UniProtKB - Q6VRB0 (ANM1B_XENLA)
Protein
Protein arginine N-methyltransferase 1-B
Gene
prmt1-b
Organism
Xenopus laevis (African clawed frog)
Status
Functioni
Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in target proteins. 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 (By similarity). Methylates ilf3 to regulate its DNA-binding activity (PubMed:18636753). Required for neural induction, playing a key role in the control of epidermal versus neural cell fate choice (PubMed:16214893).By similarity2 Publications
Catalytic activityi
- L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H+ + Nω,Nω-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteineEC:2.1.1.319
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 43 | S-adenosyl-L-methionineBy similarity | 1 | |
Binding sitei | 52 | S-adenosyl-L-methionineBy similarity | 1 | |
Binding sitei | 76 | S-adenosyl-L-methionine; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 98 | S-adenosyl-L-methionineBy similarity | 1 | |
Binding sitei | 127 | S-adenosyl-L-methionineBy similarity | 1 | |
Active sitei | 142 | By similarity | 1 | |
Active sitei | 151 | By similarity | 1 |
GO - Molecular functioni
- histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
- identical protein binding Source: UniProtKB
- N-methyltransferase activity Source: UniProtKB
- protein-arginine N-methyltransferase activity Source: UniProtKB
- protein-arginine omega-N asymmetric methyltransferase activity Source: UniProtKB-EC
- protein-arginine omega-N monomethyltransferase activity Source: UniProtKB
- S-adenosyl-L-methionine binding Source: UniProtKB
GO - Biological processi
- histone H4-R3 methylation Source: UniProtKB
- histone methylation Source: UniProtKB
- negative regulation of megakaryocyte differentiation Source: UniProtKB
- neurogenesis Source: UniProtKB
- peptidyl-arginine methylation Source: UniProtKB
- positive regulation of cell population proliferation Source: UniProtKB
- protein homooligomerization Source: UniProtKB
- regulation of megakaryocyte differentiation Source: UniProtKB
Keywordsi
Molecular function | Activator, Developmental protein, Methyltransferase, Transferase |
Biological process | Differentiation, Neurogenesis, Transcription, Transcription regulation |
Ligand | S-adenosyl-L-methionine |
Names & Taxonomyi
Protein namesi | Recommended name: Protein arginine N-methyltransferase 1-B1 Publication (EC:2.1.1.3191 Publication)Short name: xPRMT1b1 Publication Alternative name(s): Arginine methyltransferase 1bImported Histone-arginine N-methyltransferase PRMT1-B |
Gene namesi | Name:prmt1-b Synonyms:prmt1, prmt1b1 Publication |
Organismi | Xenopus laevis (African clawed frog) |
Taxonomic identifieri | 8355 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Organism-specific databases
Xenbasei | XB-GENE-865039, prmt1.L |
Subcellular locationi
Cytoplasm and Cytosol
Nucleus
- Nucleus By similarity
- nucleoplasm By similarity
Cytosol
- cytosol Source: UniProtKB-SubCell
Nucleus
- nucleoplasm Source: UniProtKB-SubCell
Other locations
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000391366 | 1 – 351 | Protein arginine N-methyltransferase 1-BAdd BLAST | 351 |
Expressioni
Tissue specificityi
From the onset of gastrulation, expressed in dorsal mesoderm, and in dorsal and ventral ectoderm. At the neurula and tail bud stages, expression is restricted to the neuroectoderm, with highest expression in the anterior neural plate.1 Publication
Developmental stagei
Expressed both maternally and zygotically. Expressed throughout all embryonic stages.1 Publication
Inductioni
By Ca2+.1 Publication
Interactioni
Subunit structurei
Homodimer. Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane. Individual homodimers can associate to form a homohexamer (By similarity).
Component of a complex with lsm14a/rap55a.
Interacts with cirbp (By similarity).
By similarityGO - Molecular functioni
- identical protein binding Source: UniProtKB
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 30 – 331 | SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST | 302 |
Sequence similaritiesi
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Phylogenomic databases
OMAi | MEEDSAM |
OrthoDBi | 840669at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR025799, Arg_MeTrfase IPR041698, Methyltransf_25 IPR029063, SAM-dependent_MTases |
Pfami | View protein in Pfam PF13649, Methyltransf_25, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
PROSITEi | View protein in PROSITE PS51678, SAM_MT_PRMT, 1 hit |
i Sequence
Sequence statusi: Complete.
Q6VRB0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAEAKTCNME VSCALPEGSV KPNAEDMTSK DYYFDSYAHF GIHEEMLKDE
60 70 80 90 100
VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG AKKVIGIECS
110 120 130 140 150
SISDYAIKIV KANKLDHVVT IIKGKVEEVE LPVEKVDIII SEWMGYCLFY
160 170 180 190 200
ESMLNTVIYA RDKWLNPDGL IFPDRATLYV TAIEDRQYKD YKIHWWENVY
210 220 230 240 250
GFDMSCIKDV AIKEPLVDVV DPKQLVSNAC LIKEVDIYTV KVDDLTFTSP
260 270 280 290 300
FCLQVKRNDY IHAMVAYFNI EFTRCHKRTG FSTSPESPYT HWKQTVFYME
310 320 330 340 350
DYLTVKTGEE IFGTISMKPN AKNNRDLDFT VDIDFKGQLC ELSCSTDYRM
R
Sequence cautioni
The sequence AAH72069 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAI06276 differs from that shown. Reason: Erroneous initiation.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 14 | A → P in AAI06276 (Ref. 2) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY330768 mRNA Translation: AAQ65243.1 BC072069 mRNA Translation: AAH72069.1 Different initiation. BC106275 mRNA Translation: AAI06276.1 Different initiation. |
RefSeqi | NP_001082771.1, NM_001089302.1 |
Genome annotation databases
GeneIDi | 398716 |
KEGGi | xla:398716 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY330768 mRNA Translation: AAQ65243.1 BC072069 mRNA Translation: AAH72069.1 Different initiation. BC106275 mRNA Translation: AAI06276.1 Different initiation. |
RefSeqi | NP_001082771.1, NM_001089302.1 |
3D structure databases
SMRi | Q6VRB0 |
ModBasei | Search... |
Genome annotation databases
GeneIDi | 398716 |
KEGGi | xla:398716 |
Organism-specific databases
CTDi | 398716 |
Xenbasei | XB-GENE-865039, prmt1.L |
Phylogenomic databases
OMAi | MEEDSAM |
OrthoDBi | 840669at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR025799, Arg_MeTrfase IPR041698, Methyltransf_25 IPR029063, SAM-dependent_MTases |
Pfami | View protein in Pfam PF13649, Methyltransf_25, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
PROSITEi | View protein in PROSITE PS51678, SAM_MT_PRMT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ANM1B_XENLA | |
Accessioni | Q6VRB0Primary (citable) accession number: Q6VRB0 Secondary accession number(s): Q3KQC7, Q6IP49 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 9, 2010 |
Last sequence update: | July 5, 2004 | |
Last modified: | December 2, 2020 | |
This is version 71 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |