NUPR1_HUMAN - dbPTM
NUPR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUPR1_HUMAN
UniProt AC O60356
Protein Name Nuclear protein 1 {ECO:0000305}
Gene Name NUPR1 {ECO:0000312|HGNC:HGNC:29990}
Organism Homo sapiens (Human).
Sequence Length 82
Subcellular Localization Nucleus .
Protein Description Chromatin-binding protein that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Interacts with MSL1 and inhibits its activity on histone H4 'Lys-16' acetylation (H4K16ac). Binds the RELB promoter and activates its transcription, leading to the transactivation of IER3. The NUPR1/RELB/IER3 survival pathway may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. In breast cancer cells, NUPR1 overexpression leads to the activation of PI3K/AKT signaling pathway, CDKN1A/p21 phosphorylation and relocalization from the nucleus to the cytoplasm, leading to resistance to chemotherapeutic agents, such as doxorubicin..
Protein Sequence MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGARR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
22PhosphorylationPGPEDEDSSLDESDL
CCCCCCCCCCCHHHH
30.6529514088
23PhosphorylationGPEDEDSSLDESDLY
CCCCCCCCCCHHHHH
52.7629514088
27PhosphorylationEDSSLDESDLYSLAH
CCCCCCHHHHHHHHH
32.3629514088
46PhosphorylationGGGRKGRTKREAAAN
CCCCCCCCHHHHHHH
43.02-
54PhosphorylationKREAAANTNRPSPGG
HHHHHHHCCCCCCCH
28.0723312004
58PhosphorylationAANTNRPSPGGHERK
HHHCCCCCCCHHHHH
32.7023312004
65AcetylationSPGGHERKLVTKLQN
CCCHHHHHHHHHHHH
44.3085003
69AcetylationHERKLVTKLQNSERK
HHHHHHHHHHHHHHH
40.3685007
73PhosphorylationLVTKLQNSERKKRGA
HHHHHHHHHHHHHCC
26.3129514088
76AcetylationKLQNSERKKRGARR-
HHHHHHHHHHCCCC-
42.6585011
76PhosphorylationKLQNSERKKRGARR-
HHHHHHHHHHCCCC-
42.6527251275
77AcetylationLQNSERKKRGARR--
HHHHHHHHHCCCC--
63.3985015

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of NUPR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUPR1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of NUPR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYOD1_HUMANMYOD1physical
19723804
EP300_HUMANEP300physical
11940591
CSN5_HUMANCOPS5physical
16300740
SET_HUMANSETphysical
21988832
MSL1_HUMANMSL1physical
24205110
MSL1_HUMANMSL1physical
19650074
MO4L1_HUMANMORF4L1physical
19650074
RAN_HUMANRANphysical
19650074
PTMA_HUMANPTMAphysical
19650074
MARE1_HUMANMAPRE1physical
19650074
MPH6_HUMANMPHOSPH6physical
19650074
NACAM_HUMANNACAphysical
19650074
NACA_HUMANNACAphysical
19650074
PSMD4_HUMANPSMD4physical
19650074
SC11A_HUMANSEC11Aphysical
19650074
RANG_HUMANRANBP1physical
19650074
STX18_HUMANSTX18physical
19650074
HNRPQ_HUMANSYNCRIPphysical
19650074
FUS_HUMANFUSphysical
19650074
NONO_HUMANNONOphysical
19650074
RL41_HUMANRPL41physical
19650074
SKAP_HUMANKNSTRNphysical
19650074
SEMG2_HUMANSEMG2physical
28514442
SEMG1_HUMANSEMG1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NUPR1_HUMAN

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Related Literatures of Post-Translational Modification

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