HBE_HUMAN - dbPTM
HBE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HBE_HUMAN
UniProt AC P02100
Protein Name Hemoglobin subunit epsilon
Gene Name HBE1
Organism Homo sapiens (Human).
Sequence Length 147
Subcellular Localization
Protein Description The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin..
Protein Sequence MVHFTAEEKAAVTSLWSKMNVEEAGGEALGRLLVVYPWTQRFFDSFGNLSSPSAILGNPKVKAHGKKVLTSFGDAIKNMDNLKPAFAKLSELHCDKLHVDPENFKLLGNVMVIILATHFGKEFTPEVQAAWQKLVSAVAIALAHKYH
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
14PhosphorylationEEKAAVTSLWSKMNV
HHHHHHHHHHHHCCH
22.6523917254
17PhosphorylationAAVTSLWSKMNVEEA
HHHHHHHHHCCHHHH
27.5926074081
18UbiquitinationAVTSLWSKMNVEEAG
HHHHHHHHCCHHHHH
23.94-
36PhosphorylationLGRLLVVYPWTQRFF
HHHHEEHHHCHHHHH
5.8824927040
39PhosphorylationLLVVYPWTQRFFDSF
HEEHHHCHHHHHHCC
12.8328857561
45PhosphorylationWTQRFFDSFGNLSSP
CHHHHHHCCCCCCCH
29.8723186163
50PhosphorylationFDSFGNLSSPSAILG
HHCCCCCCCHHHHHC
44.1722817900
51PhosphorylationDSFGNLSSPSAILGN
HCCCCCCCHHHHHCC
26.4923917254
53PhosphorylationFGNLSSPSAILGNPK
CCCCCCHHHHHCCCC
29.8623917254
60AcetylationSAILGNPKVKAHGKK
HHHHCCCCHHHCCEE
61.44132949
60UbiquitinationSAILGNPKVKAHGKK
HHHHCCCCHHHCCEE
61.44-
66AcetylationPKVKAHGKKVLTSFG
CCHHHCCEEEHHHHH
29.8230589107
67UbiquitinationKVKAHGKKVLTSFGD
CHHHCCEEEHHHHHH
47.25-
70PhosphorylationAHGKKVLTSFGDAIK
HCCEEEHHHHHHHHH
25.6221082442
71PhosphorylationHGKKVLTSFGDAIKN
CCEEEHHHHHHHHHC
24.0719664995
77UbiquitinationTSFGDAIKNMDNLKP
HHHHHHHHCHHHCHH
48.19-
77AcetylationTSFGDAIKNMDNLKP
HHHHHHHHCHHHCHH
48.1930589113
83AcetylationIKNMDNLKPAFAKLS
HHCHHHCHHHHHHHH
40.3230589101
83UbiquitinationIKNMDNLKPAFAKLS
HHCHHHCHHHHHHHH
40.32-
145AcetylationVAIALAHKYH-----
HHHHHHHHCC-----
39.1430589095

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 HBE_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HBE_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 HBE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HBE_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HBE_HUMAN

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Related Literatures of Post-Translational Modification
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-36, AND MASSSPECTROMETRY.

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