ID   QCR7_HUMAN              Reviewed;         111 AA.
AC   P14927; E5RJU0; Q6FGD1;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 224.
DE   RecName: Full=Cytochrome b-c1 complex subunit 7;
DE   AltName: Full=Complex III subunit 7;
DE   AltName: Full=Complex III subunit VII;
DE   AltName: Full=QP-C;
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex 14 kDa protein;
GN   Name=UQCRB; Synonyms=UQBP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fibroblast;
RX   PubMed=3056408; DOI=10.1016/s0006-291x(88)80941-0;
RA   Suzuki H., Yoshitaka H., Toda H., Nishikimi M., Ozawa T.;
RT   "Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-
RT   binding protein of complex III.";
RL   Biochem. Biophys. Res. Commun. 156:987-994(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=2543413; DOI=10.1016/0006-291x(89)91607-0;
RA   Suzuki H., Hosokawa Y., Toda H., Nishikimi M., Ozawa T.;
RT   "Isolation of a single nuclear gene encoding human ubiquinone-binding
RT   protein in complex III of mitochondrial respiratory chain.";
RL   Biochem. Biophys. Res. Commun. 161:371-378(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Urinary bladder;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX   PubMed=2159470; DOI=10.1016/s0021-9258(19)39051-9;
RA   Suzuki H., Hosokawa Y., Toda H., Nishikimi M., Ozawa T.;
RT   "Common protein-binding sites in the 5'-flanking regions of human genes for
RT   cytochrome c1 and ubiquinone-binding protein.";
RL   J. Biol. Chem. 265:8159-8163(1990).
RN   [8]
RP   INVOLVEMENT IN MC3DN3.
RX   PubMed=12709789; DOI=10.1007/s00439-003-0946-0;
RA   Haut S., Brivet M., Touati G., Rustin P., Lebon S., Garcia-Cazorla A.,
RA   Saudubray J.-M., Boutron A., Legrand A., Slama A.;
RT   "A deletion in the human QP-C gene causes a complex III deficiency
RT   resulting in hypoglycaemia and lactic acidosis.";
RL   Hum. Genet. 113:118-122(2003).
RN   [9]
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   [10]
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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [12]
RP   STRUCTURE BY ELECTRON MICROSCOPY.
RX   PubMed=28844695; DOI=10.1016/j.cell.2017.07.050;
RA   Guo R., Zong S., Wu M., Gu J., Yang M.;
RT   "Architecture of human mitochondrial respiratory megacomplex I2III2IV2.";
RL   Cell 170:1247-1257(2017).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC       multisubunit transmembrane complex that is part of the mitochondrial
CC       electron transport chain which drives oxidative phosphorylation. The
CC       respiratory chain contains 3 multisubunit complexes succinate
CC       dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC       (complex IV, CIV), that cooperate to transfer electrons derived from
CC       NADH and succinate to molecular oxygen, creating an electrochemical
CC       gradient over the inner membrane that drives transmembrane transport
CC       and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC       transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC       translocation of protons across the mitochondrial inner membrane, with
CC       protons being carried across the membrane as hydrogens on the quinol.
CC       In the process called Q cycle, 2 protons are consumed from the matrix,
CC       4 protons are released into the intermembrane space and 2 electrons are
CC       passed to cytochrome c. {ECO:0000250|UniProtKB:P00128}.
CC   -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC       composed of 11 subunits. The complex is composed of 3 respiratory
CC       subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC       protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC       weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC       UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC       protein UQCRFS1 (By similarity). The complex exists as an obligatory
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC       cytochrome c oxidase (complex IV, CIV), resulting in different
CC       assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC       MCI(2)III(2)IV(2)) (PubMed:28844695). {ECO:0000250|UniProtKB:P00129,
CC       ECO:0000269|PubMed:28844695}.
CC   -!- INTERACTION:
CC       P14927; Q15027: ACAP1; NbExp=3; IntAct=EBI-743128, EBI-751746;
CC       P14927; Q96QU6: ACCS; NbExp=3; IntAct=EBI-743128, EBI-743387;
CC       P14927; Q14457: BECN1; NbExp=3; IntAct=EBI-743128, EBI-949378;
CC       P14927; P08574: CYC1; NbExp=3; IntAct=EBI-743128, EBI-1224514;
CC       P14927; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-743128, EBI-21529239;
CC       P14927; P06241-3: FYN; NbExp=3; IntAct=EBI-743128, EBI-10691738;
CC       P14927; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-743128, EBI-2857315;
CC       P14927; P84074: HPCA; NbExp=3; IntAct=EBI-743128, EBI-12197079;
CC       P14927; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-743128, EBI-712105;
CC       P14927; A1A512: KIAA0355; NbExp=3; IntAct=EBI-743128, EBI-25844799;
CC       P14927; Q15012: LAPTM4A; NbExp=3; IntAct=EBI-743128, EBI-723416;
CC       P14927; Q92615: LARP4B; NbExp=3; IntAct=EBI-743128, EBI-1052558;
CC       P14927; P43358: MAGEA4; NbExp=8; IntAct=EBI-743128, EBI-743122;
CC       P14927; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-743128, EBI-10194128;
CC       P14927; O15481: MAGEB4; NbExp=3; IntAct=EBI-743128, EBI-751857;
CC       P14927; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-743128, EBI-17438286;
CC       P14927; Q19AV6: ZSWIM7; NbExp=3; IntAct=EBI-743128, EBI-5281647;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00128}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00128}; Matrix side
CC       {ECO:0000250|UniProtKB:P00128}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P14927-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P14927-2; Sequence=VSP_045601;
CC   -!- DISEASE: Mitochondrial complex III deficiency, nuclear type 3 (MC3DN3)
CC       [MIM:615158]: A disorder of the mitochondrial respiratory chain
CC       resulting in a highly variable phenotype depending on which tissues are
CC       affected. Clinical features include mitochondrial encephalopathy,
CC       psychomotor retardation, ataxia, severe failure to thrive, liver
CC       dysfunction, renal tubulopathy, muscle weakness and exercise
CC       intolerance. {ECO:0000269|PubMed:12709789}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the UQCRB/QCR7 family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be the ubiquinone-binding protein
CC       (QP-C). {ECO:0000305}.
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DR   EMBL; X13585; CAA31926.1; -; mRNA.
DR   EMBL; M22348; AAA60238.1; -; mRNA.
DR   EMBL; CR542176; CAG46973.1; -; mRNA.
DR   EMBL; CR542196; CAG46993.1; -; mRNA.
DR   EMBL; M26730; AAA60235.1; -; Genomic_DNA.
DR   EMBL; M35761; AAA60235.1; JOINED; Genomic_DNA.
DR   EMBL; M26706; AAA60235.1; JOINED; Genomic_DNA.
DR   EMBL; M26707; AAA60235.1; JOINED; Genomic_DNA.
DR   EMBL; M26700; AAA60236.1; -; mRNA.
DR   EMBL; M26701; AAA60237.1; -; Genomic_DNA.
DR   EMBL; AP003465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471060; EAW91749.1; -; Genomic_DNA.
DR   EMBL; BC005230; AAH05230.1; -; mRNA.
DR   EMBL; BU535281; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M37387; AAA60361.1; ALT_SEQ; Genomic_DNA.
DR   CCDS; CCDS59107.1; -. [P14927-2]
DR   CCDS; CCDS6269.1; -. [P14927-1]
DR   PIR; A32450; A32450.
DR   RefSeq; NP_001186904.1; NM_001199975.3.
DR   RefSeq; NP_001241681.1; NM_001254752.2. [P14927-2]
DR   RefSeq; NP_006285.1; NM_006294.5. [P14927-1]
DR   PDB; 5XTE; EM; 3.40 A; F/S=6-111.
DR   PDB; 5XTH; EM; 3.90 A; AF/AS=6-111.
DR   PDB; 5XTI; EM; 17.40 A; AF/AS=6-111.
DR   PDB; 9CG3; EM; 2.96 A; F/S=1-111.
DR   PDB; 9HZL; EM; 2.52 A; F/S=1-111.
DR   AlphaFoldDB; P14927; -.
DR   EMDB; EMD-45567; -.
DR   EMDB; EMD-52525; -.
DR   SMR; P14927; -.
DR   BioGRID; 113227; 149.
DR   ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR   FunCoup; P14927; 725.
DR   IntAct; P14927; 80.
DR   NDEx; IQUERY-CP-UQCRB; 3 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000430494; -.
DR   BindingDB; P14927; -.
DR   ChEMBL; CHEMBL1671612; -.
DR   DrugBank; DB07763; (5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE.
DR   DrugBank; DB07778; (S)-famoxadone.
DR   DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR   DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR   DrugBank; DB07636; 5-Heptyl-6-hydroxy-1,3-benzothiazole-4,7-dione.
DR   DrugBank; DB04799; 6-Hydroxy-5-undecyl-4,7-benzothiazoledione.
DR   DrugBank; DB07401; Azoxystrobin.
DR   DrugBank; DB08330; METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DR   DrugBank; DB08690; Ubiquinone Q2.
DR   CarbonylDB; P14927; -.
DR   GlyGen; P14927; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P14927; -.
DR   PhosphoSitePlus; P14927; -.
DR   SwissPalm; P14927; -.
DR   BioMuta; UQCRB; -.
DR   DMDM; 136717; -.
DR   jPOST; P14927; -.
DR   MassIVE; P14927; -.
DR   PaxDb; 9606-ENSP00000430494; -.
DR   PeptideAtlas; P14927; -.
DR   ProteomicsDB; 16706; -.
DR   ProteomicsDB; 53099; -. [P14927-1]
DR   Pumba; P14927; -.
DR   TopDownProteomics; P14927-1; -. [P14927-1]
DR   Antibodypedia; 42750; 192 antibodies from 32 providers.
DR   DNASU; 7381; -.
DR   Ensembl; ENST00000287022.10; ENSP00000287022.5; ENSG00000156467.11. [P14927-1]
DR   Ensembl; ENST00000518406.5; ENSP00000430494.1; ENSG00000156467.11. [P14927-2]
DR   GeneID; 7381; -.
DR   KEGG; hsa:7381; -.
DR   MANE-Select; ENST00000287022.10; ENSP00000287022.5; NM_006294.5; NP_006285.1.
DR   UCSC; uc003yhq.5; human. [P14927-1]
DR   AGR; HGNC:12582; -.
DR   ClinPGx; PA37213; -.
DR   CTD; 7381; -.
DR   DisGeNET; 7381; -.
DR   GeneCards; UQCRB; -.
DR   HGNC; HGNC:12582; UQCRB.
DR   HPA; ENSG00000156467; Tissue enhanced (skeletal).
DR   MalaCards; UQCRB; -.
DR   MIM; 191330; gene.
DR   MIM; 615158; phenotype.
DR   OpenTargets; ENSG00000156467; -.
DR   Orphanet; 1460; Isolated complex III deficiency.
DR   VEuPathDB; HostDB:ENSG00000156467; -.
DR   eggNOG; KOG3440; Eukaryota.
DR   GeneTree; ENSGT00390000012916; -.
DR   HOGENOM; CLU_115154_2_0_1; -.
DR   InParanoid; P14927; -.
DR   OMA; AANWYAN; -.
DR   OrthoDB; 425749at2759; -.
DR   PAN-GO; P14927; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; P14927; -.
DR   BioCyc; MetaCyc:HS08128-MONOMER; -.
DR   BRENDA; 7.1.1.8; 2681.
DR   PathwayCommons; P14927; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-9865881; Complex III assembly.
DR   SignaLink; P14927; -.
DR   SIGNOR; P14927; -.
DR   Agora; ENSG00000156467; Agora Nominated Target for Alzheimer's Disease.
DR   BioGRID-ORCS; 7381; 324 hits in 1134 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; UQCRB; human.
DR   GeneWiki; UQCRB; -.
DR   GenomeRNAi; 7381; -.
DR   Pharos; P14927; Tbio.
DR   PRO; PR:P14927; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P14927; protein.
DR   Bgee; ENSG00000156467; Expressed in heart right ventricle and 215 other cell types or tissues.
DR   ExpressionAtlas; P14927; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; HTP:FlyBase.
DR   GO; GO:0098803; C:respiratory chain complex; TAS:ProtInc.
DR   GO; GO:0045275; C:respiratory chain complex III; IPI:ComplexPortal.
DR   GO; GO:0009060; P:aerobic respiration; TAS:ProtInc.
DR   GO; GO:0045333; P:cellular respiration; NAS:ComplexPortal.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:0006119; P:oxidative phosphorylation; TAS:ProtInc.
DR   FunFam; 1.10.1090.10:FF:000001; Cytochrome b-c1 complex subunit 7; 1.
DR   Gene3D; 1.10.1090.10; Cytochrome b-c1 complex subunit 7; 1.
DR   InterPro; IPR003197; QCR7.
DR   InterPro; IPR036544; QCR7_sf.
DR   PANTHER; PTHR12022:SF12; CYTOCHROME B-C1 COMPLEX SUBUNIT 7; 1.
DR   PANTHER; PTHR12022; UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN; 1.
DR   Pfam; PF02271; UCR_14kD; 1.
DR   PIRSF; PIRSF000022; Bc1_14K; 1.
DR   SUPFAM; SSF81524; 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Electron transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Primary mitochondrial disease; Proteomics identification;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00129"
FT   CHAIN           2..111
FT                   /note="Cytochrome b-c1 complex subunit 7"
FT                   /id="PRO_0000193524"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P00129"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         12
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         78
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         78
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         83
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         96
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   VAR_SEQ         87..111
FT                   /note="ENFYLEPYLKEVIRERKEREEWAKK -> VFAVPALHSASYLDEKISPLSVP
FT                   PDPKKSFCEANSHPLNCIETRQRKISTLNRI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045601"
FT   VARIANT         30
FT                   /note="L -> P (in dbSNP:rs35895613)"
FT                   /id="VAR_052443"
FT   CONFLICT        6
FT                   /note="A -> G (in Ref. 2; AAA60236)"
FT                   /evidence="ECO:0000305"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:9HZL"
FT   HELIX           11..24
FT                   /evidence="ECO:0007829|PDB:9HZL"
FT   HELIX           26..30
FT                   /evidence="ECO:0007829|PDB:9HZL"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:9HZL"
FT   HELIX           42..50
FT                   /evidence="ECO:0007829|PDB:9HZL"
FT   HELIX           53..72
FT                   /evidence="ECO:0007829|PDB:9HZL"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:9HZL"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:9HZL"
FT   HELIX           92..109
FT                   /evidence="ECO:0007829|PDB:9HZL"
SQ   SEQUENCE   111 AA;  13530 MW;  E61629D06DFA55B7 CRC64;
     MAGKQAVSAS GKWLDGIRKW YYNAAGFNKL GLMRDDTIYE DEDVKEAIRR LPENLYNDRM
     FRIKRALDLN LKHQILPKEQ WTKYEEENFY LEPYLKEVIR ERKEREEWAK K
//