HUMAN:HBB

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Species (Taxon ID)	Homo sapiens (Human). (taxon:9606)
Gene Name(s)	HBB
Protein Name(s)	Hemoglobin subunit beta Beta-globin Hemoglobin beta chain LVV-hemorphin-7
External Links
UniProt Identifier	HBB_HUMAN
UniProt Accessions	P68871, A4GX73, B2ZUE0, P02023, Q13852, Q14481, Q14510, Q45KT0, Q549N7, Q6FI08, Q6R7N2, Q8IZI1, Q9BX96, Q9UCD6, Q9UCP8, Q9UCP9,
EMBL	M25079, V00499, DQ126270, DQ126271, DQ126272, DQ126273, DQ126274, DQ126275, DQ126276, DQ126277, DQ126278, DQ126279, DQ126280, DQ126281, DQ126282, DQ126283, DQ126284, DQ126285, DQ126286, DQ126287, DQ126288, DQ126289, DQ126290, DQ126291, DQ126292, DQ126293, DQ126294, DQ126295, DQ126296, DQ126297, DQ126298, DQ126299, DQ126300, DQ126301, DQ126302, DQ126303, DQ126304, DQ126305, DQ126306, DQ126307, DQ126308, DQ126309, DQ126310, DQ126311, DQ126312, DQ126313, DQ126314, DQ126315, DQ126316, DQ126317, DQ126318, DQ126319, DQ126320, DQ126321, DQ126322, DQ126323, DQ126324, DQ126325, AF007546, AF083883, AF117710, AF181989, AF349114, AF527577, AY136510, AY163866, AY260740, AY509193, EF450778, EU694432, AK311825, CR536530, CR541913, CH471064, BC007075, U01317, V00497, V00500, L26462, L26463, L26464, L26465, L26466, L26467, L26468, L26469, L26470, L26471, L26472, L26473, L26474, L26475, L26476, L26477, L26478, L48213, L48214, L48215, L48216, L48217, M36640, M11428, M25113, L48932,
PIR	A53136,
RefSeq	NP_000509.1,
PDB	1A00, 1A01, 1A0U, 1A0Z, 1A3N, 1A3O, 1ABW, 1ABY, 1AJ9, 1B86, 1BAB, 1BBB, 1BIJ, 1BUW, 1BZ0, 1BZ1, 1BZZ, 1C7B, 1C7C, 1C7D, 1CBL, 1CBM, 1CH4, 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, 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, 2DXM, 2H35, 2HBC, 2HBD, 2HBE, 2HBF, 2HBS, 2HCO, 2HHB, 2HHD, 2HHE, 2W6V, 2W72, 2YRS, 3B75, 3D17, 3D7O, 3DUT, 3HHB, 3HXN, 3IC0, 3IC2, 3KMF, 3NL7, 3NMM, 3ODQ, 3P5Q, 3QJB, 3QJC, 3QJD, 3QJE, 3R5I, 4HHB, 6HBW,
IntAct	P68871,
Ensembl	ENST00000335295,
Pfam	PF00042,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0005833	hemoglobin complex		TAS: Traceable Author Statement		C	Source: UniProtKB
	GO:0020037	heme binding		IEA: Inferred from Electronic Annotation		F	Source: InterPro
	GO:0030492	hemoglobin binding		IDA: Inferred from Direct Assay		F	Source: UniProtKB
	GO:0019825	oxygen binding		IDA: Inferred from Direct Assay		F	Source: UniProtKB
	GO:0005344	oxygen transporter activity		NAS: Non-traceable Author Statement		F	Source: UniProtKB
	GO:0030185	nitric oxide transport		NAS: Non-traceable Author Statement		P	Source: UniProtKB
	GO:0045429	positive regulation of nitric oxide biosynt...		NAS: Non-traceable Author Statement		P	Source: UniProtKB
	GO:0008217	regulation of blood pressure		IEA: Inferred from Electronic Annotation		P	Source: UniProtKB-KW
	GO:0050880	regulation of blood vessel size		IEA: Inferred from Electronic Annotation		P	Source: UniProtKB-KW
Contributes to	GO:0031720	haptoglobin binding	PMID:19740759^[1]	IDA: Inferred from Direct Assay		F	Fig 2 shows haemoglobin-haptoglobin complexes and how EPR signal varies compared to pure haemoglobin.	complete
	GO:0031838	haptoglobin-hemoglobin complex	PMID:19740759^[1]	IDA: Inferred from Direct Assay		C	Fig 2 shows haemoglobin-haptoglobin complexes and how EPR signal varies compared to pure haemoglobin.	complete
Contributes to	GO:0004601	peroxidase activity	PMID:19740759^[1]	IDA: Inferred from Direct Assay		F	Fig 5 shows positive peroxidase activity of haemoglobin and of haemoglobin-haptoglobin complexes.	complete
Contributes to	GO:0042542	response to hydrogen peroxide	PMID:19740759^[1]	IDA: Inferred from Direct Assay		P	Fig 3: large MW aggregates can be seen after addition of hydrogen peroxide when both haemoglobin and haptoglobin are present.	complete
	GO:0005344	oxygen transporter activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0561	F
	GO:0005344	oxygen transporter activity	PMID:11747442^[2]	NAS: Non-traceable Author Statement		F
	GO:0005344	oxygen transporter activity	PMID:1301199^[3]	NAS: Non-traceable Author Statement		F
	GO:0005506	iron ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000971	F
	GO:0005506	iron ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002337	F
	GO:0005506	iron ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012292	F
	GO:0005515	protein binding	PMID:9441940^[4]	IPI: Inferred from Physical Interaction	UniProtKB:P69905	F
	GO:0005829	cytosol	Reactome:REACT_25336	TAS: Traceable Author Statement		C
	GO:0005833	hemoglobin complex	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002337	C
	GO:0005833	hemoglobin complex	PMID:10588683^[5]	NAS: Non-traceable Author Statement		C
	GO:0005833	hemoglobin complex	PMID:1301199^[3]	NAS: Non-traceable Author Statement		C
	GO:0005833	hemoglobin complex	PMID:1540659^[6]	TAS: Traceable Author Statement		C
	GO:0005833	hemoglobin complex	PMID:19740759^[1]	IDA: Inferred from Direct Assay		C
	GO:0006810	transport	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0813	P
	GO:0007596	blood coagulation	Reactome:REACT_604	TAS: Traceable Author Statement		P
	GO:0008217	regulation of blood pressure	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0382	P
	GO:0010942	positive regulation of cell death	PMID:19740759^[1]	IDA: Inferred from Direct Assay		P
	GO:0015671	oxygen transport	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002337	P
	GO:0015671	oxygen transport	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012292	P
	GO:0015671	oxygen transport	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0561	P
	GO:0015671	oxygen transport	PMID:11747442^[2]	NAS: Non-traceable Author Statement		P
	GO:0015671	oxygen transport	PMID:1301199^[3]	NAS: Non-traceable Author Statement		P
	GO:0015671	oxygen transport	PMID:1540659^[6]	TAS: Traceable Author Statement		P
	GO:0019825	oxygen binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002337	F
	GO:0019825	oxygen binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012292	F
	GO:0019825	oxygen binding	PMID:11747442^[2]	IDA: Inferred from Direct Assay		F
	GO:0020037	heme binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000971	F
	GO:0020037	heme binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002337	F
	GO:0020037	heme binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012292	F
	GO:0030185	nitric oxide transport	PMID:8292032^[7]	NAS: Non-traceable Author Statement		P
	GO:0030492	hemoglobin binding	PMID:1512262^[8]	IDA: Inferred from Direct Assay		F
	GO:0031838	haptoglobin-hemoglobin complex	PMID:19740759^[1]	IDA: Inferred from Direct Assay		C
	GO:0042542	response to hydrogen peroxide	PMID:19740759^[1]	IDA: Inferred from Direct Assay		P
	GO:0042744	hydrogen peroxide catabolic process	PMID:19740759^[1]	IDA: Inferred from Direct Assay		P
	GO:0045429	positive regulation of nitric oxide biosynthetic process	PMID:7965120^[9]	NAS: Non-traceable Author Statement		P
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
	GO:0050880	regulation of blood vessel size	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0838	P
	GO:0051291	protein heterooligomerization	PMID:19740759^[1]	IDA: Inferred from Direct Assay		P
contributes_to	GO:0004601	peroxidase activity	PMID:19740759^[1]	IDA: Inferred from Direct Assay		F
contributes_to	GO:0031720	haptoglobin binding	PMID:19740759^[1]	IDA: Inferred from Direct Assay		F
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.00 ^1.01 ^1.02 ^1.03 ^1.04 ^1.05 ^1.06 ^1.07 ^1.08 ^1.09 ^1.10 ^1.11 Kapralov A et al. (2009) Peroxidase activity of hemoglobin-haptoglobin complexes: covalent aggregation and oxidative stress in plasma and macrophages. J Biol Chem 284: 30395-407 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Kidd RD et al. (2001) The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function. Biochemistry 40: 15669-75 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Murru S et al. (1992) A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), causing a severe beta-thalassemia intermedia phenotype. Hum Mutat 1: 124-8 PubMed GONUTS page
↑ Taylor KA et al. (1997) The use of electron tomography for structural analysis of disordered protein arrays. J Struct Biol 120: 372-86 PubMed GONUTS page
↑ Durner J et al. (1999) Ancient origins of nitric oxide signaling in biological systems. Proc Natl Acad Sci U S A 96: 14206-7 PubMed GONUTS page
↑ ^6.0 ^6.1 Wajcman H et al. (1992) Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5) Leu----His]. Biochim Biophys Acta 1138: 127-32 PubMed GONUTS page
↑ Sampath V et al. (1994) Characterization of interactions of nitric oxide with human hemoglobin A by infrared spectroscopy. Biochem Biophys Res Commun 198: 281-7 PubMed GONUTS page
↑ Silva MM et al. (1992) A third quaternary structure of human hemoglobin A at 1.7-A resolution. J Biol Chem 267: 17248-56 PubMed GONUTS page
↑ Suzuki S et al. (1994) Hemoglobin augmentation of interleukin-1 beta-induced production of nitric oxide in smooth-muscle cells. J Neurosurg 81: 895-901 PubMed GONUTS page

[PMID:19740759-0] 1.00 ^1.01 ^1.02 ^1.03 ^1.04 ^1.05 ^1.06 ^1.07 ^1.08 ^1.09 ^1.10 ^1.11 Kapralov A et al. (2009) Peroxidase activity of hemoglobin-haptoglobin complexes: covalent aggregation and oxidative stress in plasma and macrophages. J Biol Chem 284: 30395-407 PubMed GONUTS page

[PMID:11747442-1] 2.0 ^2.1 ^2.2 Kidd RD et al. (2001) The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function. Biochemistry 40: 15669-75 PubMed GONUTS page

[PMID:1301199-2] 3.0 ^3.1 ^3.2 Murru S et al. (1992) A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), causing a severe beta-thalassemia intermedia phenotype. Hum Mutat 1: 124-8 PubMed GONUTS page

[PMID:9441940-3] Taylor KA et al. (1997) The use of electron tomography for structural analysis of disordered protein arrays. J Struct Biol 120: 372-86 PubMed GONUTS page

[PMID:10588683-4] Durner J et al. (1999) Ancient origins of nitric oxide signaling in biological systems. Proc Natl Acad Sci U S A 96: 14206-7 PubMed GONUTS page

[PMID:1540659-5] 6.0 ^6.1 Wajcman H et al. (1992) Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5) Leu----His]. Biochim Biophys Acta 1138: 127-32 PubMed GONUTS page

[PMID:8292032-6] Sampath V et al. (1994) Characterization of interactions of nitric oxide with human hemoglobin A by infrared spectroscopy. Biochem Biophys Res Commun 198: 281-7 PubMed GONUTS page

[PMID:1512262-7] Silva MM et al. (1992) A third quaternary structure of human hemoglobin A at 1.7-A resolution. J Biol Chem 267: 17248-56 PubMed GONUTS page

[PMID:7965120-8] Suzuki S et al. (1994) Hemoglobin augmentation of interleukin-1 beta-induced production of nitric oxide in smooth-muscle cells. J Neurosurg 81: 895-901 PubMed GONUTS page

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HUMAN:HBB

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