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Protein Page:
HMGB1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: Nuclear receptor co-regulator; DNA repair
Cellular Component: nucleoplasm; extracellular space; neuron projection; cell surface; transcriptional repressor complex; cytoplasm; extracellular region; condensed chromosome; nucleus
Molecular Function: protein binding; RAGE receptor binding; double-stranded DNA binding; damaged DNA binding; cytokine activity; transcription factor binding; protein kinase activator activity; transcription factor activity; DNA bending activity; single-stranded DNA binding; chemoattractant activity
Biological Process: DNA topological change; positive regulation of myeloid cell differentiation; positive regulation of apoptosis; apoptosis; response to glucocorticoid stimulus; positive regulation of caspase activity; negative regulation of transcription from RNA polymerase II promoter; positive regulation of glycogen catabolic process; DNA recombination; positive chemotaxis; DNA ligation during DNA repair; dendritic cell chemotaxis; DNA fragmentation during apoptosis; neurite development; cell structure disassembly during apoptosis; positive regulation of DNA binding; negative regulation of transcriptional preinitiation complex assembly; V(D)J recombination; base-excision repair, DNA ligation; regulation of transcription from RNA polymerase II promoter; myeloid dendritic cell activation; inflammatory response to antigenic stimulus; eye development; innate immune response; positive regulation of transcription from RNA polymerase II promoter; lung development
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


 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

 
7 0 K3-a _____MGkGDPKKPR
2 5 K12-a DPKKPRGkMSSYAFF
0 2 K30-a CREEHKKkHPDAsVN
1 11 S35-p KKkHPDAsVNFsEFs
2 4 S39-p PDAsVNFsEFskkCS
1 2 S42-p sVNFsEFskkCSERW
0 13 K43-a VNFsEFskkCSERWK
0 2 K43-u VNFsEFskkCSERWK
0 8 K44-a NFsEFskkCSERWKT
0 1 K44-u NFsEFskkCSERWKT
1 0 S53-p SERWKTMsAkEKGkF
0 8 K55-a RWKTMsAkEKGkFED
0 3 K59-a MsAkEKGkFEDMAkA
0 1 K65-a GkFEDMAkADKARYE
0 1 K76-a ARYEREMkTyIPPkG
0 2 Y78-p YEREMkTyIPPkGET
5 2 K82-a MkTyIPPkGETKKKF
0 11 S100-p NAPKRPPsAFFLFCs
0 1 S107-p sAFFLFCsEyRPkIk
0 23 Y109-p FFLFCsEyRPkIkGE
0 5 K112-u FCsEyRPkIkGEHPG
0 33 K114-u sEyRPkIkGEHPGLS
0 2 K127-u LSIGDVAkkLGEMWN
0 1 K128-a SIGDVAkkLGEMWNN
0 4 K128-u SIGDVAkkLGEMWNN
0 3 Y144-p AADDKQPyEkkAAKL
0 3 K146-u DDKQPyEkkAAKLKE
0 3 K147-u DKQPyEkkAAKLKEK
0 10 K157-a KLKEKYEkDIAAyRA
0 7 K157-u KLKEKYEkDIAAyRA
0 54 Y162-p YEkDIAAyRAKGKPD
0 1 K173-a GKPDAAKkGVVkAEK
0 2 K177-a AAKkGVVkAEKsKKK
2 0 S181-p GVVkAEKsKKKKEEE
  mouse

 
K10 ENQLNMGKGDPKELR
K19 DPKELRDKTSSYAFF
K37 CWEEHKKKHPDAsVN
S42-p KKKHPDAsVNFsEFS
S46-p PDAsVNFsEFSkKCS
S49 sVNFsEFSkKCSERW
K50-a VNFsEFSkKCSERWE
K50-u VNFsEFSkKCSERWE
K51 NFsEFSkKCSERWET
K51 NFsEFSkKCSERWET
S60 SERWETMSAKEKGKC
K62 RWETMSAKEKGKCED
K66 MSAKEKGKCEDMAKA
K72 GKCEDMAKADKAHYE
K83 AHYEREMKTTFHHPP
H87 REMKTTFHHPPKAET
K91 TTFHHPPKAETKKKF
S109 NAPKRPSSAFFLFCS
S116 SAFFLFCSEYRPKIK
Y118 FFLFCSEYRPKIKGE
K121 FCSEYRPKIKGESPG
K123 SEYRPKIKGESPGLS
K136 LSIGDVAKKLGEMWN
K137 SIGDVAKKLGEMWNN
K137 SIGDVAKKLGEMWNN
Y153 AADDKQLYEKAAKLK
K155 DDKQLYEKAAKLKEK
- gap
K165 KLKEKYKKDIAAYRA
K165 KLKEKYKKDIAAYRA
Y170 YKKDIAAYRAKGKPD
K181 GKPDAVKKRVINAEK
N185 AVKKRVINAEKSKNK
S189 RVINAEKSKNKRKRK
  rat

 
K3-a _____MGkGDPKKPR
K12 DPKKPRGKMSSYAFF
K30 CREEHKKKHPDASVN
S35 KKKHPDASVNFSEFS
S39 PDASVNFSEFSKKCS
S42 SVNFSEFSKKCSERW
K43 VNFSEFSKKCSERWK
K43 VNFSEFSKKCSERWK
K44 NFSEFSKKCSERWKT
K44 NFSEFSKKCSERWKT
S53 SERWKTMSAKEKGKF
K55 RWKTMSAKEKGKFED
K59 MSAKEKGKFEDMAKA
K65 GKFEDMAKADKARYE
K76 ARYEREMKTYIPPkG
Y78 YEREMKTYIPPkGET
K82-a MKTYIPPkGETKKKF
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSEYRPKIK
Y109 FFLFCSEYRPKIKGE
K112 FCSEYRPKIKGEHPG
K114 SEYRPKIKGEHPGLS
K127 LSIGDVAKKLGEMWN
K128 SIGDVAKKLGEMWNN
K128 SIGDVAKKLGEMWNN
Y144 AADDKQPYEKKAAKL
K146 DDKQPYEKKAAKLKE
K147 DKQPYEKKAAKLKEK
K157 KLKEKYEKDIAAYRA
K157 KLKEKYEKDIAAYRA
Y162 YEKDIAAYRAKGKPD
K173 GKPDAAKKGVVKAEK
K177 AAKKGVVKAEKsKKK
S181-p GVVKAEKsKKKKEEE
  cow

 
K3 _____MGKGDPKKPR
K12 DPKKPRGKMSSYAFF
K30 CREEHKKKHPDASVN
S35 KKKHPDASVNFSEFS
S39 PDASVNFSEFSKKCS
S42 SVNFSEFSKKCSERW
K43 VNFSEFSKKCSERWK
K43 VNFSEFSKKCSERWK
K44 NFSEFSKKCSERWKT
K44 NFSEFSKKCSERWKT
S53 SERWKTMSAKEKGKF
K55 RWKTMSAKEKGKFED
K59 MSAKEKGKFEDMAKA
K65 GKFEDMAKADKARYE
K76 ARYEREMKTYIPPKG
Y78 YEREMKTYIPPKGET
K82 MKTYIPPKGETKKKF
S100 NAPKRPPSAFFLFCS
S107 SAFFLFCSEYRPKIK
Y109 FFLFCSEYRPKIKGE
K112 FCSEYRPKIKGEHPG
K114 SEYRPKIKGEHPGLS
K127 LSIGDVAKKLGEMWN
K128 SIGDVAKKLGEMWNN
K128 SIGDVAKKLGEMWNN
Y144 AADDKQPYEKKAAKL
K146 DDKQPYEKKAAKLKE
K147 DKQPYEKKAAKLKEK
K157 KLKEKYEKDIAAYRA
K157 KLKEKYEKDIAAYRA
Y162 YEKDIAAYRAKGKPD
K173 GKPDAAKKGVVKAEK
K177 AAKKGVVKAEKSKKK
S181 GVVKAEKSKKKKEEE
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