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HERC2_HUMAN
ID   HERC2_HUMAN             Reviewed;        4834 AA.
AC   O95714; Q86SV7; Q86SV8; Q86SV9; Q86YY3; Q86YY4; Q86YY5; Q86YY6; Q86YY7;
AC   Q86YY8; Q86YY9; Q86YZ0; Q86YZ1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 189.
DE   RecName: Full=E3 ubiquitin-protein ligase HERC2;
DE            EC=2.3.2.26 {ECO:0000269|PubMed:20304803};
DE   AltName: Full=HECT domain and RCC1-like domain-containing protein 2;
DE   AltName: Full=HECT-type E3 ubiquitin transferase HERC2;
GN   Name=HERC2 {ECO:0000312|EMBL:AAD08657.1};
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] {ECO:0000312|EMBL:AAD08657.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9949213; DOI=10.1093/hmg/8.3.533;
RA   Ji Y., Walkowicz M.J., Buiting K., Johnson D.K., Tarvin R.E., Rinchik E.M.,
RA   Horsthemke B., Stubbs L., Nicholls R.D.;
RT   "The ancestral gene for transcribed, low-copy repeats in the Prader-
RT   Willi/Angelman region encodes a large protein implicated in protein
RT   trafficking, which is deficient in mice with neuromuscular and spermiogenic
RT   abnormalities.";
RL   Hum. Mol. Genet. 8:533-542(1999).
RN   [2]
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   [3] {ECO:0000305, ECO:0000312|EMBL:AAO27483.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2818-2895; 2909-2957; 2963-3290;
RP   3317-3363; 3389-3430; 3458-3495; 3512-3527; 3533-3633; 3635-3821;
RP   3826-4084; 4097-4505 AND 4529-4834, AND GENE STRUCTURE.
RX   PubMed=10720573; DOI=10.1101/gr.10.3.319;
RA   Ji Y., Rebert N.A., Joslin J.M., Higgins M.J., Schultz R.A., Nicholls R.D.;
RT   "Structure of the highly conserved HERC2 gene and of multiple partially
RT   duplicated paralogs in human.";
RL   Genome Res. 10:319-329(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2454 AND SER-2928, AND
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   [5]
RP   INVOLVEMENT IN SHEP1.
RX   PubMed=18252221; DOI=10.1016/j.ajhg.2007.10.003;
RA   Kayser M., Liu F., Janssens A.C.J.W., Rivadeneira F., Lao O., van Duijn K.,
RA   Vermeulen M., Arp P., Jhamai M.M., van Ijcken W.F.J., den Dunnen J.T.,
RA   Heath S., Zelenika D., Despriet D.D.G., Klaver C.C.W., Vingerling J.R.,
RA   de Jong P.T.V.M., Hofman A., Aulchenko Y.S., Uitterlinden A.G.,
RA   Oostra B.A., van Duijn C.M.;
RT   "Three genome-wide association studies and a linkage analysis identify
RT   HERC2 as a human iris color gene.";
RL   Am. J. Hum. Genet. 82:411-423(2008).
RN   [6]
RP   INVOLVEMENT IN SHEP1.
RX   PubMed=18252222; DOI=10.1016/j.ajhg.2007.11.005;
RA   Sturm R.A., Duffy D.L., Zhao Z.Z., Leite F.P.M., Stark M.S., Hayward N.K.,
RA   Martin N.G., Montgomery G.W.;
RT   "A single SNP in an evolutionary conserved region within intron 86 of the
RT   HERC2 gene determines human blue-brown eye color.";
RL   Am. J. Hum. Genet. 82:424-431(2008).
RN   [7]
RP   INVOLVEMENT IN SHEP1, AND REGULATION OF OCA2.
RX   PubMed=18172690; DOI=10.1007/s00439-007-0460-x;
RA   Eiberg H., Troelsen J., Nielsen M., Mikkelsen A., Mengel-From J.,
RA   Kjaer K.W., Hansen L.;
RT   "Blue eye color in humans may be caused by a perfectly associated founder
RT   mutation in a regulatory element located within the HERC2 gene inhibiting
RT   OCA2 expression.";
RL   Hum. Genet. 123:177-187(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2928; SER-4810; SER-4811 AND
RP   SER-4814, AND 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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2454, AND IDENTIFICATION BY
RP   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   [11]
RP   MISCELLANEOUS.
RX   PubMed=20457063; DOI=10.1016/j.fsigen.2009.12.004;
RA   Mengel-From J., Borsting C., Sanchez J.J., Eiberg H., Morling N.;
RT   "Human eye colour and HERC2, OCA2 and MATP.";
RL   Forensic Sci. Int. Genet. 4:323-328(2010).
RN   [12]
RP   FUNCTION, INTERACTION WITH RNF8, PHOSPHORYLATION AT THR-4827, MUTAGENESIS
RP   OF THR-4827, AND SUBCELLULAR LOCATION.
RX   PubMed=20023648; DOI=10.1038/ncb2008;
RA   Bekker-Jensen S., Rendtlew Danielsen J., Fugger K., Gromova I.,
RA   Nerstedt A., Lukas C., Bartek J., Lukas J., Mailand N.;
RT   "HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on
RT   damaged chromosomes.";
RL   Nat. Cell Biol. 12:80-86(2010).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH XPA, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=20304803; DOI=10.1073/pnas.0915085107;
RA   Kang T.H., Lindsey-Boltz L.A., Reardon J.T., Sancar A.;
RT   "Circadian control of XPA and excision repair of cisplatin-DNA damage by
RT   cryptochrome and HERC2 ubiquitin ligase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:4890-4895(2010).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2454 AND SER-2928, AND
RP   IDENTIFICATION BY 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   [15]
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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-647; THR-1944 AND SER-2928,
RP   AND IDENTIFICATION BY 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   [17]
RP   SUMOYLATION, FUNCTION, SUMO-BINDING, DOMAIN, INTERACTION WITH RNF8, AND
RP   MUTAGENESIS OF CYS-2708 AND CYS-2711.
RX   PubMed=22508508; DOI=10.1083/jcb.201106152;
RA   Danielsen J.R., Povlsen L.K., Villumsen B.H., Streicher W., Nilsson J.,
RA   Wikstrom M., Bekker-Jensen S., Mailand N.;
RT   "DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a
RT   novel SUMO-binding Zinc finger.";
RL   J. Cell Biol. 197:179-187(2012).
RN   [18]
RP   INTERACTION WITH CCP110; CEP97 AND NEURL4, AND SUBCELLULAR LOCATION.
RX   PubMed=22261722; DOI=10.1074/mcp.m111.014233;
RA   Al-Hakim A.K., Bashkurov M., Gingras A.C., Durocher D., Pelletier L.;
RT   "Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as
RT   novel modulators of centrosome architecture.";
RL   Mol. Cell. Proteomics 11:M111.014233.01-M111.014233.14(2012).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-272; SER-2454 AND SER-2928,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [20]
RP   FUNCTION.
RX   PubMed=26692333; DOI=10.1038/nm.4013;
RA   Osorio F.G., Soria-Valles C., Santiago-Fernandez O., Bernal T.,
RA   Mittelbrunn M., Colado E., Rodriguez F., Bonzon-Kulichenko E., Vazquez J.,
RA   Porta-de-la-Riva M., Ceron J., Fueyo A., Li J., Green A.R., Freije J.M.,
RA   Lopez-Otin C.;
RT   "Loss of the proteostasis factor AIRAPL causes myeloid transformation by
RT   deregulating IGF-1 signaling.";
RL   Nat. Med. 22:91-96(2016).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 417-790, AND RCC1 REPEATS.
RA   Tempel W., Khan M.B., Dong A., Hu J., Li Y., Bountra C., Arrowsmith C.H.,
RA   Edwards A.M., Tong Y.;
RT   "Structure of the first RCC1-like domain of HERC2.";
RL   Submitted (JUN-2013) to the PDB data bank.
RN   [22]
RP   VARIANT MRT38 LEU-594, AND CHARACTERIZATION OF VARIANT MRT38 LEU-594.
RX   PubMed=23065719; DOI=10.1002/humu.22237;
RA   Puffenberger E.G., Jinks R.N., Wang H., Xin B., Fiorentini C.,
RA   Sherman E.A., Degrazio D., Shaw C., Sougnez C., Cibulskis K., Gabriel S.,
RA   Kelley R.I., Morton D.H., Strauss K.A.;
RT   "A homozygous missense mutation in HERC2 associated with global
RT   developmental delay and autism spectrum disorder.";
RL   Hum. Mutat. 33:1639-1646(2012).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that regulates ubiquitin-
CC       dependent retention of repair proteins on damaged chromosomes.
CC       Recruited to sites of DNA damage in response to ionizing radiation (IR)
CC       and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-
CC       induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a
CC       mediator of binding specificity between UBE2N and RNF8. Involved in the
CC       maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes
CC       the ubiquitination and proteasomal degradation of XPA which influences
CC       the circadian oscillation of DNA excision repair activity. By
CC       controlling the steady-state expression of the IGF1R receptor,
CC       indirectly regulates the insulin-like growth factor receptor signaling
CC       pathway (PubMed:26692333). {ECO:0000269|PubMed:20023648,
CC       ECO:0000269|PubMed:20304803, ECO:0000269|PubMed:22508508,
CC       ECO:0000269|PubMed:26692333}.
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; Evidence={ECO:0000269|PubMed:20304803};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts (when phosphorylated at Thr-4827 and sumoylated)
CC       with RNF8 (via FHA domain); this interaction increases after ionizing
CC       radiation (IR) treatment. Interacts with XPA. Interacts with NEURL4.
CC       Via its interaction with NEURL4, may indirectly interact with CCP110
CC       and CEP97. {ECO:0000269|PubMed:20023648, ECO:0000269|PubMed:20304803,
CC       ECO:0000269|PubMed:22261722, ECO:0000269|PubMed:22508508}.
CC   -!- INTERACTION:
CC       O95714; Q9BXG8: SPZ1; NbExp=2; IntAct=EBI-1058922, EBI-8483734;
CC       O95714; Q05086-2: UBE3A; NbExp=5; IntAct=EBI-1058922, EBI-10175863;
CC       O95714; P23025: XPA; NbExp=4; IntAct=EBI-1058922, EBI-295222;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole. Nucleus. Note=Recruited to
CC       sites of DNA damage in response to ionizing radiation (IR) via its
CC       interaction with RNF8. May loose association with centrosomes during
CC       mitosis.
CC   -!- DOMAIN: The ZZ-type zinc finger mediates binding to SUMO1, and at low
CC       level SUMO2. {ECO:0000269|PubMed:22508508}.
CC   -!- DOMAIN: The RCC1 repeats are grouped into three seven-bladed beta-
CC       propeller regions. {ECO:0000269|PubMed:22508508}.
CC   -!- PTM: Phosphorylation at Thr-4827 is required for interaction with RNF8.
CC       {ECO:0000269|PubMed:20023648}.
CC   -!- PTM: Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks
CC       (DSBs), promoting the interaction with RNF8.
CC       {ECO:0000269|PubMed:22508508}.
CC   -!- POLYMORPHISM: Genetic variants in HERC2 define the skin/hair/eye
CC       pigmentation variation locus 1 (SHEP1) [MIM:227220]; also known as
CC       skin/hair/eye pigmentation type 1, blue/nonblue eyes or skin/hair/eye
CC       pigmentation type 1, blue/brown eyes or skin/hair/eye pigmentation type
CC       1, blond/brown hair or eye color, brown/blue or eye color, blue/nonblue
CC       or eye color type 3 (EYCL3) or brown eye color type 2 (BEY2) or hair
CC       color type 3 (HCL3). Hair, eye and skin pigmentation are among the most
CC       visible examples of human phenotypic variation, with a broad normal
CC       range that is subject to substantial geographic stratification. In the
CC       case of skin, individuals tend to have lighter pigmentation with
CC       increasing distance from the equator. By contrast, the majority of
CC       variation in human eye and hair color is found among individuals of
CC       European ancestry, with most other human populations fixed for brown
CC       eyes and black hair.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal recessive 38
CC       (MRT38) [MIM:615516]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period. MRT38
CC       is characterized by global developmental delay affecting motor, speech,
CC       adaptive, and social development. Patients manifest autistic features,
CC       aggression, self-injury, impulsivity, and distractibility.
CC       {ECO:0000269|PubMed:23065719}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: A regulatory element withinin an intron of the HERC2
CC       gene inhibits OCA2 promoter. There are several single nucleotide
CC       polymorphisms within the OCA2 gene and within the HERC2 gene that have
CC       a statistical association with human eye color.
CC   -!- WEB RESOURCE: Name=Hect domain and RLD 2 (HERC2); Note=Leiden Open
CC       Variation Database (LOVD);
CC       URL="https://databases.lovd.nl/shared/genes/HERC2";
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DR   EMBL; AF071172; AAD08657.1; -; mRNA.
DR   EMBL; AC091304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF224243; AAO27473.1; -; Genomic_DNA.
DR   EMBL; AF224242; AAO27473.1; JOINED; Genomic_DNA.
DR   EMBL; AF224245; AAO27474.1; -; Genomic_DNA.
DR   EMBL; AF224244; AAO27474.1; JOINED; Genomic_DNA.
DR   EMBL; AF224249; AAO27475.1; -; Genomic_DNA.
DR   EMBL; AF224246; AAO27475.1; JOINED; Genomic_DNA.
DR   EMBL; AF224247; AAO27475.1; JOINED; Genomic_DNA.
DR   EMBL; AF224248; AAO27475.1; JOINED; Genomic_DNA.
DR   EMBL; AF224251; AAO27476.1; -; Genomic_DNA.
DR   EMBL; AF224250; AAO27476.1; JOINED; Genomic_DNA.
DR   EMBL; AF224255; AAO27479.1; -; Genomic_DNA.
DR   EMBL; AF224254; AAO27479.1; JOINED; Genomic_DNA.
DR   EMBL; AF224252; AAO27477.1; -; Genomic_DNA.
DR   EMBL; AF224253; AAO27478.1; -; Genomic_DNA.
DR   EMBL; AF224257; AAO27480.1; -; Genomic_DNA.
DR   EMBL; AF224256; AAO27480.1; JOINED; Genomic_DNA.
DR   EMBL; AF225401; AAO27481.1; -; Genomic_DNA.
DR   EMBL; AF225400; AAO27481.1; JOINED; Genomic_DNA.
DR   EMBL; AF225404; AAO27482.1; -; Genomic_DNA.
DR   EMBL; AF225402; AAO27482.1; JOINED; Genomic_DNA.
DR   EMBL; AF225403; AAO27482.1; JOINED; Genomic_DNA.
DR   EMBL; AF225407; AAO27483.1; -; Genomic_DNA.
DR   EMBL; AF225405; AAO27483.1; JOINED; Genomic_DNA.
DR   EMBL; AF225406; AAO27483.1; JOINED; Genomic_DNA.
DR   EMBL; AF225409; AAO27484.1; -; Genomic_DNA.
DR   EMBL; AF225408; AAO27484.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS10021.1; -.
DR   RefSeq; NP_004658.3; NM_004667.5.
DR   PDB; 2KEO; NMR; -; A=1203-1296.
DR   PDB; 3KCI; X-ray; 1.80 A; A=3951-4321.
DR   PDB; 4L1M; X-ray; 2.60 A; A/B/C=417-790.
DR   PDB; 6WW3; X-ray; 2.10 A; A/B=2702-2755.
DR   PDB; 6WW4; X-ray; 2.25 A; A/B=2702-2751.
DR   PDBsum; 2KEO; -.
DR   PDBsum; 3KCI; -.
DR   PDBsum; 4L1M; -.
DR   PDBsum; 6WW3; -.
DR   PDBsum; 6WW4; -.
DR   SMR; O95714; -.
DR   BioGRID; 114438; 444.
DR   CORUM; O95714; -.
DR   DIP; DIP-37632N; -.
DR   IntAct; O95714; 136.
DR   MINT; O95714; -.
DR   STRING; 9606.ENSP00000261609; -.
DR   GlyConnect; 1191; 2 N-Linked glycans (2 sites).
DR   GlyGen; O95714; 4 sites, 3 N-linked glycans (2 sites), 1 O-linked glycan (2 sites).
DR   iPTMnet; O95714; -.
DR   PhosphoSitePlus; O95714; -.
DR   BioMuta; HERC2; -.
DR   EPD; O95714; -.
DR   jPOST; O95714; -.
DR   MassIVE; O95714; -.
DR   MaxQB; O95714; -.
DR   PaxDb; O95714; -.
DR   PeptideAtlas; O95714; -.
DR   PRIDE; O95714; -.
DR   ProteomicsDB; 51008; -.
DR   Antibodypedia; 22335; 53 antibodies from 11 providers.
DR   DNASU; 8924; -.
DR   Ensembl; ENST00000261609.13; ENSP00000261609.8; ENSG00000128731.18.
DR   GeneID; 8924; -.
DR   KEGG; hsa:8924; -.
DR   MANE-Select; ENST00000261609.13; ENSP00000261609.8; NM_004667.6; NP_004658.3.
DR   UCSC; uc001zbj.5; human.
DR   CTD; 8924; -.
DR   DisGeNET; 8924; -.
DR   GeneCards; HERC2; -.
DR   GeneReviews; HERC2; -.
DR   HGNC; HGNC:4868; HERC2.
DR   HPA; ENSG00000128731; Low tissue specificity.
DR   MalaCards; HERC2; -.
DR   MIM; 227220; phenotype.
DR   MIM; 605837; gene.
DR   MIM; 615516; phenotype.
DR   neXtProt; NX_O95714; -.
DR   OpenTargets; ENSG00000128731; -.
DR   Orphanet; 329195; Developmental delay with autism spectrum disorder and gait instability.
DR   PharmGKB; PA29243; -.
DR   VEuPathDB; HostDB:ENSG00000128731; -.
DR   eggNOG; KOG1426; Eukaryota.
DR   GeneTree; ENSGT00940000154975; -.
DR   HOGENOM; CLU_000101_0_0_1; -.
DR   InParanoid; O95714; -.
DR   OMA; GPRFKCK; -.
DR   OrthoDB; 1062377at2759; -.
DR   PhylomeDB; O95714; -.
DR   TreeFam; TF320636; -.
DR   PathwayCommons; O95714; -.
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; O95714; -.
DR   SIGNOR; O95714; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 8924; 41 hits in 1125 CRISPR screens.
DR   ChiTaRS; HERC2; human.
DR   EvolutionaryTrace; O95714; -.
DR   GeneWiki; HERC2; -.
DR   GenomeRNAi; 8924; -.
DR   Pharos; O95714; Tbio.
DR   PRO; PR:O95714; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; O95714; protein.
DR   Bgee; ENSG00000128731; Expressed in sural nerve and 94 other tissues.
DR   ExpressionAtlas; O95714; baseline and differential.
DR   Genevisible; O95714; HS.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; NAS:UniProtKB.
DR   GO; GO:0032183; F:SUMO binding; IDA:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   CDD; cd08664; APC10-HERC2; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd02344; ZZ_HERC2; 1.
DR   Gene3D; 2.130.10.30; -; 3.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 3.10.120.10; -; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   InterPro; IPR004939; APC_su10/DOC_dom.
DR   InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR   InterPro; IPR021097; CPH_domain.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR037976; HERC2_APC10.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR037252; Mib_Herc2_sf.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   InterPro; IPR041987; ZZ_HERC2.
DR   Pfam; PF03256; ANAPC10; 1.
DR   Pfam; PF11515; Cul7; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF06701; MIB_HERC2; 1.
DR   Pfam; PF00415; RCC1; 16.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM01337; APC10; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00706; TECPR; 5.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF159034; SSF159034; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF50985; SSF50985; 3.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS51416; MIB_HERC2; 1.
DR   PROSITE; PS00626; RCC1_2; 1.
DR   PROSITE; PS50012; RCC1_3; 18.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Disease variant;
KW   DNA damage; DNA repair; Intellectual disability; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..4834
FT                   /note="E3 ubiquitin-protein ligase HERC2"
FT                   /id="PRO_0000229739"
FT   REPEAT          415..461
FT                   /note="RCC1 1-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          462..512
FT                   /note="RCC1 1-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          513..568
FT                   /note="RCC1 1-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          569..620
FT                   /note="RCC1 1-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          623..674
FT                   /note="RCC1 1-5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          675..726
FT                   /note="RCC1 1-6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          728..778
FT                   /note="RCC1 1-7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   DOMAIN          1207..1283
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   DOMAIN          1859..1932
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT   DOMAIN          2759..2936
FT                   /note="DOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT   REPEAT          2958..3009
FT                   /note="RCC1 2-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          3010..3064
FT                   /note="RCC1 2-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          3065..3116
FT                   /note="RCC1 2-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          3118..3168
FT                   /note="RCC1 2-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          3171..3222
FT                   /note="RCC1 2-5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          3224..3274
FT                   /note="RCC1 2-6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          3275..3326
FT                   /note="RCC1 2-7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          3951..4002
FT                   /note="RCC1 3-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          4004..4056
FT                   /note="RCC1 3-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          4058..4108
FT                   /note="RCC1 3-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          4110..4162
FT                   /note="RCC1 3-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          4164..4214
FT                   /note="RCC1 3-5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          4216..4266
FT                   /note="RCC1 3-6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   REPEAT          4268..4318
FT                   /note="RCC1 3-7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00235,
FT                   ECO:0000269|Ref.21"
FT   DOMAIN          4457..4794
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   ZN_FING         2703..2755
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   REGION          50..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1555..1575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1933..1958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3602..3629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4804..4834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          948..980
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        57..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4808..4822
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        4762
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   BINDING         2708
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         2711
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         2723
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         2726
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         2732
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         2735
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         2741
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         2745
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   MOD_RES         272
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         647
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4U2R1"
FT   MOD_RES         1942
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4U2R1"
FT   MOD_RES         1944
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         2454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         2928
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         4810
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         4811
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         4814
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         4827
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:20023648"
FT   VARIANT         594
FT                   /note="P -> L (in MRT38; less stable than wild-type;
FT                   diffuse cytosolic localization with the formation of
FT                   abnormal aggregates; dbSNP:rs397518474)"
FT                   /evidence="ECO:0000269|PubMed:23065719"
FT                   /id="VAR_069282"
FT   MUTAGEN         2708
FT                   /note="C->S: Abolishes binding to SUMO; when associated
FT                   with S-2711."
FT                   /evidence="ECO:0000269|PubMed:22508508"
FT   MUTAGEN         2711
FT                   /note="C->S: Abolishes binding to SUMO; when associated
FT                   with S-2708."
FT                   /evidence="ECO:0000269|PubMed:22508508"
FT   MUTAGEN         4827
FT                   /note="T->A: Prevents HERC2 C-terminal fragment binding to
FT                   endogenous RNF8."
FT                   /evidence="ECO:0000269|PubMed:20023648"
FT   CONFLICT        1053
FT                   /note="L -> W (in Ref. 1; AAD08657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1150
FT                   /note="G -> D (in Ref. 1; AAD08657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1354
FT                   /note="S -> R (in Ref. 1; AAD08657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1566
FT                   /note="T -> M (in Ref. 1; AAD08657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1753
FT                   /note="K -> T (in Ref. 1; AAD08657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2444
FT                   /note="R -> H (in Ref. 1; AAD08657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2881
FT                   /note="C -> Y (in Ref. 1; AAD08657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3070
FT                   /note="S -> W (in Ref. 3; AAO27475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3346
FT                   /note="P -> R (in Ref. 3; AAO27476)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3583..3584
FT                   /note="VA -> MP (in Ref. 3; AAO27480)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3597
FT                   /note="D -> N (in Ref. 3; AAO27480)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3808
FT                   /note="F -> S (in Ref. 3; AAO27481)"
FT                   /evidence="ECO:0000305"
FT   STRAND          425..430
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   TURN            436..438
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           446..449
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          453..458
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          460..467
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          472..476
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          495..499
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          505..511
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          516..520
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           523..525
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          528..531
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          535..540
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           542..544
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           549..551
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          552..558
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          560..567
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          572..576
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           579..581
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          585..587
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          591..596
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           598..600
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          605..610
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          616..621
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          626..630
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           633..635
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          638..642
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          645..650
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           652..654
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          659..665
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          668..673
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          678..682
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           685..687
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          691..693
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          697..702
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           704..706
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          711..716
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          718..725
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          730..735
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          746..754
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          763..768
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   STRAND          770..777
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   TURN            781..783
FT                   /evidence="ECO:0007829|PDB:4L1M"
FT   HELIX           1212..1221
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   STRAND          1225..1228
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   STRAND          1231..1234
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   HELIX           1235..1242
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   HELIX           1250..1252
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   HELIX           1257..1266
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   HELIX           1270..1273
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   HELIX           1274..1277
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   STRAND          1278..1282
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   HELIX           1285..1288
FT                   /evidence="ECO:0007829|PDB:2KEO"
FT   TURN            2709..2711
FT                   /evidence="ECO:0007829|PDB:6WW3"
FT   STRAND          2714..2718
FT                   /evidence="ECO:0007829|PDB:6WW3"
FT   STRAND          2720..2728
FT                   /evidence="ECO:0007829|PDB:6WW3"
FT   HELIX           2733..2738
FT                   /evidence="ECO:0007829|PDB:6WW3"
FT   STRAND          2747..2752
FT                   /evidence="ECO:0007829|PDB:6WW3"
FT   STRAND          3954..3959
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          3971..3978
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           3980..3984
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          3987..3993
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          3996..4001
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4006..4010
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4013..4015
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4018..4022
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4025..4030
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4032..4034
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4039..4043
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4049..4055
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4060..4064
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4067..4069
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4073..4075
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4079..4084
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4086..4088
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4093..4098
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4100..4107
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4112..4116
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4119..4121
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4125..4127
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4131..4136
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4138..4140
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4145..4150
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4156..4161
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   TURN            4162..4164
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4165..4170
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4173..4175
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4178..4181
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4185..4190
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4192..4194
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4199..4205
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4208..4213
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4218..4222
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4225..4227
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4231..4233
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4237..4242
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4244..4246
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4251..4256
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4258..4265
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4270..4274
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4283..4285
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4289..4294
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   HELIX           4296..4298
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4305..4309
FT                   /evidence="ECO:0007829|PDB:3KCI"
FT   STRAND          4312..4316
FT                   /evidence="ECO:0007829|PDB:3KCI"
SQ   SEQUENCE   4834 AA;  527228 MW;  A323DC1DA6B221D0 CRC64;
     MPSESFCLAA QARLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT ESTQNGELPP
     RKDDSVEPSG TKKEDLNDKE KKDEEETPAP IYRAKSILDS WVWGKQPDVN ELKECLSVLV
     KEQQALAVQS ATTTLSALRL KQRLVILERY FIALNRTVFQ ENVKVKWKSS GISLPPVDKK
     SSRPAGKGVE GLARVGSRAA LSFAFAFLRR AWRSGEDADL CSELLQESLD ALRALPEASL
     FDESTVSSVW LEVVERATRF LRSVVTGDVH GTPATKGPGS IPLQDQHLAL AILLELAVQR
     GTLSQMLSAI LLLLQLWDSG AQETDNERSA QGTSAPLLPL LQRFQSIICR KDAPHSEGDM
     HLLSGPLSPN ESFLRYLTLP QDNELAIDLR QTAVVVMAHL DRLATPCMPP LCSSPTSHKG
     SLQEVIGWGL IGWKYYANVI GPIQCEGLAN LGVTQIACAE KRFLILSRNG RVYTQAYNSD
     TLAPQLVQGL ASRNIVKIAA HSDGHHYLAL AATGEVYSWG CGDGGRLGHG DTVPLEEPKV
     ISAFSGKQAG KHVVHIACGS TYSAAITAEG ELYTWGRGNY GRLGHGSSED EAIPMLVAGL
     KGLKVIDVAC GSGDAQTLAV TENGQVWSWG DGDYGKLGRG GSDGCKTPKL IEKLQDLDVV
     KVRCGSQFSI ALTKDGQVYS WGKGDNQRLG HGTEEHVRYP KLLEGLQGKK VIDVAAGSTH
     CLALTEDSEV HSWGSNDQCQ HFDTLRVTKP EPAALPGLDT KHIVGIACGP AQSFAWSSCS
     EWSIGLRVPF VVDICSMTFE QLDLLLRQVS EGMDGSADWP PPQEKECVAV ATLNLLRLQL
     HAAISHQVDP EFLGLGLGSI LLNSLKQTVV TLASSAGVLS TVQSAAQAVL QSGWSVLLPT
     AEERARALSA LLPCAVSGNE VNISPGRRFM IDLLVGSLMA DGGLESALHA AITAEIQDIE
     AKKEAQKEKE IDEQEANAST FHRSRTPLDK DLINTGICES SGKQCLPLVQ LIQQLLRNIA
     SQTVARLKDV ARRISSCLDF EQHSRERSAS LDLLLRFQRL LISKLYPGES IGQTSDISSP
     ELMGVGSLLK KYTALLCTHI GDILPVAASI ASTSWRHFAE VAYIVEGDFT GVLLPELVVS
     IVLLLSKNAG LMQEAGAVPL LGGLLEHLDR FNHLAPGKER DDHEELAWPG IMESFFTGQN
     CRNNEEVTLI RKADLENHNK DGGFWTVIDG KVYDIKDFQT QSLTGNSILA QFAGEDPVVA
     LEAALQFEDT RESMHAFCVG QYLEPDQEIV TIPDLGSLSS PLIDTERNLG LLLGLHASYL
     AMSTPLSPVE IECAKWLQSS IFSGGLQTSQ IHYSYNEEKD EDHCSSPGGT PASKSRLCSH
     RRALGDHSQA FLQAIADNNI QDHNVKDFLC QIERYCRQCH LTTPIMFPPE HPVEEVGRLL
     LCCLLKHEDL GHVALSLVHA GALGIEQVKH RTLPKSVVDV CRVVYQAKCS LIKTHQEQGR
     SYKEVCAPVI ERLRFLFNEL RPAVCNDLSI MSKFKLLSSL PRWRRIAQKI IRERRKKRVP
     KKPESTDDEE KIGNEESDLE EACILPHSPI NVDKRPIAIK SPKDKWQPLL STVTGVHKYK
     WLKQNVQGLY PQSPLLSTIA EFALKEEPVD VEKMRKCLLK QLERAEVRLE GIDTILKLAS
     KNFLLPSVQY AMFCGWQRLI PEGIDIGEPL TDCLKDVDLI PPFNRMLLEV TFGKLYAWAV
     QNIRNVLMDA SAKFKELGIQ PVPLQTITNE NPSGPSLGTI PQARFLLVML SMLTLQHGAN
     NLDLLLNSGM LALTQTALRL IGPSCDNVEE DMNASAQGAS ATVLEETRKE TAPVQLPVSG
     PELAAMMKIG TRVMRGVDWK WGDQDGPPPG LGRVIGELGE DGWIRVQWDT GSTNSYRMGK
     EGKYDLKLAE LPAAAQPSAE DSDTEDDSEA EQTERNIHPT AMMFTSTINL LQTLCLSAGV
     HAEIMQSEAT KTLCGLLRML VESGTTDKTS SPNRLVYREQ HRSWCTLGFV RSIALTPQVC
     GALSSPQWIT LLMKVVEGHA PFTATSLQRQ ILAVHLLQAV LPSWDKTERA RDMKCLVEKL
     FDFLGSLLTT CSSDVPLLRE STLRRRRVRP QASLTATHSS TLAEEVVALL RTLHSLTQWN
     GLINKYINSQ LRSITHSFVG RPSEGAQLED YFPDSENPEV GGLMAVLAVI GGIDGRLRLG
     GQVMHDEFGE GTVTRITPKG KITVQFSDMR TCRVCPLNQL KPLPAVAFNV NNLPFTEPML
     SVWAQLVNLA GSKLEKHKIK KSTKQAFAGQ VDLDLLRCQQ LKLYILKAGR ALLSHQDKLR
     QILSQPAVQE TGTVHTDDGA VVSPDLGDMS PEGPQPPMIL LQQLLASATQ PSPVKAIFDK
     QELEAAALAV CQCLAVESTH PSSPGFEDCS SSEATTPVAV QHIRPARVKR RKQSPVPALP
     IVVQLMEMGF SRRNIEFALK SLTGASGNAS SLPGVEALVG WLLDHSDIQV TELSDADTVS
     DEYSDEEVVE DVDDAAYSMS TGAVVTESQT YKKRADFLSN DDYAVYVREN IQVGMMVRCC
     RAYEEVCEGD VGKVIKLDRD GLHDLNVQCD WQQKGGTYWV RYIHVELIGY PPPSSSSHIK
     IGDKVRVKAS VTTPKYKWGS VTHQSVGVVK AFSANGKDII VDFPQQSHWT GLLSEMELVP
     SIHPGVTCDG CQMFPINGSR FKCRNCDDFD FCETCFKTKK HNTRHTFGRI NEPGQSAVFC
     GRSGKQLKRC HSSQPGMLLD SWSRMVKSLN VSSSVNQASR LIDGSEPCWQ SSGSQGKHWI
     RLEIFPDVLV HRLKMIVDPA DSSYMPSLVV VSGGNSLNNL IELKTININP SDTTVPLLND
     CTEYHRYIEI AIKQCRSSGI DCKIHGLILL GRIRAEEEDL AAVPFLASDN EEEEDEKGNS
     GSLIRKKAAG LESAATIRTK VFVWGLNDKD QLGGLKGSKI KVPSFSETLS ALNVVQVAGG
     SKSLFAVTVE GKVYACGEAT NGRLGLGISS GTVPIPRQIT ALSSYVVKKV AVHSGGRHAT
     ALTVDGKVFS WGEGDDGKLG HFSRMNCDKP RLIEALKTKR IRDIACGSSH SAALTSSGEL
     YTWGLGEYGR LGHGDNTTQL KPKMVKVLLG HRVIQVACGS RDAQTLALTD EGLVFSWGDG
     DFGKLGRGGS EGCNIPQNIE RLNGQGVCQI ECGAQFSLAL TKSGVVWTWG KGDYFRLGHG
     SDVHVRKPQV VEGLRGKKIV HVAVGALHCL AVTDSGQVYA WGDNDHGQQG NGTTTVNRKP
     TLVQGLEGQK ITRVACGSSH SVAWTTVDVA TPSVHEPVLF QTARDPLGAS YLGVPSDADS
     SAASNKISGA SNSKPNRPSL AKILLSLDGN LAKQQALSHI LTALQIMYAR DAVVGALMPA
     AMIAPVECPS FSSAAPSDAS AMASPMNGEE CMLAVDIEDR LSPNPWQEKR EIVSSEDAVT
     PSAVTPSAPS ASARPFIPVT DDLGAASIIA ETMTKTKEDV ESQNKAAGPE PQALDEFTSL
     LIADDTRVVV DLLKLSVCSR AGDRGRDVLS AVLSGMGTAY PQVADMLLEL CVTELEDVAT
     DSQSGRLSSQ PVVVESSHPY TDDTSTSGTV KIPGAEGLRV EFDRQCSTER RHDPLTVMDG
     VNRIVSVRSG REWSDWSSEL RIPGDELKWK FISDGSVNGW GWRFTVYPIM PAAGPKELLS
     DRCVLSCPSM DLVTCLLDFR LNLASNRSIV PRLAASLAAC AQLSALAASH RMWALQRLRK
     LLTTEFGQSI NINRLLGEND GETRALSFTG SALAALVKGL PEALQRQFEY EDPIVRGGKQ
     LLHSPFFKVL VALACDLELD TLPCCAETHK WAWFRRYCMA SRVAVALDKR TPLPRLFLDE
     VAKKIRELMA DSENMDVLHE SHDIFKREQD EQLVQWMNRR PDDWTLSAGG SGTIYGWGHN
     HRGQLGGIEG AKVKVPTPCE ALATLRPVQL IGGEQTLFAV TADGKLYATG YGAGGRLGIG
     GTESVSTPTL LESIQHVFIK KVAVNSGGKH CLALSSEGEV YSWGEAEDGK LGHGNRSPCD
     RPRVIESLRG IEVVDVAAGG AHSACVTAAG DLYTWGKGRY GRLGHSDSED QLKPKLVEAL
     QGHRVVDIAC GSGDAQTLCL TDDDTVWSWG DGDYGKLGRG GSDGCKVPMK IDSLTGLGVV
     KVECGSQFSV ALTKSGAVYT WGKGDYHRLG HGSDDHVRRP RQVQGLQGKK VIAIATGSLH
     CVCCTEDGEV YTWGDNDEGQ LGDGTTNAIQ RPRLVAALQG KKVNRVACGS AHTLAWSTSK
     PASAGKLPAQ VPMEYNHLQE IPIIALRNRL LLLHHLSELF CPCIPMFDLE GSLDETGLGP
     SVGFDTLRGI LISQGKEAAF RKVVQATMVR DRQHGPVVEL NRIQVKRSRS KGGLAGPDGT
     KSVFGQMCAK MSSFGPDSLL LPHRVWKVKF VGESVDDCGG GYSESIAEIC EELQNGLTPL
     LIVTPNGRDE SGANRDCYLL SPAARAPVHS SMFRFLGVLL GIAIRTGSPL SLNLAEPVWK
     QLAGMSLTIA DLSEVDKDFI PGLMYIRDNE ATSEEFEAMS LPFTVPSASG QDIQLSSKHT
     HITLDNRAEY VRLAINYRLH EFDEQVAAVR EGMARVVPVP LLSLFTGYEL ETMVCGSPDI
     PLHLLKSVAT YKGIEPSASL IQWFWEVMES FSNTERSLFL RFVWGRTRLP RTIADFRGRD
     FVIQVLDKYN PPDHFLPESY TCFFLLKLPR YSCKQVLEEK LKYAIHFCKS IDTDDYARIA
     LTGEPAADDS SDDSDNEDVD SFASDSTQDY LTGH
 
 
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