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Protein

RNA-binding protein with multiple splicing 2

Gene

rbpms2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Contributes to the regulation of smooth muscle cell differentiation and proliferation in the gastrointestinal system. Binds nog mRNA. Mediates an increase of nog mRNA levels, and thereby contributes to the negative regulation of the bmp signaling pathway. This promotes reversible dedifferentiation of smooth muscle cells and promotes smooth muscle cell proliferation.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein with multiple splicing 2
Alternative name(s):
Heart and RRM expressed sequence1 Publication
Short name:
Hermes1 Publication
Gene namesi
Name:rbpms2Curated
Synonyms:hermes1 Publication
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196RNA-binding protein with multiple splicing 2PRO_0000081796Add
BLAST

Expressioni

Tissue specificityi

Expressed in developing heart, pronephros, retina and epiphysis. In adult, high expression in heart, moderate in kidney, undetectable in liver, lung and skeletal muscle.1 Publication

Developmental stagei

mRNA first detected in the tailbud embryo (stage 26) in the paired heart primordia and in the condensing epithelium that will form the pronephros; at the late tailbud stage (stage 34) in the developing retina and epiphysis. As development proceeds, detected through the entire length of the heart tube, in the muscular tissue of the outflow tract, and in the duct epithelium of the pronephros. During later development, mRNA found in all subregions of the heart, in the glomus, tubules and duct of the pronephros, in the retinal ganglion cell layer (gcl) and in the epiphysis.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9YGP5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9778RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 4011Important for homodimerizationBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 144Poly-Asn
Compositional biasi167 – 1726Poly-Ala

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG069897.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR024888. RRM_U1_A/B''.
[Graphical view]
PANTHERiPTHR10501. PTHR10501. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9YGP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGIKSDTEH NNNNIEEEVR TLFVSGLPID IKPRELYLLF RPFKGYEGSL
60 70 80 90 100
IKLTSKQPVG FVTFDNRAGA EAAKNALNGI RFDPENPQTL RLEFAKANTK
110 120 130 140 150
MAKNKLMATP NPTNFHPALG AHFIARDPYD FTGAALIPAS PEAWAPYPLY
160 170 180 190
TAELAPAIPH AAFTYPAAAA AALHAQMRWY PPSEATQQGW KSRQFC
Length:196
Mass (Da):21,676
Last modified:May 1, 1999 - v1
Checksum:i7964198C1122A3D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF107889 mRNA. Translation: AAD16971.1.
BC097507 mRNA. Translation: AAH97507.1.
RefSeqiNP_001081864.1. NM_001088395.1.
UniGeneiXl.449.

Genome annotation databases

GeneIDi398092.
KEGGixla:398092.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF107889 mRNA. Translation: AAD16971.1.
BC097507 mRNA. Translation: AAH97507.1.
RefSeqiNP_001081864.1. NM_001088395.1.
UniGeneiXl.449.

3D structure databases

ProteinModelPortaliQ9YGP5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398092.
KEGGixla:398092.

Organism-specific databases

CTDi11030.

Phylogenomic databases

HOVERGENiHBG069897.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR024888. RRM_U1_A/B''.
[Graphical view]
PANTHERiPTHR10501. PTHR10501. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRBPS2_XENLA
AccessioniPrimary (citable) accession number: Q9YGP5
Secondary accession number(s): Q4V877
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.