| UniProt ID | HBB2_MOUSE | |
|---|---|---|
| UniProt AC | P02089 | |
| Protein Name | Hemoglobin subunit beta-2 | |
| Gene Name | Hbb-b2 | |
| 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 | MVHLTDAEKSAVSCLWAKVNPDEVGGEALGRLLVVYPWTQRYFDSFGDLSSASAIMGNPKVKAHGKKVITAFNEGLKNLDNLKGTFASLSELHCDKLHVDPENFRLLGNAIVIVLGHHLGKDFTPAAQAAFQKVVAGVATALAHKYH | |
| 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 | ---MVHLTDAEKSAV ---CCCCCHHHHHHH | 20.48 | 21183079 | |
| 9 | Ubiquitination | VHLTDAEKSAVSCLW CCCCHHHHHHHHHHE | 45.49 | 22790023 | |
| 10 | Phosphorylation | HLTDAEKSAVSCLWA CCCHHHHHHHHHHEE | 25.96 | 19060867 | |
| 13 | Phosphorylation | DAEKSAVSCLWAKVN HHHHHHHHHHEEECC | 11.83 | 19060867 | |
| 14 | S-palmitoylation | AEKSAVSCLWAKVNP HHHHHHHHHEEECCH | 2.71 | 28526873 | |
| 14 | S-nitrosylation | AEKSAVSCLWAKVNP HHHHHHHHHEEECCH | 2.71 | 24895380 | |
| 18 | Ubiquitination | AVSCLWAKVNPDEVG HHHHHEEECCHHHCC | 30.84 | - | |
| 18 | Acetylation | AVSCLWAKVNPDEVG HHHHHEEECCHHHCC | 30.84 | 21728379 | |
| 18 | Succinylation | AVSCLWAKVNPDEVG HHHHHEEECCHHHCC | 30.84 | - | |
| 18 | Malonylation | AVSCLWAKVNPDEVG HHHHHEEECCHHHCC | 30.84 | 26073543 | |
| 18 | Succinylation | AVSCLWAKVNPDEVG HHHHHEEECCHHHCC | 30.84 | 23806337 | |
| 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 EEECCHHHHHCCCCC | 11.26 | 24925903 | |
| 45 | Phosphorylation | WTQRYFDSFGDLSSA CCHHHHHCCCCCCCH | 22.64 | 24925903 | |
| 50 | Phosphorylation | FDSFGDLSSASAIMG HHCCCCCCCHHHHCC | 28.70 | 24925903 | |
| 51 | Phosphorylation | DSFGDLSSASAIMGN HCCCCCCCHHHHCCC | 33.27 | 24925903 | |
| 53 | Phosphorylation | FGDLSSASAIMGNPK CCCCCCHHHHCCCCC | 21.92 | 24925903 | |
| 56 | Oxidation | LSSASAIMGNPKVKA CCCHHHHCCCCCHHC | 4.19 | 17242355 | |
| 60 | Ubiquitination | SAIMGNPKVKAHGKK HHHCCCCCHHCCCCC | 61.44 | - | |
| 60 | Acetylation | SAIMGNPKVKAHGKK HHHCCCCCHHCCCCC | 61.44 | 23806337 | |
| 60 | Succinylation | SAIMGNPKVKAHGKK HHHCCCCCHHCCCCC | 61.44 | 23806337 | |
| 60 | Succinylation | SAIMGNPKVKAHGKK HHHCCCCCHHCCCCC | 61.44 | - | |
| 67 | Ubiquitination | KVKAHGKKVITAFNE CHHCCCCCHHHHHHH | 43.38 | 22790023 | |
| 67 | Phosphoglycerylation | KVKAHGKKVITAFNE CHHCCCCCHHHHHHH | 43.38 | - | |
| 77 | Acetylation | TAFNEGLKNLDNLKG HHHHHHHHCHHHHCC | 67.34 | 7617255 | |
| 77 | Ubiquitination | TAFNEGLKNLDNLKG HHHHHHHHCHHHHCC | 67.34 | 22790023 | |
| 83 | Acetylation | LKNLDNLKGTFASLS HHCHHHHCCHHHHHH | 63.26 | 7753599 | |
| 83 | Malonylation | LKNLDNLKGTFASLS HHCHHHHCCHHHHHH | 63.26 | 26073543 | |
| 83 | Ubiquitination | LKNLDNLKGTFASLS HHCHHHHCCHHHHHH | 63.26 | - | |
| 83 | Phosphoglycerylation | LKNLDNLKGTFASLS HHCHHHHCCHHHHHH | 63.26 | - | |
| 85 | Phosphorylation | NLDNLKGTFASLSEL CHHHHCCHHHHHHHH | 17.91 | 22324799 | |
| 88 | Phosphorylation | NLKGTFASLSELHCD HHCCHHHHHHHHCCC | 28.39 | 24925903 | |
| 90 | Phosphorylation | KGTFASLSELHCDKL CCHHHHHHHHCCCCC | 35.30 | 24925903 | |
| 94 | S-nitrosocysteine | ASLSELHCDKLHVDP HHHHHHCCCCCCCCH | 8.46 | - | |
| 96 | Acetylation | LSELHCDKLHVDPEN HHHHCCCCCCCCHHH | 45.98 | 160873 | |
| 96 | Ubiquitination | LSELHCDKLHVDPEN HHHHCCCCCCCCHHH | 45.98 | 22790023 | |
| 105 | Methylation | HVDPENFRLLGNAIV CCCHHHHHHHHCEEE | 40.35 | 24129315 | |
| 105 | Asymmetric dimethylarginine | HVDPENFRLLGNAIV CCCHHHHHHHHCEEE | 40.35 | - | |
| 121 | Ubiquitination | VLGHHLGKDFTPAAQ EECCCCCCCCCHHHH | 56.90 | - | |
| 121 | Acetylation | VLGHHLGKDFTPAAQ EECCCCCCCCCHHHH | 56.90 | 7669929 | |
| 124 | Phosphorylation | HHLGKDFTPAAQAAF CCCCCCCCHHHHHHH | 23.35 | 27742792 | |
| 133 | Ubiquitination | AAQAAFQKVVAGVAT HHHHHHHHHHHHHHH | 32.02 | - | |
| 133 | Acetylation | AAQAAFQKVVAGVAT HHHHHHHHHHHHHHH | 32.02 | 7684881 | |
| 140 | Phosphorylation | KVVAGVATALAHKYH HHHHHHHHHHHHHCC | 21.57 | 19060867 | |
| 145 | Ubiquitination | VATALAHKYH----- HHHHHHHHCC----- | 39.14 | - | |
| 145 | Acetylation | VATALAHKYH----- HHHHHHHHCC----- | 39.14 | 109327 | |
| 145 | Malonylation | VATALAHKYH----- HHHHHHHHCC----- | 39.14 | 26073543 | |
| 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 HBB2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HBB2_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 HBB2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of HBB2_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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 TYR-42 AND SER-45, AND MASSSPECTROMETRY. | |
| "Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASSSPECTROMETRY. | |