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 27-MAR-2024, entry version 192.
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; 166.
DR CORUM; Q15751; -.
DR IntAct; Q15751; 43.
DR MINT; Q15751; -.
DR STRING; 9606.ENSP00000390158; -.
DR GlyGen; Q15751; 2 sites, 1 O-linked glycan (2 sites).
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; 9606-ENSP00000390158; -.
DR PeptideAtlas; Q15751; -.
DR ProteomicsDB; 60743; -.
DR Pumba; Q15751; -.
DR Antibodypedia; 25716; 74 antibodies from 11 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 AGR; HGNC:4867; -.
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; LAICCQN; -.
DR OrthoDB; 5491782at2759; -.
DR PhylomeDB; Q15751; -.
DR TreeFam; TF106426; -.
DR PathwayCommons; Q15751; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q15751; -.
DR SIGNOR; Q15751; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8925; 30 hits in 1204 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 197 other cell types or 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:0022038; P:corpus callosum development; 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 GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd12881; SPRY_HERC1; 1.
DR CDD; cd14401; UBA_HERC1; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22872; BTK-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR22872:SF6; E3 UBIQUITIN-PROTEIN LIGASE HERC1-RELATED; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00415; RCC1; 10.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00449; SPRY; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
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 (found in a patient with childhood apraxia of
FT speech; uncertain 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
//
