CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001936
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Hemoglobin subunit beta-2 
Protein Synonyms/Alias
 Beta-2-globin; Hemoglobin beta-2 chain; Hemoglobin beta-minor chain 
Gene Name
 Hbb-b2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
9VHLTDAEKSAVSCLWubiquitination[1]
18AVSCLWAKVNPDEVGacetylation[2, 3]
18AVSCLWAKVNPDEVGsuccinylation[3]
18AVSCLWAKVNPDEVGubiquitination[1]
60SAIMGNPKVKAHGKKacetylation[3]
60SAIMGNPKVKAHGKKsuccinylation[3]
60SAIMGNPKVKAHGKKubiquitination[1]
67KVKAHGKKVITAFNEphosphoglycerylation[4]
67KVKAHGKKVITAFNEubiquitination[1]
77TAFNEGLKNLDNLKGubiquitination[1]
83LKNLDNLKGTFASLSphosphoglycerylation[4]
83LKNLDNLKGTFASLSubiquitination[1]
96LSELHCDKLHVDPENubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237
Functional Description
 Involved in oxygen transport from the lung to the various peripheral tissues. 
Sequence Annotation
 METAL 64 64 Iron (heme distal ligand).
 METAL 93 93 Iron (heme proximal ligand).
 MOD_RES 36 36 Phosphotyrosine.
 MOD_RES 42 42 Phosphotyrosine.
 MOD_RES 45 45 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Heme; Iron; Metal-binding; Oxygen transport; Phosphoprotein; Polymorphism; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 147 AA 
Protein Sequence
MVHLTDAEKS AVSCLWAKVN PDEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNPK 60
VKAHGKKVIT AFNEGLKNLD NLKGTFASLS ELHCDKLHVD PENFRLLGNA IVIVLGHHLG 120
KDFTPAAQAA FQKVVAGVAT ALAHKYH 147 
Gene Ontology
 GO:0005833; C:hemoglobin complex; IMP:MGI.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0019825; F:oxygen binding; IMP:MGI.
 GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
 GO:0048821; P:erythrocyte development; IGI:MGI.
 GO:0045639; P:positive regulation of myeloid cell differentiation; IMP:MGI.
 GO:0045646; P:regulation of erythrocyte differentiation; IMP:MGI. 
Interpro
 IPR000971; Globin.
 IPR009050; Globin-like.
 IPR012292; Globin_dom.
 IPR002337; Haemoglobin_b. 
Pfam
 PF00042; Globin 
SMART
  
PROSITE
 PS01033; GLOBIN 
PRINTS
 PR00814; BETAHAEM.