CISD1_HUMAN
ID CISD1_HUMAN Reviewed; 108 AA.
AC Q9NZ45; Q1X902;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein 1;
DE AltName: Full=MitoNEET;
GN Name=CISD1; Synonyms=C10orf70, ZCD1; ORFNames=MDS029;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=18047834; DOI=10.1016/j.bbrc.2007.11.076;
RA Taminelli G.L., Sotomayor V., Valdivieso A.G., Teiber M.L., Marin M.C.,
RA Santa-Coloma T.A.;
RT "CISD1 codifies a mitochondrial protein upregulated by the CFTR channel.";
RL Biochem. Biophys. Res. Commun. 365:856-862(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hematopoietic stem cell;
RA Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Brain, and Lung;
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 [6]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF CYS-72; CYS-74; CYS-83; ASP-84 AND
RP HIS-87.
RX PubMed=17584744; DOI=10.1074/jbc.c700107200;
RA Wiley S.E., Paddock M.L., Abresch E.C., Gross L., van der Geer P.,
RA Nechushtai R., Murphy A.N., Jennings P.A., Dixon J.E.;
RT "The outer mitochondrial membrane protein mitoNEET contains a novel redox-
RT active 2Fe-2S cluster.";
RL J. Biol. Chem. 282:23745-23749(2007).
RN [7]
RP SUBCELLULAR LOCATION, AND COFACTOR.
RX PubMed=17376863; DOI=10.1073/pnas.0701078104;
RA Wiley S.E., Murphy A.N., Ross S.A., van der Geer P., Dixon J.E.;
RT "MitoNEET is an iron-containing outer mitochondrial membrane protein that
RT regulates oxidative capacity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5318-5323(2007).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19580816; DOI=10.1016/j.jmb.2009.06.079;
RA Conlan A.R., Axelrod H.L., Cohen A.E., Abresch E.C., Zuris J., Yee D.,
RA Nechushtai R., Jennings P.A., Paddock M.L.;
RT "Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in
RT Wolfram Syndrome 2.";
RL J. Mol. Biol. 392:143-153(2009).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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 [12]
RP UBIQUITINATION AT LYS-42; LYS-55; LYS-68; LYS-78; LYS-79; LYS-89; LYS-104;
RP LYS-105 AND LYS-106.
RX PubMed=25621951; DOI=10.1038/ncb3097;
RA Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
RA Kirkpatrick D.S., Bingol B., Corn J.E.;
RT "USP30 and parkin homeostatically regulate atypical ubiquitin chains on
RT mitochondria.";
RL Nat. Cell Biol. 17:160-169(2015).
RN [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 33-108, COFACTOR, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17905743; DOI=10.1074/jbc.c700172200;
RA Hou X., Liu R., Ross S., Smart E.J., Zhu H., Gong W.;
RT "Crystallographic studies of human MitoNEET.";
RL J. Biol. Chem. 282:33242-33246(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 33-108, FUNCTION, COFACTOR, AND
RP SUBUNIT.
RX PubMed=17766440; DOI=10.1073/pnas.0707189104;
RA Paddock M.L., Wiley S.E., Axelrod H.L., Cohen A.E., Roy M., Abresch E.C.,
RA Capraro D., Murphy A.N., Nechushtai R., Dixon J.E., Jennings P.A.;
RT "MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein
RT stabilized by pioglitazone.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14342-14347(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 32-108, COFACTOR, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17766439; DOI=10.1073/pnas.0702426104;
RA Lin J., Zhou T., Ye K., Wang J.;
RT "Crystal structure of human mitoNEET reveals distinct groups of iron sulfur
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14640-14645(2007).
CC -!- FUNCTION: Plays a key role in regulating maximal capacity for electron
CC transport and oxidative phosphorylation (By similarity). May be
CC involved in Fe-S cluster shuttling and/or in redox reactions.
CC {ECO:0000250, ECO:0000269|PubMed:17584744,
CC ECO:0000269|PubMed:17766440}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:17376863, ECO:0000269|PubMed:17584744,
CC ECO:0000269|PubMed:17766439, ECO:0000269|PubMed:17766440,
CC ECO:0000269|PubMed:17905743};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is
CC redox-active and pH labile and is significantly less stable at pH 4.5
CC as compared with pH 7.0. {ECO:0000269|PubMed:17376863,
CC ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:17766439,
CC ECO:0000269|PubMed:17766440, ECO:0000269|PubMed:17905743};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E is 0 +/- 10 mV for 2Fe-2S at pH 7.5. {ECO:0000269|PubMed:19580816};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17766439,
CC ECO:0000269|PubMed:17766440, ECO:0000269|PubMed:17905743}.
CC -!- INTERACTION:
CC Q9NZ45; Q9NZ45: CISD1; NbExp=4; IntAct=EBI-1050885, EBI-1050885;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:17376863, ECO:0000269|PubMed:17766439,
CC ECO:0000269|PubMed:17905743, ECO:0000269|PubMed:18047834}; Single-pass
CC type III membrane protein {ECO:0000269|PubMed:17376863,
CC ECO:0000269|PubMed:17766439, ECO:0000269|PubMed:17905743,
CC ECO:0000269|PubMed:18047834}.
CC -!- TISSUE SPECIFICITY: Expression is reduced in cells derived from cystic
CC fibrosis patients. {ECO:0000269|PubMed:18047834}.
CC -!- INDUCTION: Expression is down-regulated by glibenclamide and 5-[(4-
CC carboxyphenyl)methylene]-2-thioxo-3-(3-trifluoromethyl)phenyl-4-
CC thiazolidinone (CFTR(inh)172), and up-regulated by
CC cAMP/isoproterenol/IBMX, components that inhibit and stimulate chloride
CC transport activity respectively. {ECO:0000269|PubMed:18047834}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000269|PubMed:25621951}.
CC -!- MISCELLANEOUS: Binds pioglitazone, an anti-diabetes drug. Binding
CC increases the stability of the 2Fe-2S cluster.
CC -!- SIMILARITY: Belongs to the CISD protein family. {ECO:0000305}.
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DR EMBL; AY960578; AAY32336.1; -; mRNA.
DR EMBL; AF220049; AAF67642.1; -; mRNA.
DR EMBL; AK312017; BAG34955.1; -; mRNA.
DR EMBL; CH471083; EAW54163.1; -; Genomic_DNA.
DR EMBL; BC005962; AAH05962.1; -; mRNA.
DR EMBL; BC007043; AAH07043.1; -; mRNA.
DR EMBL; BC008474; AAH08474.1; -; mRNA.
DR EMBL; BC059168; AAH59168.1; -; mRNA.
DR CCDS; CCDS7251.1; -.
DR RefSeq; NP_060934.1; NM_018464.4.
DR PDB; 2QD0; X-ray; 1.81 A; A/B=32-108.
DR PDB; 2QH7; X-ray; 1.50 A; A/B=33-108.
DR PDB; 2R13; X-ray; 1.80 A; A=33-108.
DR PDB; 3EW0; X-ray; 1.40 A; A/B=33-108.
DR PDB; 3LPQ; X-ray; 1.70 A; A/B=33-107.
DR PDB; 3REE; X-ray; 1.76 A; A=32-108.
DR PDB; 4EZF; X-ray; 1.19 A; A/B=33-108.
DR PDB; 4F1E; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=33-108.
DR PDB; 4F28; X-ray; 1.55 A; A/B=33-108.
DR PDB; 4F2C; X-ray; 1.35 A; A/B=33-108.
DR PDB; 6DE9; X-ray; 1.95 A; A=32-108.
DR PDBsum; 2QD0; -.
DR PDBsum; 2QH7; -.
DR PDBsum; 2R13; -.
DR PDBsum; 3EW0; -.
DR PDBsum; 3LPQ; -.
DR PDBsum; 3REE; -.
DR PDBsum; 4EZF; -.
DR PDBsum; 4F1E; -.
DR PDBsum; 4F28; -.
DR PDBsum; 4F2C; -.
DR PDBsum; 6DE9; -.
DR AlphaFoldDB; Q9NZ45; -.
DR SMR; Q9NZ45; -.
DR BioGRID; 120949; 96.
DR DIP; DIP-46446N; -.
DR IntAct; Q9NZ45; 17.
DR MINT; Q9NZ45; -.
DR STRING; 9606.ENSP00000363041; -.
DR BindingDB; Q9NZ45; -.
DR ChEMBL; CHEMBL1795168; -.
DR GlyGen; Q9NZ45; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZ45; -.
DR MetOSite; Q9NZ45; -.
DR PhosphoSitePlus; Q9NZ45; -.
DR SwissPalm; Q9NZ45; -.
DR BioMuta; CISD1; -.
DR DMDM; 25453105; -.
DR EPD; Q9NZ45; -.
DR jPOST; Q9NZ45; -.
DR MassIVE; Q9NZ45; -.
DR MaxQB; Q9NZ45; -.
DR PaxDb; Q9NZ45; -.
DR PeptideAtlas; Q9NZ45; -.
DR PRIDE; Q9NZ45; -.
DR ProteomicsDB; 83323; -.
DR TopDownProteomics; Q9NZ45; -.
DR ABCD; Q9NZ45; 2 sequenced antibodies.
DR Antibodypedia; 45107; 256 antibodies from 29 providers.
DR DNASU; 55847; -.
DR Ensembl; ENST00000333926.6; ENSP00000363041.4; ENSG00000122873.12.
DR GeneID; 55847; -.
DR KEGG; hsa:55847; -.
DR MANE-Select; ENST00000333926.6; ENSP00000363041.4; NM_018464.5; NP_060934.1.
DR UCSC; uc001jkc.6; human.
DR CTD; 55847; -.
DR DisGeNET; 55847; -.
DR GeneCards; CISD1; -.
DR HGNC; HGNC:30880; CISD1.
DR HPA; ENSG00000122873; Tissue enhanced (parathyroid).
DR MIM; 611932; gene.
DR neXtProt; NX_Q9NZ45; -.
DR OpenTargets; ENSG00000122873; -.
DR PharmGKB; PA162382289; -.
DR VEuPathDB; HostDB:ENSG00000122873; -.
DR eggNOG; KOG3461; Eukaryota.
DR GeneTree; ENSGT00940000154445; -.
DR HOGENOM; CLU_132293_1_0_1; -.
DR InParanoid; Q9NZ45; -.
DR OMA; VVDMIDI; -.
DR OrthoDB; 1393750at2759; -.
DR PhylomeDB; Q9NZ45; -.
DR TreeFam; TF324661; -.
DR PathwayCommons; Q9NZ45; -.
DR SignaLink; Q9NZ45; -.
DR BioGRID-ORCS; 55847; 21 hits in 1016 CRISPR screens.
DR ChiTaRS; CISD1; human.
DR EvolutionaryTrace; Q9NZ45; -.
DR GenomeRNAi; 55847; -.
DR Pharos; Q9NZ45; Tchem.
DR PRO; PR:Q9NZ45; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NZ45; protein.
DR Bgee; ENSG00000122873; Expressed in pons and 210 other tissues.
DR ExpressionAtlas; Q9NZ45; baseline and differential.
DR Genevisible; Q9NZ45; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR GO; GO:0043457; P:regulation of cellular respiration; IEA:Ensembl.
DR Gene3D; 3.40.5.90; -; 1.
DR InterPro; IPR045131; CISD1/2.
DR InterPro; IPR018967; FeS-contain_CDGSH-typ.
DR InterPro; IPR019610; FeS-contain_mitoNEET_N.
DR InterPro; IPR042216; MitoNEET_CISD.
DR PANTHER; PTHR13680; PTHR13680; 1.
DR Pfam; PF10660; MitoNEET_N; 1.
DR Pfam; PF09360; zf-CDGSH; 1.
DR SMART; SM00704; ZnF_CDGSH; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Acetylation; Iron; Iron-sulfur; Isopeptide bond;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..108
FT /note="CDGSH iron-sulfur domain-containing protein 1"
FT /id="PRO_0000089803"
FT TRANSMEM 14..31
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 72
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 74
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT MOD_RES 104
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 105
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT MUTAGEN 72
FT /note="C->S: Abolishes absorption in the 300-500 nm range."
FT /evidence="ECO:0000269|PubMed:17584744"
FT MUTAGEN 74
FT /note="C->S: Abolishes absorption in the 300-500 nm range."
FT /evidence="ECO:0000269|PubMed:17584744"
FT MUTAGEN 83
FT /note="C->S: Abolishes absorption in the 300-500 nm range."
FT /evidence="ECO:0000269|PubMed:17584744"
FT MUTAGEN 84
FT /note="D->N: Does not affect absorption in the 300-500 nm
FT range."
FT /evidence="ECO:0000269|PubMed:17584744"
FT MUTAGEN 87
FT /note="H->C: Affects absorption in the 300-500 nm range but
FT it is not reduced. Increased stability of the 2Fe-2S
FT cluster at low pH."
FT /evidence="ECO:0000269|PubMed:17584744"
FT MUTAGEN 87
FT /note="H->Q: Abolishes absorption in the 300-500 nm range."
FT /evidence="ECO:0000269|PubMed:17584744"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4EZF"
FT STRAND 53..66
FT /evidence="ECO:0007829|PDB:4EZF"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4EZF"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4EZF"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:4EZF"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:4EZF"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4EZF"
SQ SEQUENCE 108 AA; 12199 MW; 2E47000F0635CBB7 CRC64;
MSLTSSSSVR VEWIAAVTIA AGTAAIGYLA YKRFYVKDHR NKAMINLHIQ KDNPKIVHAF
DMEDLGDKAV YCRCWRSKKF PFCDGAHTKH NEETGDNVGP LIIKKKET
