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Protein

Growth arrest and DNA damage-inducible protein GADD45 gamma

Gene

GADD45G

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK.

GO - Biological processi

  • activation of MAPKKK activity Source: UniProtKB
  • apoptotic process Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of JNK cascade Source: UniProtKB
  • positive regulation of p38MAPK cascade Source: UniProtKB
  • regulation of cell cycle Source: GO_Central
  • response to stress Source: InterPro

Keywordsi

Molecular functionDevelopmental protein
Biological processApoptosis, Differentiation

Enzyme and pathway databases

SignaLinkiO95257

Names & Taxonomyi

Protein namesi
Recommended name:
Growth arrest and DNA damage-inducible protein GADD45 gamma
Alternative name(s):
Cytokine-responsive protein CR6
DNA damage-inducible transcript 2 protein
Short name:
DDIT-2
Gene namesi
Name:GADD45G
Synonyms:CR6, DDIT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000130222.10
HGNCiHGNC:4097 GADD45G
MIMi604949 gene
neXtProtiNX_O95257

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47A → R: 30-fold reduction in homodimerization affinity and 90% decrease in growth inhibition activity and ability to stop cell cycle; when associated with E-77, E-80 and R-83. 1 Publication1
Mutagenesisi76I → E: 30-fold reduction in homodimerization affinity and 90% decrease in growth inhibition activity and ability to stop cell cycle; when associated with R-47, E-80 and R-83. 1 Publication1
Mutagenesisi80L → E: 30-fold reduction in homodimerization affinity and 90% decrease in growth inhibition activity and ability to stop cell cycle; when associated with R-47, E-77 and R-83. 1 Publication1
Mutagenesisi83A → R: 30-fold reduction in homodimerization affinity and 90% decrease in growth inhibition activity and ability to stop cell cycle; when associated with R-47, E-77 and E-80. 1 Publication1
Mutagenesisi87E → K: Reduced growth inhibition activity; when associated with K-89. 1 Publication1
Mutagenesisi89D → K: Reduced growth inhibition activity; when associated with K-87. 1 Publication1

Organism-specific databases

DisGeNETi10912
OpenTargetsiENSG00000130222
PharmGKBiPA28512

Polymorphism and mutation databases

BioMutaiGADD45G

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001483361 – 159Growth arrest and DNA damage-inducible protein GADD45 gammaAdd BLAST159

Proteomic databases

PaxDbiO95257
PRIDEiO95257
ProteomicsDBi50751

Expressioni

Gene expression databases

BgeeiENSG00000130222
CleanExiHS_GADD45G
ExpressionAtlasiO95257 baseline and differential
GenevisibleiO95257 HS

Organism-specific databases

HPAiHPA023606

Interactioni

Subunit structurei

Undergoes concentration-dependent homodimerization, which is required for growth inhibititory activity and enhances interaction with PCNA. Interacts with GADD45GIP1. Interacts with PCNA.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi116117, 55 interactors
CORUMiO95257
DIPiDIP-24218N
IntActiO95257, 49 interactors
MINTiO95257
STRINGi9606.ENSP00000252506

Structurei

Secondary structure

1159
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 35Combined sources19
Beta strandi39 – 42Combined sources4
Helixi43 – 52Combined sources10
Helixi54 – 56Combined sources3
Beta strandi57 – 63Combined sources7
Helixi66 – 68Combined sources3
Helixi72 – 87Combined sources16
Beta strandi91 – 96Combined sources6
Helixi98 – 105Combined sources8
Beta strandi111 – 113Combined sources3
Beta strandi118 – 123Combined sources6
Beta strandi125 – 128Combined sources4
Helixi133 – 147Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WALX-ray2.40A/B1-159[»]
3FFMX-ray2.30A1-159[»]
ProteinModelPortaliO95257
SMRiO95257
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95257

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 86HomodimerizationAdd BLAST44

Domaini

Two central helices mediate homodimerization through parallel packing.

Sequence similaritiesi

Belongs to the GADD45 family.Curated

Phylogenomic databases

eggNOGiENOG410IW58 Eukaryota
ENOG4111FXB LUCA
GeneTreeiENSGT00390000016506
HOGENOMiHOG000013221
HOVERGENiHBG051684
InParanoidiO95257
KOiK04402
OMAiDWVPTIT
OrthoDBiEOG091G0RHU
PhylomeDBiO95257
TreeFamiTF300196

Family and domain databases

Gene3Di3.30.1330.30, 1 hit
InterProiView protein in InterPro
IPR024824 GADD45
IPR029064 L30e-like
IPR004038 Ribosomal_L7Ae/L30e/S12e/Gad45
PANTHERiPTHR10411 PTHR10411, 1 hit
PfamiView protein in Pfam
PF01248 Ribosomal_L7Ae, 1 hit
SUPFAMiSSF55315 SSF55315, 1 hit

Sequencei

Sequence statusi: Complete.

O95257-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLEEVRGQD TVPESTARMQ GAGKALHELL LSAQRQGCLT AGVYESAKVL
60 70 80 90 100
NVDPDNVTFC VLAAGEEDEG DIALQIHFTL IQAFCCENDI DIVRVGDVQR
110 120 130 140 150
LAAIVGAGEE AGAPGDLHCI LISNPNEDAW KDPALEKLSL FCEESRSVND

WVPSITLPE
Length:159
Mass (Da):17,121
Last modified:May 1, 1999 - v1
Checksum:i26427E5881941E64
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34 – 35QR → HG in AAK00414 (PubMed:10773677).Curated2
Sequence conflicti113 – 115APG → CAC in AAK00414 (PubMed:10773677).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018888112G → S2 PublicationsCorresponds to variant dbSNP:rs3138505Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF078078 mRNA Translation: AAC83329.1
AF079806 mRNA Translation: AAD28544.1
AF265659 Genomic DNA Translation: AAF73468.1
AF087883 mRNA Translation: AAK00414.1
AK313689 mRNA Translation: BAG36438.1
BT007234 mRNA Translation: AAP35898.1
AF494037 Genomic DNA Translation: AAM00007.1
CH471089 Genomic DNA Translation: EAW62774.1
BC000465 mRNA Translation: AAH00465.1
BC019325 mRNA Translation: AAH19325.1
CCDSiCCDS6686.1
RefSeqiNP_006696.1, NM_006705.3
UniGeneiHs.9701

Genome annotation databases

EnsembliENST00000252506; ENSP00000252506; ENSG00000130222
GeneIDi10912
KEGGihsa:10912
UCSCiuc004aqq.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiGA45G_HUMAN
AccessioniPrimary (citable) accession number: O95257
Secondary accession number(s): Q5VZ87, Q9C076
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: June 20, 2018
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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