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Protein

RNMT-activating mini protein

Gene

FAM103A1

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

Functioni

Regulatory subunit of the mRNA-capping methyltransferase RNMT:RAM/FAM103A1 complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs (PubMed:22099306, PubMed:27422871). Promotes the recruitment of the methyl donor, S-adenosyl-L-methionine, to RNMT (PubMed:27422871). Regulates RNMT expression by a post-transcriptional stabilizing mechanism (PubMed:22099306). Binds RNA (PubMed:22099306).2 Publications

GO - Molecular functioni

  • RNA binding Source: UniProtKB

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: UniProtKB
  • methylation Source: UniProtKB
  • recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex Source: UniProtKB
  • RNA 5'-cap (guanine-N7)-methylation Source: GOC

Keywordsi

Molecular functionRNA-binding
Biological processmRNA capping, mRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
RNMT-activating mini protein
Short name:
RAM
Alternative name(s):
Protein FAM103A1
Gene namesi
Name:FAM103A1
Synonyms:C15orf18
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000169612.3
HGNCiHGNC:31022 FAM103A1
MIMi614547 gene
neXtProtiNX_Q9BTL3

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi83640
PharmGKBiPA142671786

Polymorphism and mutation databases

BioMutaiFAM103A1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000899832 – 118RNMT-activating mini proteinAdd BLAST117

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei36PhosphoserineCombined sources1
Modified residuei85Omega-N-methylarginineCombined sources1
Modified residuei86PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ9BTL3
MaxQBiQ9BTL3
PaxDbiQ9BTL3
PeptideAtlasiQ9BTL3
PRIDEiQ9BTL3

PTM databases

iPTMnetiQ9BTL3
PhosphoSitePlusiQ9BTL3

Expressioni

Gene expression databases

BgeeiENSG00000169612
CleanExiHS_FAM103A1
GenevisibleiQ9BTL3 HS

Organism-specific databases

HPAiHPA041923
HPA041948

Interactioni

Subunit structurei

Interacts with RNMT; this interaction enhances mRNA binding and cap methyltransferase activity.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi123704, 26 interactors
IntActiQ9BTL3, 48 interactors
STRINGi9606.ENSP00000307181

Structurei

Secondary structure

1118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Turni15 – 19Combined sources5
Helixi24 – 30Combined sources7
Beta strandi39 – 41Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5E8JX-ray2.35C/D2-45[»]
ProteinModelPortaliQ9BTL3
SMRiQ9BTL3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 55Interaction with RNMT1 PublicationAdd BLAST54
Regioni56 – 118RNA-binding1 PublicationAdd BLAST63

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi36 – 42RNMT-activating domain1 Publication7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi91 – 118Gln/Tyr-richAdd BLAST28

Sequence similaritiesi

Belongs to the RAM family.Curated

Phylogenomic databases

eggNOGiENOG410IY7E Eukaryota
ENOG41122CR LUCA
GeneTreeiENSGT00390000011190
HOGENOMiHOG000112423
HOVERGENiHBG081491
InParanoidiQ9BTL3
KOiK18708
OMAiPYYPHQY
OrthoDBiEOG091G172R
PhylomeDBiQ9BTL3
TreeFamiTF335880

Family and domain databases

InterProiView protein in InterPro
IPR028271 RAM
PfamiView protein in Pfam
PF15320 RAM, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9BTL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDTAEAVPK FEEMFASRFT ENDKEYQEYL KRPPESPPIV EEWNSRAGGN
60 70 80 90 100
QRNRGNRLQD NRQFRGRDNR WGWPSDNRSN QWHGRSWGNN YPQHRQEPYY
110
PQQYGHYGYN QRPPYGYY
Length:118
Mass (Da):14,381
Last modified:June 1, 2001 - v1
Checksum:i266B56E66A73A1AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC003627 mRNA Translation: AAH03627.1
BC027181 mRNA Translation: AAH27181.1
BC112329 mRNA Translation: AAI12330.1
CCDSiCCDS10321.1
RefSeqiNP_113640.1, NM_031452.3
UniGeneiHs.80624

Genome annotation databases

EnsembliENST00000304191; ENSP00000307181; ENSG00000169612
GeneIDi83640
KEGGihsa:83640
UCSCiuc002bjl.3 human

Similar proteinsi

Entry informationi

Entry nameiRAM_HUMAN
AccessioniPrimary (citable) accession number: Q9BTL3
Secondary accession number(s): Q2M1J8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2001
Last modified: May 23, 2018
This is version 121 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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