| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MVHLTDAEK ------CCCCCHHHH | 5.21 | - | |
| 5 | Phosphorylation | ---MVHLTDAEKAAV ---CCCCCHHHHHHH | 20.48 | 21183079 | |
| 9 | Ubiquitination | VHLTDAEKAAVSCLW CCCCHHHHHHHHHHH | 43.28 | - | |
| 13 | Phosphorylation | DAEKAAVSCLWGKVN HHHHHHHHHHHCCCC | 9.96 | 17242355 | |
| 14 | S-nitrosylation | AEKAAVSCLWGKVNS HHHHHHHHHHCCCCC | 2.73 | 24895380 | |
| 14 | S-palmitoylation | AEKAAVSCLWGKVNS HHHHHHHHHHCCCCC | 2.73 | 28526873 | |
| 18 | Succinylation | AVSCLWGKVNSDEVG HHHHHHCCCCCCCCC | 27.02 | 23806337 | |
| 18 | Malonylation | AVSCLWGKVNSDEVG HHHHHHCCCCCCCCC | 27.02 | 26073543 | |
| 18 | Ubiquitination | AVSCLWGKVNSDEVG HHHHHHCCCCCCCCC | 27.02 | 27667366 | |
| 18 | Succinylation | AVSCLWGKVNSDEVG HHHHHHCCCCCCCCC | 27.02 | - | |
| 18 | Acetylation | AVSCLWGKVNSDEVG HHHHHHCCCCCCCCC | 27.02 | 21728379 | |
| 21 | Phosphorylation | CLWGKVNSDEVGGEA HHHCCCCCCCCCHHH | 37.83 | 27742792 | |
| 31 | Dimethylation | VGGEALGRLLVVYPW CCHHHHHHHEEEEEC | 26.21 | - | |
| 36 | Phosphorylation | LGRLLVVYPWTQRYF HHHHEEEEECCHHHH | 5.88 | 27180971 | |
| 39 | Phosphorylation | LLVVYPWTQRYFDSF HEEEEECCHHHHHCC | 9.92 | 23737553 | |
| 41 | Methylation | VVYPWTQRYFDSFGD EEEECCHHHHHCCCC | 27.06 | - | |
| 42 | Phosphorylation | VYPWTQRYFDSFGDL EEECCHHHHHCCCCH | 11.26 | 24925903 | |
| 45 | Phosphorylation | WTQRYFDSFGDLSSA CCHHHHHCCCCHHHH | 22.64 | 24925903 | |
| 50 | Phosphorylation | FDSFGDLSSASAIMG HHCCCCHHHHHHHHC | 28.70 | 24925903 | |
| 51 | Phosphorylation | DSFGDLSSASAIMGN HCCCCHHHHHHHHCC | 33.27 | 24925903 | |
| 53 | Phosphorylation | FGDLSSASAIMGNAK CCCHHHHHHHHCCCE | 21.92 | 25521595 | |
| 56 | Oxidation | LSSASAIMGNAKVKA HHHHHHHHCCCEEEE | 3.19 | 17242355 | |
| 60 | Acetylation | SAIMGNAKVKAHGKK HHHHCCCEEEECCCE | 48.55 | 23806337 | |
| 60 | Succinylation | SAIMGNAKVKAHGKK HHHHCCCEEEECCCE | 48.55 | - | |
| 60 | Ubiquitination | SAIMGNAKVKAHGKK HHHHCCCEEEECCCE | 48.55 | 27667366 | |
| 60 | Succinylation | SAIMGNAKVKAHGKK HHHHCCCEEEECCCE | 48.55 | 23806337 | |
| 62 | Acetylation | IMGNAKVKAHGKKVI HHCCCEEEECCCEEE | 33.68 | 7612865 | |
| 62 | Ubiquitination | IMGNAKVKAHGKKVI HHCCCEEEECCCEEE | 33.68 | - | |
| 67 | Acetylation | KVKAHGKKVITAFND EEEECCCEEEEECCC | 43.38 | 22733758 | |
| 67 | Ubiquitination | KVKAHGKKVITAFND EEEECCCEEEEECCC | 43.38 | - | |
| 70 | Phosphorylation | AHGKKVITAFNDGLN ECCCEEEEECCCCCH | 28.34 | 27180971 | |
| 81 | Phosphorylation | DGLNHLDSLKGTFAS CCCHHHHHHCHHHHH | 38.04 | 25521595 | |
| 83 | Ubiquitination | LNHLDSLKGTFASLS CHHHHHHCHHHHHHH | 60.91 | - | |
| 83 | Acetylation | LNHLDSLKGTFASLS CHHHHHHCHHHHHHH | 60.91 | 23954790 | |
| 83 | Malonylation | LNHLDSLKGTFASLS CHHHHHHCHHHHHHH | 60.91 | 26073543 | |
| 85 | Phosphorylation | HLDSLKGTFASLSEL HHHHHCHHHHHHHHH | 17.91 | 22324799 | |
| 88 | Phosphorylation | SLKGTFASLSELHCD HHCHHHHHHHHHCCC | 28.39 | 24925903 | |
| 90 | Phosphorylation | KGTFASLSELHCDKL CHHHHHHHHHCCCCC | 35.30 | 24925903 | |
| 94 | S-palmitoylation | ASLSELHCDKLHVDP HHHHHHCCCCCCCCH | 8.46 | 28526873 | |
| 94 | S-nitrosylation | ASLSELHCDKLHVDP HHHHHHCCCCCCCCH | 8.46 | 22178444 | |
| 94 | S-nitrosocysteine | ASLSELHCDKLHVDP HHHHHHCCCCCCCCH | 8.46 | - | |
| 96 | Malonylation | LSELHCDKLHVDPEN HHHHCCCCCCCCHHH | 45.98 | 25418362 | |
| 96 | Acetylation | LSELHCDKLHVDPEN HHHHCCCCCCCCHHH | 45.98 | 23954790 | |
| 96 | Ubiquitination | LSELHCDKLHVDPEN HHHHCCCCCCCCHHH | 45.98 | - | |
| 105 | Methylation | HVDPENFRLLGNMIV CCCHHHHHHHHHEEE | 40.35 | - | |
| 105 | Asymmetric dimethylarginine | HVDPENFRLLGNMIV CCCHHHHHHHHHEEE | 40.35 | - | |
| 121 | Ubiquitination | VLGHHLGKDFTPAAQ EECCCCCCCCCHHHH | 56.90 | - | |
| 121 | Acetylation | VLGHHLGKDFTPAAQ EECCCCCCCCCHHHH | 56.90 | 156751 | |
| 124 | Phosphorylation | HHLGKDFTPAAQAAF CCCCCCCCHHHHHHH | 23.35 | 27742792 | |
| 133 | Ubiquitination | AAQAAFQKVVAGVAT HHHHHHHHHHHHHHH | 32.02 | - | |
| 133 | Acetylation | AAQAAFQKVVAGVAT HHHHHHHHHHHHHHH | 32.02 | 21728379 | |
| 140 | Phosphorylation | KVVAGVATALAHKYH HHHHHHHHHHHHHCC | 21.57 | 19060867 | |
| 145 | Malonylation | VATALAHKYH----- HHHHHHHHCC----- | 39.14 | 26073543 | |
| 145 | Phosphoglycerylation | VATALAHKYH----- HHHHHHHHCC----- | 39.14 | - | |
| 145 | Ubiquitination | VATALAHKYH----- HHHHHHHHCC----- | 39.14 | 27667366 | |
| 145 | Acetylation | VATALAHKYH----- HHHHHHHHCC----- | 39.14 | 21728379 | |
| 146 | Phosphorylation | ATALAHKYH------ HHHHHHHCC------ | 11.68 | - |
| 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 !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HBB1_MOUSE !! | ||||||
* 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 !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of HBB1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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. | |