PSMD7_HUMAN
ID PSMD7_HUMAN Reviewed; 324 AA.
AC P51665; D3DWS9; Q6PKI2; Q96E97;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 7;
DE AltName: Full=26S proteasome regulatory subunit RPN8;
DE AltName: Full=26S proteasome regulatory subunit S12;
DE AltName: Full=Mov34 protein homolog;
DE AltName: Full=Proteasome subunit p40;
GN Name=PSMD7; Synonyms=MOV34L;
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].
RX PubMed=7755639; DOI=10.1006/bbrc.1995.1701;
RA Tsurumi C., DeMartino G.N., Slaughter C., Shimbara N., Tanaka K.;
RT "cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and
RT a homolog of the Mov-34 gene product.";
RL Biochem. Biophys. Res. Commun. 210:600-608(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [4]
RP FUNCTION.
RX PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
RA Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T.,
RA Tanaka K., Ichihara A.;
RT "Demonstration that a human 26S proteolytic complex consists of a
RT proteasome and multiple associated protein components and hydrolyzes ATP
RT and ubiquitin-ligated proteins by closely linked mechanisms.";
RL Eur. J. Biochem. 206:567-578(1992).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
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 [8]
RP INTERACTION WITH TRIM5.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in complex
RT with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [9]
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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-186, AND LACK OF METAL-BINDING.
RX PubMed=17559875; DOI=10.1016/j.jmb.2007.04.084;
RA Sanches M., Alves B.S.C., Zanchin N.I.T., Guimaraes B.G.;
RT "The crystal structure of the human Mov34 MPN domain reveals a metal-free
RT dimer.";
RL J. Mol. Biol. 370:846-855(2007).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-389, AND SUBUNIT.
RX PubMed=27428775; DOI=10.1038/nsmb.3273;
RA Huang X., Luan B., Wu J., Shi Y.;
RT "An atomic structure of the human 26S proteasome.";
RL Nat. Struct. Mol. Biol. 23:778-785(2016).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) OF 1-389, AND SUBUNIT.
RX PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. {ECO:0000269|PubMed:1317798}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits including PSMD7, a base containing 6 ATPases and
CC few additional components (PubMed:27428775, PubMed:27342858). Within
CC the complex, PSMD7 interacts with subunit PSMD4 through their
CC respective MPN domain. Interacts with TRIM5 (PubMed:22078707).
CC {ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:27342858,
CC ECO:0000269|PubMed:27428775}.
CC -!- INTERACTION:
CC P51665; P54252: ATXN3; NbExp=9; IntAct=EBI-357659, EBI-946046;
CC P51665; P42858: HTT; NbExp=10; IntAct=EBI-357659, EBI-466029;
CC P51665; O00487: PSMD14; NbExp=14; IntAct=EBI-357659, EBI-722193;
CC -!- MISCELLANEOUS: Does not bind a metal ion.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00338.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; D50063; BAA08780.1; -; mRNA.
DR EMBL; CH471166; EAW59162.1; -; Genomic_DNA.
DR EMBL; CH471166; EAW59163.1; -; Genomic_DNA.
DR EMBL; BC000338; AAH00338.1; ALT_SEQ; mRNA.
DR EMBL; BC012606; AAH12606.1; -; mRNA.
DR CCDS; CCDS10910.1; -.
DR PIR; JC4154; JC4154.
DR PIR; S65491; S65491.
DR RefSeq; NP_002802.2; NM_002811.4.
DR PDB; 2O95; X-ray; 1.95 A; A/B=1-186.
DR PDB; 2O96; X-ray; 3.00 A; A/B=1-177.
DR PDB; 5GJQ; EM; 4.50 A; U=1-324.
DR PDB; 5GJR; EM; 3.50 A; 8/U=1-324.
DR PDB; 5L4K; EM; 4.50 A; U=1-324.
DR PDB; 5LN3; EM; 6.80 A; U=1-324.
DR PDB; 5M32; EM; 3.80 A; n=1-324.
DR PDB; 5T0C; EM; 3.80 A; AZ/BZ=1-324.
DR PDB; 5T0G; EM; 4.40 A; Z=1-324.
DR PDB; 5T0H; EM; 6.80 A; Z=1-324.
DR PDB; 5T0I; EM; 8.00 A; Z=1-324.
DR PDB; 5T0J; EM; 8.00 A; Z=1-324.
DR PDB; 5VFP; EM; 4.20 A; Z=5-290.
DR PDB; 5VFQ; EM; 4.20 A; Z=5-290.
DR PDB; 5VFR; EM; 4.90 A; Z=5-290.
DR PDB; 5VFS; EM; 3.60 A; Z=5-290.
DR PDB; 5VFT; EM; 7.00 A; Z=5-290.
DR PDB; 5VFU; EM; 5.80 A; Z=5-290.
DR PDB; 5VGZ; EM; 3.70 A; Z=5-290.
DR PDB; 5VHF; EM; 5.70 A; Z=5-290.
DR PDB; 5VHH; EM; 6.10 A; Z=5-290.
DR PDB; 5VHI; EM; 6.80 A; Z=5-290.
DR PDB; 5VHS; EM; 8.80 A; Z=5-290.
DR PDB; 6MSB; EM; 3.00 A; Z=1-324.
DR PDB; 6MSD; EM; 3.20 A; Z=1-324.
DR PDB; 6MSG; EM; 3.50 A; Z=1-324.
DR PDB; 6MSH; EM; 3.60 A; Z=1-324.
DR PDB; 6MSJ; EM; 3.30 A; Z=1-324.
DR PDB; 6MSK; EM; 3.20 A; Z=1-324.
DR PDB; 6WJD; EM; 4.80 A; Z=1-324.
DR PDB; 6WJN; EM; 5.70 A; Z=5-290.
DR PDBsum; 2O95; -.
DR PDBsum; 2O96; -.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4K; -.
DR PDBsum; 5LN3; -.
DR PDBsum; 5M32; -.
DR PDBsum; 5T0C; -.
DR PDBsum; 5T0G; -.
DR PDBsum; 5T0H; -.
DR PDBsum; 5T0I; -.
DR PDBsum; 5T0J; -.
DR PDBsum; 5VFP; -.
DR PDBsum; 5VFQ; -.
DR PDBsum; 5VFR; -.
DR PDBsum; 5VFS; -.
DR PDBsum; 5VFT; -.
DR PDBsum; 5VFU; -.
DR PDBsum; 5VGZ; -.
DR PDBsum; 5VHF; -.
DR PDBsum; 5VHH; -.
DR PDBsum; 5VHI; -.
DR PDBsum; 5VHS; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR AlphaFoldDB; P51665; -.
DR SMR; P51665; -.
DR BioGRID; 111685; 181.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P51665; -.
DR DIP; DIP-27572N; -.
DR IntAct; P51665; 99.
DR MINT; P51665; -.
DR STRING; 9606.ENSP00000219313; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; M67.973; -.
DR GlyGen; P51665; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51665; -.
DR MetOSite; P51665; -.
DR PhosphoSitePlus; P51665; -.
DR BioMuta; PSMD7; -.
DR DMDM; 20532412; -.
DR EPD; P51665; -.
DR jPOST; P51665; -.
DR MassIVE; P51665; -.
DR MaxQB; P51665; -.
DR PaxDb; P51665; -.
DR PeptideAtlas; P51665; -.
DR PRIDE; P51665; -.
DR ProteomicsDB; 56361; -.
DR Antibodypedia; 30221; 331 antibodies from 32 providers.
DR DNASU; 5713; -.
DR Ensembl; ENST00000219313.9; ENSP00000219313.4; ENSG00000103035.11.
DR GeneID; 5713; -.
DR KEGG; hsa:5713; -.
DR MANE-Select; ENST00000219313.9; ENSP00000219313.4; NM_002811.5; NP_002802.2.
DR UCSC; uc002fcq.3; human.
DR CTD; 5713; -.
DR DisGeNET; 5713; -.
DR GeneCards; PSMD7; -.
DR HGNC; HGNC:9565; PSMD7.
DR HPA; ENSG00000103035; Low tissue specificity.
DR MIM; 157970; gene.
DR neXtProt; NX_P51665; -.
DR OpenTargets; ENSG00000103035; -.
DR PharmGKB; PA33911; -.
DR VEuPathDB; HostDB:ENSG00000103035; -.
DR eggNOG; KOG1556; Eukaryota.
DR GeneTree; ENSGT00950000183073; -.
DR HOGENOM; CLU_027018_3_0_1; -.
DR InParanoid; P51665; -.
DR OMA; HAMSIKT; -.
DR OrthoDB; 1275837at2759; -.
DR PhylomeDB; P51665; -.
DR PathwayCommons; P51665; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P51665; -.
DR SIGNOR; P51665; -.
DR BioGRID-ORCS; 5713; 706 hits in 1099 CRISPR screens.
DR ChiTaRS; PSMD7; human.
DR EvolutionaryTrace; P51665; -.
DR GeneWiki; PSMD7; -.
DR GenomeRNAi; 5713; -.
DR Pharos; P51665; Tbio.
DR PRO; PR:P51665; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P51665; protein.
DR Bgee; ENSG00000103035; Expressed in gastrocnemius and 203 other tissues.
DR ExpressionAtlas; P51665; baseline and differential.
DR Genevisible; P51665; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd08062; MPN_RPN7_8; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033858; MPN_RPN7_8.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Proteasome; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..324
FT /note="26S proteasome non-ATPase regulatory subunit 7"
FT /id="PRO_0000213943"
FT DOMAIN 9..144
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 281..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 316
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26516"
FT MOD_RES 317
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26516"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CONFLICT 27
FT /note="G -> V (in Ref. 1; BAA08780)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..145
FT /note="VH -> DQ (in Ref. 1; BAA08780)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="A -> G (in Ref. 1; BAA08780)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2O95"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:2O95"
FT STRAND 36..56
FT /evidence="ECO:0007829|PDB:2O95"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2O95"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2O95"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:2O95"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2O95"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2O95"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:2O95"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2O95"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2O95"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:2O95"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:2O95"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:2O95"
SQ SEQUENCE 324 AA; 37025 MW; 3F7B343996B102B7 CRC64;
MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV SNSFAVPFDE
DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK LHKNDIAINE LMKRYCPNSV
LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK
DTTVGTLSQR ITNQVHGLKG LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV
SLQEFVKAFY LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR
KEDKEKDKDK EKSDVKKEEK KEKK
