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Protein

RNMT-activating mini protein

Gene

FAM103A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for efficient mRNA cap methylation. Regulates RNMT expression by a post-transcriptional stabilizing mechanism.1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • 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
Complete GO annotation...

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

RNA-binding

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

HGNCiHGNC:31022. FAM103A1.

Subcellular locationi

GO - Cellular componenti

  • mRNA cap binding complex Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671786.

Polymorphism and mutation databases

BioMutaiFAM103A1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 118117RNMT-activating mini proteinPRO_0000089983Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources
Modified residuei36 – 361PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9BTL3.
MaxQBiQ9BTL3.
PaxDbiQ9BTL3.
PRIDEiQ9BTL3.

PTM databases

iPTMnetiQ9BTL3.
PhosphoSiteiQ9BTL3.

Expressioni

Gene expression databases

BgeeiQ9BTL3.
CleanExiHS_FAM103A1.
GenevisibleiQ9BTL3. HS.

Organism-specific databases

HPAiHPA041923.
HPA041948.

Interactioni

Subunit structurei

Interacts with RNMT, enhancing its mRNA binding capacity and cap methyltransferase activity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DAB1O755533EBI-744023,EBI-7875264
INCA1Q0VD863EBI-744023,EBI-6509505
KRT31Q153233EBI-744023,EBI-948001
LZTS2Q9BRK43EBI-744023,EBI-741037
PSMA3P257883EBI-744023,EBI-348380
RBMY1JQ154153EBI-744023,EBI-8642021
TRIM23P364063EBI-744023,EBI-740098
TRIM27P143733EBI-744023,EBI-719493
TRIM42A1L4B63EBI-744023,EBI-10172216

Protein-protein interaction databases

BioGridi123704. 26 interactions.
IntActiQ9BTL3. 17 interactions.
MINTiMINT-1452092.
STRINGi9606.ENSP00000307181.

Structurei

3D structure databases

ProteinModelPortaliQ9BTL3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5554Interaction with RNMTAdd
BLAST
Regioni56 – 11863RNA-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi91 – 11828Gln/Tyr-richAdd
BLAST

Sequence similaritiesi

Belongs to the RAM family.Curated

Phylogenomic databases

eggNOGiENOG410IY7E. Eukaryota.
ENOG41122CR. LUCA.
GeneTreeiENSGT00390000011190.
HOGENOMiHOG000112423.
HOVERGENiHBG081491.
InParanoidiQ9BTL3.
KOiK18708.
OMAiSRRGWPS.
OrthoDBiEOG7JT708.
PhylomeDBiQ9BTL3.
TreeFamiTF335880.

Family and domain databases

InterProiIPR028271. RAM.
[Graphical view]
PfamiPF15320. RAM. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9BTL3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123704. 26 interactions.
IntActiQ9BTL3. 17 interactions.
MINTiMINT-1452092.
STRINGi9606.ENSP00000307181.

PTM databases

iPTMnetiQ9BTL3.
PhosphoSiteiQ9BTL3.

Polymorphism and mutation databases

BioMutaiFAM103A1.

Proteomic databases

EPDiQ9BTL3.
MaxQBiQ9BTL3.
PaxDbiQ9BTL3.
PRIDEiQ9BTL3.

Protocols and materials databases

DNASUi83640.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi83640.
GeneCardsiFAM103A1.
H-InvDBHIX0012517.
HIX0200864.
HGNCiHGNC:31022. FAM103A1.
HPAiHPA041923.
HPA041948.
MIMi614547. gene.
neXtProtiNX_Q9BTL3.
PharmGKBiPA142671786.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IY7E. Eukaryota.
ENOG41122CR. LUCA.
GeneTreeiENSGT00390000011190.
HOGENOMiHOG000112423.
HOVERGENiHBG081491.
InParanoidiQ9BTL3.
KOiK18708.
OMAiSRRGWPS.
OrthoDBiEOG7JT708.
PhylomeDBiQ9BTL3.
TreeFamiTF335880.

Miscellaneous databases

GenomeRNAii83640.
NextBioi72587.
PROiQ9BTL3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BTL3.
CleanExiHS_FAM103A1.
GenevisibleiQ9BTL3. HS.

Family and domain databases

InterProiIPR028271. RAM.
[Graphical view]
PfamiPF15320. RAM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH RNMT.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAM_HUMAN
AccessioniPrimary (citable) accession number: Q9BTL3
Secondary accession number(s): Q2M1J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2001
Last modified: April 13, 2016
This is version 107 of the entry and version 1 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.