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HBBZ_MOUSE
ID   HBBZ_MOUSE              Reviewed;         147 AA.
AC   P04444; Q61347;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Hemoglobin subunit beta-H1;
DE   AltName: Full=Beta-H1-globin;
DE   AltName: Full=Hemoglobin beta-H1 chain;
DE   AltName: Full=Protein Z;
GN   Name=Hbb-bh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2926808; DOI=10.1016/0022-2836(89)90363-x;
RA   Shehee W.R., Loeb D.D., Adey N.B., Burton F.H., Casavant N.C., Cole P.,
RA   Davies C.J., McGraw R.A., Schichman S.A., Severynse D.M., Voliva C.F.,
RA   Weyter F.W., Wisely G.B., Edgell M.H., Hutchison C.A. III;
RT   "Nucleotide sequence of the BALB/c mouse beta-globin complex.";
RL   J. Mol. Biol. 205:41-62(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6323438; DOI=10.1016/s0021-9258(17)43157-7;
RA   Hill A., Hardies S.C., Phillips S.J., Davis M.G., Hutchison C.A. III,
RA   Edgell M.H.;
RT   "Two mouse early embryonic beta-globin gene sequences. Evolution of the
RT   nonadult beta-globins.";
RL   J. Biol. Chem. 259:3739-3747(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-105.
RX   PubMed=6250710; DOI=10.1016/0092-8674(80)90123-3;
RA   Jahn C.L., Hutchison C.A. III, Phillips S.J., Weaver S., Haigwood N.L.,
RA   Voliva C.F., Edgell M.H.;
RT   "DNA sequence organization of the beta-globin complex in the BALB/c
RT   mouse.";
RL   Cell 21:159-168(1980).
CC   -!- FUNCTION: This is an embryonic beta-type chain.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; X14061; CAA32221.1; -; Genomic_DNA.
DR   EMBL; J00417; AAB59638.1; -; Genomic_DNA.
DR   EMBL; AK028208; BAC25815.1; -; mRNA.
DR   EMBL; BC052008; AAH52008.1; -; mRNA.
DR   EMBL; V00724; CAA24103.1; -; Genomic_DNA.
DR   CCDS; CCDS21592.1; -.
DR   PIR; A02419; HBMSH1.
DR   RefSeq; NP_032245.1; NM_008219.3.
DR   AlphaFoldDB; P04444; -.
DR   SMR; P04444; -.
DR   ComplexPortal; CPX-2938; Early embryonic hemoglobin complex.
DR   STRING; 10090.ENSMUSP00000064865; -.
DR   PhosphoSitePlus; P04444; -.
DR   PaxDb; P04444; -.
DR   PeptideAtlas; P04444; -.
DR   PRIDE; P04444; -.
DR   ProteomicsDB; 269816; -.
DR   DNASU; 15132; -.
DR   Ensembl; ENSMUST00000063957; ENSMUSP00000064865; ENSMUSG00000052217.
DR   GeneID; 15132; -.
DR   KEGG; mmu:15132; -.
DR   UCSC; uc009iur.1; mouse.
DR   CTD; 15132; -.
DR   MGI; MGI:96024; Hbb-bh1.
DR   VEuPathDB; HostDB:ENSMUSG00000052217; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000164134; -.
DR   HOGENOM; CLU_003827_10_0_1; -.
DR   InParanoid; P04444; -.
DR   OMA; ETAIMGN; -.
DR   OrthoDB; 1370439at2759; -.
DR   PhylomeDB; P04444; -.
DR   TreeFam; TF333268; -.
DR   BioGRID-ORCS; 15132; 0 hits in 71 CRISPR screens.
DR   PRO; PR:P04444; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P04444; protein.
DR   Bgee; ENSMUSG00000052217; Expressed in pharyngeal arch 2 and 96 other tissues.
DR   ExpressionAtlas; P04444; baseline and differential.
DR   Genevisible; P04444; MM.
DR   GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR   GO; GO:0005833; C:hemoglobin complex; ISO:MGI.
DR   GO; GO:0020037; F:heme binding; ISO:MGI.
DR   GO; GO:0031721; F:hemoglobin alpha binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR   GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR   GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR   GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0015671; P:oxygen transport; IC:ComplexPortal.
DR   GO; GO:0010942; P:positive regulation of cell death; IC:ComplexPortal.
DR   CDD; cd08925; Hb-beta-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR002337; Hemoglobin_b.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   CHAIN           1..147
FT                   /note="Hemoglobin subunit beta-H1"
FT                   /id="PRO_0000053023"
FT   BINDING         64
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   BINDING         93
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"
SQ   SEQUENCE   147 AA;  16494 MW;  158D57A33F002DAA CRC64;
     MVHFTAEEKA AITSIWDKVD LEKVGGETLG RLLIVYPWTQ RFFDKFGNLS SALAIMGNPR
     IRAHGKKVLT SLGLGVKNMD NLKETFAHLS ELHCDKLHVD PENFKLLGNM LVIVLSTHFA
     KEFTPEVQAA WQKLVIGVAN ALSHKYH
 
 
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