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Protein

mRNA decay activator protein ZFP36

Gene

Zfp36

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Zinc-finger RNA-binding protein that destabilizes numerous cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:10330172, PubMed:10706852, PubMed:10805719, PubMed:15014438, PubMed:15187092, PubMed:15634918, PubMed:17030620, PubMed:19188452, PubMed:20595389, PubMed:21078877, PubMed:22701344, PubMed:27193233). Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (PubMed:21278420). Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation (PubMed:21278420). Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs (PubMed:21278420). Self regulates by destabilizing its own mRNA (PubMed:15187092, PubMed:17288565). Binds to 3'-UTR ARE of numerous mRNAs and of its own mRNA (PubMed:11533235, PubMed:15187092, PubMed:16508014, PubMed:17288565, PubMed:17971298, PubMed:20595389, PubMed:21078877, PubMed:21278420, PubMed:22701344, PubMed:27193233). Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages (PubMed:8630730, PubMed:9703499, PubMed:15014438, PubMed:16514065). Plays also a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response (By similarity). Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia (By similarity). Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (PubMed:22701344). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA (By similarity). Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE-mediated mRNA decay of the myogenic determination factor MYOD1 mRNA (PubMed:25815583). Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs (By similarity). Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs (By similarity). May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro (By similarity). Involved in the delivery of target ARE-mRNAs to processing bodies (PBs) (By similarity). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing (PubMed:22844456). Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages (PubMed:22844456). Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion (PubMed:15967811). Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis (By similarity). Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells (By similarity).By similarity23 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri95 – 123C3H1-type 1PROSITE-ProRule annotationAdd BLAST29
Zinc fingeri133 – 161C3H1-type 2PROSITE-ProRule annotationAdd BLAST29

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • AU-rich element binding Source: UniProtKB
  • C-C chemokine binding Source: MGI
  • DNA binding Source: UniProtKB-KW
  • enzyme binding Source: MGI
  • heat shock protein binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • mRNA 3'-UTR AU-rich region binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: GO_Central
  • mRNA binding Source: UniProtKB
  • poly(A) RNA binding Source: MGI
  • protein kinase binding Source: MGI
  • RNA polymerase binding Source: UniProtKB

GO - Biological processi

  • 3'-UTR-mediated mRNA destabilization Source: UniProtKB
  • 3'-UTR-mediated mRNA stabilization Source: UniProtKB
  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • cellular response to fibroblast growth factor stimulus Source: UniProtKB
  • cellular response to glucocorticoid stimulus Source: UniProtKB
  • cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
  • cellular response to lipopolysaccharide Source: UniProtKB
  • cellular response to tumor necrosis factor Source: UniProtKB
  • intracellular signal transduction Source: MGI
  • MAPK cascade Source: UniProtKB
  • miRNA mediated inhibition of translation Source: UniProtKB
  • mRNA catabolic process Source: UniProtKB
  • mRNA transport Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of erythrocyte differentiation Source: UniProtKB
  • negative regulation of inflammatory response Source: UniProtKB
  • negative regulation of interleukin-2 biosynthetic process Source: UniProtKB
  • negative regulation of myeloid cell differentiation Source: MGI
  • negative regulation of polynucleotide adenylyltransferase activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of viral transcription Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: MGI
  • nuclear-transcribed mRNA catabolic process, deadenylation-independent decay Source: UniProtKB
  • nuclear-transcribed mRNA poly(A) tail shortening Source: MGI
  • p38MAPK cascade Source: UniProtKB
  • positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA Source: UniProtKB
  • positive regulation of fat cell differentiation Source: UniProtKB
  • positive regulation of gene silencing by miRNA Source: UniProtKB
  • positive regulation of intracellular mRNA localization Source: UniProtKB
  • positive regulation of mRNA catabolic process Source: UniProtKB
  • positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
  • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
  • regulation of keratinocyte apoptotic process Source: UniProtKB
  • regulation of keratinocyte differentiation Source: UniProtKB
  • regulation of keratinocyte proliferation Source: UniProtKB
  • regulation of mRNA stability Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of tumor necrosis factor production Source: UniProtKB
  • response to starvation Source: UniProtKB
  • response to wounding Source: UniProtKB
  • RNA destabilization Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ribonucleoprotein

Keywords - Biological processi

mRNA transport, Transport

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA decay activator protein ZFP36Curated
Alternative name(s):
Growth factor-inducible nuclear protein NUP475Curated
TPA-induced sequence 111 Publication
Tristetraprolin1 Publication
Zinc finger protein 361 PublicationImported
Short name:
Zfp-361 Publication
Gene namesi
Name:Zfp361 PublicationImported
Synonyms:Nup4751 Publication, Tis111 Publication, Tis11a, Ttp1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:99180. Zfp36.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytoplasmic stress granule Source: UniProtKB
  • cytosol Source: MGI
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • nucleus Source: UniProtKB
  • ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice appear normal at birth, but within 1-8 weeks after birth they develop a complex syndrome of cachexia, arthritis, autoimmunity, myeloid hyperplasia and general inflammation (PubMed:8630730). Show precocious skeletal muscle satellite cell activation and increased satellite cell fusion into myofibers (PubMed:25815583). Show higher levels of tumor necrosis factor (TNF)-alpha mRNA and protein in macrophages and an excess of circulating TNF-alpha (PubMed:8630730, PubMed:9703499, PubMed:16508014). Show higher levels of granulocyte-macrophage colony-stimulating factor (GM-CSF) expression in macrophages and an excess of GM-CSF secretion upon lipopolysaccharide (LPS) stimulation (PubMed:10706852). Show higher levels of serine/threonine-protein kinase PLK3 expression in macrophages (PubMed:19188452). Show higher levels of interleukin IL2 expression in splenocytes and T lymphocytes and an excess of IL2 secretion upon T cell activation (PubMed:15634918). Show an increase in the stability of numerous mRNAs, such as TNF-alpha, GM-CSF, IL2 and PLK3 mRNAs (PubMed:9703499, PubMed:10706852, PubMed:15634918, PubMed:17030620, PubMed:19188452). Show an absence of ARE-containing transcript deadenylation (PubMed:10330172). Mice with a double knockout of ZFP36 and MAPKAPK2 show increased amounts of TNF in macrophages almost comparable to single ZFP36 knockout (PubMed:16508014).9 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52S → A: Impairs phosphorylation by MAPKAPK2, decreases its stability and cytoplasmic localization, increases interaction with PPP2CA, inhibits binding to 14-3-3 proteins, but does not impair binding to ARE-containing transcripts, recruitment of mRNA decay factors and ZFP36-mediated deadenylation and decay of ARE-containing transcripts; when associated with A-178. 6 Publications1
Mutagenesisi178S → A: Reduces both interaction with 14-3-3 proteins and YWHAB-induced cytoplasmic localization. Impairs phosphorylation by MAPKAPK2, decreases its stability and cytoplasmic localization, increases interaction with PPP2CA, inhibits binding to 14-3-3 proteins, but does not impair binding to ARE-containing transcripts, recruitment of mRNA decay factors and ZFP36-mediated deadenylation and decay of ARE-containing transcripts; when associated with A-52. 7 Publications1
Mutagenesisi303P → A: Stimulates interaction with SH3KBP1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000891641 – 319mRNA decay activator protein ZFP36Add BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52Phosphoserine; by MAPKAPK23 Publications1
Modified residuei58PhosphoserineBy similarity1
Modified residuei80Phosphoserine1 Publication1
Modified residuei82Phosphoserine1 Publication1
Modified residuei84PhosphothreonineBy similarity1
Modified residuei85Phosphoserine1 Publication1
Modified residuei178Phosphoserine; by MAPKAPK23 Publications1
Modified residuei189PhosphoserineBy similarity1
Modified residuei210PhosphoserineBy similarity1
Modified residuei220Phosphoserine; by MAPK1; in vitro1 Publication1
Modified residuei250Phosphothreonine1 Publication1
Modified residuei269PhosphoserineBy similarity1
Modified residuei289PhosphoserineBy similarity1
Modified residuei316Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated (PubMed:11533235). Phosphorylation at serine and/or threonine residues occurs in a p38 MAPK- and MAPKAPK2-dependent manner (PubMed:11533235). Phosphorylated by MAPKAPK2 at Ser-52 and Ser-178; phosphorylation increases its stability and cytoplasmic localization, promotes binding to 14-3-3 adapter proteins and inhibits the recruitment of cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase complexes to the mRNA decay machinery, thereby inhibiting ZFP36-induced ARE-containing mRNA deadenylation and decay processes (PubMed:15014438, PubMed:14688255, PubMed:16508014, PubMed:16508015, PubMed:17170118, PubMed:20595389, PubMed:21078877). Phosphorylation by MAPKAPK2 does not impair ARE-containing RNA-binding (PubMed:20595389, PubMed:21078877). Phosphorylated in a MAPKAPK2- and p38 MAPK-dependent manner upon skeletal muscle satellite cell activation; this phosphorylation inhibits ZFP36-mediated mRNA decay activity, and hence stabilizes MYOD1 mRNA (PubMed:25815583). Phosphorylated by MAPK1 upon mitogen stimulation (PubMed:7768935, PubMed:14688255). Phosphorylated at Ser-58 and Ser-85; these phosphorylations increase in a SH3KBP1-dependent manner (By similarity). Phosphorylated at serine and threonine residues in a pyruvate kinase PKM- and p38 MAPK-dependent manner (By similarity). Phosphorylation at Ser-52 may participate in the PKM-mediated degradation of ZFP36 in a p38 MAPK-dependent manner (By similarity). Dephosphorylated by serine/threonine phosphatase 2A at Ser-178 (PubMed:11533235, PubMed:17170118).By similarity10 Publications
Ubiquitinated; pyruvate kinase (PKM)-dependent ubiquitination leads to proteasomal degradation through a p38 MAPK signaling pathway.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP22893.
PeptideAtlasiP22893.
PRIDEiP22893.

PTM databases

iPTMnetiP22893.
PhosphoSitePlusiP22893.

Expressioni

Tissue specificityi

Expressed in skeletal muscle satellite cells (PubMed:25815583). Strongly expressed in differentiated adipocytes compared to preadipocytes (at protein level) (PubMed:22701344). Expressed in embryonic stem cells (ESCs) (PubMed:24733888). Expressed in heart, placenta, kidney, intestine, liver, lung, thymus, fat and spleen (PubMed:2204625, PubMed:1699942).5 Publications

Inductioni

Up-regulated during adipocyte differentiation (PubMed:17288565, PubMed:22701344). Up-regulated transiently in response to fibroblast growth factor FGF4 in a MAPK-dependent manner in embryonic stem cells (ESCs) (PubMed:24733888). Up-regulated by interferons and/or lipopolysaccharide (LPS) in a STAT1- and p38 MAPK-dependent manner (PubMed:11533235, PubMed:16514065, PubMed:16508014, PubMed:16508015). Down-regulated in muscle satellite cells upon muscle injury (at protein level) (PubMed:25815583). Up-regulated by various mitogens (PubMed:7559666). Up-regulated by LPS and TNF-alpha (PubMed:9703499). Up-regulated by interferon IFN-gamma and/or LPS in a STAT1- and p38 MAPK-dependent manner (PubMed:15187092, PubMed:16514065). Up-regulated during adipocyte differentiation (PubMed:22701344). Up-regulated in keratinocytes during epidermal repair after wound healing (PubMed:20166898). Down-regulated during the conversion from quiescence to activated satellite cells upon muscle injury (PubMed:23046558, PubMed:25815583).13 Publications

Gene expression databases

BgeeiENSMUSG00000044786.
CleanExiMM_ZFP36.
ExpressionAtlasiP22893. baseline and differential.
GenevisibleiP22893. MM.

Interactioni

Subunit structurei

Associates with cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase complexes to trigger ARE-containing mRNA deadenylation and decay processes (PubMed:20595389, PubMed:21078877). Part of a mRNA decay activation complex at least composed of poly(A)-specific exoribonucleases CNOT6, EXOSC2 and XRN1 and mRNA-decapping enzymes DCP1A and DCP2 (By similarity). Associates with the RNA exosome complex (By similarity). Interacts (via phosphorylated form) with 14-3-3 proteins; these interactions promote exclusion of ZFP36 from cytoplasmic stress granules in response to arsenite treatment in a MAPKAPK2-dependent manner and does not prevent CCR4-NOT deadenylase complex recruitment or ZFP36-induced ARE-containing mRNA deadenylation and decay processes (PubMed:15014438, PubMed:20595389). Interacts with 14-3-3 proteins; these interactions occur in response to rapamycin in an Akt-dependent manner (By similarity). Interacts with AGO2 and AGO4 (By similarity). Interacts (via C-terminus) with CNOT1; this interaction occurs in a RNA-independent manner and induces mRNA deadenylation (PubMed:21278420). Interacts (via N-terminus) with CNOT6 (By similarity). Interacts with CNOT6L (PubMed:21078877). Interacts (via C-terminus) with CNOT7; this interaction occurs in a RNA-independent manner, induces mRNA deadenylation and is inhibited in a phosphorylation MAPKAPK2-dependent manner (PubMed:20595389, PubMed:21278420). Interacts (via unphosphorylated form) with CNOT8; this interaction occurs in a RNA-independent manner and is inhibited in a phosphorylation MAPKAPK2-dependent manner (PubMed:20595389). Interacts with DCP1A (By similarity). Interacts (via N-terminus) with DCP2 (By similarity). Interacts with EDC3 (By similarity). Interacts (via N-terminus) with EXOSC2 (By similarity). Interacts with heat shock 70 kDa proteins (By similarity). Interacts with KHSRP; this interaction increases upon cytokine-induced treatment (By similarity). Interacts with MAP3K4; this interaction enhances the association with SH3KBP1/CIN85 (By similarity). Interacts with MAPKAPK2; this interaction occurs upon skeletal muscle satellite cell activation (PubMed:25815583). Interacts with NCL (By similarity). Interacts with NUP214; this interaction increases upon lipopolysaccharide (LPS) stimulation (By similarity). Interacts with PABPC1; this interaction occurs in a RNA-dependent manner (PubMed:20595389, PubMed:21078877). Interacts (via hypophosphorylated form) with PABPN1 (via RRM domain and C-terminal arginine-rich region); this interaction occurs in the nucleus in a RNA-independent manner, decreases in presence of single-stranded poly(A) RNA-oligomer and in a p38 MAPK-dependent-manner and inhibits nuclear poly(A) tail synthesis (PubMed:22844456). Interacts with PAN2 (PubMed:21078877). Interacts (via C3H1-type zinc finger domains) with PKM (By similarity). Interacts (via C3H1-type zinc finger domains) with nuclear RNA poly(A) polymerase (PubMed:22844456). Interacts with PPP2CA; this interaction occurs in LPS-stimulated cells and induces ZFP36 dephosphorylation, and hence may promote ARE-containing mRNAs decay (PubMed:17170118). Interacts (via C-terminus) with PRR5L (via C-terminus); this interaction may accelerate ZFP36-mediated mRNA decay during stress (By similarity). Interacts (via C-terminus) with SFN; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Interacts (via extreme C-terminal region) with SH3KBP1/CIN85 (via SH3 domains); this interaction enhances MAP3K4-induced phosphorylation of ZFP36 at Ser-58 and Ser-85 and does not alter neither ZFP36 binding to ARE-containing transcripts nor TNF-alpha mRNA decay (By similarity). Interacts with XRN1 (By similarity). Interacts (via C-terminus and Ser-178 phosphorylated form) with YWHAB; this interaction occurs in a p38/MAPKAPK2-dependent manner, increases cytoplasmic localization of ZFP36 and protects ZFP36 from Ser-178 dephosphorylation by serine/threonine phosphatase 2A, and hence may be crucial for stabilizing ARE-containing mRNAs (PubMed:14688255, PubMed:17170118). Interacts (via phosphorylated form) with YWHAE (PubMed:21078877). Interacts (via C-terminus) with YWHAG; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Interacts with YWHAH; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Interacts with YWHAQ; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Interacts with (via C-terminus) YWHAZ; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Does not interact with SH3KBP1 (PubMed:20221403).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CNOT1A5YKK65EBI-647803,EBI-1222758From a different organism.
CNOT7Q9UIV13EBI-647803,EBI-2105113From a different organism.
YWHABP319465EBI-647803,EBI-359815From a different organism.

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • C-C chemokine binding Source: MGI
  • enzyme binding Source: MGI
  • heat shock protein binding Source: MGI
  • protein kinase binding Source: MGI
  • RNA polymerase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi204658. 3 interactors.
IntActiP22893. 34 interactors.
MINTiMINT-225240.
STRINGi10090.ENSMUSP00000057815.

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi103 – 106Combined sources4
Turni111 – 115Combined sources5
Beta strandi120 – 122Combined sources3
Helixi125 – 127Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M9ONMR-A91-163[»]
ProteinModelPortaliP22893.
SMRiP22893.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22893.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati63 – 67P-P-P-P-G5
Repeati190 – 194P-P-P-P-G5
Repeati211 – 215P-P-P-P-G5

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 166Necessary for localization of ARE-containing mRNAs to processing bodies (PBs)By similarityAdd BLAST166
Regioni1 – 92Necessary and sufficient for the association with mRNA decay enzymes and mRNA decay activationBy similarityAdd BLAST92
Regioni1 – 15Necessary for nuclear exportBy similarityAdd BLAST15
Regioni87 – 160Necessary for nuclear localizationBy similarityAdd BLAST74
Regioni89 – 165Necessary for RNA-bindingBy similarityAdd BLAST77
Regioni92 – 319Necessary for localization of ARE-containing mRNAs to processing bodies (PBs)By similarityAdd BLAST228
Regioni95 – 186Necessary for interaction with PABPN11 PublicationAdd BLAST92
Regioni166 – 319Necessary for mRNA decay activationBy similarityAdd BLAST154
Regioni305 – 319Interaction with CNOT1By similarityAdd BLAST15

Domaini

The C3H1-type zinc finger domains are necessary for ARE-binding activity.By similarity

Sequence similaritiesi

Contains 2 C3H1-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri95 – 123C3H1-type 1PROSITE-ProRule annotationAdd BLAST29
Zinc fingeri133 – 161C3H1-type 2PROSITE-ProRule annotationAdd BLAST29

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1677. Eukaryota.
COG5063. LUCA.
GeneTreeiENSGT00530000063262.
HOGENOMiHOG000233479.
HOVERGENiHBG008483.
InParanoidiP22893.
KOiK15308.
OMAiPACCPSC.
OrthoDBiEOG091G0957.
PhylomeDBiP22893.
TreeFamiTF315463.

Family and domain databases

Gene3Di4.10.1000.10. 2 hits.
InterProiIPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00642. zf-CCCH. 2 hits.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 2 hits.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 2 hits.
PROSITEiPS50103. ZF_C3H1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22893-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLSAIYESL QSMSHDLSSD HGGTESLGGL WNINSDSIPS GVTSRLTGRS
60 70 80 90 100
TSLVEGRSCG WVPPPPGFAP LAPRPGPELS PSPTSPTATP TTSSRYKTEL
110 120 130 140 150
CRTYSESGRC RYGAKCQFAH GLGELRQANR HPKYKTELCH KFYLQGRCPY
160 170 180 190 200
GSRCHFIHNP TEDLALPGQP HVLRQSISFS GLPSGRRSSP PPPGFSGPSL
210 220 230 240 250
SSCSFSPSSS PPPPGDLPLS PSAFSAAPGT PVTRRDPNQA CCPSCRRSTT
260 270 280 290 300
PSTIWGPLGG LARSPSAHSL GSDPDDYASS GSSLGGSDSP VFEAGVFGPP
310
QTPAPPRRLP IFNRISVSE
Length:319
Mass (Da):33,613
Last modified:August 1, 1991 - v1
Checksum:i860DD6DDA80386F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57422 mRNA. Translation: AAA40498.1.
M58691 mRNA. Translation: AAA39837.1.
X14678 mRNA. Translation: CAA32807.1. Sequence problems.
M58565 mRNA. Translation: AAA72947.1.
L42317 Genomic DNA. Translation: AAC37676.1.
BC021391 mRNA. Translation: AAH21391.1.
CCDSiCCDS21041.1.
PIRiA36600.
S04743.
RefSeqiNP_035886.1. NM_011756.4.
UniGeneiMm.389856.

Genome annotation databases

EnsembliENSMUST00000051241; ENSMUSP00000057815; ENSMUSG00000044786.
GeneIDi22695.
KEGGimmu:22695.
UCSCiuc009fys.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57422 mRNA. Translation: AAA40498.1.
M58691 mRNA. Translation: AAA39837.1.
X14678 mRNA. Translation: CAA32807.1. Sequence problems.
M58565 mRNA. Translation: AAA72947.1.
L42317 Genomic DNA. Translation: AAC37676.1.
BC021391 mRNA. Translation: AAH21391.1.
CCDSiCCDS21041.1.
PIRiA36600.
S04743.
RefSeqiNP_035886.1. NM_011756.4.
UniGeneiMm.389856.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M9ONMR-A91-163[»]
ProteinModelPortaliP22893.
SMRiP22893.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204658. 3 interactors.
IntActiP22893. 34 interactors.
MINTiMINT-225240.
STRINGi10090.ENSMUSP00000057815.

PTM databases

iPTMnetiP22893.
PhosphoSitePlusiP22893.

Proteomic databases

PaxDbiP22893.
PeptideAtlasiP22893.
PRIDEiP22893.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051241; ENSMUSP00000057815; ENSMUSG00000044786.
GeneIDi22695.
KEGGimmu:22695.
UCSCiuc009fys.1. mouse.

Organism-specific databases

CTDi7538.
MGIiMGI:99180. Zfp36.

Phylogenomic databases

eggNOGiKOG1677. Eukaryota.
COG5063. LUCA.
GeneTreeiENSGT00530000063262.
HOGENOMiHOG000233479.
HOVERGENiHBG008483.
InParanoidiP22893.
KOiK15308.
OMAiPACCPSC.
OrthoDBiEOG091G0957.
PhylomeDBiP22893.
TreeFamiTF315463.

Miscellaneous databases

EvolutionaryTraceiP22893.
PROiP22893.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000044786.
CleanExiMM_ZFP36.
ExpressionAtlasiP22893. baseline and differential.
GenevisibleiP22893. MM.

Family and domain databases

Gene3Di4.10.1000.10. 2 hits.
InterProiIPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00642. zf-CCCH. 2 hits.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 2 hits.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 2 hits.
PROSITEiPS50103. ZF_C3H1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTTP_MOUSE
AccessioniPrimary (citable) accession number: P22893
Secondary accession number(s): P11520
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 30, 2016
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.