HUMAN:HBB

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HBB
Protein Name(s)	Hemoglobin subunit beta Beta-globin Hemoglobin beta chain LVV-hemorphin-7 Spinorphin
External Links
UniProt	P68871
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
CCDS	CCDS7753.1
PIR	A53136
RefSeq	NP_000509.1
UniGene	Hs.523443
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 2M6Z 2W6V 2W72 2YRS 3B75 3D17 3D7O 3DUT 3HHB 3HXN 3IC0 3IC2 3KMF 3NL7 3NMM 3ODQ 3ONZ 3OO4 3OO5 3P5Q 3QJB 3QJC 3QJD 3QJE 3R5I 3S65 3S66 3SZK 3W4U 3WCP 3WHM 4FC3 4HHB 4IJ2 4L7Y 4M4A 4M4B 4MQC 4MQG 4MQH 4MQI 4N7N 4N7O 4N7P 4N8T 4NI0 4NI1 6HBW
PDBsum	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 2M6Z 2W6V 2W72 2YRS 3B75 3D17 3D7O 3DUT 3HHB 3HXN 3IC0 3IC2 3KMF 3NL7 3NMM 3ODQ 3ONZ 3OO4 3OO5 3P5Q 3QJB 3QJC 3QJD 3QJE 3R5I 3S65 3S66 3SZK 3W4U 3WCP 3WHM 4FC3 4HHB 4IJ2 4L7Y 4M4A 4M4B 4MQC 4MQG 4MQH 4MQI 4N7N 4N7O 4N7P 4N8T 4NI0 4NI1 6HBW
ProteinModelPortal	P68871
SMR	P68871
BioGrid	109293
IntAct	P68871
MINT	MINT-5000306
ChEMBL	CHEMBL2095168
DrugBank	DB00893
PhosphoSite	P68871
DMDM	56749856
REPRODUCTION-2DPAGE	IPI00654755 P68871
SWISS-2DPAGE	P68871
UCD-2DPAGE	P02023 P68871
MaxQB	P68871
PaxDb	P68871
PeptideAtlas	P68871
PRIDE	P68871
DNASU	3043
Ensembl	ENST00000335295
GeneID	3043
KEGG	hsa:3043
UCSC	uc001mae.1
CTD	3043
GeneCards	GC11M005264
GeneReviews	HBB
HGNC	HGNC:4827
HPA	CAB009526 HPA043234
MIM	140700 141900 603902 603903 613985
neXtProt	NX_P68871
Orphanet	330041 231222 231214 231237 231226 178330 231242 2132 90039 231249 2133 330032 46532 251380 251359 251365 251370 251375 232
PharmGKB	PA29202
eggNOG	NOG269316
GeneTree	ENSGT00760000119197
HOVERGEN	HBG009709
InParanoid	P68871
KO	K13823
OMA	WTRRFFE
OrthoDB	EOG7B8S5H
PhylomeDB	P68871
TreeFam	TF333268
Reactome	REACT_121329 REACT_121380 REACT_160163 REACT_24970
ChiTaRS	HBB
EvolutionaryTrace	P68871
GeneWiki	HBB
GenomeRNAi	3043
NextBio	12048
PMAP-CutDB	P68871
PRO	PR:P68871
Proteomes	UP000005640
Bgee	P68871
ExpressionAtlas	P68871
Genevestigator	P68871
GO	GO:0072562 GO:0005829 GO:0071682 GO:0005576 GO:0070062 GO:0031838 GO:0005833 GO:0020037 GO:0030492 GO:0005506 GO:0019825 GO:0005344 GO:0015701 GO:0007596 GO:0042744 GO:0030185 GO:0055114 GO:0015671 GO:0070527 GO:0010942 GO:0045429 GO:0051291 GO:0008217 GO:0050880 GO:0070293 GO:0042542 GO:0044281
Gene3D	1.10.490.10
InterPro	IPR000971 IPR009050 IPR012292 IPR002337
Pfam	PF00042
PRINTS	PR00814
SUPFAM	SSF46458
PROSITE	PS01033

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
Contributes to	GO:0031720	haptoglobin binding	PMID:19740759^[1]	ECO:0000314			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]	ECO:0000314			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]	ECO:0000314			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]	ECO:0000314			P		Fig 3: large MW aggregates can be seen after addition of hydrogen peroxide when both haemoglobin and haptoglobin are present.	complete
part_of	GO:0005615	extracellular space	PMID:21805676^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019825	oxygen binding	PMID:28066926^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070527	platelet aggregation	PMID:23382103^[5]	ECO:0007001	high throughput mutant phenotypic evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0072562	blood microparticle	PMID:22516433^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	PMID:19740759^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042744	hydrogen peroxide catabolic process	PMID:19740759^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042542	response to hydrogen peroxide	PMID:19740759^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031838	haptoglobin-hemoglobin complex	PMID:19740759^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
contributes_to	GO:0031720	haptoglobin binding	PMID:19740759^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010942	positive regulation of cell death	PMID:19740759^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005833	hemoglobin complex	PMID:19740759^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
contributes_to	GO:0004601	peroxidase activity	PMID:19740759^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0070293	renal absorption	PMID:18465053^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070293	renal absorption	PMID:18974585^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045429	positive regulation of nitric oxide biosynthetic process	PMID:7965120^[10]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030492	hemoglobin binding	PMID:1512262^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030185	nitric oxide transport	PMID:8292032^[12]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019825	oxygen binding	PMID:11747442^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0015671	oxygen transport	PMID:11747442^[13]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0015671	oxygen transport	PMID:1301199^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005833	hemoglobin complex	PMID:1301199^[14]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005833	hemoglobin complex	PMID:10588683^[15]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005344	oxygen carrier activity	PMID:11747442^[13]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005344	oxygen carrier activity	PMID:1301199^[14]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043177	organic acid binding	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154218 RGD:1359209	F		Seeded From UniProt	complete
involved_in	GO:0042744	hydrogen peroxide catabolic process	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154218 UniProtKB:P68871 UniProtKB:P69905	P		Seeded From UniProt	complete
part_of	GO:0031838	haptoglobin-hemoglobin complex	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154218 UniProtKB:P68871 UniProtKB:P69905	C		Seeded From UniProt	complete
enables	GO:0031721	hemoglobin alpha binding	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154350 RGD:2783	F		Seeded From UniProt	complete
contributes_to	GO:0031720	haptoglobin binding	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154218 UniProtKB:P68871 UniProtKB:P69905	F		Seeded From UniProt	complete
enables	GO:0020037	heme binding	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154218 RGD:1359209 RGD:620306	F		Seeded From UniProt	complete
enables	GO:0019825	oxygen binding	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96022 PANTHER:PTN000154218 UniProtKB:P68871 UniProtKB:Q5QRU6	F		Seeded From UniProt	complete
enables	GO:0019825	oxygen binding	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96022 PANTHER:PTN000154218 RGD:1359209 RGD:2783 UniProtKB:P68871 UniProtKB:Q5QRU6	F		Seeded From UniProt	complete
part_of	GO:0005833	hemoglobin complex	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96021 MGI:MGI:96022 PANTHER:PTN000154218 RGD:1305115 RGD:1359209 RGD:2783 RGD:620306 UniProtKB:P68871 UniProtKB:P69905	C		Seeded From UniProt	complete
enables	GO:0005344	oxygen carrier activity	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96021 PANTHER:PTN000154218	F		Seeded From UniProt	complete
contributes_to	GO:0004601	peroxidase activity	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154218 UniProtKB:P68871 UniProtKB:P69905	F		Seeded From UniProt	complete
involved_in	GO:0098869	cellular oxidant detoxification	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004601	P		Seeded From UniProt	complete
involved_in	GO:0098869	cellular oxidant detoxification	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004601	P		Seeded From UniProt	complete
part_of	GO:0005833	hemoglobin complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002337	C		Seeded From UniProt	complete
involved_in	GO:0015671	oxygen transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002337	P		Seeded From UniProt	complete
enables	GO:0019825	oxygen binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012292	F		Seeded From UniProt	complete
enables	GO:0020037	heme binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000971 InterPro:IPR002337 InterPro:IPR012292	F		Seeded From UniProt	complete
involved_in	GO:0015671	oxygen transport	PMID:1540659^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005833	hemoglobin complex	PMID:1540659^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1904724	tertiary granule lumen	Reactome:R-HSA-6798745	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0071682	endocytic vesicle lumen	Reactome:R-HSA-2230938	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0015701	bicarbonate transport	Reactome:R-HSA-1247673 Reactome:R-HSA-1237044	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007596	blood coagulation	Reactome:R-HSA-109582	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006898	receptor-mediated endocytosis	Reactome:R-HSA-2173782	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-6806831 Reactome:R-HSA-1247668 Reactome:R-HSA-1237325 Reactome:R-HSA-1008220	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6800434 Reactome:R-HSA-6798745 Reactome:R-HSA-2230938 Reactome:R-HSA-2168889 Reactome:R-HSA-2168885 Reactome:R-HSA-2168884 Reactome:R-HSA-2168883	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005344	oxygen carrier activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0561	F		Seeded From UniProt	complete
involved_in	GO:0050880	regulation of blood vessel size	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0838	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
involved_in	GO:0015671	oxygen transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0561	P		Seeded From UniProt	complete
involved_in	GO:0008217	regulation of blood pressure	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0382	P		Seeded From UniProt	complete
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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
↑ Fornander, L et al. (2011) Innate immunity proteins and a new truncated form of SPLUNC1 in nasopharyngeal aspirates from infants with respiratory syncytial virus infection. Proteomics Clin Appl 5 513-22 PubMed GONUTS page
↑ Mañú Pereira, MD et al. (2017) Low affinity hemoglobinopathy (Hb Vigo) due to a new mutation of beta globin gene (c200 A>T; Lys>Ile). A cause of rare anemia misdiagnosis. Am. J. Hematol. 92 E38-E40 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Fröbel, J et al. (2013) Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes. Mol. Cell Proteomics 12 1272-80 PubMed GONUTS page
↑ Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Sadeghi-Bojd, S et al. (2008) Renal tubular function in patients with beta-thalassaemia major in Zahedan, southeast Iran. Singapore Med J 49 410-2 PubMed GONUTS page
↑ Prabahar, MR et al. (2008) Renal tubular dysfunction with nephrocalcinosis in a patient with beta thalassemia minor. Saudi J Kidney Dis Transpl 19 964-8 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
↑ 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
↑ 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
↑ ^13.0 ^13.1 ^13.2 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
↑ ^14.0 ^14.1 ^14.2 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
↑ 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
↑ ^16.00 ^16.01 ^16.02 ^16.03 ^16.04 ^16.05 ^16.06 ^16.07 ^16.08 ^16.09 ^16.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^17.0 ^17.1 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:19740759-1] 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:21805676-2] Fornander, L et al. (2011) Innate immunity proteins and a new truncated form of SPLUNC1 in nasopharyngeal aspirates from infants with respiratory syncytial virus infection. Proteomics Clin Appl 5 513-22 PubMed GONUTS page

[PMID:28066926-3] Mañú Pereira, MD et al. (2017) Low affinity hemoglobinopathy (Hb Vigo) due to a new mutation of beta globin gene (c200 A>T; Lys>Ile). A cause of rare anemia misdiagnosis. Am. J. Hematol. 92 E38-E40 PubMed GONUTS page

[PMID:23533145-4] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:23382103-5] Fröbel, J et al. (2013) Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes. Mol. Cell Proteomics 12 1272-80 PubMed GONUTS page

[PMID:22516433-6] Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page

[PMID:19056867-7] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:18465053-8] Sadeghi-Bojd, S et al. (2008) Renal tubular function in patients with beta-thalassaemia major in Zahedan, southeast Iran. Singapore Med J 49 410-2 PubMed GONUTS page

[PMID:18974585-9] Prabahar, MR et al. (2008) Renal tubular dysfunction with nephrocalcinosis in a patient with beta thalassemia minor. Saudi J Kidney Dis Transpl 19 964-8 PubMed GONUTS page

[PMID:7965120-10] 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:1512262-11] 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:8292032-12] 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:11747442-13] 13.0 ^13.1 ^13.2 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:1301199-14] 14.0 ^14.1 ^14.2 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:10588683-15] 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:21873635-16] 16.00 ^16.01 ^16.02 ^16.03 ^16.04 ^16.05 ^16.06 ^16.07 ^16.08 ^16.09 ^16.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:1540659-17] 17.0 ^17.1 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

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