HBG2_HUMAN - dbPTM
HBG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HBG2_HUMAN
UniProt AC P69892
Protein Name Hemoglobin subunit gamma-2
Gene Name HBG2
Organism Homo sapiens (Human).
Sequence Length 147
Subcellular Localization
Protein Description Gamma chains make up the fetal hemoglobin F, in combination with alpha chains..
Protein Sequence MGHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTGVASALSSRYH
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
2Acetylation------MGHFTEEDK
------CCCCCHHHH
25.315554303
5Phosphorylation---MGHFTEEDKATI
---CCCCCHHHHHHH
32.5624719451
9AcetylationGHFTEEDKATITSLW
CCCCHHHHHHHHHHH
51.1930584561
9UbiquitinationGHFTEEDKATITSLW
CCCCHHHHHHHHHHH
51.19-
11PhosphorylationFTEEDKATITSLWGK
CCHHHHHHHHHHHEE
30.4523186163
13PhosphorylationEEDKATITSLWGKVN
HHHHHHHHHHHEEEC
17.2623186163
14PhosphorylationEDKATITSLWGKVNV
HHHHHHHHHHEEECH
20.4823917254
18UbiquitinationTITSLWGKVNVEDAG
HHHHHHEEECHHHCC
21.03-
28PhosphorylationVEDAGGETLGRLLVV
HHHCCCCCCHHHEEE
37.4728857561
36PhosphorylationLGRLLVVYPWTQRFF
CHHHEEEECCHHHHH
5.8824927040
39PhosphorylationLLVVYPWTQRFFDSF
HEEEECCHHHHHHHC
12.8328857561
45PhosphorylationWTQRFFDSFGNLSSA
CHHHHHHHCCCCCCH
29.8722673903
50PhosphorylationFDSFGNLSSASAIMG
HHHCCCCCCHHHHCC
28.0530242111
51PhosphorylationDSFGNLSSASAIMGN
HHCCCCCCHHHHCCC
29.4330242111
53PhosphorylationFGNLSSASAIMGNPK
CCCCCCHHHHCCCCC
21.9230242111
60UbiquitinationSAIMGNPKVKAHGKK
HHHCCCCCHHHHHHH
61.44-
60AcetylationSAIMGNPKVKAHGKK
HHHCCCCCHHHHHHH
61.4430584569
62UbiquitinationIMGNPKVKAHGKKVL
HCCCCCHHHHHHHHH
40.57-
62AcetylationIMGNPKVKAHGKKVL
HCCCCCHHHHHHHHH
40.577289975
66AcetylationPKVKAHGKKVLTSLG
CCHHHHHHHHHHHHH
29.8230584573
66UbiquitinationPKVKAHGKKVLTSLG
CCHHHHHHHHHHHHH
29.82-
67UbiquitinationKVKAHGKKVLTSLGD
CHHHHHHHHHHHHHH
47.25-
70PhosphorylationAHGKKVLTSLGDAIK
HHHHHHHHHHHHHHH
25.5428857561
71PhosphorylationHGKKVLTSLGDAIKH
HHHHHHHHHHHHHHC
26.6228857561
77UbiquitinationTSLGDAIKHLDDLKG
HHHHHHHHCHHHHCC
39.57-
77AcetylationTSLGDAIKHLDDLKG
HHHHHHHHCHHHHCC
39.5730584577
83AcetylationIKHLDDLKGTFAQLS
HHCHHHHCCHHHHHH
64.00156877
83UbiquitinationIKHLDDLKGTFAQLS
HHCHHHHCCHHHHHH
64.00-
94S-nitrosylationAQLSELHCDKLHVDP
HHHHHHCCCCCCCCH
8.46-
96UbiquitinationLSELHCDKLHVDPEN
HHHHCCCCCCCCHHH
45.98-
96AcetylationLSELHCDKLHVDPEN
HHHHCCCCCCCCHHH
45.9830584565
113PhosphorylationLLGNVLVTVLAIHFG
HHHHHHHHHHHHHHC
12.97-
124PhosphorylationIHFGKEFTPEVQASW
HHHCCCCCHHHHHHH
21.4530242111
130PhosphorylationFTPEVQASWQKMVTG
CCHHHHHHHHHHHHH
16.9828857561
133UbiquitinationEVQASWQKMVTGVAS
HHHHHHHHHHHHHHH
29.13-
136PhosphorylationASWQKMVTGVASALS
HHHHHHHHHHHHHHH
23.5730242111
140PhosphorylationKMVTGVASALSSRYH
HHHHHHHHHHHHCCC
27.6030242111
143PhosphorylationTGVASALSSRYH---
HHHHHHHHHCCC---
16.7030242111
144PhosphorylationGVASALSSRYH----
HHHHHHHHCCC----
37.396186522

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 HBG2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2GAcetylation

5554303

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 HBG2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HBG2_HUMANHBG2physical
11514664
A4_HUMANAPPphysical
21832049
RSSA_HUMANRPSAphysical
21988832

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613977Cyanosis transient neonatal (TNCY)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HBG2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Human fetal hemoglobin F 1. Acetylation status.";
Stegink L.D., Meyer P.D., Brummel M.C.;
J. Biol. Chem. 246:3001-3007(1971).
Cited for: ACETYLATION AT GLY-2.
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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