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Q9BTL3 (RAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNMT-activating mini protein

Short name=RAM
Alternative name(s):
Protein FAM103A1
Gene names
Name:FAM103A1
Synonyms:C15orf18
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for efficient mRNA cap methylation. Regulates RNMT expression by a post-transcriptional stabilizing mechanism. Ref.5

Subunit structure

Interacts with RNMT, enhancing its mRNA binding capacity and cap methyltransferase activity. Ref.5

Subcellular location

Nucleus Ref.5.

Sequence similarities

Belongs to the RAM family.

Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
   Cellular componentNucleus
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 118118RNMT-activating mini protein
PRO_0000089983

Regions

Region1 – 5555Interaction with RNMT
Region56 – 11863RNA-binding
Compositional bias91 – 11828Gln/Tyr-rich

Amino acid modifications

Modified residue361Phosphoserine Ref.2 Ref.3 Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9BTL3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 266B56E66A73A1AE

FASTA11814,381
        10         20         30         40         50         60 
MTDTAEAVPK FEEMFASRFT ENDKEYQEYL KRPPESPPIV EEWNSRAGGN QRNRGNRLQD 

        70         80         90        100        110 
NRQFRGRDNR WGWPSDNRSN QWHGRSWGNN YPQHRQEPYY PQQYGHYGYN QRPPYGYY 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Melanoma, Ovarian adenocarcinoma and Skin.
[2]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[3]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[4]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[5]"RAM/Fam103a1 is required for mRNA cap methylation."
Gonatopoulos-Pournatzis T., Dunn S., Bounds R., Cowling V.H.
Mol. Cell 44:585-596(2011) [PubMed: 22099306] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH RNMT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC003627 mRNA. Translation: AAH03627.1.
BC027181 mRNA. Translation: AAH27181.1.
BC112329 mRNA. Translation: AAI12330.1.
IPIIPI00027798.
RefSeqNP_113640.1. NM_031452.2.
UniGeneHs.727661.

3D structure databases

ProteinModelPortalQ9BTL3.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BTL3. 4 interactions.
MINTMINT-1452092.

PTM databases

PhosphoSiteQ9BTL3.

Proteomic databases

PRIDEQ9BTL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304191; ENSP00000307181; ENSG00000169612.
GeneID83640.
KEGGhsa:83640.
UCSCuc002bjl.1. human.

Organism-specific databases

CTD83640.
GeneCardsGC15P083654.
H-InvDBHIX0012517.
HGNCHGNC:31022. FAM103A1.
HPAHPA041923.
HPA041948.
neXtProtNX_Q9BTL3.
PharmGKBPA142671786.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG20835.
GeneTreeENSGT00390000011190.
HOGENOMHBG126961.
HOVERGENHBG081491.
InParanoidQ9BTL3.
OMADNRRGWP.
OrthoDBEOG44TP98.
PhylomeDBQ9BTL3.

Gene expression databases

ArrayExpressQ9BTL3.
BgeeQ9BTL3.
CleanExHS_FAM103A1.
GenevestigatorQ9BTL3.
GermOnlineENSG00000169612. Homo sapiens.

Family and domain databases

ProtoNetSearch...

Other

NextBio72587.

Entry information

Entry nameRAM_HUMAN
AccessionPrimary (citable) accession number: Q9BTL3
Secondary accession number(s): Q2M1J8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

SIMILARITY comments

Index of protein domains and families