Full text data of CYB5B
CYB5B
(CYB5M, OMB5)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Cytochrome b5 type B (Cytochrome b5 outer mitochondrial membrane isoform; Flags: Precursor)
Cytochrome b5 type B (Cytochrome b5 outer mitochondrial membrane isoform; Flags: Precursor)
UniProt
O43169
ID CYB5B_HUMAN Reviewed; 146 AA.
AC O43169; A8K6B1; Q96CC3; Q9BT35;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2005, sequence version 2.
DT 22-JAN-2014, entry version 123.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA 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.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA 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 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which
CC function as an electron carrier for several membrane bound
CC oxygenases (By similarity).
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane (By
CC similarity).
CC -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB009282; BAA23735.1; -; mRNA.
DR EMBL; AK291576; BAF84265.1; -; mRNA.
DR EMBL; AC026464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004373; AAH04373.1; -; mRNA.
DR EMBL; BC014431; AAH14431.2; -; mRNA.
DR RefSeq; NP_085056.2; NM_030579.2.
DR UniGene; Hs.461131; -.
DR PDB; 3NER; X-ray; 1.45 A; A/B=12-103.
DR PDBsum; 3NER; -.
DR ProteinModelPortal; O43169; -.
DR SMR; O43169; 12-102.
DR IntAct; O43169; 1.
DR MINT; MINT-5000089; -.
DR STRING; 9606.ENSP00000308430; -.
DR PhosphoSite; O43169; -.
DR PaxDb; O43169; -.
DR PRIDE; O43169; -.
DR DNASU; 80777; -.
DR Ensembl; ENST00000512062; ENSP00000423679; ENSG00000103018.
DR GeneID; 80777; -.
DR KEGG; hsa:80777; -.
DR CTD; 80777; -.
DR GeneCards; GC16P069458; -.
DR HGNC; HGNC:24374; CYB5B.
DR HPA; HPA007893; -.
DR MIM; 611964; gene.
DR neXtProt; NX_O43169; -.
DR PharmGKB; PA143485445; -.
DR eggNOG; COG5274; -.
DR HOGENOM; HOG000039853; -.
DR HOVERGEN; HBG002653; -.
DR InParanoid; O43169; -.
DR OrthoDB; EOG78H3W2; -.
DR ChiTaRS; CYB5B; human.
DR GenomeRNAi; 80777; -.
DR NextBio; 71179; -.
DR PMAP-CutDB; O43169; -.
DR PRO; PR:O43169; -.
DR ArrayExpress; O43169; -.
DR Bgee; O43169; -.
DR CleanEx; HS_CYB5B; -.
DR Genevestigator; O43169; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
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; Complete proteome; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT PROPEP 2 11 By similarity.
FT /FTId=PRO_0000006471.
FT CHAIN 12 146 Cytochrome b5 type B.
FT /FTId=PRO_0000006472.
FT TRANSMEM 119 136 Helical; (Potential).
FT DOMAIN 20 96 Cytochrome b5 heme-binding.
FT METAL 55 55 Iron (heme axial ligand) (By similarity).
FT METAL 79 79 Iron (heme axial ligand) (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 30 30 N6-acetyllysine.
FT CONFLICT 111 111 K -> Q (in Ref. 1; BAA23735).
FT HELIX 25 28
FT STRAND 36 41
FT STRAND 44 47
FT HELIX 49 51
FT TURN 52 54
FT HELIX 60 63
FT TURN 64 67
FT HELIX 71 76
FT HELIX 81 87
FT HELIX 88 90
FT STRAND 91 95
FT HELIX 97 99
SQ SEQUENCE 146 AA; 16332 MW; 2FF7DBB62859AE19 CRC64;
MATAEASGSD GKGQEVETSV TYYRLEEVAK RNSLKELWLV IHGRVYDVTR FLNEHPGGEE
VLLEQAGVDA SESFEDVGHS SDAREMLKQY YIGDIHPSDL KPESGSKDPS KNDTCKSCWA
YWILPIIGAV LLGFLYRYYT SESKSS
//
ID CYB5B_HUMAN Reviewed; 146 AA.
AC O43169; A8K6B1; Q96CC3; Q9BT35;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2005, sequence version 2.
DT 22-JAN-2014, entry version 123.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA 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.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA 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 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which
CC function as an electron carrier for several membrane bound
CC oxygenases (By similarity).
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane (By
CC similarity).
CC -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB009282; BAA23735.1; -; mRNA.
DR EMBL; AK291576; BAF84265.1; -; mRNA.
DR EMBL; AC026464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004373; AAH04373.1; -; mRNA.
DR EMBL; BC014431; AAH14431.2; -; mRNA.
DR RefSeq; NP_085056.2; NM_030579.2.
DR UniGene; Hs.461131; -.
DR PDB; 3NER; X-ray; 1.45 A; A/B=12-103.
DR PDBsum; 3NER; -.
DR ProteinModelPortal; O43169; -.
DR SMR; O43169; 12-102.
DR IntAct; O43169; 1.
DR MINT; MINT-5000089; -.
DR STRING; 9606.ENSP00000308430; -.
DR PhosphoSite; O43169; -.
DR PaxDb; O43169; -.
DR PRIDE; O43169; -.
DR DNASU; 80777; -.
DR Ensembl; ENST00000512062; ENSP00000423679; ENSG00000103018.
DR GeneID; 80777; -.
DR KEGG; hsa:80777; -.
DR CTD; 80777; -.
DR GeneCards; GC16P069458; -.
DR HGNC; HGNC:24374; CYB5B.
DR HPA; HPA007893; -.
DR MIM; 611964; gene.
DR neXtProt; NX_O43169; -.
DR PharmGKB; PA143485445; -.
DR eggNOG; COG5274; -.
DR HOGENOM; HOG000039853; -.
DR HOVERGEN; HBG002653; -.
DR InParanoid; O43169; -.
DR OrthoDB; EOG78H3W2; -.
DR ChiTaRS; CYB5B; human.
DR GenomeRNAi; 80777; -.
DR NextBio; 71179; -.
DR PMAP-CutDB; O43169; -.
DR PRO; PR:O43169; -.
DR ArrayExpress; O43169; -.
DR Bgee; O43169; -.
DR CleanEx; HS_CYB5B; -.
DR Genevestigator; O43169; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
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; Complete proteome; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT PROPEP 2 11 By similarity.
FT /FTId=PRO_0000006471.
FT CHAIN 12 146 Cytochrome b5 type B.
FT /FTId=PRO_0000006472.
FT TRANSMEM 119 136 Helical; (Potential).
FT DOMAIN 20 96 Cytochrome b5 heme-binding.
FT METAL 55 55 Iron (heme axial ligand) (By similarity).
FT METAL 79 79 Iron (heme axial ligand) (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 30 30 N6-acetyllysine.
FT CONFLICT 111 111 K -> Q (in Ref. 1; BAA23735).
FT HELIX 25 28
FT STRAND 36 41
FT STRAND 44 47
FT HELIX 49 51
FT TURN 52 54
FT HELIX 60 63
FT TURN 64 67
FT HELIX 71 76
FT HELIX 81 87
FT HELIX 88 90
FT STRAND 91 95
FT HELIX 97 99
SQ SEQUENCE 146 AA; 16332 MW; 2FF7DBB62859AE19 CRC64;
MATAEASGSD GKGQEVETSV TYYRLEEVAK RNSLKELWLV IHGRVYDVTR FLNEHPGGEE
VLLEQAGVDA SESFEDVGHS SDAREMLKQY YIGDIHPSDL KPESGSKDPS KNDTCKSCWA
YWILPIIGAV LLGFLYRYYT SESKSS
//
MIM
611964
*RECORD*
*FIELD* NO
611964
*FIELD* TI
*611964 CYTOCHROME b5, TYPE B (OUTER MITOCHONDRIAL MEMBRANE); CYB5B
;;OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME b5; OMB5;;
read moreCYPB5M;;
CYTB5, TYPE 2
*FIELD* TX
CLONING
By PCR of human placenta, liver, and testis cDNA libraries, followed by
database analysis, Soucy and Luu-The (2002) isolated CYB5B. The deduced
153-amino acid protein shares 45.8% homology with CYB5A (613218), and
RT-PCR analysis showed CYB5B expression in human liver, testis, and
adrenal tissues. CYB5B had 17,20-lyase activity as measured by the
conversion of pregnenolone to dehydroepiandrosterone (DHEA) when
expressed in HEK293 cells.
MAPPING
Hartz (2010) mapped the CYB5B gene to chromosome 16q22.1 based on an
alignment of the CYB5B sequence (GenBank GENBANK AB009282) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/20/2010.
2. Soucy, P.; Luu-The, V.: Assessment of the ability of type 2 cytochrome
b5 to modulate 17,20-lyase activity of human P450c17. J. Steroid
Biochem. Molec. Biol. 80: 71-75, 2002.
*FIELD* CD
Dorothy S. Reilly: 4/17/2008
*FIELD* ED
carol: 02/11/2011
carol: 1/20/2010
wwang: 4/17/2008
*RECORD*
*FIELD* NO
611964
*FIELD* TI
*611964 CYTOCHROME b5, TYPE B (OUTER MITOCHONDRIAL MEMBRANE); CYB5B
;;OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME b5; OMB5;;
read moreCYPB5M;;
CYTB5, TYPE 2
*FIELD* TX
CLONING
By PCR of human placenta, liver, and testis cDNA libraries, followed by
database analysis, Soucy and Luu-The (2002) isolated CYB5B. The deduced
153-amino acid protein shares 45.8% homology with CYB5A (613218), and
RT-PCR analysis showed CYB5B expression in human liver, testis, and
adrenal tissues. CYB5B had 17,20-lyase activity as measured by the
conversion of pregnenolone to dehydroepiandrosterone (DHEA) when
expressed in HEK293 cells.
MAPPING
Hartz (2010) mapped the CYB5B gene to chromosome 16q22.1 based on an
alignment of the CYB5B sequence (GenBank GENBANK AB009282) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/20/2010.
2. Soucy, P.; Luu-The, V.: Assessment of the ability of type 2 cytochrome
b5 to modulate 17,20-lyase activity of human P450c17. J. Steroid
Biochem. Molec. Biol. 80: 71-75, 2002.
*FIELD* CD
Dorothy S. Reilly: 4/17/2008
*FIELD* ED
carol: 02/11/2011
carol: 1/20/2010
wwang: 4/17/2008