..4150
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4155..4159
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4162..4164
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4168..4170
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4174..4179
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4181..4183
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4188..4193
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4195..4202
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4208..4212
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4215..4217
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4221..4223
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4227..4232
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4234..4236
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4237..4239
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4241..4246
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4248..4255
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4260..4264
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4266..4268
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4273..4278
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4286..4288
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4293..4298
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4300..4307
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4312..4316
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4325..4327
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4331..4336
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   HELIX           4338..4340
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4347..4350
FT                   /evidence="ECO:0007829|PDB:4O2W"
FT   STRAND          4352..4358
FT                   /evidence="ECO:0007829|PDB:4O2W"
SQ   SEQUENCE   4861 AA;  532228 MW;  31B2C1A1430B9622 CRC64;
     MATMIPPVKL KWLEHLNSSW ITEDSESIAT REGVAVLYSK LVSNKEVVPL PQQVLCLKGP
     QLPDFERESL SSDEQDHYLD ALLSSQLALA KMVCSDSPFA GALRKRLLVL QRVFYALSNK
     YHDKGKVKQQ QHSPESSSGS ADVHSVSERP RSSTDALIEM GVRTGLSLLF ALLRQSWMMP
     VSGPGLSLCN DVIHTAIEVV SSLPPLSLAN ESKIPPMGLD CLSQVTTFLK GVTIPNSGAD
     TLGRRLASEL LLGLAAQRGS LRYLLEWIEM ALGASAVVHT MEKGKLLSSQ EGMISFDCFM
     TILMQMRRSL GSSADRSQWR EPTRTSDGLC SLYEAALCLF EEVCRMASDY SRTCASPDSI
     QTGDAPIVSE TCEVYVWGSN SSHQLVEGTQ EKILQPKLAP SFSDAQTIEA GQYCTFVIST
     DGSVRACGKG SYGRLGLGDS NNQSTLKKLT FEPHRSIKKV SSSKGSDGHT LAFTTEGEVF
     SWGDGDYGKL GHGNSSTQKY PKLIQGPLQG KVVVCVSAGY RHSAAVTEDG ELYTWGEGDF
     GRLGHGDSNS RNIPTLVKDI SNVGEVSCGS SHTIALSKDG RTVWSFGGGD NGKLGHGDTN
     RVYKPKVIEA LQGMFIRKVC AGSQSSLALT STGQVYAWGC GACLGCGSSE ATALRPKLIE
     ELAATRIVDV SIGDSHCLAL SHDNEVYAWG NNSMGQCGQG NSTGPITKPK KVSGLDGIAI
     QQISAGTSHS LAWTALPRDR QVVAWHRPYC VDLEESTFSH LRSFLERYCD KINSEIPPLP
     FPSSREHHSF LKLCLKLLSN HLALALAGGV ATSILGRQAG PLRNLLFRLM DSTVPDEIQE
     VVIETLSVGA TMLLPPLRER MELLHSLLPQ GPDRWESLSK GQRMQLDIIL TSLQDHTHVA
     SLLGYSSPSD AADLSSVCTG YGNLSDQPYG TQSCHPDTHL AEILMKTLLR NLGFYTDQAF
     GELEKNSDKF LLGTSSSENS QPAHLHELLC SLQKQLLAFC HINNISENSS SVALLHKHLQ
     LLLPHATDIY SRSANLLKES PWNGSVGEKL RDVIYVSAAG SMLCQIVNSL LLLPVSVARP
     LLSYLLDLLP PLDCLNRLLP AADLLEDQEL QWPLHGGPEL IDPAGLPLPQ PAQSWVWLVD
     LERTIALLIG RCLGGMLQGS PVSPEEQDTA YWMKTPLFSD GVEMDTPQLD KCMSCLLEVA
     LSGNEEQKPF DYKLRPEIAV YVDLALGCSK EPARSLWISM QDYAVSKDWD SATLSNESLL
     DTVSRFVLAA LLKHTNLLSQ ACGESRYQPG KHLSEVYRCV YKVRSRLLAC KNLELIQTRS
     SSRDRWISEN QDSADVDPQE HSFTRTIDEE AEMEEQAERD REEGHPEPED EEEEREHEVM
     TAGKIFQCFL SAREVARSRD RDRMNSGAGS GARADDPPPQ SQQERRVSTD LPEGQDVYTA
     ACNSVIHRCA LLILGVSPVI DELQKRREEG QLQQPSTSAS EGGGLMTRSE SLTAESRLVH
     TSPNYRLIKS RSESDLSQPE SDEEGYALSG RRNVDLDLAA SHRKRGPMHS QLESLSDSWA
     RLKHSRDWLC NSSYSFESDF DLTKSLGVHT LIENVVSFVS GDVGNAPGFK EPEESMSTSP
     QASIIAMEQQ QLRAELRLEA LHQILVLLSG MEEKGSISLA GSRLSSGFQS STLLTSVRLQ
     FLAGCFGLGT VGHTGGKGES GRLHHYQDGI RAAKRNIQIE IQVAVHKIYQ QLSATLERAL
     QANKHHIEAQ QRLLLVTVFA LSVHYQPVDV SLAISTGLLN VLSQLCGTDT MLGQPLQLLP
     KTGVSQLSTA LKVASTRLLQ ILAITTGTYA DKLSPKVVQS LLDLLCSQLK NLLSQTGVLH
     MASFGEGEQE DGEEEEKKVD SSGETEKKDF RAALRKQHAA ELHLGDFLVF LRRVVSSKAI
     QSKMASPKWT EVLLNIASQK CSSGIPLVGN LRTRLLALHV LEAVLPACES GVEDDQMAQI
     VERLFSLLSD CMWETPIAQA KHAIQIKEKE QEIKLQKQGE LEEEDENLPI QEVSFDPEKA
     QCCLVENGQI LTHGSGGKGY GLASTGVTSG CYQWKFYIVK ENRGNEGTCV GVSRWPVHDF
     NHRTTSDMWL YRAYSGNLYH NGEQTLTLSS FTQGDFITCV LDMEARTISF GKNGEEPKLA
     FEDVDAAELY PCVMFYSSNP GEKVKICDMQ MRGTPRDLLP GDPICSPVAA VLAEATIQLI
     RILHRTDRWT YCINKKMMER LHKIKICIKE SGQKLKKSRS VQSREENEMR EEKESKEEEK
     GKHTRHGLAD LSELQLRTLC IEVWPVLAVI GGVDAGLRVG GRCVHKQTGR HATLLGVVKE
     GSTSAKVQWD EAEITISFPT FWSPSDTPLY NLEPCEPLPF DVARFRGLTA SVLLDLTYLT
     GVHEDMGKQS TKRHEKKHRH ESEEKGDVEQ KPESESALDM RTGLTSDDVK SQSTTSSKSE
     NEIASFSLDP TLPSVESQHQ ITEGKRKNHE HMSKNHDVAQ SEIRAVQLSY LYLGAMKSLS
     ALLGCSKYAE LLLIPKVLAE NGHNSDCASS PVVHEDVEMR AALQFLMRHM VKRAVMRSPI
     KRALGLADLE RAQAMIYKLV VHGLLEDQFG GKIKQEIDQQ AEESDPAQQA QTPVTTSPSA
     SSTTSFMSSS LEDTTTATTP VTDTETVPAS ESPGVMPLSL LRQMFSSYPT TTVLPTRRAQ
     TPPISSLPTS PSDEVGRRQS LTSPDSQSAR PANRTALSDP SSRLSTSPPP PAIAVPLLEM
     GFSLRQIAKA MEATGARGEA DAQNITVLAM WMIEHPGHED EEEPQSGSTA DSRPGAAVLG
     SGGKSNDPCY LQSPGDIPSA DAAEMEEGFS ESPDNLDHTE NAASGSGPSA RGRSAVTRRH
     KFDLAARTLL ARAAGLYRSV QAHRNQSRRE GISLQQDPGA LYDFNLDEEL EIDLDDEAME
     AMFGQDLTSD NDILGMWIPE VLDWPTWHVC ESEDREEVVV CELCECSVVS FNQHMKRNHP
     GCGRSANRQG YRSNGSYVDG WFGGECGSGN PYYLLCGTCR EKYLAMKTKS KSTSSERYKG
     QAPDLIGKQD SVYEEDWDML DVDEDEKLTG EEEFELLAGP LGLNDRRIVP EPVQFPDSDP
     LGASVAMVTA TNSMEETLMQ IGCHGSVEKS SSGRITLGEQ AAALANPHDR VVALRRVTAA
     AQVLLARTMV MRALSLLSVS GSSCSLAAGL ESLGLTDIRT LVRLMCLAAA GRAGLSTSPS
     AMASTSERSR GGHSKANKPI SCLAYLSTAV GCLASNAPSA AKLLVQLCTQ NLISAATGVN
     LTTVDDSIQR KFLPSFLRGI AEENKLVTSP NFVVTQALVA LLADKGAKLR PNYDKSEVEK
     KGPLELANAL AACCLSSRLS SQHRQWAAQQ LVRTLAAHDR DNQTTLQTLA DMGGDLRKCS
     FIKLEAHQNR VMTCVWCNKK GLLATSGNDG TIRVWNVTKK QYSLQQTCVF NRLEGDAEES
     LGSPSDPSFS PVSWSISGKY LAGALEKMVN IWQVNGGKGL VDIQPHWVSA LAWPEEGPAT
     AWSGESPELL LVGRMDGSLG LIEVVDVSTM HRRELEHCYR KDVSVTCIAW FSEDRPFAVG
     YFDGKLLLGT KEPLEKGGIV LIDAHKDTLI SMKWDPTGHI LMTCAKEDSV KLWGSISGCW
     CCLHSLCHPS IVNGIAWCRL PGKGSKLQLL MATGCQSGLV CVWRIPQDTT QTNVTSAEGW
     WEQESNCQDG YRKSSGAKCV YQLRGHITPV RTVAFSSDGL ALVSGGLGGL MNIWSLRDGS
     VLQTVVIGSG AIQTTVWIPE VGVAACSNRS KDVLVVNCTA EWAAANHVLA TCRTALKQQG
     VLGLNMAPCM RAFLERLPMM LQEQYAYEKP HVVCGDQLVH SPYMQCLASL AVGLHLDQLL
     CNPPVPPHHQ NCLPDPASWN PNEWAWLECF STTIKAAEAL TNGAQFPESF TVPDLEPVPE
     DELVFLMDNS KWINGMDEQI MSWATSRPED WHLGGKCDVY LWGAGRHGQL AEAGRNVMVP
     AAAPSFSQAQ QVICGQNCTF VIQANGTVLA CGEGSYGRLG QGNSDDLHVL TVISALQGFV
     VTQLVTSCGS DGHSMALTES GEVFSWGDGD YGKLGHGNSD RQRRPRQIEA LQGEEVVQMS
     CGFKHSAVVT SDGKLFTFGN GDYGRLGLGN TSNKKLPERV TALEGYQIGQ VACGLNHTLA
     VSADGSMVWA FGDGDYGKLG LGNSTAKSSP QKIDVLCGIG IKKVACGTQF SVALTKDGHV
     YTFGQDRLIG LPEGRARNHN RPQQIPVLAG VIIEDVAVGA EHTLALASNG DVYAWGSNSE
     GQLGLGHTNH VREPTLVTGL QGKNVRQISA GRCHSAAWTA PPVPPRAPGV SVPLQLGLPD
     TVPPQYGALR EVSIHTVRAR LRLLYHFSDL MYSSWRLLNL SPNNQNSTSH YNAGTWGIVQ
     GQLRPLLAPR VYTLPMVRSI GKTMVQGKNY GPQITVKRIS TRGRKCKPIF VQIARQVVKL
     NASDLRLPSR AWKVKLVGEG ADDAGGVFDD TITEMCQELE TGIVDLLIPS PNATAEVGYN
     RDRFLFNPSA CLDEHLMQFK FLGILMGVAI RTKKPLDLHL APLVWKQLCC VPLTLEDLEE
     VDLLYVQTLN SILHIEDSGI TEESFHEMIP LDSFVGQSAD GKMVPIIPGG NSIPLTFSNR
     KEYVERAIEY RLHEMDRQVA AVREGMSWIV PVPLLSLLTA KQLEQMVCGM PEISVEVLKK
     VVRYREVDEQ HQLVQWFWHT LEEFSNEERV LFMRFVSGRS RLPANTADIS QRFQIMKVDR
     PYDSLPTSQT CFFQLRLPPY SSQLVMAERL RYAINNCRSI DMDNYMLSRN VDNAEGSDTD
     Y
 
 
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