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Protein Page:
HMGB1 (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
HMGB1 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). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells. Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2. Belongs to the HMGB family. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 13q12
Cellular Component: cell surface; condensed chromosome; extracellular region; extracellular space; nucleoplasm; nucleus; transcriptional repressor complex
Molecular Function: bubble DNA binding; C-X-C chemokine binding; chemoattractant activity; cytokine activity; damaged DNA binding; DNA bending activity; double-stranded DNA binding; four-way junction DNA binding; lipopolysaccharide binding; lyase activity; phosphatidylserine binding; protein binding; RAGE receptor binding; single-stranded DNA binding; transcription factor activity; transcription factor binding
Biological Process: activation of innate immune response; apoptotic cell clearance; dendritic cell chemotaxis; DNA fragmentation during apoptosis; DNA geometric change; DNA ligation during DNA repair; DNA recombination; DNA topological change; elevation of cytosolic calcium ion concentration; inflammatory response; inflammatory response to antigenic stimulus; innate immune response; myeloid dendritic cell activation; negative regulation of blood vessel endothelial cell migration; negative regulation of CD4-positive, alpha beta T cell differentiation; negative regulation of interferon-gamma production; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcriptional preinitiation complex assembly; neurite development; positive regulation of activated T cell proliferation; positive regulation of apoptosis; positive regulation of caspase activity; positive regulation of DNA binding; positive regulation of DNA ligation; positive regulation of interleukin-1 secretion; positive regulation of interleukin-10 production; positive regulation of interleukin-12 production; positive regulation of JNK cascade; positive regulation of MAPKKK cascade; positive regulation of mismatch repair; positive regulation of toll-like receptor 9 signaling pathway; positive regulation of transcription from RNA polymerase II promoter; regulation of autophagy; regulation of restriction endodeoxyribonuclease activity; regulation of T cell mediated immune response to tumor cell; regulation of tolerance induction; regulation of transcription from RNA polymerase II promoter; T-helper 1 cell differentiation; V(D)J recombination
Reference #:  P09429 (UniProtKB)
Alt. Names/Synonyms: Amphoterin; DKFZp686A04236; high mobility group box 1; High mobility group protein 1; High mobility group protein B1; high-mobility group (nonhistone chromosomal) protein 1; high-mobility group box 1; HMG-1; HMG1; HMG3; HMGB1; SBP-1; Sulfoglucuronyl carbohydrate binding protein
Gene Symbols: HMGB1
Molecular weight: 24,894 Da
Basal Isoelectric point: 5.62  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HMGB1

Protein Structure Not Found.
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Sites Implicated In
cell motility, altered: S35‑p, S39‑p, S42‑p
intracellular localization: S35‑p, S39‑p, S42‑p

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

 
8 0 K3‑ac _____MGkGDPKKPR
3 9 K12‑ac DPKKPRGkMSSYAFF
0 6 K30‑ac CREEHKKkHPDAsVN
0 1 K30‑ub CREEHKKkHPDAsVN
4 19 S35‑p KKkHPDAsVNFsEFs
4 5 S39‑p PDAsVNFsEFskkCs
3 2 S42‑p sVNFsEFskkCsERW
0 16 K43‑ac VNFsEFskkCsERWK
0 2 K43‑ub VNFsEFskkCsERWK
0 8 K44‑ac NFsEFskkCsERWKT
0 1 K44‑ub NFsEFskkCsERWKT
1 0 S46‑p sEFskkCsERWKTMs
1 3 S53‑p sERWKTMsAkEKGkF
0 10 K55‑ac RWKTMsAkEKGkFED
0 6 K59‑ac MsAkEKGkFEDMAkA
0 2 K65‑ac GkFEDMAkADKARyE
0 2 Y71‑p AkADKARyEREMkty
0 1 K76‑ac ARyEREMktyIPPkG
0 1 K76 ARyEREMKtyIPPkG
0 2 T77‑p RyEREMktyIPPkGE
0 3 Y78‑p yEREMktyIPPkGET
5 3 K82‑ac MktyIPPkGETKKKF
0 1 K82 MktyIPPKGETKKKF
0 1 K88 PkGETKKKFkDPNAP
0 2 K90‑ac GETKKKFkDPNAPKR
0 1 K90 GETKKKFKDPNAPKR
0 21 S100‑p NAPKRPPsAFFLFCs
0 2 S107‑p sAFFLFCsEyRPkIk
0 30 Y109‑p FFLFCsEyRPkIkGE
1 0 K112‑me FCsEyRPkIkGEHPG
0 5 K112‑ub FCsEyRPkIkGEHPG
0 1 K114 sEyRPkIKGEHPGLs
0 44 K114‑ub sEyRPkIkGEHPGLs
0 1 K114‑sm sEyRPkIkGEHPGLs
0 6 S121‑p kGEHPGLsIGDVAkk
0 1 K127 LsIGDVAKkLGEMWN
0 3 K127‑ub LsIGDVAkkLGEMWN
0 1 K127‑sc LsIGDVAkkLGEMWN
0 2 K128‑ac sIGDVAkkLGEMWNN
0 6 K128‑ub sIGDVAkkLGEMWNN
0 1 T136‑p LGEMWNNtAADDKQP
0 1 K141 NNtAADDKQPyEkkA
0 3 Y144‑p AADDKQPyEkkAAKL
0 5 K146‑ub DDKQPyEkkAAKLKE
0 4 K147‑ub DKQPyEkkAAKLKEk
0 3 K154‑ac kAAKLKEkYEkDIAA
0 1 K154 kAAKLKEKYEkDIAA
0 12 K157‑ac KLKEkYEkDIAAyRA
0 13 K157‑ub KLKEkYEkDIAAyRA
0 58 Y162‑p YEkDIAAyRAKGKPD
0 1 K173‑ac GKPDAAKkGVVkAEK
0 3 K177‑ac AAKkGVVkAEKsKKK
0 1 K177‑sm AAKkGVVkAEKsKKK
3 0 S181‑p GVVkAEKsKKKKEEE
  mouse

 
K3 _____MGKGDPKKPR
K12‑ac DPKKPRGkMSSYAFF
K30 CREEHKKKHPDAsVN
K30 CREEHKKKHPDAsVN
S35‑p KKKHPDAsVNFsEFS
S39‑p PDAsVNFsEFSkKCS
S42 sVNFsEFSkKCSERW
K43‑ac VNFsEFSkKCSERWK
K43‑ub VNFsEFSkKCSERWK
K44 NFsEFSkKCSERWKT
K44 NFsEFSkKCSERWKT
S46 sEFSkKCSERWKTMs
S53‑p SERWKTMsAkEKGkF
K55‑ac RWKTMsAkEKGkFED
K59‑ac MsAkEKGkFEDMAKA
K65 GkFEDMAKADKARYE
Y71 AKADKARYEREMkTY
K76 ARYEREMKTYIPPkG
K76‑ub ARYEREMkTYIPPkG
T77 RYEREMkTYIPPkGE
Y78 YEREMkTYIPPkGET
K82 MkTYIPPKGETKKKF
K82‑ub MkTYIPPkGETKKKF
K88 PkGETKKKFkDPNAP
K90 GETKKKFKDPNAPKR
K90‑ub GETKKKFkDPNAPKR
S100‑p NAPKRPPsAFFLFCS
S107 sAFFLFCSEYRPKIk
Y109 FFLFCSEYRPKIkGE
K112 FCSEYRPKIkGEHPG
K112 FCSEYRPKIkGEHPG
K114 SEYRPKIKGEHPGLs
K114‑ub SEYRPKIkGEHPGLs
K114 SEYRPKIKGEHPGLs
S121‑p kGEHPGLsIGDVAkk
K127 LsIGDVAKkLGEMWN
K127‑ub LsIGDVAkkLGEMWN
K127 LsIGDVAKkLGEMWN
K128 sIGDVAkKLGEMWNN
K128‑ub sIGDVAkkLGEMWNN
T136 LGEMWNNTAADDKQP
K141 NNTAADDKQPYEkkA
Y144 AADDKQPYEkkAAKL
K146‑ub DDKQPYEkkAAKLKE
K147‑ub DKQPYEkkAAKLKEk
K154 kAAKLKEKYEkDIAA
K154‑ub kAAKLKEkYEkDIAA
K157‑ac KLKEkYEkDIAAyRA
K157‑ub KLKEkYEkDIAAyRA
Y162‑p YEkDIAAyRAKGKPD
K173 GKPDAAKKGVVKAEK
K177 AAKKGVVKAEKSKKK
K177 AAKKGVVKAEKSKKK
S181 GVVKAEKSKKKKEEE
  rat

 
K3‑ac _____MGkGDPKKPR
K12‑ac DPKKPRGkMSSYAFF
K30‑ac CREEHKKkHPDASVN
K30 CREEHKKKHPDASVN
S35 KKkHPDASVNFSEFS
S39 PDASVNFSEFSkKCS
S42 SVNFSEFSkKCSERW
K43‑ac VNFSEFSkKCSERWK
K43 VNFSEFSKKCSERWK
K44 NFSEFSkKCSERWKT
K44 NFSEFSkKCSERWKT
S46 SEFSkKCSERWKTMS
S53 SERWKTMSAKEKGkF
K55 RWKTMSAKEKGkFED
K59‑ac MSAKEKGkFEDMAkA
K65‑ac GkFEDMAkADKARYE
Y71 AkADKARYEREMKTY
K76 ARYEREMKTYIPPkG
K76 ARYEREMKTYIPPkG
T77 RYEREMKTYIPPkGE
Y78 YEREMKTYIPPkGET
K82‑ac MKTYIPPkGETKKkF
K82 MKTYIPPKGETKKkF
K88‑ac PkGETKKkFkDPNAP
K90‑ac GETKKkFkDPNAPKR
K90 GETKKkFKDPNAPKR
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSEYRPKIk
Y109 FFLFCSEYRPKIkGE
K112 FCSEYRPKIkGEHPG
K112 FCSEYRPKIkGEHPG
K114‑ac SEYRPKIkGEHPGLS
K114 SEYRPKIKGEHPGLS
K114 SEYRPKIKGEHPGLS
S121 kGEHPGLSIGDVAkk
K127‑ac LSIGDVAkkLGEMWN
K127 LSIGDVAKkLGEMWN
K127 LSIGDVAKkLGEMWN
K128‑ac SIGDVAkkLGEMWNN
K128 SIGDVAkKLGEMWNN
T136 LGEMWNNTAADDkQP
K141‑ac NNTAADDkQPYEKKA
Y144 AADDkQPYEKKAAKL
K146 DDkQPYEKKAAKLKE
K147 DkQPYEKKAAKLKEk
K154‑ac KAAKLKEkYEKDIPA
K154 KAAKLKEKYEKDIPA
K157 KLKEkYEKDIPAYRA
K157 KLKEkYEKDIPAYRA
Y162 YEKDIPAYRAKGKPD
K173 GKPDAAKKGVVkAEK
K177‑ac AAKKGVVkAEKsKKK
K177 AAKKGVVKAEKsKKK
S181‑p GVVkAEKsKKKKEEE
  cow

 
K3‑ac _____MGkGDPKKPR
K12‑ac DPKKPRGkMSSYAFF
K30 CREEHKKKHPDASVN
K30 CREEHKKKHPDASVN
S35 KKKHPDASVNFSEFS
S39 PDASVNFSEFSKKCS
S42 SVNFSEFSKKCSERW
K43 VNFSEFSKKCSERWK
K43 VNFSEFSKKCSERWK
K44 NFSEFSKKCSERWKT
K44 NFSEFSKKCSERWKT
S46 SEFSKKCSERWKTMS
S53 SERWKTMSAKEKGKF
K55 RWKTMSAKEKGKFED
K59 MSAKEKGKFEDMAKA
K65 GKFEDMAKADKARYE
Y71 AKADKARYEREMKTY
K76 ARYEREMKTYIPPKG
K76 ARYEREMKTYIPPKG
T77 RYEREMKTYIPPKGE
Y78 YEREMKTYIPPKGET
K82 MKTYIPPKGETKKKF
K82 MKTYIPPKGETKKKF
K88 PKGETKKKFKDPNAP
K90 GETKKKFKDPNAPKR
K90 GETKKKFKDPNAPKR
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSEYRPKIK
Y109 FFLFCSEYRPKIKGE
K112 FCSEYRPKIKGEHPG
K112 FCSEYRPKIKGEHPG
K114 SEYRPKIKGEHPGLS
K114 SEYRPKIKGEHPGLS
K114 SEYRPKIKGEHPGLS
S121 KGEHPGLSIGDVAKK
K127 LSIGDVAKKLGEMWN
K127 LSIGDVAKKLGEMWN
K127 LSIGDVAKKLGEMWN
K128 SIGDVAKKLGEMWNN
K128 SIGDVAKKLGEMWNN
T136 LGEMWNNTAADDKQP
K141 NNTAADDKQPYEKKA
Y144 AADDKQPYEKKAAKL
K146 DDKQPYEKKAAKLKE
K147 DKQPYEKKAAKLKEK
K154 KAAKLKEKYEKDIAA
K154 KAAKLKEKYEKDIAA
K157 KLKEKYEKDIAAYRA
K157 KLKEKYEKDIAAYRA
Y162 YEKDIAAYRAKGKPD
K173 GKPDAAKKGVVKAEK
K177 AAKKGVVKAEKSKKK
K177 AAKKGVVKAEKSKKK
S181 GVVKAEKSKKKKEEE
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