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Protein Page:
HMGN1 (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
HMGN1 a nonhistone chromosomal protein of the HMG-14/HMG-17 protein family. Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein
Cellular Component: cytoplasm; chromatin; nucleus
Molecular Function: nucleosomal DNA binding; DNA binding
Biological Process: regulation of transcription from RNA polymerase II promoter; establishment and/or maintenance of chromatin architecture; transcription-coupled nucleotide-excision repair; positive regulation of RNA elongation; pyrimidine dimer repair via nucleotide-excision repair; regulation of development, heterochronic; post-embryonic camera-type eye morphogenesis; response to UV-C; regulation of epithelial cell proliferation; response to UV-B
Reference #:  P05114 (UniProtKB)
Alt. Names/Synonyms: FLJ27265; FLJ31471; High mobility group nucleosome-binding domain-containing protein 1; high-mobility group (nonhistone chromosomal) protein 14; high-mobility group nucleosome binding 1; high-mobility group nucleosome binding domain 1; HMG14; HMGN1; MGC104230; MGC117425; Non-histone chromosomal protein HMG-14; nonhistone chromosomal protein HMG-14
Gene Symbols: HMGN1
Molecular weight: 10,659 Da
Basal Isoelectric point: 9.6  Predict pI for various phosphorylation states
CST Pathways:  Growth And Differentiation Control by MAPKs  |  Regulation of P38 MAPKs
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HMGN1

Protein Structure Not Found.


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Sites Implicated In
intracellular localization: S7‑p, S8‑p, S21‑p, S25‑p
molecular association, regulation: S21‑p, S25‑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

 
2 0 K3-ac _____MPkRkVssAE
1 0 K5-ac ___MPkRkVssAEGA
6 38 S7-p _MPkRkVssAEGAAk
2 8 S8-p MPkRkVssAEGAAkE
1 15 K14-ac ssAEGAAkEEPkRRs
0 1 K14-ub ssAEGAAkEEPkRRs
1 6 K18-ac GAAkEEPkRRsARLs
4 19 S21-p kEEPkRRsARLsAkP
5 6 S25-p kRRsARLsAkPPAkV
1 0 K27-ac RsARLsAkPPAkVEA
0 2 K27-ub RsARLsAkPPAkVEA
1 2 K31-ac LsAkPPAkVEAKPKk
0 1 K31 LsAkPPAKVEAKPKk
1 0 K38-ac kVEAKPKkAAAkDKS
1 0 K42-ac KPKkAAAkDKSSDkK
1 0 K48-ac AkDKSSDkKVQTkGk
1 0 K53-ac SDkKVQTkGkRGAkG
1 0 K55-ac kKVQTkGkRGAkGkQ
1 1 K59-ac TkGkRGAkGkQAEVA
1 1 K61-ac GkRGAkGkQAEVANQ
0 4 K61-ub GkRGAkGkQAEVANQ
0 1 T70-p AEVANQEtkEDLPAE
0 5 K71-ub EVANQEtkEDLPAEN
0 1 E72 VANQEtkEDLPAENG
0 6 T81-p LPAENGEtktEEsPA
1 1 K82-ac PAENGEtktEEsPAs
0 1 K82-ub PAENGEtktEEsPAs
0 2 T83-p AENGEtktEEsPAsD
1 40 S86-p GEtktEEsPAsDEAG
3 44 S89-p ktEEsPAsDEAGEkE
0 3 K95-ub AsDEAGEkEAKsD__
0 3 K98 EAGEkEAKsD_____
2 19 S99-p AGEkEAKsD______
  mouse

 
K3 _____MPKRKVsADG
K5 ___MPKRKVsADGAA
S7-p _MPKRKVsADGAAkA
- gap
K13-ac VsADGAAkAEPKRRs
K13 VsADGAAKAEPKRRs
K17 GAAkAEPKRRsARLs
S20-p kAEPKRRsARLsAkP
S24-p KRRsARLsAkPAPAk
K26 RsARLsAKPAPAkVD
K26-ub RsARLsAkPAPAkVD
K31 sAkPAPAKVDAKPKK
K31-ub sAkPAPAkVDAKPKK
K38 kVDAKPKKAAGKDKA
K42 KPKKAAGKDKASDKK
K48 GKDKASDKKVQIKGK
K53 SDKKVQIKGKRGAKG
K55 KKVQIKGKRGAKGkQ
K59 IKGKRGAKGkQADVA
K61 GKRGAKGKQADVADQ
K61-ub GKRGAKGkQADVADQ
T70-p ADVADQQttELPAEN
- gap
T71-p DVADQQttELPAENG
T80-p LPAENGEtENQsPAs
- gap
- gap
- gap
S84-p NGEtENQsPAsEEEk
S87-p tENQsPAsEEEkEAk
K91-ub sPAsEEEkEAksD__
K94-ub sEEEkEAksD_____
S95-p EEEkEAksD______
  rat

 
K3 _____MPKRKVsADG
K5 ___MPKRKVsADGAA
S7-p _MPKRKVsADGAAkA
- gap
K13-ac VsADGAAkAEPKRRS
K13 VsADGAAKAEPKRRS
K17 GAAkAEPKRRSARLS
S20 kAEPKRRSARLSAkP
S24 KRRSARLSAkPAPAK
K26-ac RSARLSAkPAPAKVD
K26 RSARLSAKPAPAKVD
K31 SAkPAPAKVDAKPKK
K31 SAkPAPAKVDAKPKK
K38 KVDAKPKKAAGKDKA
K42 KPKKAAGKDKASDKK
K48 GKDKASDKKAQIKGK
K53 SDKKAQIKGKRGAKG
K55 KKAQIKGKRGAKGkQ
K59 IKGKRGAKGkQAEVA
K61-ac GKRGAKGkQAEVADQ
K61 GKRGAKGKQAEVADQ
T70 AEVADQQTTDLPAEN
- gap
T71 EVADQQTTDLPAENG
T80-p LPAENGEtENQsPAs
- gap
- gap
- gap
S84-p NGEtENQsPAsEEEK
S87-p tENQsPAsEEEKEAK
K91 sPAsEEEKEAKsD__
K94 sEEEKEAKsD_____
S95-p EEEKEAKsD______
  cow

 
K3 _____MPKRKVsSAE
K5 ___MPKRKVsSAEGA
S7-p _MPKRKVsSAEGAAK
S8 MPKRKVsSAEGAAKE
K14 sSAEGAAKEEPKRRS
K14 sSAEGAAKEEPKRRS
K18 GAAKEEPKRRSARLs
S21 KEEPKRRSARLsAKP
S25-p KRRSARLsAKPAPAK
K27 RSARLsAKPAPAKVE
K27 RSARLsAKPAPAKVE
K32 sAKPAPAKVETKPKK
K32 sAKPAPAKVETKPKK
K39 KVETKPKKAAGKDKS
K43 KPKKAAGKDKSSDKK
K49 GKDKSSDKKVQTKGK
K54 SDKKVQTKGKRGAKG
K56 KKVQTKGKRGAKGKQ
K60 TKGKRGAKGKQAEVA
K62 GKRGAKGKQAEVANQ
K62 GKRGAKGKQAEVANQ
T71 AEVANQETKEDLPAE
K72 EVANQETKEDLPAEN
E73 VANQETKEDLPAENG
T82 LPAENGETKNEESPA
K83 PAENGETKNEESPAs
K83 PAENGETKNEESPAs
- gap
S87 GETKNEESPAsDEAE
S90-p KNEESPAsDEAEEKE
K96 AsDEAEEKEAKsD__
K99 EAEEKEAKsD_____
S100-p AEEKEAKsD______
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