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Protein

RNA-binding protein CP29B, chloroplastic

Gene

CP29B

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Could be involved in splicing and/or processing of chloroplast RNA's.Curated

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(U) RNA binding Source: TAIR

GO - Biological processi

  • innate immune response Source: TAIR
  • mRNA processing Source: UniProtKB-KW
  • response to abscisic acid Source: TAIR
  • response to cold Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein CP29B, chloroplasticCurated
Alternative name(s):
Ribonucleoprotein At2g37220
Gene namesi
Name:CP29BCurated
Ordered Locus Names:At2g37220
ORF Names:F3G5.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G37220.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • chloroplast thylakoid Source: TAIR
  • chloroplast thylakoid membrane Source: TAIR
  • intracellular ribonucleoprotein complex Source: UniProtKB-KW
  • stromule Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 62ChloroplastCombined sourcesAdd BLAST62
ChainiPRO_000003101963 – 289RNA-binding protein CP29B, chloroplasticAdd BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63N-acetylvalineCombined sources1

Post-translational modificationi

ADP-ribosylated by the Pseudomonas syringae type III effector HopU1. ADP-ribosylation reduces the ability of the protein to bind RNA.1 Publication
Phosphorylated on tyrosine residues after treatment with abscisic acid (ABA). Phosphorylation may reduce the ability of the protein to bind RNA.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9ZUU4.
PRIDEiQ9ZUU4.

2D gel databases

SWISS-2DPAGEQ9ZUU4.

PTM databases

iPTMnetiQ9ZUU4.

Expressioni

Gene expression databases

GenevisibleiQ9ZUU4. AT.

Interactioni

Protein-protein interaction databases

BioGridi3643. 2 interactors.
IntActiQ9ZUU4. 2 interactors.
STRINGi3702.AT2G37220.1.

Structurei

3D structure databases

ProteinModelPortaliQ9ZUU4.
SMRiQ9ZUU4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 169RRM 1PROSITE-ProRule annotationAdd BLAST79
Domaini204 – 282RRM 2PROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni170 – 203Linker (Gly-rich)Add BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 57Ser-richAdd BLAST54
Compositional biasi168 – 171Poly-Pro4

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiENOG410IQX9. Eukaryota.
ENOG4111MZ2. LUCA.
HOGENOMiHOG000276232.
InParanoidiQ9ZUU4.
KOiK11294.
OMAiSHRFISR.
OrthoDBiEOG09360LZZ.
PhylomeDBiQ9ZUU4.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ZUU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASASSLAL SSFNPKSLPF GVSRPASVSL LSPSLSFKLN SDSVSFSIAA
60 70 80 90 100
KWNSPASRFA RNVAITSEFE VEEDGFADVA PPKEQSFSAD LKLFVGNLPF
110 120 130 140 150
NVDSAQLAQL FESAGNVEMV EVIYDKITGR SRGFGFVTMS SVSEVEAAAQ
160 170 180 190 200
QFNGYELDGR PLRVNAGPPP PKREDGFSRG PRSSFGSSGS GYGGGGGSGA
210 220 230 240 250
GSGNRVYVGN LSWGVDDMAL ESLFSEQGKV VEARVIYDRD SGRSKGFGFV
260 270 280
TYDSSQEVQN AIKSLDGADL DGRQIRVSEA EARPPRRQY
Length:289
Mass (Da):30,718
Last modified:May 1, 1999 - v1
Checksum:iE500C3C0518369AD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti60A → V in AAM66970 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005896 Genomic DNA. Translation: AAC98043.1.
AC006260 Genomic DNA. Translation: AAM15222.1.
CP002685 Genomic DNA. Translation: AEC09369.1.
AF370167 mRNA. Translation: AAK43982.1.
AY048251 mRNA. Translation: AAK82513.1.
AY059129 mRNA. Translation: AAL15235.1.
AY088648 mRNA. Translation: AAM66970.1.
PIRiA84790.
RefSeqiNP_181259.1. NM_129278.4.
UniGeneiAt.25300.

Genome annotation databases

EnsemblPlantsiAT2G37220.1; AT2G37220.1; AT2G37220.
GeneIDi818299.
GrameneiAT2G37220.1; AT2G37220.1; AT2G37220.
KEGGiath:AT2G37220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005896 Genomic DNA. Translation: AAC98043.1.
AC006260 Genomic DNA. Translation: AAM15222.1.
CP002685 Genomic DNA. Translation: AEC09369.1.
AF370167 mRNA. Translation: AAK43982.1.
AY048251 mRNA. Translation: AAK82513.1.
AY059129 mRNA. Translation: AAL15235.1.
AY088648 mRNA. Translation: AAM66970.1.
PIRiA84790.
RefSeqiNP_181259.1. NM_129278.4.
UniGeneiAt.25300.

3D structure databases

ProteinModelPortaliQ9ZUU4.
SMRiQ9ZUU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3643. 2 interactors.
IntActiQ9ZUU4. 2 interactors.
STRINGi3702.AT2G37220.1.

PTM databases

iPTMnetiQ9ZUU4.

2D gel databases

SWISS-2DPAGEQ9ZUU4.

Proteomic databases

PaxDbiQ9ZUU4.
PRIDEiQ9ZUU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G37220.1; AT2G37220.1; AT2G37220.
GeneIDi818299.
GrameneiAT2G37220.1; AT2G37220.1; AT2G37220.
KEGGiath:AT2G37220.

Organism-specific databases

TAIRiAT2G37220.

Phylogenomic databases

eggNOGiENOG410IQX9. Eukaryota.
ENOG4111MZ2. LUCA.
HOGENOMiHOG000276232.
InParanoidiQ9ZUU4.
KOiK11294.
OMAiSHRFISR.
OrthoDBiEOG09360LZZ.
PhylomeDBiQ9ZUU4.

Miscellaneous databases

PROiQ9ZUU4.

Gene expression databases

GenevisibleiQ9ZUU4. AT.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCP29B_ARATH
AccessioniPrimary (citable) accession number: Q9ZUU4
Secondary accession number(s): Q7GA50, Q8L941
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.