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Q9JIF0

- ANM1_MOUSE

UniProt

Q9JIF0 - ANM1_MOUSE

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Protein

Protein arginine N-methyltransferase 1

Gene

Prmt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631S-adenosyl-L-methionineBy similarity
Binding sitei72 – 721S-adenosyl-L-methionineBy similarity
Binding sitei96 – 961S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei118 – 1181S-adenosyl-L-methionineBy similarity
Binding sitei147 – 1471S-adenosyl-L-methionineBy similarity
Active sitei162 – 1621By similarity
Active sitei171 – 1711By similarity

GO - Molecular functioni

  1. histone methyltransferase activity Source: MGI
  2. histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
  3. N-methyltransferase activity Source: UniProtKB
  4. poly(A) RNA binding Source: Ensembl
  5. protein-arginine N-methyltransferase activity Source: MGI
  6. protein-arginine omega-N asymmetric methyltransferase activity Source: RefGenome
  7. protein methyltransferase activity Source: MGI

GO - Biological processi

  1. histone H4-R3 methylation Source: UniProtKB
  2. in utero embryonic development Source: MGI
  3. negative regulation of megakaryocyte differentiation Source: UniProtKB
  4. neuron projection development Source: Ensembl
  5. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: RefGenome
  6. regulation of transcription, DNA-templated Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_244207. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 1 (EC:2.1.1.-)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT1 (EC:2.1.1.125)
Gene namesi
Name:Prmt1
Synonyms:Hrmt1l2, Mrmt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:107846. Prmt1.

Subcellular locationi

Nucleus. Nucleusnucleoplasm. Cytoplasmcytosol
Note: Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction.

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 371371Protein arginine N-methyltransferase 1PRO_0000212322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341N6-succinyllysine1 Publication

Proteomic databases

MaxQBiQ9JIF0.
PaxDbiQ9JIF0.
PRIDEiQ9JIF0.

PTM databases

PhosphoSiteiQ9JIF0.

Expressioni

Gene expression databases

BgeeiQ9JIF0.
CleanExiMM_PRMT1.
ExpressionAtlasiQ9JIF0. baseline and differential.
GenevestigatoriQ9JIF0.

Interactioni

Subunit structurei

Homodimer and heterodimer with PRMT8. Individual homodimers can associate to form a homohexamer. Interacts with BTG1, BTG2 and IFNAR1. Interacts with ILF3 and SUPT5H. Interacts with and methylates FOXO1, leading to the nuclear retention of FOXO1 and the stimulation of FOXO1 transcriptional activity. Methylation of FOXO1 is increased upon oxidative stress (By similarity). Interacts with NFATC2IP. Interacts with and methylates CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Axin1Q14DJ83EBI-519055,EBI-4312125
ChtopQ9CY578EBI-519055,EBI-6393116
Khdrbs1Q607492EBI-519055,EBI-519077
Smad6O351823EBI-519055,EBI-4321242

Protein-protein interaction databases

BioGridi200423. 11 interactions.
IntActiQ9JIF0. 14 interactions.
MINTiMINT-3981922.

Structurei

3D structure databases

ProteinModelPortaliQ9JIF0.
SMRiQ9JIF0. Positions 59-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 371322SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ9JIF0.
KOiK11434.
OMAiRCHKRIG.
OrthoDBiEOG7S7SDJ.
PhylomeDBiQ9JIF0.
TreeFamiTF300608.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9JIF0-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAEAANCI MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK
60 70 80 90 100
DYYFDSYAHF GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG
110 120 130 140 150
ILCMFAAKAG ARKVIGIECS SISDYAVKIV KANKLDHVVT IIKGKVEEVE
160 170 180 190 200
LPVEKVDIII SEWMGYCLFY ESMLNTVLHA RDKWLAPDGL IFPDRATLYV
210 220 230 240 250
TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVTNAC
260 270 280 290 300
LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG
310 320 330 340 350
FSTSPESPYT HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT
360 370
IDLDFKGQLC ELSCSTDYRM R
Length:371
Mass (Da):42,436
Last modified:October 1, 2000 - v1
Checksum:iAEFCF63001B1A38C
GO
Isoform 2 (identifier: Q9JIF0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     13-30: Missing.

Show »
Length:353
Mass (Da):40,522
Checksum:iEDBB0587784C527E
GO
Isoform 3 (identifier: Q9JIF0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MAAAEAANCIMENFVATLANGMSLQPPLE → M

Show »
Length:343
Mass (Da):39,576
Checksum:i257BAC1C484B274E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929MAAAE…QPPLE → M in isoform 3. 1 PublicationVSP_005211Add
BLAST
Alternative sequencei13 – 3018Missing in isoform 2. 1 PublicationVSP_005210Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232716 mRNA. Translation: AAF37292.1.
AF232717 mRNA. Translation: AAF37293.1.
BC002249 mRNA. Translation: AAH02249.1.
CCDSiCCDS21222.1. [Q9JIF0-1]
CCDS57547.1. [Q9JIF0-2]
RefSeqiNP_001239405.1. NM_001252476.1. [Q9JIF0-2]
NP_062804.1. NM_019830.3. [Q9JIF0-1]
UniGeneiMm.27545.

Genome annotation databases

EnsembliENSMUST00000107842; ENSMUSP00000103473; ENSMUSG00000052429. [Q9JIF0-2]
ENSMUST00000107843; ENSMUSP00000103474; ENSMUSG00000052429. [Q9JIF0-1]
GeneIDi15469.
KEGGimmu:15469.
UCSCiuc009gsg.2. mouse. [Q9JIF0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232716 mRNA. Translation: AAF37292.1 .
AF232717 mRNA. Translation: AAF37293.1 .
BC002249 mRNA. Translation: AAH02249.1 .
CCDSi CCDS21222.1. [Q9JIF0-1 ]
CCDS57547.1. [Q9JIF0-2 ]
RefSeqi NP_001239405.1. NM_001252476.1. [Q9JIF0-2 ]
NP_062804.1. NM_019830.3. [Q9JIF0-1 ]
UniGenei Mm.27545.

3D structure databases

ProteinModelPortali Q9JIF0.
SMRi Q9JIF0. Positions 59-371.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200423. 11 interactions.
IntActi Q9JIF0. 14 interactions.
MINTi MINT-3981922.

PTM databases

PhosphoSitei Q9JIF0.

Proteomic databases

MaxQBi Q9JIF0.
PaxDbi Q9JIF0.
PRIDEi Q9JIF0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000107842 ; ENSMUSP00000103473 ; ENSMUSG00000052429 . [Q9JIF0-2 ]
ENSMUST00000107843 ; ENSMUSP00000103474 ; ENSMUSG00000052429 . [Q9JIF0-1 ]
GeneIDi 15469.
KEGGi mmu:15469.
UCSCi uc009gsg.2. mouse. [Q9JIF0-1 ]

Organism-specific databases

CTDi 3276.
MGIi MGI:107846. Prmt1.

Phylogenomic databases

eggNOGi COG0500.
GeneTreei ENSGT00550000074406.
HOGENOMi HOG000198521.
HOVERGENi HBG001793.
InParanoidi Q9JIF0.
KOi K11434.
OMAi RCHKRIG.
OrthoDBi EOG7S7SDJ.
PhylomeDBi Q9JIF0.
TreeFami TF300608.

Enzyme and pathway databases

Reactomei REACT_244207. RMTs methylate histone arginines.

Miscellaneous databases

NextBioi 288310.
PROi Q9JIF0.
SOURCEi Search...

Gene expression databases

Bgeei Q9JIF0.
CleanExi MM_PRMT1.
ExpressionAtlasi Q9JIF0. baseline and differential.
Genevestigatori Q9JIF0.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR11006. PTHR11006. 1 hit.
Pfami PF13847. Methyltransf_31. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable."
    Pawlak M.R., Scherer C.A., Chen J., Roshon M.J., Ruley H.E.
    Mol. Cell. Biol. 20:4859-4869(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "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] (ISOFORM 3).
  3. "Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes."
    Mowen K.A., Schurter B.T., Fathman J.W., David M., Glimcher L.H.
    Mol. Cell 15:559-571(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NFATC2IP.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CHTOP, SUBCELLULAR LOCATION.
    Tissue: Erythroblast.
  5. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
    Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
    Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHTOP, SUBCELLULAR LOCATION.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiANM1_MOUSE
AccessioniPrimary (citable) accession number: Q9JIF0
Secondary accession number(s): Q99LS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3