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HBB





Hemoglobin, beta
PDB rendering based on 1a00.
Available structures: 1a00, 1a01, 1a0u, 1a0z, 1a3n, 1a3o, 1abw, 1aby, 1aj9, 1b86, 1bab, 1bbb, 1bij, 1buw, 1bz0, 1bz1, 1bzz, 1c7b, 1c7c, 1c7d, 1cbl, 1cbm, 1cls, 1cmy, 1coh, 1dke, 1dxt, 1dxu, 1dxv, 1fn3, 1g9v, 1gbu, 1gbv, 1gli, 1gzx, 1hab, 1hac, 1hba, 1hbb, 1hbs, 1hco, 1hdb, 1hga, 1hgb, 1hgc, 1hho, 1ird, 1j3y, 1j3z, 1j40, 1j41, 1j7s, 1j7w, 1j7y, 1jy7, 1k0y, 1k1k, 1kd2, 1lfl, 1lfq, 1lft, 1lfv, 1lfy, 1lfz, 1ljw, 1m9p, 1mko, 1nej, 1nih, 1nqp, 1o1i, 1o1j, 1o1k, 1o1l, 1o1m, 1o1n, 1o1o, 1o1p, 1qi8, 1qsh, 1qsi, 1qxd, 1qxe, 1r1x, 1r1y, 1rps, 1rq3, 1rq4, 1rqa, 1rvw, 1sdk, 1sdl, 1shr, 1si4, 1thb, 1uiw, 1vwt, 1xxt, 1xy0, 1xye, 1xz2, 1xz4, 1xz5, 1xz7, 1xzu, 1xzv, 1y09, 1y0a, 1y0c, 1y0d, 1y0t, 1y0w, 1y22, 1y2z, 1y31, 1y35, 1y45, 1y46, 1y4b, 1y4f, 1y4g, 1y4p, 1y4q, 1y4r, 1y4v, 1y5f, 1y5j, 1y5k, 1y7c, 1y7d, 1y7g, 1y7z, 1y83, 1y85, 1y8w, 1ydz, 1ye0, 1ye1, 1ye2, 1yen, 1yeo, 1yeq, 1yeu, 1yev, 1yff, 1yg5, 1ygd, 1ygf, 1yh9, 1yhe, 1yhr, 1yie, 1yih, 1yvq, 1yvt, 1yzi, 2d5z, 2d60, 2dn1, 2dn2, 2dn3, 2h35, 2hbc, 2hbd, 2hbe, 2hbf, 2hbs, 2hco, 2hhb, 2hhd, 2hhe, 3hhb, 4hhb, 6hbw
Identifiers
Symbol(s) HBB; CD113t-C; HBD
External IDs OMIM: 141900 MGI: 96022 Homologene: 68066
Orthologs
Human Mouse
Entrez 3043 15130


Refseq NM_000518 (mRNA)
NP_000509 (protein) 		NM_016956 (mRNA)
NP_058652 (protein)
Pubmed search [1] [2]

Beta globin (HBB, β-globin) is a protein that, along with alpha globin (HBA), makes up the most common form of hemoglobin in adult humans. The gene is located in the β-globin locus. Mutant beta globin is responsible for the sickling of red blood cells seen in sickle cell anemia. Expression of beta globin and the neighboring globins in the β-globin locus is controlled by single locus control region (LCR).[1]


See also

Human β-globin locus


References

  1. ^ Levings & Bungert (2002)
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "HBB". A list of authors is available in Wikipedia.
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