UBE2B_HUMAN
ID UBE2B_HUMAN Reviewed; 152 AA.
AC P63146; B2R503; D3DQA2; P23567; Q4PJ15; Q9D0J6;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 B;
DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
DE AltName: Full=E2 ubiquitin-conjugating enzyme B;
DE AltName: Full=RAD6 homolog B;
DE Short=HR6B;
DE Short=hHR6B;
DE AltName: Full=Ubiquitin carrier protein B;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa;
DE AltName: Full=Ubiquitin-protein ligase B;
GN Name=UBE2B; Synonyms=RAD6B;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=2158443; DOI=10.1002/j.1460-2075.1990.tb08259.x;
RA Schneider R., Eckerskorn C., Lottspeich F., Schweiger M.;
RT "The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the
RT yeast DNA repair gene RAD6.";
RL EMBO J. 9:1431-1435(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1883845; DOI=10.1016/0167-4781(91)90039-o;
RA Woffendin C., Chen Z.Y., Staskus K., Retzel E.F., Plagemann P.G.;
RT "Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating
RT enzyme encoded by yeast DNA repair gene RAD6.";
RL Biochim. Biophys. Acta 1090:81-85(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=1717990; DOI=10.1073/pnas.88.20.8865;
RA Koken M.H.M., Reynolds P., Jaspers-Dekker I., Prakash L., Prakash S.,
RA Bootsma D., Hoeijmakers J.H.J.;
RT "Structural and functional conservation of two human homologs of the yeast
RT DNA repair gene RAD6.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8865-8869(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Brain;
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 [10]
RP INTERACTION WITH RAD18.
RX PubMed=10908344; DOI=10.1093/nar/28.14.2847;
RA Xin H., Lin W., Sumanasekera W., Zhang Y., Wu X., Wang Z.;
RT "The human RAD18 gene product interacts with HHR6A and HHR6B.";
RL Nucleic Acids Res. 28:2847-2854(2000).
RN [11]
RP FUNCTION.
RX PubMed=16337599; DOI=10.1016/j.molcel.2005.11.012;
RA Kim J., Hake S.B., Roeder R.G.;
RT "The human homolog of yeast BRE1 functions as a transcriptional coactivator
RT through direct activator interactions.";
RL Mol. Cell 20:759-770(2005).
RN [12]
RP FUNCTION.
RX PubMed=17130289; DOI=10.1083/jcb.200606145;
RA Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.;
RT "Human SHPRH suppresses genomic instability through proliferating cell
RT nuclear antigen polyubiquitination.";
RL J. Cell Biol. 175:703-708(2006).
RN [13]
RP FUNCTION.
RX PubMed=17108083; DOI=10.1073/pnas.0608595103;
RA Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V.,
RA Hurwitz J., Prakash L., Prakash S., Haracska L.;
RT "Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
RT polyubiquitylation of proliferating cell nuclear antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20061386; DOI=10.1074/jbc.m109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [15]
RP INTERACTION WITH WAC.
RX PubMed=21329877; DOI=10.1016/j.molcel.2011.01.024;
RA Zhang F., Yu X.;
RT "WAC, a functional partner of RNF20/40, regulates histone H2B
RT ubiquitination and gene transcription.";
RL Mol. Cell 41:384-397(2011).
RN [16]
RP STRUCTURE BY NMR.
RX PubMed=11885984; DOI=10.1023/a:1013807519703;
RA Miura T., Klaus W., Ross A., Guntert P., Senn H.;
RT "The NMR structure of the class I human ubiquitin-conjugating enzyme 2b.";
RL J. Biomol. NMR 22:89-92(2002).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In association with the E3
CC enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription
CC regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-
CC 120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic
CC transcriptional activation, elongation by RNA polymerase II, telomeric
CC silencing, and is also a prerequisite for H3K4me and H3K79me formation.
CC In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked
CC polyubiquitination. Required for postreplication repair of UV-damaged
CC DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18
CC ubiquitin ligase complex involved in mono-ubiquitination of DNA-
CC associated PCNA on 'Lys-164'. May be involved in neurite outgrowth.
CC {ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:17108083,
CC ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:1717990,
CC ECO:0000269|PubMed:20061386}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133, ECO:0000269|PubMed:20061386};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with RAD18, UBR2 and WAC.
CC {ECO:0000269|PubMed:10908344, ECO:0000269|PubMed:21329877}.
CC -!- INTERACTION:
CC P63146; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-712629, EBI-742054;
CC P63146; Q7L7L0: H2AW; NbExp=2; IntAct=EBI-712629, EBI-5325551;
CC P63146; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-712629, EBI-2868124;
CC P63146; Q9NS91: RAD18; NbExp=6; IntAct=EBI-712629, EBI-2339393;
CC P63146; Q8IWV7: UBR1; NbExp=2; IntAct=EBI-712629, EBI-711736;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63149}.
CC Nucleus {ECO:0000250|UniProtKB:P63149}. Note=In peripheral neurons,
CC expressed both at the plasma membrane and in nuclei.
CC {ECO:0000250|UniProtKB:P63149}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ube2b/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M74525; AAA35982.1; -; mRNA.
DR EMBL; X53251; CAA37339.1; -; mRNA.
DR EMBL; BT007071; AAP35734.1; -; mRNA.
DR EMBL; CR407634; CAG28562.1; -; mRNA.
DR EMBL; DQ090910; AAY68224.1; -; Genomic_DNA.
DR EMBL; AK312012; BAG34950.1; -; mRNA.
DR EMBL; CH471062; EAW62257.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62258.1; -; Genomic_DNA.
DR EMBL; BC005979; AAH05979.1; -; mRNA.
DR EMBL; BC008404; AAH08404.1; -; mRNA.
DR EMBL; BC008470; AAH08470.1; -; mRNA.
DR CCDS; CCDS4174.1; -.
DR PIR; B41222; B41222.
DR RefSeq; NP_003328.1; NM_003337.3.
DR PDB; 1JAS; NMR; -; A=1-152.
DR PDB; 2Y4W; NMR; -; A=1-152.
DR PDB; 2YB6; X-ray; 1.50 A; A=1-152.
DR PDB; 2YBF; X-ray; 2.00 A; A=1-152.
DR PDBsum; 1JAS; -.
DR PDBsum; 2Y4W; -.
DR PDBsum; 2YB6; -.
DR PDBsum; 2YBF; -.
DR AlphaFoldDB; P63146; -.
DR BMRB; P63146; -.
DR SMR; P63146; -.
DR BioGRID; 113168; 86.
DR DIP; DIP-29832N; -.
DR IntAct; P63146; 24.
DR MINT; P63146; -.
DR STRING; 9606.ENSP00000265339; -.
DR BindingDB; P63146; -.
DR ChEMBL; CHEMBL3784907; -.
DR iPTMnet; P63146; -.
DR PhosphoSitePlus; P63146; -.
DR BioMuta; UBE2B; -.
DR DMDM; 52783814; -.
DR EPD; P63146; -.
DR jPOST; P63146; -.
DR MassIVE; P63146; -.
DR MaxQB; P63146; -.
DR PaxDb; P63146; -.
DR PeptideAtlas; P63146; -.
DR PRIDE; P63146; -.
DR ProteomicsDB; 57496; -.
DR TopDownProteomics; P63146; -.
DR Antibodypedia; 26297; 272 antibodies from 33 providers.
DR DNASU; 7320; -.
DR Ensembl; ENST00000265339.7; ENSP00000265339.2; ENSG00000119048.8.
DR GeneID; 7320; -.
DR KEGG; hsa:7320; -.
DR MANE-Select; ENST00000265339.7; ENSP00000265339.2; NM_003337.4; NP_003328.1.
DR UCSC; uc003kzh.4; human.
DR CTD; 7320; -.
DR DisGeNET; 7320; -.
DR GeneCards; UBE2B; -.
DR HGNC; HGNC:12473; UBE2B.
DR HPA; ENSG00000119048; Tissue enhanced (skeletal).
DR MIM; 179095; gene.
DR neXtProt; NX_P63146; -.
DR OpenTargets; ENSG00000119048; -.
DR PharmGKB; PA37123; -.
DR VEuPathDB; HostDB:ENSG00000119048; -.
DR eggNOG; KOG0419; Eukaryota.
DR GeneTree; ENSGT00940000156580; -.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P63146; -.
DR OMA; EDTIWEC; -.
DR OrthoDB; 1292821at2759; -.
DR PhylomeDB; P63146; -.
DR TreeFam; TF101128; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; P63146; -.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P63146; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7320; 9 hits in 1084 CRISPR screens.
DR ChiTaRS; UBE2B; human.
DR EvolutionaryTrace; P63146; -.
DR GeneWiki; UBE2B; -.
DR GenomeRNAi; 7320; -.
DR Pharos; P63146; Tchem.
DR PRO; PR:P63146; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P63146; protein.
DR Bgee; ENSG00000119048; Expressed in hindlimb stylopod muscle and 202 other tissues.
DR ExpressionAtlas; P63146; baseline and differential.
DR Genevisible; P63146; HS.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0033503; C:HULC complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005657; C:replication fork; IDA:UniProtKB.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0051026; P:chiasma assembly; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IGI:UniProtKB.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0033522; P:histone H2A ubiquitination; IMP:UniProtKB.
DR GO; GO:0070076; P:histone lysine demethylation; IEA:Ensembl.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0045141; P:meiotic telomere clustering; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; IEA:Ensembl.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IEA:Ensembl.
DR GO; GO:0006301; P:postreplication repair; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IGI:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0007288; P:sperm axoneme assembly; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; TAS:UniProtKB.
DR GO; GO:0070193; P:synaptonemal complex organization; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR IDEAL; IID00558; -.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Direct protein sequencing;
KW DNA damage; DNA repair; Membrane; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..152
FT /note="Ubiquitin-conjugating enzyme E2 B"
FT /id="PRO_0000082447"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 22..23
FT /note="VG -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="F -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="K -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:2YB6"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2YB6"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:2YB6"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:2YB6"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:2YB6"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2YB6"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2YB6"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2YBF"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2YB6"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2YB6"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:2YB6"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:2YB6"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:2YB6"
SQ SEQUENCE 152 AA; 17312 MW; CFDEEEE7E06840BE CRC64;
MSTPARRRLM RDFKRLQEDP PVGVSGAPSE NNIMQWNAVI FGPEGTPFED GTFKLVIEFS
EEYPNKPPTV RFLSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS
PANSQAAQLY QENKREYEKR VSAIVEQSWN DS
