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Protein Page:
HMGB2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
HMGB2 DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Belongs to the HMGB family. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; Nuclear receptor co-regulator
Cellular Component: nucleoplasm; extracellular space; protein complex; perinuclear region of cytoplasm; cytoplasm; condensed chromosome; nucleus
Molecular Function: protein domain specific binding; protein binding; RAGE receptor binding; DNA binding; double-stranded DNA binding; damaged DNA binding; DNA bending activity; transcription factor activity; single-stranded DNA binding; chemoattractant activity
Biological Process: positive regulation of nuclease activity; establishment and/or maintenance of chromatin architecture; V(D)J recombination; DNA topological change; phosphoinositide-mediated signaling; apoptosis; positive regulation of erythrocyte differentiation; positive regulation of transcription, DNA-dependent; male gonad development; spermatid nuclear differentiation; base-excision repair, DNA ligation; regulation of transcription from RNA polymerase II promoter; nucleosome assembly; positive chemotaxis; response to steroid hormone stimulus; DNA ligation during DNA repair; positive regulation of endothelial cell proliferation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of megakaryocyte differentiation; DNA fragmentation during apoptosis; negative regulation of transcription, DNA-dependent; cell structure disassembly during apoptosis; positive regulation of DNA binding
Reference #:  P26583 (UniProtKB)
Alt. Names/Synonyms: High mobility group protein 2; High mobility group protein B2; high-mobility group (nonhistone chromosomal) protein 2; high-mobility group box 2; HMG-2; HMG2; HMGB2
Gene Symbols: HMGB2
Molecular weight: 24,034 Da
Basal Isoelectric point: 7.62  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HMGB2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
1 0 K3-a _____MGkGDPNKPR
1 1 R10 kGDPNKPRGkMSSyA
0 6 K12-a DPNKPRGkMSSyAFF
1 6 Y16-p PRGkMSSyAFFVQTC
0 1 K30-a CREEHKKkHPDSsVN
0 7 S35-p KKkHPDSsVNFAEFs
0 4 S42-p sVNFAEFskkCSERW
0 2 K43-a VNFAEFskkCSERWK
0 2 K44-a NFAEFskkCSERWKT
0 10 K55-a RWKTMSAkEKSkFED
0 1 K59-a MSAkEKSkFEDMAKS
0 1 K65 SkFEDMAKSDKARYD
0 4 Y78-p YDREMKNyVPPKGDk
0 9 K85-a yVPPKGDkKGKKKDP
0 5 S100-p NAPKRPPsAFFLFCS
0 4 R110-m2 FLFCSEHrPkIkSEH
0 1 K112-m2 FCSEHrPkIkSEHPG
0 19 K114-u SEHrPkIkSEHPGLS
0 3 K128 SIGDTAKKLGEMWsE
0 1 S134-p KKLGEMWsEQsAkDk
0 1 S137-p GEMWsEQsAkDkQPY
0 7 K139-a MWsEQsAkDkQPYEQ
0 7 K139-u MWsEQsAkDkQPYEQ
0 3 K141-u sEQsAkDkQPYEQkA
0 1 Q146 kDkQPYEQkAAkLKE
0 11 K147-u DkQPYEQkAAkLKEK
0 1 K150-u PYEQkAAkLKEKyEk
0 1 K154 kAAkLKEKyEkDIAA
0 6 Y155-p AAkLKEKyEkDIAAy
0 10 K157-a kLKEKyEkDIAAyRA
0 12 K157-u kLKEKyEkDIAAyRA
0 57 Y162-p yEkDIAAyRAKGKsE
0 2 S168-p AyRAKGKsEAGkkGP
0 2 K172-a KGKsEAGkkGPGRPt
0 2 K173-a GKsEAGkkGPGRPtG
0 1 T179-p kkGPGRPtGSkkKNE
0 75 K182-a PGRPtGSkkKNEPED
0 4 K183-a GRPtGSkkKNEPEDE
  HMGB2 iso2  
K3 _____MGKGDPKKPt
T10-p KGDPKKPtGKMSSyA
K12 DPKKPtGKMSSyAFF
Y16-p PtGKMSSyAFFVQTC
K29 TCREEHKKKHPDAsV
S35-p KKKHPDAsVNFSEFs
S42-p sVNFSEFsKKCSERW
K43 VNFSEFsKKCSERWK
K44 NFSEFsKKCSERWKT
K55 RWKTMSAKEKGKFED
K59 MSAKEKGKFEDMAKA
K65 GKFEDMAKADKARYE
Y78-p YEREMKTyIPPKGET
T85 yIPPKGETKKKFKDP
S100 NAPKRLPSAFFLFCS
R110 FLFCSEYRPKIkGEH
K112 FCSEYRPKIkGEHPG
K114-u SEYRPKIkGEHPGLS
K128-u SIGDVAKkLGEMWNN
N134 KkLGEMWNNTAADDK
A137 GEMWNNTAADDKQPY
D139 MWNNTAADDKQPYEk
D139 MWNNTAADDKQPYEk
K141 NNTAADDKQPYEkKA
K146-u DDKQPYEkKAAKLKE
K147 DKQPYEkKAAKLKEK
K150 PYEkKAAKLKEKYEK
K154 KAAKLKEKYEKDIAA
Y155 AAKLKEKYEKDIAAy
K157 KLKEKYEKDIAAyRA
K157 KLKEKYEKDIAAyRA
Y162-p YEKDIAAyRAKGKPD
P168 AyRAKGKPDAAKKGV
K172 KGKPDAAKKGVVKAE
K173 GKPDAAKKGVVKAEK
E179 KKGVVKAEKSKKKKE
K182 VVKAEKSKKKKEEEE
K183 VKAEKSKKKKEEEED
  mouse

 
K3 _____MGKGDPNKPR
R10 KGDPNKPRGkMSSYA
K12-a DPNKPRGkMSSYAFF
Y16 PRGkMSSYAFFVQTC
K30 CREEHKKKHPDSsVN
S35-p KKKHPDSsVNFAEFs
S42-p sVNFAEFsKKCSERW
K43 VNFAEFsKKCSERWK
K44 NFAEFsKKCSERWKT
K55-a RWKTMSAkEKSKFED
K59 MSAkEKSKFEDLAkS
K65-a SKFEDLAkSDKARYD
Y78 YDREMKNYVPPKGDk
K85-a YVPPKGDkKGKKKDP
S100 NAPKRPPSAFFLFCS
R110 FLFCSENRPKIkIEH
K112 FCSENRPKIkIEHPG
K114-u SENRPKIkIEHPGLS
K128-u SIGDTAKkLGEMWSE
S134 KkLGEMWSEQSAkDk
S137 GEMWSEQSAkDkQPY
K139-a MWSEQSAkDkQPYEQ
K139-u MWSEQSAkDkQPYEQ
K141-u SEQSAkDkQPYEQkA
Q146 kDkQPYEQkAAKLKE
K147-u DkQPYEQkAAKLKEk
K150 PYEQkAAKLKEkYEk
K154-u kAAKLKEkYEkDIAA
Y155 AAKLKEkYEkDIAAy
K157 KLKEkYEKDIAAyRA
K157-u KLKEkYEkDIAAyRA
Y162-p YEkDIAAyRAKGKSE
S168 AyRAKGKSEAGKKGP
K172 KGKSEAGKKGPGRPT
K173 GKSEAGKKGPGRPTG
T179 KKGPGRPTGSkKKNE
K182-a PGRPTGSkKKNEPED
K183 GRPTGSkKKNEPEDE
  rat

 
K3 _____MGKGDPNKPR
R10 KGDPNKPRGKMSSYA
K12 DPNKPRGKMSSYAFF
Y16 PRGKMSSYAFFVQTC
K30 CREEHKKKHPDSSVN
S35 KKKHPDSSVNFAEFS
S42 SVNFAEFSKKCSERW
K43 VNFAEFSKKCSERWK
K44 NFAEFSKKCSERWKT
K55 RWKTMSAKEKSKFED
K59 MSAKEKSKFEDLAKS
K65 SKFEDLAKSDKARYD
Y78 YDREMKNYVPPKGDK
K85 YVPPKGDKKGKKKDP
S100 NAPKRPPSAFFLFCS
R110 FLFCSEHRPKIKSEH
K112 FCSEHRPKIKSEHPG
K114 SEHRPKIKSEHPGLS
K128 SIGDTAKKLGEMWSE
S134 KKLGEMWSEQSAKDK
S137 GEMWSEQSAKDKQPY
K139 MWSEQSAKDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K141 SEQSAKDKQPYEQKA
Q146 KDKQPYEQKAAKLKE
K147 DKQPYEQKAAKLKEK
K150 PYEQKAAKLKEKYEK
K154 KAAKLKEKYEKDIAA
Y155 AAKLKEKYEKDIAAY
K157 KLKEKYEKDIAAYRA
K157 KLKEKYEKDIAAYRA
Y162 YEKDIAAYRAKGKSE
S168 AYRAKGKSEVGKKGP
K172 KGKSEVGKKGPGRPT
K173 GKSEVGKKGPGRPTG
T179 KKGPGRPTGSKKKNE
K182 PGRPTGSKKKNEPED
K183 GRPTGSKKKNEPEDE
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