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Protein Page:
HMGB2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: DNA-binding; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 4q31
Cellular Component: cell; condensed chromosome; cytoplasm; extracellular space; nuclear chromatin; nucleolus; nucleoplasm; nucleus; perinuclear region of cytoplasm; protein complex
Molecular Function: chemoattractant activity; damaged DNA binding; DNA bending activity; DNA binding; double-stranded DNA binding; drug binding; four-way junction DNA binding; protein binding; RAGE receptor binding; single-stranded DNA binding; transcription factor activity; transcription factor binding
Biological Process: defense response to Gram-negative bacterium; defense response to Gram-positive bacterium; DNA fragmentation during apoptosis; DNA geometric change; DNA ligation during DNA repair; DNA topological change; inflammatory response to antigenic stimulus; negative regulation of transcription, DNA-dependent; positive regulation of DNA binding; positive regulation of endothelial cell proliferation; positive regulation of erythrocyte differentiation; positive regulation of megakaryocyte differentiation; positive regulation of nuclease activity; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; regulation of neurogenesis; regulation of transcription from RNA polymerase II promoter; response to drug; response to lipopolysaccharide; V(D)J recombination
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



 LTP 

LTP: 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.


 HTP 

HTP: 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 1 K8 MGkGDPNKPRGkMSS
0 9 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 3 K59‑ac MSAkEKSkFEDMAKs
0 1 K59‑ub MSAkEKSkFEDMAKs
0 2 K65 SkFEDMAKsDKARYD
0 1 S66‑p kFEDMAKsDKARYDR
0 3 Y78‑p YDREMKNyVPPKGDk
0 10 K85‑ac yVPPKGDkKGKKKDP
0 11 S100‑p NAPKRPPsAFFLFCs
0 6 S107‑p sAFFLFCsEHrPkIk
0 4 R110‑m2 FLFCsEHrPkIksEH
0 1 K112‑m2 FCsEHrPkIksEHPG
0 1 K114 sEHrPkIKsEHPGLs
0 18 K114‑ub sEHrPkIksEHPGLs
0 1 S115‑p EHrPkIksEHPGLsI
0 1 S121‑p ksEHPGLsIGDTAKk
0 1 K127 LsIGDTAKkLGEMWs
0 1 K128 sIGDTAKKLGEMWsE
0 2 K128‑ub sIGDTAKkLGEMWsE
0 1 S134‑p KkLGEMWsEQsAkDk
0 1 S137‑p GEMWsEQsAkDkQPY
0 8 K139‑ac MWsEQsAkDkQPYEQ
0 7 K139‑ub MWsEQsAkDkQPYEQ
0 1 K139‑sc MWsEQsAkDkQPYEQ
0 3 K141‑ub sEQsAkDkQPYEQkA
0 2 K147‑ac DkQPYEQkAAkLKEk
0 11 K147‑ub DkQPYEQkAAkLKEk
0 1 K150‑ub PYEQkAAkLKEkYEk
0 1 K154 kAAkLKEKYEkDIAA
0 3 K154‑ac kAAkLKEkYEkDIAA
0 13 K157‑ac kLKEkYEkDIAAyRA
0 13 K157‑ub kLKEkYEkDIAAyRA
0 57 Y162‑p YEkDIAAyRAKGKsE
0 2 S168‑p AyRAKGKsEAGkkGP
0 2 K172‑ac KGKsEAGkkGPGRPt
0 2 K173‑ac GKsEAGkkGPGRPtG
0 2 T179‑p kkGPGRPtGSkkKNE
0 75 K182‑ac PGRPtGSkkKNEPED
0 4 K183‑ac GRPtGSkkKNEPEDE
  mouse

 
K3 _____MGKGDPNKPR
K8 MGKGDPNKPRGkMSS
K12‑ac DPNKPRGkMSSYAFF
K30 CREEHKKKHPDSsVN
S35‑p KKKHPDSsVNFAEFs
S42‑p sVNFAEFsKKCSERW
K43 VNFAEFsKKCSERWK
K43 VNFAEFsKKCSERWK
K44 NFAEFsKKCSERWKT
K55‑ac RWKTMSAkEKSKFED
K59 MSAkEKSKFEDLAkS
K59 MSAkEKSKFEDLAkS
K65‑ac SKFEDLAkSDKARYD
S66 KFEDLAkSDKARYDR
Y78 YDREMKNYVPPKGDk
K85‑ac YVPPKGDkKGKKKDP
S100‑p NAPKRPPsAFFLFCS
S107 sAFFLFCSENRPKIk
R110 FLFCSENRPKIkIEH
K112 FCSENRPKIkIEHPG
K114 SENRPKIKIEHPGLS
K114‑ub SENRPKIkIEHPGLS
I115 ENRPKIkIEHPGLSI
S121 kIEHPGLSIGDTAKk
K127 LSIGDTAKkLGEMWS
K128 SIGDTAKKLGEMWSE
K128‑ub SIGDTAKkLGEMWSE
S134 KkLGEMWSEQSAkDk
S137 GEMWSEQSAkDkQPY
K139‑ac MWSEQSAkDkQPYEQ
K139‑ub MWSEQSAkDkQPYEQ
K139 MWSEQSAKDkQPYEQ
K141‑ub SEQSAkDkQPYEQkA
K147 DkQPYEQKAAKLKEk
K147‑ub DkQPYEQkAAKLKEk
K150 PYEQkAAKLKEkYEk
K154‑ub kAAKLKEkYEkDIAA
K154 kAAKLKEKYEkDIAA
K157‑ac KLKEkYEkDIAAyRA
K157‑ub KLKEkYEkDIAAyRA
Y162‑p YEkDIAAyRAKGKSE
S168 AyRAKGKSEAGKKGP
K172 KGKSEAGKKGPGRPt
K173 GKSEAGKKGPGRPtG
T179‑p KKGPGRPtGSkKKNE
K182‑ac PGRPtGSkKKNEPED
K183 GRPtGSkKKNEPEDE
  rat

 
K3 _____MGKGDPNkPR
K8‑ac MGKGDPNkPRGkMSS
K12‑ac DPNkPRGkMSSYAFF
K30 CREEHKKKHPDSSVN
S35 KKKHPDSSVNFAEFS
S42 SVNFAEFSKKCSERW
K43 VNFAEFSKKCSERWK
K43 VNFAEFSKKCSERWK
K44 NFAEFSKKCSERWKT
K55 RWKTMSAKEKSkFED
K59‑ac MSAKEKSkFEDLAkS
K59 MSAKEKSKFEDLAkS
K65‑ac SkFEDLAkSDKARYD
S66 kFEDLAkSDKARYDR
Y78 YDREMKNYVPPKGDk
K85‑ac YVPPKGDkKGKKKDP
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSEHRPKIk
R110 FLFCSEHRPKIkSEH
K112 FCSEHRPKIkSEHPG
K114‑ac SEHRPKIkSEHPGLS
K114 SEHRPKIKSEHPGLS
S115 EHRPKIkSEHPGLSI
S121 kSEHPGLSIGDTAkk
K127‑ac LSIGDTAkkLGEMWS
K128‑ac SIGDTAkkLGEMWSE
K128 SIGDTAkKLGEMWSE
S134 kkLGEMWSEQSAkDK
S137 GEMWSEQSAkDKQPY
K139‑ac MWSEQSAkDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K141 SEQSAkDKQPYEQkA
K147‑ac DKQPYEQkAAKLKEk
K147 DKQPYEQKAAKLKEk
K150 PYEQkAAKLKEkYEk
K154 kAAKLKEKYEkDIAA
K154‑ac kAAKLKEkYEkDIAA
K157‑ac KLKEkYEkDIAAYRA
K157 KLKEkYEKDIAAYRA
Y162 YEkDIAAYRAKGKSE
S168 AYRAKGKSEVGKKGP
K172 KGKSEVGKKGPGRPT
K173 GKSEVGKKGPGRPTG
T179 KKGPGRPTGSKKKNE
K182 PGRPTGSKKKNEPED
K183 GRPTGSKKKNEPEDE
  pig

 
K3 _____MGKGDPNKPR
K8 MGKGDPNKPRGKMSS
K12 DPNKPRGKMSSYAFF
K30 CREEHKKKHPDSSVN
S35 KKKHPDSSVNFAEFS
S42 SVNFAEFSKKCSERW
K43 VNFAEFSKKCSERWK
K43 VNFAEFSKKCSERWK
K44 NFAEFSKKCSERWKT
K55 RWKTMSAKEKSKFED
K59 MSAKEKSKFEDMAKS
K59 MSAKEKSKFEDMAKS
K65 SKFEDMAKSDKARYD
S66 KFEDMAKSDKARYDR
Y78 YDREMKNYVPPKGDK
K85 YVPPKGDKKGKKKDP
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSEHRPKIK
R110 FLFCSEHRPKIKSEH
K112 FCSEHRPKIKSEHPG
K114 SEHRPKIKSEHPGLS
K114 SEHRPKIKSEHPGLS
S115 EHRPKIKSEHPGLSI
S121 KSEHPGLSIGDTAKK
K127 LSIGDTAKKLGEMWS
K128 SIGDTAKKLGEMWSE
K128 SIGDTAKKLGEMWSE
S134 KKLGEMWSEQSAKDK
S137 GEMWSEQSAKDKQPY
K139 MWSEQSAKDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K139 MWSEQSAKDKQPYEQ
K141 SEQSAKDKQPYEQKA
K147 DKQPYEQKAAKLKEK
K147 DKQPYEQKAAKLKEK
K150 PYEQKAAKLKEKYEK
K154 KAAKLKEKYEKDIAA
K154 KAAKLKEKYEKDIAA
K157 KLKEKYEKDIAAYRA
K157 KLKEKYEKDIAAYRA
Y162 YEKDIAAYRAKGKGE
G168 AYRAKGKGEAGKKGP
K172 KGKGEAGKKGPGRPT
K173 GKGEAGKKGPGRPTG
T179 KKGPGRPTGSKKKNE
K182 PGRPTGSKKKNEPED
K183 GRPTGSKKKNEPEDE
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