CYB5B_HUMAN
ID CYB5B_HUMAN Reviewed; 150 AA.
AC O43169; A8K6B1; J3KNF8; Q96CC3; Q9BT35;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Cytochrome b5 type B;
DE AltName: Full=Cytochrome b5 outer mitochondrial membrane isoform;
DE Flags: Precursor;
GN Name=CYB5B; Synonyms=CYB5M, OMB5;
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=Testis;
RA Ishibashi K.;
RT "Cytochrome b5 and aquaporins share the last transmembrane amino acids
RT sequence.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(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=Lymph, and Pancreas;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, AND IDENTIFICATION BY MASS
RP 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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 METHYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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).
CC -!- FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as
CC an electron carrier for several membrane-bound oxygenases.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase (CYB5R3) and MTARC2. {ECO:0000250}.
CC -!- INTERACTION:
CC O43169; Q8IVF2-3: AHNAK2; NbExp=3; IntAct=EBI-1058710, EBI-12078468;
CC O43169; Q13520: AQP6; NbExp=3; IntAct=EBI-1058710, EBI-13059134;
CC O43169; Q13323: BIK; NbExp=3; IntAct=EBI-1058710, EBI-700794;
CC O43169; O60238: BNIP3L; NbExp=3; IntAct=EBI-1058710, EBI-849893;
CC O43169; Q6UXG8-3: BTNL9; NbExp=3; IntAct=EBI-1058710, EBI-17953245;
CC O43169; P20138: CD33; NbExp=3; IntAct=EBI-1058710, EBI-3906571;
CC O43169; P11912: CD79A; NbExp=3; IntAct=EBI-1058710, EBI-7797864;
CC O43169; Q99675: CGRRF1; NbExp=3; IntAct=EBI-1058710, EBI-2130213;
CC O43169; O95471: CLDN7; NbExp=3; IntAct=EBI-1058710, EBI-740744;
CC O43169; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-1058710, EBI-18013275;
CC O43169; Q15125: EBP; NbExp=3; IntAct=EBI-1058710, EBI-3915253;
CC O43169; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-1058710, EBI-18304435;
CC O43169; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-1058710, EBI-18938272;
CC O43169; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-1058710, EBI-12142257;
CC O43169; A2A2Y4: FRMD3; NbExp=3; IntAct=EBI-1058710, EBI-6911547;
CC O43169; O95377: GJB5; NbExp=3; IntAct=EBI-1058710, EBI-3909454;
CC O43169; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-1058710, EBI-13345167;
CC O43169; Q9P2J2-2: IGSF9; NbExp=3; IntAct=EBI-1058710, EBI-17451184;
CC O43169; O95279: KCNK5; NbExp=3; IntAct=EBI-1058710, EBI-3934936;
CC O43169; P43628: KIR2DL3; NbExp=3; IntAct=EBI-1058710, EBI-8632435;
CC O43169; Q5T0T0: MARCHF8; NbExp=3; IntAct=EBI-1058710, EBI-14061946;
CC O43169; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-1058710, EBI-11956541;
CC O43169; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-1058710, EBI-373355;
CC O43169; Q5TF39: MFSD4B; NbExp=3; IntAct=EBI-1058710, EBI-11922631;
CC O43169; Q6N075: MFSD5; NbExp=3; IntAct=EBI-1058710, EBI-3920969;
CC O43169; P15941-11: MUC1; NbExp=3; IntAct=EBI-1058710, EBI-17263240;
CC O43169; Q8N183: NDUFAF2; NbExp=3; IntAct=EBI-1058710, EBI-2682365;
CC O43169; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-1058710, EBI-716063;
CC O43169; Q96KR7: PHACTR3; NbExp=3; IntAct=EBI-1058710, EBI-717068;
CC O43169; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-1058710, EBI-10485931;
CC O43169; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-1058710, EBI-7545592;
CC O43169; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-1058710, EBI-10192441;
CC O43169; Q5VUM1: SDHAF4; NbExp=3; IntAct=EBI-1058710, EBI-16769525;
CC O43169; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-1058710, EBI-18159983;
CC O43169; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-1058710, EBI-2823239;
CC O43169; P27105: STOM; NbExp=3; IntAct=EBI-1058710, EBI-1211440;
CC O43169; Q16623: STX1A; NbExp=3; IntAct=EBI-1058710, EBI-712466;
CC O43169; P21579: SYT1; NbExp=3; IntAct=EBI-1058710, EBI-524909;
CC O43169; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-1058710, EBI-7238458;
CC O43169; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-1058710, EBI-10982110;
CC O43169; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-1058710, EBI-11722971;
CC O43169; Q96HV5: TMEM41A; NbExp=3; IntAct=EBI-1058710, EBI-10288884;
CC O43169; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-1058710, EBI-2548832;
CC O43169; PRO_0000045601 [Q99IB8]; Xeno; NbExp=5; IntAct=EBI-1058710, EBI-6928570;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P04166}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04373.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH14431.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA23735.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF84265.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB009282; BAA23735.1; ALT_INIT; mRNA.
DR EMBL; AK291576; BAF84265.1; ALT_INIT; mRNA.
DR EMBL; AC009032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83275.1; -; Genomic_DNA.
DR EMBL; CH471092; EAW83276.1; -; Genomic_DNA.
DR EMBL; BC004373; AAH04373.1; ALT_INIT; mRNA.
DR EMBL; BC014431; AAH14431.2; ALT_INIT; mRNA.
DR CCDS; CCDS10880.2; -.
DR RefSeq; NP_085056.2; NM_030579.2.
DR PDB; 3NER; X-ray; 1.45 A; A/B=16-107.
DR PDBsum; 3NER; -.
DR AlphaFoldDB; O43169; -.
DR SMR; O43169; -.
DR BioGRID; 123309; 270.
DR IntAct; O43169; 64.
DR MINT; O43169; -.
DR STRING; 9606.ENSP00000308430; -.
DR ChEMBL; CHEMBL4523134; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; O43169; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43169; -.
DR PhosphoSitePlus; O43169; -.
DR SwissPalm; O43169; -.
DR BioMuta; CYB5B; -.
DR EPD; O43169; -.
DR jPOST; O43169; -.
DR MassIVE; O43169; -.
DR MaxQB; O43169; -.
DR PaxDb; O43169; -.
DR PeptideAtlas; O43169; -.
DR PRIDE; O43169; -.
DR ProteomicsDB; 48787; -.
DR TopDownProteomics; O43169; -.
DR Antibodypedia; 2014; 89 antibodies from 21 providers.
DR DNASU; 80777; -.
DR Ensembl; ENST00000307892.13; ENSP00000308430.8; ENSG00000103018.18.
DR GeneID; 80777; -.
DR KEGG; hsa:80777; -.
DR MANE-Select; ENST00000307892.13; ENSP00000308430.8; NM_030579.3; NP_085056.2.
DR UCSC; uc002exg.1; human.
DR UCSC; uc059wli.1; human.
DR CTD; 80777; -.
DR DisGeNET; 80777; -.
DR GeneCards; CYB5B; -.
DR HGNC; HGNC:24374; CYB5B.
DR HPA; ENSG00000103018; Tissue enhanced (adrenal).
DR MIM; 611964; gene.
DR neXtProt; NX_O43169; -.
DR OpenTargets; ENSG00000103018; -.
DR PharmGKB; PA143485445; -.
DR VEuPathDB; HostDB:ENSG00000103018; -.
DR eggNOG; KOG0537; Eukaryota.
DR GeneTree; ENSGT00940000155584; -.
DR HOGENOM; CLU_102602_3_3_1; -.
DR InParanoid; O43169; -.
DR OMA; KNNTCKS; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; O43169; -.
DR TreeFam; TF314537; -.
DR PathwayCommons; O43169; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR SignaLink; O43169; -.
DR BioGRID-ORCS; 80777; 171 hits in 1092 CRISPR screens.
DR ChiTaRS; CYB5B; human.
DR GenomeRNAi; 80777; -.
DR Pharos; O43169; Tbio.
DR PRO; PR:O43169; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O43169; protein.
DR Bgee; ENSG00000103018; Expressed in right adrenal gland cortex and 195 other tissues.
DR ExpressionAtlas; O43169; baseline and differential.
DR Genevisible; O43169; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:1903958; C:nitric-oxide synthase complex; IDA:FlyBase.
DR GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; ISS:FlyBase.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:FlyBase.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Methylation; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..15
FT /evidence="ECO:0000250|UniProtKB:P04166"
FT /id="PRO_0000006471"
FT CHAIN 16..150
FT /note="Cytochrome b5 type B"
FT /id="PRO_0000006472"
FT TRANSMEM 123..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 24..100
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 83
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQX2"
FT MOD_RES 39
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQX2"
FT CONFLICT 115
FT /note="K -> Q (in Ref. 1; BAA23735)"
FT /evidence="ECO:0000305"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:3NER"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3NER"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3NER"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3NER"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3NER"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3NER"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:3NER"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:3NER"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3NER"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3NER"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:3NER"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3NER"
SQ SEQUENCE 150 AA; 16695 MW; 4E1CA5FE92D21D9C CRC64;
MSGSMATAEA SGSDGKGQEV ETSVTYYRLE EVAKRNSLKE LWLVIHGRVY DVTRFLNEHP
GGEEVLLEQA GVDASESFED VGHSSDAREM LKQYYIGDIH PSDLKPESGS KDPSKNDTCK
SCWAYWILPI IGAVLLGFLY RYYTSESKSS
