HBB1_MOUSE - dbPTM
HBB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HBB1_MOUSE
UniProt AC P02088
Protein Name Hemoglobin subunit beta-1
Gene Name Hbb-b1
Organism Mus musculus (Mouse).
Sequence Length 147
Subcellular Localization
Protein Description Involved in oxygen transport from the lung to the various peripheral tissues..
Protein Sequence MVHLTDAEKAAVSCLWGKVNSDEVGGEALGRLLVVYPWTQRYFDSFGDLSSASAIMGNAKVKAHGKKVITAFNDGLNHLDSLKGTFASLSELHCDKLHVDPENFRLLGNMIVIVLGHHLGKDFTPAAQAAFQKVVAGVATALAHKYH
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------MVHLTDAEK
------CCCCCHHHH
5.21-
5Phosphorylation---MVHLTDAEKAAV
---CCCCCHHHHHHH
20.4821183079
9UbiquitinationVHLTDAEKAAVSCLW
CCCCHHHHHHHHHHH
43.28-
13PhosphorylationDAEKAAVSCLWGKVN
HHHHHHHHHHHCCCC
9.9617242355
14S-nitrosylationAEKAAVSCLWGKVNS
HHHHHHHHHHCCCCC
2.7324895380
14S-palmitoylationAEKAAVSCLWGKVNS
HHHHHHHHHHCCCCC
2.7328526873
18SuccinylationAVSCLWGKVNSDEVG
HHHHHHCCCCCCCCC
27.0223806337
18MalonylationAVSCLWGKVNSDEVG
HHHHHHCCCCCCCCC
27.0226073543
18UbiquitinationAVSCLWGKVNSDEVG
HHHHHHCCCCCCCCC
27.0227667366
18SuccinylationAVSCLWGKVNSDEVG
HHHHHHCCCCCCCCC
27.02-
18AcetylationAVSCLWGKVNSDEVG
HHHHHHCCCCCCCCC
27.0221728379
21PhosphorylationCLWGKVNSDEVGGEA
HHHCCCCCCCCCHHH
37.8327742792
31DimethylationVGGEALGRLLVVYPW
CCHHHHHHHEEEEEC
26.21-
36PhosphorylationLGRLLVVYPWTQRYF
HHHHEEEEECCHHHH
5.8827180971
39PhosphorylationLLVVYPWTQRYFDSF
HEEEEECCHHHHHCC
9.9223737553
41MethylationVVYPWTQRYFDSFGD
EEEECCHHHHHCCCC
27.06-
42PhosphorylationVYPWTQRYFDSFGDL
EEECCHHHHHCCCCH
11.2624925903
45PhosphorylationWTQRYFDSFGDLSSA
CCHHHHHCCCCHHHH
22.6424925903
50PhosphorylationFDSFGDLSSASAIMG
HHCCCCHHHHHHHHC
28.7024925903
51PhosphorylationDSFGDLSSASAIMGN
HCCCCHHHHHHHHCC
33.2724925903
53PhosphorylationFGDLSSASAIMGNAK
CCCHHHHHHHHCCCE
21.9225521595
56OxidationLSSASAIMGNAKVKA
HHHHHHHHCCCEEEE
3.1917242355
60AcetylationSAIMGNAKVKAHGKK
HHHHCCCEEEECCCE
48.5523806337
60SuccinylationSAIMGNAKVKAHGKK
HHHHCCCEEEECCCE
48.55-
60UbiquitinationSAIMGNAKVKAHGKK
HHHHCCCEEEECCCE
48.5527667366
60SuccinylationSAIMGNAKVKAHGKK
HHHHCCCEEEECCCE
48.5523806337
62AcetylationIMGNAKVKAHGKKVI
HHCCCEEEECCCEEE
33.687612865
62UbiquitinationIMGNAKVKAHGKKVI
HHCCCEEEECCCEEE
33.68-
67AcetylationKVKAHGKKVITAFND
EEEECCCEEEEECCC
43.3822733758
67UbiquitinationKVKAHGKKVITAFND
EEEECCCEEEEECCC
43.38-
70PhosphorylationAHGKKVITAFNDGLN
ECCCEEEEECCCCCH
28.3427180971
81PhosphorylationDGLNHLDSLKGTFAS
CCCHHHHHHCHHHHH
38.0425521595
83UbiquitinationLNHLDSLKGTFASLS
CHHHHHHCHHHHHHH
60.91-
83AcetylationLNHLDSLKGTFASLS
CHHHHHHCHHHHHHH
60.9123954790
83MalonylationLNHLDSLKGTFASLS
CHHHHHHCHHHHHHH
60.9126073543
85PhosphorylationHLDSLKGTFASLSEL
HHHHHCHHHHHHHHH
17.9122324799
88PhosphorylationSLKGTFASLSELHCD
HHCHHHHHHHHHCCC
28.3924925903
90PhosphorylationKGTFASLSELHCDKL
CHHHHHHHHHCCCCC
35.3024925903
94S-palmitoylationASLSELHCDKLHVDP
HHHHHHCCCCCCCCH
8.4628526873
94S-nitrosylationASLSELHCDKLHVDP
HHHHHHCCCCCCCCH
8.4622178444
94S-nitrosocysteineASLSELHCDKLHVDP
HHHHHHCCCCCCCCH
8.46-
96MalonylationLSELHCDKLHVDPEN
HHHHCCCCCCCCHHH
45.9825418362
96AcetylationLSELHCDKLHVDPEN
HHHHCCCCCCCCHHH
45.9823954790
96UbiquitinationLSELHCDKLHVDPEN
HHHHCCCCCCCCHHH
45.98-
105MethylationHVDPENFRLLGNMIV
CCCHHHHHHHHHEEE
40.35-
105Asymmetric dimethylarginineHVDPENFRLLGNMIV
CCCHHHHHHHHHEEE
40.35-
121UbiquitinationVLGHHLGKDFTPAAQ
EECCCCCCCCCHHHH
56.90-
121AcetylationVLGHHLGKDFTPAAQ
EECCCCCCCCCHHHH
56.90156751
124PhosphorylationHHLGKDFTPAAQAAF
CCCCCCCCHHHHHHH
23.3527742792
133UbiquitinationAAQAAFQKVVAGVAT
HHHHHHHHHHHHHHH
32.02-
133AcetylationAAQAAFQKVVAGVAT
HHHHHHHHHHHHHHH
32.0221728379
140PhosphorylationKVVAGVATALAHKYH
HHHHHHHHHHHHHCC
21.5719060867
145MalonylationVATALAHKYH-----
HHHHHHHHCC-----
39.1426073543
145PhosphoglycerylationVATALAHKYH-----
HHHHHHHHCC-----
39.14-
145UbiquitinationVATALAHKYH-----
HHHHHHHHCC-----
39.1427667366
145AcetylationVATALAHKYH-----
HHHHHHHHCC-----
39.1421728379
146PhosphorylationATALAHKYH------
HHHHHHHCC------
11.68-

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 HBB1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HBB1_MOUSE !!

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 HBB1_MOUSE !!

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

Oops, there are no PPI records of HBB1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HBB1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-81, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASSSPECTROMETRY.

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