HBA_HUMAN - dbPTM
HBA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HBA_HUMAN
UniProt AC P69905
Protein Name Hemoglobin subunit alpha
Gene Name HBA1
Organism Homo sapiens (Human).
Sequence Length 142
Subcellular Localization
Protein Description Involved in oxygen transport from the lung to the various peripheral tissues..
Protein Sequence MVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MVLSPADKTNV
----CCCCHHHCCCC
13.4623401153
4O-linked_Glycosylation----MVLSPADKTNV
----CCCCHHHCCCC
13.469402357
8AcetylationMVLSPADKTNVKAAW
CCCCHHHCCCCHHHH
44.077617745
8SuccinylationMVLSPADKTNVKAAW
CCCCHHHCCCCHHHH
44.07-
8GlycationMVLSPADKTNVKAAW
CCCCHHHCCCCHHHH
44.07-
8N-linked_GlycosylationMVLSPADKTNVKAAW
CCCCHHHCCCCHHHH
44.077358733
8SuccinylationMVLSPADKTNVKAAW
CCCCHHHCCCCHHHH
44.07-
9PhosphorylationVLSPADKTNVKAAWG
CCCHHHCCCCHHHHH
45.8824972180
12AcetylationPADKTNVKAAWGKVG
HHHCCCCHHHHHHCC
34.1627178108
12SuccinylationPADKTNVKAAWGKVG
HHHCCCCHHHHHHCC
34.16-
12SuccinylationPADKTNVKAAWGKVG
HHHCCCCHHHHHHCC
34.16-
17GlycationNVKAAWGKVGAHAGE
CCHHHHHHCCHHHHH
27.13-
17N-linked_GlycosylationNVKAAWGKVGAHAGE
CCHHHHHHCCHHHHH
27.137358733
17SuccinylationNVKAAWGKVGAHAGE
CCHHHHHHCCHHHHH
27.13-
17AcetylationNVKAAWGKVGAHAGE
CCHHHHHHCCHHHHH
27.1319608861
17SuccinylationNVKAAWGKVGAHAGE
CCHHHHHHCCHHHHH
27.13-
17UbiquitinationNVKAAWGKVGAHAGE
CCHHHHHHCCHHHHH
27.13-
21MethylationAWGKVGAHAGEYGAE
HHHHCCHHHHHHHHH
28.47-
25NitrationVGAHAGEYGAEALER
CCHHHHHHHHHHHHH
22.25-
25PhosphorylationVGAHAGEYGAEALER
CCHHHHHHHHHHHHH
22.2523911959
36O-linked_GlycosylationALERMFLSFPTTKTY
HHHHHHHHCCCCCCC
20.229402381
36PhosphorylationALERMFLSFPTTKTY
HHHHHHHHCCCCCCC
20.2223025827
39PhosphorylationRMFLSFPTTKTYFPH
HHHHHCCCCCCCCCC
38.6223025827
40PhosphorylationMFLSFPTTKTYFPHF
HHHHCCCCCCCCCCC
22.9423025827
41UbiquitinationFLSFPTTKTYFPHFD
HHHCCCCCCCCCCCC
43.64-
41AcetylationFLSFPTTKTYFPHFD
HHHCCCCCCCCCCCC
43.6426051181
41GlycationFLSFPTTKTYFPHFD
HHHCCCCCCCCCCCC
43.64-
41SuccinylationFLSFPTTKTYFPHFD
HHHCCCCCCCCCCCC
43.64-
41N-linked_GlycosylationFLSFPTTKTYFPHFD
HHHCCCCCCCCCCCC
43.647358733
41SuccinylationFLSFPTTKTYFPHFD
HHHCCCCCCCCCCCC
43.64-
42PhosphorylationLSFPTTKTYFPHFDL
HHCCCCCCCCCCCCC
28.4419060867
43NitrationSFPTTKTYFPHFDLS
HCCCCCCCCCCCCCC
19.37-
43PhosphorylationSFPTTKTYFPHFDLS
HCCCCCCCCCCCCCC
19.3721253578
50PhosphorylationYFPHFDLSHGSAQVK
CCCCCCCCCCCEECC
27.8723025827
53PhosphorylationHFDLSHGSAQVKGHG
CCCCCCCCEECCCCH
15.3123025827
57UbiquitinationSHGSAQVKGHGKKVA
CCCCEECCCCHHHHH
32.86-
57AcetylationSHGSAQVKGHGKKVA
CCCCEECCCCHHHHH
32.867640557
61UbiquitinationAQVKGHGKKVADALT
EECCCCHHHHHHHHH
38.10-
61AcetylationAQVKGHGKKVADALT
EECCCCHHHHHHHHH
38.107612859
62N-linked_GlycosylationQVKGHGKKVADALTN
ECCCCHHHHHHHHHH
47.447358733
62GlycationQVKGHGKKVADALTN
ECCCCHHHHHHHHHH
47.44-
62AcetylationQVKGHGKKVADALTN
ECCCCHHHHHHHHHH
47.447824027
68PhosphorylationKKVADALTNAVAHVD
HHHHHHHHHHHHCCC
23.8928857561
77SulfoxidationAVAHVDDMPNALSAL
HHHCCCCCCHHHHHH
2.0821192028
82PhosphorylationDDMPNALSALSDLHA
CCCCHHHHHHHHHHH
25.4228192239
91AcetylationLSDLHAHKLRVDPVN
HHHHHHHCCCCCCCC
38.4827178108
100AcetylationRVDPVNFKLLSHCLL
CCCCCCHHHHHHHHH
43.237664937
103PhosphorylationPVNFKLLSHCLLVTL
CCCHHHHHHHHHHHH
23.6922673903
105S-nitrosocysteineNFKLLSHCLLVTLAA
CHHHHHHHHHHHHHH
2.56-
105S-nitrosylationNFKLLSHCLLVTLAA
CHHHHHHHHHHHHHH
2.5622178444
109PhosphorylationLSHCLLVTLAAHLPA
HHHHHHHHHHHCCCC
15.6222673903
119PhosphorylationAHLPAEFTPAVHASL
HCCCCCCCHHHHHHH
11.2222673903
125PhosphorylationFTPAVHASLDKFLAS
CCHHHHHHHHHHHHH
23.4022673903
132PhosphorylationSLDKFLASVSTVLTS
HHHHHHHHHHHHHHC
20.8123025827
134PhosphorylationDKFLASVSTVLTSKY
HHHHHHHHHHHHCCC
15.4229691806
134O-linked_GlycosylationDKFLASVSTVLTSKY
HHHHHHHHHHHHCCC
15.429402513
135PhosphorylationKFLASVSTVLTSKYR
HHHHHHHHHHHCCCC
19.8523025827
138PhosphorylationASVSTVLTSKYR---
HHHHHHHHCCCC---
20.8823025827
139PhosphorylationSVSTVLTSKYR----
HHHHHHHCCCC----
24.4323025827
140AcetylationVSTVLTSKYR-----
HHHHHHCCCC-----
39.5527178108
141PhosphorylationSTVLTSKYR------
HHHHHCCCC------
22.71-
141NitrationSTVLTSKYR------
HHHHHCCCC------
22.71-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of HBA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HBA_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of HBA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HBB_HUMANHBBphysical
16169070
CRYAB_HUMANCRYABphysical
22815750

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
OMIM Disease
140700Heinz body anemias (HEIBAN)
604131Alpha-thalassemia (A-THAL)
Note=Alpha(0)-thalassemia is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.
613978
Kegg Drug
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
DrugBank
DB00893Iron Dextran
DB00358Mefloquine
Regulatory Network of HBA_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Sites of nonenzymatic glycosylation of human hemoglobin A.";
Shapiro R., McManus M.J., Zalut C., Bunn H.F.;
J. Biol. Chem. 255:3120-3127(1980).
Cited for: GLYCATION AT LYS-8; LYS-17; LYS-41 AND LYS-62, AND LACK OF GLYCATIONAT LYS-12; LYS-57; LYS-61; LYS-91 AND LYS-100.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-43, AND MASSSPECTROMETRY.

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