CYGB_HUMAN
ID CYGB_HUMAN Reviewed; 190 AA.
AC Q8WWM9; Q541Y7; Q8N2X5;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytoglobin;
DE AltName: Full=Histoglobin;
DE Short=HGb;
DE AltName: Full=Stellate cell activation-associated protein;
GN Name=CYGB; Synonyms=STAP;
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].
RC TISSUE=Brain;
RX PubMed=11919282; DOI=10.1093/oxfordjournals.molbev.a004096;
RA Burmester T., Ebner B., Weich B., Hankeln T.;
RT "Cytoglobin: a novel globin type ubiquitously expressed in vertebrate
RT tissues.";
RL Mol. Biol. Evol. 19:416-421(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=12359339; DOI=10.1016/s0167-4781(02)00477-3;
RA Asahina K., Kawada N., Kristensen D.B., Nakatani K., Seki S., Shiokawa M.,
RA Tateno C., Obara M., Yoshizato K.;
RT "Characterization of human stellate cell activation-associated protein and
RT its expression in human liver.";
RL Biochim. Biophys. Acta 1577:471-475(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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=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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=11893755; DOI=10.1074/jbc.m201934200;
RA Trent J.T. III, Hargrove M.S.;
RT "A ubiquitously expressed human hexacoordinate hemoglobin.";
RL J. Biol. Chem. 277:19538-19545(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=15044115; DOI=10.1016/j.bbrc.2004.03.007;
RA de Sanctis D., Dewilde S., Pesce A., Moens L., Ascenzi P., Hankeln T.,
RA Burmester T., Bolognesi M.;
RT "Mapping protein matrix cavities in human cytoglobin through Xe atom
RT binding.";
RL Biochem. Biophys. Res. Commun. 316:1217-1221(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=15095869; DOI=10.1016/j.jmb.2003.12.063;
RA de Sanctis D., Dewilde S., Pesce A., Moens L., Ascenzi P., Hankeln T.,
RA Burmester T., Bolognesi M.;
RT "Crystal structure of cytoglobin: the fourth globin type discovered in man
RT displays heme hexa-coordination.";
RL J. Mol. Biol. 336:917-927(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=15165856; DOI=10.1016/j.jmb.2004.04.024;
RA Sugimoto H., Makino M., Sawai H., Kawada N., Yoshizato K., Shiro Y.;
RT "Structural basis of human cytoglobin for ligand binding.";
RL J. Mol. Biol. 339:873-885(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS), SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=16699195; DOI=10.1107/s0907444906013813;
RA Makino M., Sugimoto H., Sawai H., Kawada N., Yoshizato K., Shiro Y.;
RT "High-resolution structure of human cytoglobin: identification of extra
RT N- and C-termini and a new dimerization mode.";
RL Acta Crystallogr. D 62:671-677(2006).
CC -!- FUNCTION: May have a protective function during conditions of oxidative
CC stress. May be involved in intracellular oxygen storage or transfer.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:16699195}.
CC -!- INTERACTION:
CC Q8WWM9; O43488: AKR7A2; NbExp=3; IntAct=EBI-6309037, EBI-748855;
CC Q8WWM9; P85298-4: ARHGAP8; NbExp=3; IntAct=EBI-6309037, EBI-9523517;
CC Q8WWM9; Q8WTU0: DDI1; NbExp=6; IntAct=EBI-6309037, EBI-748248;
CC Q8WWM9; Q96KN4: LRATD1; NbExp=3; IntAct=EBI-6309037, EBI-11477916;
CC Q8WWM9; Q08AG7: MZT1; NbExp=3; IntAct=EBI-6309037, EBI-2637198;
CC Q8WWM9; B1AHC3: PRR5-ARHGAP8; NbExp=3; IntAct=EBI-6309037, EBI-17437404;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in
CC heart, stomach, bladder and small intestine.
CC {ECO:0000269|PubMed:11893755}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AJ315162; CAC86186.1; -; mRNA.
DR EMBL; AB057769; BAB87840.1; -; mRNA.
DR EMBL; AK098057; BAC05223.1; -; mRNA.
DR EMBL; CH471099; EAW89406.1; -; Genomic_DNA.
DR EMBL; BC029798; AAH29798.1; -; mRNA.
DR CCDS; CCDS11746.1; -.
DR RefSeq; NP_599030.1; NM_134268.4.
DR PDB; 1UMO; X-ray; 2.59 A; A/B=1-190.
DR PDB; 1URV; X-ray; 2.00 A; A/B=1-190.
DR PDB; 1URY; X-ray; 2.40 A; A/B=1-190.
DR PDB; 1UT0; X-ray; 2.10 A; A/B=1-190.
DR PDB; 1UX9; X-ray; 2.40 A; A/B=1-190.
DR PDB; 1V5H; X-ray; 2.40 A; A=1-190.
DR PDB; 2DC3; X-ray; 1.68 A; A/B=1-190.
DR PDB; 3AG0; X-ray; 2.60 A; A=1-190.
DR PDB; 4B3W; X-ray; 2.80 A; A/B=1-190.
DR PDBsum; 1UMO; -.
DR PDBsum; 1URV; -.
DR PDBsum; 1URY; -.
DR PDBsum; 1UT0; -.
DR PDBsum; 1UX9; -.
DR PDBsum; 1V5H; -.
DR PDBsum; 2DC3; -.
DR PDBsum; 3AG0; -.
DR PDBsum; 4B3W; -.
DR AlphaFoldDB; Q8WWM9; -.
DR SMR; Q8WWM9; -.
DR BioGRID; 125335; 12.
DR IntAct; Q8WWM9; 11.
DR STRING; 9606.ENSP00000293230; -.
DR TCDB; 1.A.107.1.5; the pore-forming globin (globin) family.
DR iPTMnet; Q8WWM9; -.
DR PhosphoSitePlus; Q8WWM9; -.
DR BioMuta; CYGB; -.
DR DMDM; 21263504; -.
DR jPOST; Q8WWM9; -.
DR MassIVE; Q8WWM9; -.
DR MaxQB; Q8WWM9; -.
DR PaxDb; Q8WWM9; -.
DR PeptideAtlas; Q8WWM9; -.
DR PRIDE; Q8WWM9; -.
DR ProteomicsDB; 74913; -.
DR Antibodypedia; 2901; 326 antibodies from 32 providers.
DR DNASU; 114757; -.
DR Ensembl; ENST00000293230.10; ENSP00000293230.4; ENSG00000161544.10.
DR GeneID; 114757; -.
DR KEGG; hsa:114757; -.
DR MANE-Select; ENST00000293230.10; ENSP00000293230.4; NM_134268.5; NP_599030.1.
DR UCSC; uc002jru.3; human.
DR CTD; 114757; -.
DR DisGeNET; 114757; -.
DR GeneCards; CYGB; -.
DR HGNC; HGNC:16505; CYGB.
DR HPA; ENSG00000161544; Low tissue specificity.
DR MalaCards; CYGB; -.
DR MIM; 608759; gene.
DR neXtProt; NX_Q8WWM9; -.
DR OpenTargets; ENSG00000161544; -.
DR PharmGKB; PA27080; -.
DR VEuPathDB; HostDB:ENSG00000161544; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000155004; -.
DR HOGENOM; CLU_003827_10_1_1; -.
DR InParanoid; Q8WWM9; -.
DR OMA; ETQRAWT; -.
DR PhylomeDB; Q8WWM9; -.
DR TreeFam; TF332967; -.
DR PathwayCommons; Q8WWM9; -.
DR Reactome; R-HSA-203615; eNOS activation.
DR Reactome; R-HSA-8981607; Intracellular oxygen transport.
DR SignaLink; Q8WWM9; -.
DR BioGRID-ORCS; 114757; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; CYGB; human.
DR EvolutionaryTrace; Q8WWM9; -.
DR GeneWiki; Cytoglobin; -.
DR GenomeRNAi; 114757; -.
DR Pharos; Q8WWM9; Tbio.
DR PRO; PR:Q8WWM9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8WWM9; protein.
DR Bgee; ENSG00000161544; Expressed in cardiac muscle of right atrium and 149 other tissues.
DR ExpressionAtlas; Q8WWM9; baseline and differential.
DR Genevisible; Q8WWM9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0004096; F:catalase activity; IEA:Ensembl.
DR GO; GO:0047888; F:fatty acid peroxidase activity; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; NAS:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB.
DR GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:2000490; P:negative regulation of hepatic stellate cell activation; IEA:Ensembl.
DR GO; GO:0015671; P:oxygen transport; NAS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR013314; Globin_lamprey/hagfish.
DR PANTHER; PTHR46783; PTHR46783; 1.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR01906; FISHGLOBIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Heme; Iron; Metal-binding;
KW Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..190
FT /note="Cytoglobin"
FT /id="PRO_0000053384"
FT REGION 17..167
FT /note="Globin"
FT BINDING 81
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 113
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT DISULFID 38
FT /note="Interchain (with C-83)"
FT /evidence="ECO:0000269|PubMed:16699195"
FT DISULFID 83
FT /note="Interchain (with C-38)"
FT /evidence="ECO:0000269|PubMed:16699195"
FT CONFLICT 37
FT /note="N -> S (in Ref. 5; AAH29798)"
FT /evidence="ECO:0000305"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:2DC3"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 76..94
FT /evidence="ECO:0007829|PDB:2DC3"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 121..138
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2DC3"
FT HELIX 145..168
FT /evidence="ECO:0007829|PDB:2DC3"
SQ SEQUENCE 190 AA; 21405 MW; B5D7F9976D0BA118 CRC64;
MEKVPGEMEI ERRERSEELS EAERKAVQAM WARLYANCED VGVAILVRFF VNFPSAKQYF
SQFKHMEDPL EMERSPQLRK HACRVMGALN TVVENLHDPD KVSSVLALVG KAHALKHKVE
PVYFKILSGV ILEVVAEEFA SDFPPETQRA WAKLRGLIYS HVTAAYKEVG WVQQVPNATT
PPATLPSSGP
