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Protein Page:
HBB (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
HBB Involved in oxygen transport from the lung to the various peripheral tissues. Defects in HBB may be a cause of Heinz body anemias (HEIBAN). This is a form of non-spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. Defects in HBB are the cause of beta-thalassemia (B-THAL). A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of beta-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. Absence of beta chain causes beta(0)-thalassemia, while reduced amounts of detectable beta globin causes beta(+)-thalassemia. In the severe forms of beta-thalassemia, the excess alpha globin chains accumulate in the developing erythroid precursors in the marrow. Their deposition leads to a vast increase in erythroid apoptosis that in turn causes ineffective erythropoiesis and severe microcytic hypochromic anemia. Clinically, beta-thalassemia is divided into thalassemia major which is transfusion dependent, thalassemia intermedia (of intermediate severity), and thalassemia minor that is asymptomatic. Defects in HBB are the cause of sickle cell anemia (SKCA); also known as sickle cell disease. Sickle cell anemia is characterized by abnormally shaped red cells resulting in chronic anemia and periodic episodes of pain, serious infections and damage to vital organs. Normal red blood cells are round and flexible and flow easily through blood vessels, but in sickle cell anemia, the abnormal hemoglobin (called Hb S) causes red blood cells to become stiff. They are C-shaped and resembles a sickle. These stiffer red blood cells can led to microvascular occlusion thus cutting off the blood supply to nearby tissues. Defects in HBB are the cause of beta-thalassemia dominant inclusion body type (B-THALIB). An autosomal dominant form of beta thalassemia characterized by moderate anemia, lifelong jaundice, cholelithiasis and splenomegaly, marked morphologic changes in the red cells, erythroid hyperplasia of the bone marrow with increased numbers of multinucleate red cell precursors, and the presence of large inclusion bodies in the normoblasts, both in the marrow and in the peripheral blood after splenectomy. Belongs to the globin family. Note: This description may include information from UniProtKB.
Protein type: Carrier protein
Chromosomal Location of Human Ortholog: 11p15.5
Cellular Component: hemoglobin complex; extracellular region; cytosol
Molecular Function: haptoglobin binding; protein binding; peroxidase activity; hemoglobin binding; iron ion binding; heme binding; oxygen binding; oxygen transporter activity
Biological Process: positive regulation of nitric oxide biosynthetic process; response to hydrogen peroxide; nitric oxide transport; oxygen transport; bicarbonate transport; hydrogen peroxide catabolic process; protein heterooligomerization; regulation of blood pressure; blood coagulation; regulation of blood vessel size
Reference #:  P68871 (UniProtKB)
Alt. Names/Synonyms: beta globin chain; Beta-globin; CD113t-C; HBB; Hemoglobin beta chain; Hemoglobin subunit beta; hemoglobin, beta; LVV-hemorphin-7
Gene Symbols: HBB
Molecular weight: 15,998 Da
Basal Isoelectric point: 6.74  Predict pI for various phosphorylation states
Select Structure to View Below

HBB

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 T5-p ___MVHLtPEEksAV
0 6 K9-ac VHLtPEEksAVtALW
0 3 K9 VHLtPEEKsAVtALW
0 4 S10-p HLtPEEksAVtALWG
0 2 T13-p PEEksAVtALWGkVN
0 4 K18-ac AVtALWGkVNVDEVG
0 9 K18 AVtALWGKVNVDEVG
0 281 Y36-p LGRLLVVyPWtQRFF
0 8 T39-p LLVVyPWtQRFFEsF
0 2 R41 VVyPWtQRFFEsFGD
0 3 F42 VyPWtQRFFEsFGDL
0 27 S45-p WtQRFFEsFGDLstP
0 7 S50-p FEsFGDLstPDAVMG
0 1 S50-gl FEsFGDLstPDAVMG
0 8 T51-p EsFGDLstPDAVMGN
0 8 D53 FGDLstPDAVMGNPk
0 37 K60-ac DAVMGNPkVkAHGkK
0 13 K60 DAVMGNPKVkAHGkK
0 7 K62-ac VMGNPkVkAHGkKVL
0 2 K62 VMGNPkVKAHGkKVL
0 1 K66-ac PkVkAHGkKVLGAFs
0 4 K67 kVkAHGkKVLGAFsD
0 1 S73-gl kKVLGAFsDGLAHLD
0 1 A77 GAFsDGLAHLDNLkG
0 5 A77 GAFsDGLAHLDNLkG
0 11 K83-ac LAHLDNLkGtFAtLS
0 6 K83 LAHLDNLKGtFAtLS
0 1 T85-gl HLDNLkGtFAtLSEL
0 23 T88-p NLkGtFAtLSELHCD
0 4 S90 kGtFAtLSELHCDKL
0 5 K96 LSELHCDKLHVDPEN
0 15 K96 LSELHCDKLHVDPEN
0 1 R105 HVDPENFRLLGNVLV
0 28 K121-ac VLAHHFGkEFtPPVQ
0 5 T124-p HHFGkEFtPPVQAAy
0 353 Y131-p tPPVQAAyQkVVAGV
0 4 K133-ac PVQAAyQkVVAGVAN
0 1 K133 PVQAAyQKVVAGVAN
0 20 N140 kVVAGVANALAHkyH
0 62 K145-ac VANALAHkyH_____
0 4 K145 VANALAHKyH_____
0 538 Y146-p ANALAHkyH______
  mouse

 
T5-p ___MVHLtDAEksAV
K9 VHLtDAEKsAVsCLW
K9-ub VHLtDAEksAVsCLW
S10-p HLtDAEksAVsCLWA
S13-p DAEksAVsCLWAkVN
K18-ac AVsCLWAkVNPDEVG
K18-ub AVsCLWAkVNPDEVG
Y36-p LGRLLVVyPWtQryF
T39-p LLVVyPWtQryFDsF
R41-m1 VVyPWtQryFDsFGD
Y42-p VyPWtQryFDsFGDL
S45-p WtQryFDsFGDLssA
S50-p FDsFGDLssAsAIMG
S50 FDsFGDLSsAsAIMG
S51-p DsFGDLssAsAIMGN
S53-p FGDLssAsAIMGNPk
K60-ac sAIMGNPkVKAHGKk
K60-ub sAIMGNPkVKAHGKk
K62 IMGNPkVKAHGKkVI
K62 IMGNPkVKAHGKkVI
K66 PkVKAHGKkVITAFN
K67-ub kVKAHGKkVITAFNE
N73 KkVITAFNEGLkNLD
K77-ac TAFNEGLkNLDNLkG
K77-ub TAFNEGLkNLDNLkG
K83-ac LkNLDNLkGTFAsLs
K83-ub LkNLDNLkGTFAsLs
T85 NLDNLkGTFAsLsEL
S88-p NLkGTFAsLsELHCD
S90-p kGTFAsLsELHCDkL
K96-ac LsELHCDkLHVDPEN
K96-ub LsELHCDkLHVDPEN
R105-m2 HVDPENFrLLGNAIV
K121-ac VLGHHLGkDFtPAAQ
T124-p HHLGkDFtPAAQAAF
F131 tPAAQAAFQkVVAGV
K133-ac AAQAAFQkVVAGVAt
K133-ub AAQAAFQkVVAGVAt
T140-p kVVAGVAtALAHkyH
K145-ac VAtALAHkyH_____
K145-ub VAtALAHkyH_____
Y146-p AtALAHkyH______
  rat

 
T5 ___MVHLTDAEkAAV
K9-ac VHLTDAEkAAVNGLW
K9 VHLTDAEKAAVNGLW
A10 HLTDAEkAAVNGLWG
N13 DAEkAAVNGLWGkVN
K18-ac AVNGLWGkVNPDDVG
K18-ub AVNGLWGkVNPDDVG
Y36-p LGRLLVVyPWTQRyF
T39 LLVVyPWTQRyFDsF
R41 VVyPWTQRyFDsFGD
Y42-p VyPWTQRyFDsFGDL
S45-p WTQRyFDsFGDLSsA
S50 FDsFGDLSsAsAIMG
S50 FDsFGDLSsAsAIMG
S51-p DsFGDLSsAsAIMGN
S53-p FGDLSsAsAIMGNPk
K60 sAIMGNPKVkAHGKK
K60-ub sAIMGNPkVkAHGKK
K62 IMGNPkVKAHGKKVI
K62-ub IMGNPkVkAHGKKVI
K66 PkVkAHGKKVINAFN
K67 kVkAHGKKVINAFND
N73 KKVINAFNDGLkHLD
K77-ac NAFNDGLkHLDNLkG
K77-ub NAFNDGLkHLDNLkG
K83-ac LkHLDNLkGTFAHLS
K83 LkHLDNLKGTFAHLS
T85 HLDNLkGTFAHLSEL
H88 NLkGTFAHLSELHCD
S90 kGTFAHLSELHCDkL
K96-ac LSELHCDkLHVDPEN
K96-ub LSELHCDkLHVDPEN
R105 HVDPENFRLLGNMIV
K121 VLGHHLGKEFTPCAQ
T124 HHLGKEFTPCAQAAF
F131 TPCAQAAFQkVVAGV
K133-ac CAQAAFQkVVAGVAs
K133 CAQAAFQKVVAGVAs
S140-p kVVAGVAsALAHkyH
K145-ac VAsALAHkyH_____
K145 VAsALAHKyH_____
Y146-p AsALAHkyH______
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