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Protein Page:
HMGB2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Nuclear receptor co-regulator; DNA binding protein
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; transcription factor activity; DNA bending 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 transcription, DNA-dependent; positive regulation of erythrocyte differentiation; 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 transcription from RNA polymerase II promoter; positive regulation of megakaryocyte differentiation; positive regulation of endothelial cell proliferation; DNA fragmentation during apoptosis; negative regulation of transcription, DNA-dependent; positive regulation of DNA binding; cell structure disassembly during apoptosis
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

 
1 0 K3-ac _____MGkGDPNKPR
0 7 K12-ac DPNKPRGkMSSYAFF
0 1 K30-ac CREEHKKkHPDSsVN
0 4 S35-p KKkHPDSsVNFAEFs
0 2 S42-p sVNFAEFskkCSERW
0 2 K43-ac VNFAEFskkCSERWK
0 1 K43-ub VNFAEFskkCSERWK
0 2 K44-ac NFAEFskkCSERWKT
0 10 K55-ac RWKTMSAkEKSkFED
0 1 K59-ac MSAkEKSkFEDMAKS
0 1 K65 SkFEDMAKSDKARYD
0 3 Y78-p YDREMKNyVPPKGDk
0 9 K85-ac yVPPKGDkKGKKKDP
0 9 S100-p NAPKRPPsAFFLFCs
0 6 S107-p sAFFLFCsEHrPkIk
0 4 R110-m2 FLFCsEHrPkIkSEH
0 1 K112-m2 FCsEHrPkIkSEHPG
0 17 K114-ub sEHrPkIkSEHPGLS
0 1 K128 SIGDTAKKLGEMWsE
0 1 S134-p KKLGEMWsEQsAkDk
0 1 S137-p GEMWsEQsAkDkQPY
0 7 K139-ac MWsEQsAkDkQPYEQ
0 7 K139-ub MWsEQsAkDkQPYEQ
0 1 K139-sc MWsEQsAkDkQPYEQ
0 3 K141-ub sEQsAkDkQPYEQkA
0 11 K147-ub DkQPYEQkAAkLKEK
0 1 K150-ub PYEQkAAkLKEKyEk
0 1 K154 kAAkLKEKyEkDIAA
0 8 Y155-p AAkLKEKyEkDIAAy
0 11 K157-ac kLKEKyEkDIAAyRA
0 12 K157-ub kLKEKyEkDIAAyRA
0 57 Y162-p yEkDIAAyRAKGKsE
0 2 S168-p AyRAKGKsEAGkkGP
0 2 K172-ac KGKsEAGkkGPGRPt
0 2 K173-ac GKsEAGkkGPGRPtG
0 1 T179-p kkGPGRPtGSkkKNE
0 75 K182-ac PGRPtGSkkKNEPED
0 4 K183-ac GRPtGSkkKNEPEDE
  mouse

 
K3 _____MGKGDPNKPR
K12-ac DPNKPRGkMSSYAFF
K30 CREEHKKKHPDSsVN
S35-p KKKHPDSsVNFAEFs
S42-p sVNFAEFsKKCSERW
K43 VNFAEFsKKCSERWK
K43 VNFAEFsKKCSERWK
K44 NFAEFsKKCSERWKT
K55-ac RWKTMSAkEKSKFED
K59 MSAkEKSKFEDLAkS
K65-ac SKFEDLAkSDKARYD
Y78 YDREMKNYVPPKGDk
K85-ac YVPPKGDkKGKKKDP
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSENRPKIk
R110 FLFCSENRPKIkIEH
K112 FCSENRPKIkIEHPG
K114-ub SENRPKIkIEHPGLS
K128-ub SIGDTAKkLGEMWSE
S134 KkLGEMWSEQSAkDk
S137 GEMWSEQSAkDkQPY
K139-ac MWSEQSAkDkQPYEQ
K139-ub MWSEQSAkDkQPYEQ
K139 MWSEQSAKDkQPYEQ
K141-ub SEQSAkDkQPYEQkA
K147-ub DkQPYEQkAAKLKEk
K150 PYEQkAAKLKEkYEk
K154-ub kAAKLKEkYEkDIAA
Y155 AAKLKEkYEkDIAAy
K157-ac KLKEkYEkDIAAyRA
K157-ub KLKEkYEkDIAAyRA
Y162-p YEkDIAAyRAKGKSE
S168 AyRAKGKSEAGKKGP
K172 KGKSEAGKKGPGRPT
K173 GKSEAGKKGPGRPTG
T179 KKGPGRPTGSkKKNE
K182-ac PGRPTGSkKKNEPED
K183 GRPTGSkKKNEPEDE
  rat

 
K3 _____MGKGDPNKPR
K12 DPNKPRGKMSSYAFF
K30 CREEHKKKHPDSSVN
S35 KKKHPDSSVNFAEFS
S42 SVNFAEFSKKCSERW
K43 VNFAEFSKKCSERWK
K43 VNFAEFSKKCSERWK
K44 NFAEFSKKCSERWKT
K55 RWKTMSAKEKSKFED
K59 MSAKEKSKFEDLAKS
K65 SKFEDLAKSDKARYD
Y78 YDREMKNYVPPKGDK
K85 YVPPKGDKKGKKKDP
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSEHRPKIK
R110 FLFCSEHRPKIKSEH
K112 FCSEHRPKIKSEHPG
K114 SEHRPKIKSEHPGLS
K128 SIGDTAKKLGEMWSE
S134 KKLGEMWSEQSAKDK
S137 GEMWSEQSAKDKQPY
K139 MWSEQSAKDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K141 SEQSAKDKQPYEQKA
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
  pig

 
K3 _____MGKGDPNKPR
K12 DPNKPRGKMSSYAFF
K30 CREEHKKKHPDSSVN
S35 KKKHPDSSVNFAEFS
S42 SVNFAEFSKKCSERW
K43 VNFAEFSKKCSERWK
K43 VNFAEFSKKCSERWK
K44 NFAEFSKKCSERWKT
K55 RWKTMSAKEKSKFED
K59 MSAKEKSKFEDMAKS
K65 SKFEDMAKSDKARYD
Y78 YDREMKNYVPPKGDK
K85 YVPPKGDKKGKKKDP
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSEHRPKIK
R110 FLFCSEHRPKIKSEH
K112 FCSEHRPKIKSEHPG
K114 SEHRPKIKSEHPGLS
K128 SIGDTAKKLGEMWSE
S134 KKLGEMWSEQSAKDK
S137 GEMWSEQSAKDKQPY
K139 MWSEQSAKDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K141 SEQSAKDKQPYEQKA
K147 DKQPYEQKAAKLKEK
K150 PYEQKAAKLKEKYEK
K154 KAAKLKEKYEKDIAA
Y155 AAKLKEKYEKDIAAY
K157 KLKEKYEKDIAAYRA
K157 KLKEKYEKDIAAYRA
Y162 YEKDIAAYRAKGKGE
G168 AYRAKGKGEAGKKGP
K172 KGKGEAGKKGPGRPT
K173 GKGEAGKKGPGRPTG
T179 KKGPGRPTGSKKKNE
K182 PGRPTGSKKKNEPED
K183 GRPTGSKKKNEPEDE
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