PRMT1

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, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP and MAP3K5/ASK1 (PubMed:10749851, PubMed:16879614, PubMed:26876602, PubMed:22095282, PubMed:26575292, PubMed:18951090, PubMed:25284789).

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. 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. Methylates RBM15, promoting ubiquitination and degradation of RBM15 (PubMed:26575292).

Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity (PubMed:18951090).

Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed:25284789).

Methylates MAP3K5/ASK1 at 'Arg-78' and 'Arg-80' which promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5-induced activation of JNK (PubMed:22095282).

Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789).

Plays a role in regulating alternative splicing in the heart (By similarity).

By similarity16 Publications

Caution

A paper showing that PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling has been retracted, because some of the data was found to be deliberately falsified.2 Publications

Catalytic activityⁱ

L-arginyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+ 2
S-adenosyl-L-methionine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
= 2
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N^ω,N^ω-dimethyl-L-arginyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+ 2
S-adenosyl-L-homocysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
6 Publications
Manual assertion based on experiment inⁱ
- Ref.11
  "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1."
  Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H., Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.
  Curr. Biol. 11:996-1000(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY.
- Ref.12
  "Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor."
  Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H., Strahl B.D., Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.
  Science 293:853-857(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Ref.20
  "Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4."
  Lakowski T.M., Frankel A.
  Biochem. J. 421:253-261(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Ref.26
  "Arginine methylation-dependent regulation of ASK1 signaling by PRMT1."
  Cho J.H., Lee M.K., Yoon K.W., Lee J., Cho S.G., Choi E.J.
  Cell Death Differ. 19:859-870(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAP3K5.
- Ref.29
  "Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing."
  Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A., Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X., Zhou W., Laha S., Abdel-Wahab O., Levine R.L.
  Zhao X.
  Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY.
- Ref.33
  "FAM98A associates with DDX1-C14orf166-FAM98B in a novel complex involved in colorectal cancer progression."
  Akter K.A., Mansour M.A., Hyodo T., Senga T.
  Int. J. Biochem. Cell Biol. 84:1-13(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
EC:
2.1.1.319
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
6 Publications
Manual assertion based on experiment inⁱ
- Ref.11
  "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1."
  Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H., Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.
  Curr. Biol. 11:996-1000(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY.
- Ref.12
  "Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor."
  Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H., Strahl B.D., Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.
  Science 293:853-857(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Ref.20
  "Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4."
  Lakowski T.M., Frankel A.
  Biochem. J. 421:253-261(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Ref.26
  "Arginine methylation-dependent regulation of ASK1 signaling by PRMT1."
  Cho J.H., Lee M.K., Yoon K.W., Lee J., Cho S.G., Choi E.J.
  Cell Death Differ. 19:859-870(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAP3K5.
- Ref.29
  "Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing."
  Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A., Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X., Zhou W., Laha S., Abdel-Wahab O., Levine R.L.
  Zhao X.
  Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY.
- Ref.33
  "FAM98A associates with DDX1-C14orf166-FAM98B in a novel complex involved in colorectal cancer progression."
  Akter K.A., Mansour M.A., Hyodo T., Senga T.
  Int. J. Biochem. Cell Biol. 84:1-13(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
L-arginyl-[protein]
L-arginine residue
zoom
+
2
S-adenosyl-L-methionine
zoom
=
2
H⁺
+
N^ω,N^ω-dimethyl-L-arginyl-[protein]
N^ω,N^ω-dimethyl-L-arginine residue
zoom
+
2
S-adenosyl-L-homocysteine
zoom

Activity regulationⁱ

By BTG1, BTG2 and ILF3.

Kineticsⁱ

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	63	S-adenosyl-L-methionineBy similarity	1
Binding siteⁱ	72	S-adenosyl-L-methionineBy similarity	1
Binding siteⁱ	96	S-adenosyl-L-methionine; via carbonyl oxygenBy similarity	1
Binding siteⁱ	118	S-adenosyl-L-methionineBy similarity	1
Binding siteⁱ	147	S-adenosyl-L-methionineBy similarity	1
Active siteⁱ	162	By similarity	1
Active siteⁱ	171	By similarity	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Methyltransferase, Transferase
Ligand	S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAⁱ	2.1.1.319, 2681
PathwayCommonsⁱ	Q99873
Reactomeⁱ	R-HSA-3214858, RMTs methylate histone arginines R-HSA-6804114, TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest R-HSA-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-HSA-9009391, Extra-nuclear estrogen signaling R-HSA-9018519, Estrogen-dependent gene expression R-HSA-9694631, Maturation of nucleoprotein
SABIO-RKⁱ	Q99873
SignaLinkⁱ	Q99873
SIGNORⁱ	Q99873

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Protein arginine N-methyltransferase 1Curated (EC:2.1.1.3196 Publications) Alternative name(s): Histone-arginine N-methyltransferase PRMT1 Interferon receptor 1-bound protein 4
Gene namesⁱ	Name:PRMT1Imported Synonyms:HMT2, HRMT1L22 Publications, IR1B4
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:5187, PRMT1
MIMⁱ	602950, gene
neXtProtⁱ	NX_Q99873
VEuPathDBⁱ	HostDB:ENSG00000126457

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	92	V → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication	1
Mutagenesisⁱ	93	L → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication	1
Mutagenesisⁱ	94	D → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication	1
Mutagenesisⁱ	280	Y → A: No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-322 and A-359. No effect on homodimerization but loss of homooligomerization; when associated with A-322 and A-359. 1 Publication	1
Mutagenesisⁱ	322	Y → A: No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-280 and A-359. No effect on homodimerization but loss of homooligomerization; when associated with A-280 and A-359. 1 Publication	1
Mutagenesisⁱ	359	L → A: No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-280 and A-322. No effect on homodimerization but loss of homooligomerization; when associated with A-280 and A-322. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3276
Open Targets More...OpenTargetsⁱ	ENSG00000126457
PharmGKBⁱ	PA29461

Miscellaneous databases

Pharosⁱ	Q99873, Tchem

Pharosⁱ

Q99873, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL5524
Drug and drug target database More...DrugBankⁱ	DB01752, S-adenosyl-L-homocysteine
DrugCentral More...DrugCentralⁱ	Q99873
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1252

Genetic variation databases

BioMutaⁱ	PRMT1
DMDMⁱ	161789011

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000212321	1 – 371	Protein arginine N-methyltransferase 1Add BLAST		371

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	134	N6-succinyllysineBy similarity	1
Cross-linkⁱ	145	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	228	N6-acetyllysineBy similarity	1
Modified residueⁱ	233	N6-acetyllysineBy similarity	1
Modified residueⁱ	304	PhosphoserineCombined sources	1
Modified residueⁱ	307	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Polyubiquitinated at Lys-145 by the SCF(FBXL17) complex, leading to its subsequent degradation (By similarity). Ubiquitination is regulated by acetylation at Lys-228 and Lys-233 (By similarity). Polyubiquitinated by E3 ubiquitin-protein ligase TRIM48, leading to suppression of MAP3K5/ASK1 methylation and subsequent MAP3K5 activation (PubMed:29186683).By similarity1 Publication

Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the SCF(FBXL17) complex. Acetylated at Lys-233 by p300/EP300. Deacetylated at Lys-228 and Lys-233 by SIRT1.By similarity

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q99873
jPOSTⁱ	Q99873
MassIVEⁱ	Q99873
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q99873
PaxDbⁱ	Q99873
PeptideAtlas More...PeptideAtlasⁱ	Q99873
PRIDEⁱ	Q99873
ProteomicsDBⁱ	33891 44996 78511 [Q99873-1] 78512 [Q99873-2] 78513 [Q99873-3]

PTM databases

GlyGenⁱ	Q99873, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	Q99873
PhosphoSitePlusⁱ	Q99873
SwissPalmⁱ	Q99873

Expressionⁱ

Tissue specificityⁱ

Widely expressed (PubMed:11097842). Expressed strongly in colorectal cancer cells (at protein level) (PubMed:28040436). Expressed strongly in colorectal cancer tissues compared to wild-type colon samples (at protein level) (PubMed:28040436). Expressed strongly in colorectal cancer tissues compared to wild-type colon samples (PubMed:28040436).2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000126457, Expressed in embryo and 231 other tissues
ExpressionAtlasⁱ	Q99873, baseline and differential
Genevisibleⁱ	Q99873, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000126457, Low tissue specificity

HPAⁱ

ENSG00000126457, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:16879614, PubMed:26876602). Homooctamer; individual homodimers associates to form a homooctamer (PubMed:26876602). Individual homodimers can associate to form a homohexamer. Heterodimer with PRMT8.

Interacts with BTG1, BTG2, NFATC2IP and IFNAR1 (By similarity).

Interacts with and methylates CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex (PubMed:25284789).

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.

Interacts with and probably methylates ATXN2L (PubMed:25748791).

Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH (PubMed:25284789).

Interacts with DHX9 (via RGG region) (PubMed:15084609).

Interacts (via N-terminus) with HABP4 (PubMed:16879614).

Interacts with MAP3K5/ASK1; the interaction results in MAP3K5 methylation by PRMT1 which inhibits MAP3K5 activation (PubMed:22095282).

Interacts with TRIM48; the interaction results in ubiquitination of PRMT1 by TRIM48, leading to PRMT1 proteasomal degradation and activation of MAP3K5 (PubMed:29186683).

By similarity12 Publications

Binary interactionsⁱ

Hide details

Q99873

With	#Exp.	IntAct
CHTOP [Q9Y3Y2]	2	EBI-78738,EBI-347794
DCAF8 [Q5TAQ9]	2	EBI-78738,EBI-740686
DHX9 [Q08211]	2	EBI-78738,EBI-352022
EWSR1 [Q01844]	2	EBI-78738,EBI-739737
FAM9A [Q8IZU1]	2	EBI-78738,EBI-8468186
FUS [P35637]	5	EBI-78738,EBI-400434
H4C9 [P62805]	2	EBI-78738,EBI-302023
HABP4 [Q5JVS0]	2	EBI-78738,EBI-523625
HNRNPK [P61978]	3	EBI-78738,EBI-304185
HNRNPR [O43390]	5	EBI-78738,EBI-713419
ILF3 [Q12906]	2	EBI-78738,EBI-78756
NR4A1 [P22736]	6	EBI-78738,EBI-721550
NRIP1 [P48552]	4	EBI-78738,EBI-746484
NTAQ1 [Q96HA8]	3	EBI-78738,EBI-741158
OFCC1 [Q8IZS5]	2	EBI-78738,EBI-8477661
itself	4	EBI-78738,EBI-78738
PRMT8 [Q9NR22]	3	EBI-78738,EBI-745545
PRMT8 - isoform 2 [Q9NR22-2]	5	EBI-78738,EBI-10186886
SPEG [Q15772]	3	EBI-78738,EBI-1384196
SPSB1 [Q96BD6]	2	EBI-78738,EBI-2659201
SPSB2 [Q99619]	2	EBI-78738,EBI-2323209
SYNCRIP [O60506]	2	EBI-78738,EBI-1024357
VHL [P40337]	2	EBI-78738,EBI-301246
Nucleocapsid protein p7 (PRO_0000038596) from Human immunodeficiency virus type 1 group M subtype B (isolate HXB2).	2	EBI-78738,EBI-6179727
N [P0DTC9] from Severe acute respiratory syndrome coronavirus 2.	3	EBI-78738,EBI-25475856

Isoform 2 [Q99873-2]

With	#Exp.	IntAct
DR1 [Q01658]	3	EBI-16399024,EBI-750300

PRMT1 - isoform 3 [Q99873-3]

With	#Exp.	IntAct
CDC37 [Q16543]	3	EBI-17165527,EBI-295634
FUS [P35637]	3	EBI-17165527,EBI-400434
itself	3	EBI-17165527,EBI-17165527
PRMT8 [Q9NR22]	10	EBI-17165527,EBI-745545
SPEG - isoform 3 [Q15772-4]	3	EBI-17165527,EBI-12175897
SYNCRIP - isoform 4 [O60506-4]	4	EBI-17165527,EBI-11123832

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	109512, 330 interactors
CORUMⁱ	Q99873
Database of interacting proteins More...DIPⁱ	DIP-30878N
IntActⁱ	Q99873, 131 interactors
Molecular INTeraction database More...MINTⁱ	Q99873
STRINGⁱ	9606.ENSP00000406162

Chemistry databases

BindingDBⁱ

Q99873

Miscellaneous databases

RNActⁱ	Q99873, protein

RNActⁱ

Q99873, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	44 – 46	Combined sources	3
Helixⁱ	49 – 52	Combined sources	4
Helixⁱ	56 – 58	Combined sources	3
Helixⁱ	60 – 68	Combined sources	9
Helixⁱ	70 – 81	Combined sources	12
Helixⁱ	84 – 87	Combined sources	4
Beta strandⁱ	91 – 96	Combined sources	6
Helixⁱ	101 – 108	Combined sources	8
Beta strandⁱ	112 – 118	Combined sources	7
Helixⁱ	123 – 132	Combined sources	10
Turnⁱ	136 – 138	Combined sources	3
Beta strandⁱ	139 – 144	Combined sources	6
Helixⁱ	146 – 148	Combined sources	3
Beta strandⁱ	152 – 154	Combined sources	3
Beta strandⁱ	156 – 160	Combined sources	5
Turnⁱ	169 – 171	Combined sources	3
Helixⁱ	174 – 184	Combined sources	11
Beta strandⁱ	185 – 193	Combined sources	9
Beta strandⁱ	195 – 203	Combined sources	9
Helixⁱ	206 – 212	Combined sources	7
Helixⁱ	214 – 217	Combined sources	4
Helixⁱ	225 – 231	Combined sources	7
Beta strandⁱ	236 – 238	Combined sources	3
Helixⁱ	242 – 244	Combined sources	3
Beta strandⁱ	250 – 256	Combined sources	7
Turnⁱ	257 – 259	Combined sources	3
Helixⁱ	262 – 265	Combined sources	4
Beta strandⁱ	266 – 275	Combined sources	10
Beta strandⁱ	277 – 291	Combined sources	15
Beta strandⁱ	295 – 297	Combined sources	3
Beta strandⁱ	300 – 302	Combined sources	3
Beta strandⁱ	314 – 325	Combined sources	12
Beta strandⁱ	330 – 339	Combined sources	10
Beta strandⁱ	346 – 356	Combined sources	11
Beta strandⁱ	361 – 370	Combined sources	10

Show more details

3D structure databases

AlphaFoldDBⁱ	Q99873
SMRⁱ	Q99873
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	50 – 361	SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST		312

Sequence similaritiesⁱ

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGⁱ	KOG1499, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000154700
InParanoidⁱ	Q99873
OMAⁱ	TTDRMEV
Database of Orthologous Groups More...OrthoDBⁱ	840669at2759
PhylomeDBⁱ	Q99873
TreeFamⁱ	TF300608

Family and domain databases

Gene3Dⁱ	3.40.50.150, 1 hit
InterProⁱ	View protein in InterPro IPR025799, Arg_MeTrfase IPR041698, Methyltransf_25 IPR029063, SAM-dependent_MTases
PANTHERⁱ	PTHR11006, PTHR11006, 1 hit
Pfam protein domain database More...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

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 8 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q99873-1) [UniParc]FASTA Add to basket

Also known as: V2

This isoform has been chosen as the canonicalⁱ 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 ESMLNTVLYA 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):42,462

Last modified:March 28, 2018 - v3

Checksum:ⁱ544349801B0E1396

GO

Isoform 2 (identifier: Q99873-2) [UniParc]FASTA Add to basket

Also known as: V3

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

« Hide

        10         20         30         40         50
MVGVAEVSCG QAESSEKPNA EDMTSKDYYF DSYAHFGIHE EMLKDEVRTL 
        60         70         80         90        100
TYRNSMFHNR HLFKDKVVLD VGSGTGILCM FAAKAGARKV IGIECSSISD 
       110        120        130        140        150
YAVKIVKANK LDHVVTIIKG KVEEVELPVE KVDIIISEWM GYCLFYESML 
       160        170        180        190        200
NTVLYARDKW LAPDGLIFPD RATLYVTAIE DRQYKDYKIH WWENVYGFDM 
       210        220        230        240        250
SCIKDVAIKE PLVDVVDPKQ LVTNACLIKE VDIYTVKVED LTFTSPFCLQ 
       260        270        280        290        300
VKRNDYVHAL VAYFNIEFTR CHKRTGFSTS PESPYTHWKQ TVFYMEDYLT 
       310        320        330        340 
VKTGEEIFGT IGMRPNAKNN RDLDFTIDLD FKGQLCELSC STDYRMR

Show »

Length:347

Mass (Da):39,929

Checksum:ⁱ2546A25EF744E265

GO

Isoform 3 (identifier: Q99873-3) [UniParc]FASTA Add to basket

Also known as: V1

The sequence of this isoform differs from the canonical sequence as follows:
11-30: MENFVATLANGMSLQPPLEE → ME

« Hide

        10         20         30         40         50
MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK 
        60         70         80         90        100
DEVRTLTYRN SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE 
       110        120        130        140        150
CSSISDYAVK IVKANKLDHV VTIIKGKVEE VELPVEKVDI IISEWMGYCL 
       160        170        180        190        200
FYESMLNTVL YARDKWLAPD GLIFPDRATL YVTAIEDRQY KDYKIHWWEN 
       210        220        230        240        250
VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY TVKVEDLTFT 
       260        270        280        290        300
SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY 
       310        320        330        340        350
MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY 

RMR

Show »

Length:353

Mass (Da):40,548

Checksum:ⁱ1704BA3762F3E264

GO

Isoform 4 (identifier: Q99873-5) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
13-30: Missing.
186-253: Missing.

« Hide

        10         20         30         40         50
MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK 
        60         70         80         90        100
DEVRTLTYRN SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE 
       110        120        130        140        150
CSSISDYAVK IVKANKLDHV VTIIKGKVEE VELPVEKVDI IISEWMGYCL 
       160        170        180        190        200
FYESMLNTVL YARDKWLEVD IYTVKVEDLT FTSPFCLQVK RNDYVHALVA 
       210        220        230        240        250
YFNIEFTRCH KRTGFSTSPE SPYTHWKQTV FYMEDYLTVK TGEEIFGTIG 
       260        270        280 
MRPNAKNNRD LDFTIDLDFK GQLCELSCST DYRMR

Show »

Length:285

Mass (Da):32,693

Checksum:ⁱ7D985F187D73F7E3

GO

Computationally mapped potential isoform sequencesⁱ

There are 8 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0YDE4	H0YDE4_HUMAN	Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 1	PRMT1	238	Annotation score:
E9PKG1	E9PKG1_HUMAN	Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 1	PRMT1	325	Annotation score:
E9PQ98	E9PQ98_HUMAN	Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 1	PRMT1	205	Annotation score:
E9PIX6	E9PIX6_HUMAN	Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 1	PRMT1	207	Annotation score:
E9PNR9	E9PNR9_HUMAN	Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 1	PRMT1	160	Annotation score:
E9PMW9	E9PMW9_HUMAN	Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 1	PRMT1	110	Annotation score:
E9PMZ2	E9PMZ2_HUMAN	Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 1	PRMT1	63	Annotation score:
E9PIE2	E9PIE2_HUMAN	Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 1	PRMT1	54	Annotation score:

Sequence cautionⁱ

The sequence AAF62894 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

The sequence AAF62895 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

The sequence AAI09283 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

The sequence AAI09284 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

The sequence BAA11029 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

The sequence CAA71764 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

The sequence CAA71765 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	118	E → V in CAA71763 (PubMed:9545638).Curated	1
Sequence conflictⁱ	118	E → V in CAA71764 (PubMed:9545638).Curated	1
Sequence conflictⁱ	118	E → V in CAA71765 (PubMed:9545638).Curated	1
Sequence conflictⁱ	118	E → V in BAA11029 (PubMed:8675017).Curated	1
Sequence conflictⁱ	157 – 185	DIIIS…RDKWL → ASSSASGWATASSTSPCSTP CSMPGTSV in BAA11029 (PubMed:8675017).CuratedAdd BLAST	29
Sequence conflictⁱ	212	K → E in BAG65435 (PubMed:14702039).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_037501	88	K → M. Corresponds to variant dbSNP:rs1804486Ensembl.		1
Natural variantⁱVAR_037502	168	L → F. Corresponds to variant dbSNP:rs11673683Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_005208	1 – 29	MAAAE…QPPLE → MVGVA in isoform 2. 1 PublicationAdd BLAST	29
Alternative sequenceⁱVSP_005209	11 – 30	MENFV…PPLEE → ME in isoform 3. 2 PublicationsAdd BLAST	20
Alternative sequenceⁱVSP_059419	13 – 30	Missing in isoform 4. Add BLAST	18
Alternative sequenceⁱVSP_059420	186 – 253	Missing in isoform 4. Add BLAST	68

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y10805 mRNA Translation: CAA71763.1 Y10806 mRNA Translation: CAA71764.1 Different initiation. Y10807 mRNA Translation: CAA71765.1 Different initiation. D66904 mRNA Translation: BAA11029.1 Different initiation. AF222689 Genomic DNA Translation: AAF62893.1 AF222689 Genomic DNA Translation: AAF62894.1 Different initiation. AF222689 Genomic DNA Translation: AAF62895.1 Different initiation. AK304660 mRNA Translation: BAG65435.1 CR407608 mRNA Translation: CAG28536.1 AC011495 Genomic DNA No translation available. CH471177 Genomic DNA Translation: EAW52521.1 CH471177 Genomic DNA Translation: EAW52519.1 BC019268 mRNA Translation: AAH19268.2 BC109282 mRNA Translation: AAI09283.2 Different initiation. BC109283 mRNA Translation: AAI09284.2 Different initiation.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS42592.1 [Q99873-3] CCDS46145.1 [Q99873-1] CCDS74425.1 [Q99873-5]
NCBI Reference Sequences More...RefSeqⁱ	NP_001193971.1, NM_001207042.2 [Q99873-5] NP_001527.3, NM_001536.5 [Q99873-1] NP_938074.2, NM_198318.4 [Q99873-3] XP_016882223.1, XM_017026734.1 [Q99873-2] XP_016882224.1, XM_017026735.1 [Q99873-2]

Genome annotation databases

Ensemblⁱ	ENST00000391851.8; ENSP00000375724.4; ENSG00000126457.22 [Q99873-3] ENST00000454376.7; ENSP00000406162.2; ENSG00000126457.22 ENST00000610806.4; ENSP00000484505.1; ENSG00000126457.22 [Q99873-5]
GeneIDⁱ	3276
KEGGⁱ	hsa:3276
MANE-Selectⁱ	ENST00000454376.7; ENSP00000406162.2; NM_001536.6; NP_001527.3
UCSC genome browser More...UCSCⁱ	uc002ppe.4, human [Q99873-1] uc010enf.3, human

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q99873	Protein arginine methyltransferase 1		CAPHI		371	UniRef100_Q99873
Protein arginine N-methyltransferase 1		wild yak		371
Protein arginine methyltransferase 1		CANLF		371
Protein arginine methyltransferase 1		PANTR		371
Protein arginine methyltransferase 1		pale spear-nosed bat		371
+53
Q99873-2	Protein arginine methyltransferase 1		PONAB		347	UniRef100_A0A8I5T3P9
protein arginine N-methyltransferase 1 isoform X5		ACIJB		347
Protein arginine methyltransferase 1		MOLMO		347
protein arginine N-methyltransferase 1 isoform X3		VULVU		347
protein arginine N-methyltransferase 1 isoform X4		Enhydra lutris kenyoni		347
+20
Q99873-3	Protein arginine methyltransferase 1		PANTR		353	UniRef100_K7CNS8
Protein arginine methyltransferase 1		CANLF		353
Protein arginine N-methyltransferase 1 isoform 3		MACMU		353
HMT1 hnRNP methyltransferase-like 2 isoform 3		BOVIN		353
protein arginine N-methyltransferase 1 isoform X3		SHEEP		353
+59
Q99873-5	Protein arginine methyltransferase 1		PANTR		285	UniRef100_K7D7S7
Protein arginine methyltransferase 1		BOBOX		285
Protein arginine methyltransferase 1		CANLF		285
Uncharacterized protein		RHIRO		285
Protein arginine methyltransferase 1		PANLE		285
+28

Protein	Similar proteins		Species	Score	Length	Source
Q99873	Protein arginine N-methyltransferase 1		MOUSE		371	UniRef90_Q99873
Protein arginine methyltransferase 1		CAPHI		371
Protein arginine N-methyltransferase 1		wild yak		371
Protein arginine methyltransferase 1		CANLF		371
Protein arginine methyltransferase 1		PANTR		371
+129
Q99873-2	Methyltransf_25 domain-containing protein		MOUSE		345	UniRef90_Q3TPF5
Protein arginine methyltransferase 1		CAPHI		430
protein arginine N-methyltransferase 1 isoform X3		CAMFR		359
Protein arginine methyltransferase 1		MOLMO		356
Protein arginine methyltransferase 1		BOVIN		355
+142
Q99873-5	Methyltransf_25 domain-containing protein		OTOGA		353	UniRef90_H0X5U3
Protein arginine methyltransferase 1		MICMU		353
Protein arginine methyltransferase 1		PROCO		353
Protein arginine methyltransferase 1		PIG		286
Uncharacterized protein		CALJA		285
+47

Protein	Similar proteins		Species	Score	Length	Source
Q99873	Protein arginine N-methyltransferase 1		MOUSE		371	UniRef50_Q99873
Protein arginine N-methyltransferase 1		XENTR		351
Protein arginine methyltransferase 1		CAPHI		371
Protein arginine N-methyltransferase 1		wild yak		371
Protein arginine methyltransferase 1		CANLF		371
+1162
Q99873-2	Protein arginine N-methyltransferase 1	)	RAT		353	UniRef50_Q63009
Protein arginine methyltransferase 1		NANGA		353
Methyltransf_25 domain-containing protein		NEOLE		353
Methyltransf_25 domain-containing protein		MOUSE		353
Protein arginine methyltransferase 1		JACJA		353
+507
Q99873-5	Protein arginine N-methyltransferase 1-B		XENLA		351	UniRef50_Q6VRB0
Protein arginine N-methyltransferase 1		CHLRE		345
Protein arginine N-methyltransferase 1		DICDI		341
Probable protein arginine N-methyltransferase 1.2		ARATH		366
Methyltransf_25 domain-containing protein		MACFA		371
+662

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y10805 mRNA Translation: CAA71763.1 Y10806 mRNA Translation: CAA71764.1 Different initiation. Y10807 mRNA Translation: CAA71765.1 Different initiation. D66904 mRNA Translation: BAA11029.1 Different initiation. AF222689 Genomic DNA Translation: AAF62893.1 AF222689 Genomic DNA Translation: AAF62894.1 Different initiation. AF222689 Genomic DNA Translation: AAF62895.1 Different initiation. AK304660 mRNA Translation: BAG65435.1 CR407608 mRNA Translation: CAG28536.1 AC011495 Genomic DNA No translation available. CH471177 Genomic DNA Translation: EAW52521.1 CH471177 Genomic DNA Translation: EAW52519.1 BC019268 mRNA Translation: AAH19268.2 BC109282 mRNA Translation: AAI09283.2 Different initiation. BC109283 mRNA Translation: AAI09284.2 Different initiation.
CCDSⁱ	CCDS42592.1 [Q99873-3] CCDS46145.1 [Q99873-1] CCDS74425.1 [Q99873-5]
RefSeqⁱ	NP_001193971.1, NM_001207042.2 [Q99873-5] NP_001527.3, NM_001536.5 [Q99873-1] NP_938074.2, NM_198318.4 [Q99873-3] XP_016882223.1, XM_017026734.1 [Q99873-2] XP_016882224.1, XM_017026735.1 [Q99873-2]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	6NT2	X-ray	2.48	A/B/C/D	1-371	[»]
AlphaFoldDBⁱ	Q99873
SMRⁱ	Q99873
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	109512, 330 interactors
CORUMⁱ	Q99873
DIPⁱ	DIP-30878N
IntActⁱ	Q99873, 131 interactors
MINTⁱ	Q99873
STRINGⁱ	9606.ENSP00000406162

Chemistry databases

BindingDBⁱ	Q99873
ChEMBLⁱ	CHEMBL5524
DrugBankⁱ	DB01752, S-adenosyl-L-homocysteine
DrugCentralⁱ	Q99873
GuidetoPHARMACOLOGYⁱ	1252

PTM databases

GlyGenⁱ	Q99873, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	Q99873
PhosphoSitePlusⁱ	Q99873
SwissPalmⁱ	Q99873

Genetic variation databases

BioMutaⁱ	PRMT1
DMDMⁱ	161789011

Proteomic databases

EPDⁱ	Q99873
jPOSTⁱ	Q99873
MassIVEⁱ	Q99873
MaxQBⁱ	Q99873
PaxDbⁱ	Q99873
PeptideAtlasⁱ	Q99873
PRIDEⁱ	Q99873
ProteomicsDBⁱ	33891 44996 78511 [Q99873-1] 78512 [Q99873-2] 78513 [Q99873-3]

Protocols and materials databases

Antibodypediaⁱ	18668, 546 antibodies from 40 providers
The DNASU plasmid repository More...DNASUⁱ	3276

Genome annotation databases

Ensemblⁱ	ENST00000391851.8; ENSP00000375724.4; ENSG00000126457.22 [Q99873-3] ENST00000454376.7; ENSP00000406162.2; ENSG00000126457.22 ENST00000610806.4; ENSP00000484505.1; ENSG00000126457.22 [Q99873-5]
GeneIDⁱ	3276
KEGGⁱ	hsa:3276
MANE-Selectⁱ	ENST00000454376.7; ENSP00000406162.2; NM_001536.6; NP_001527.3
UCSCⁱ	uc002ppe.4, human [Q99873-1] uc010enf.3, human

Organism-specific databases

CTDⁱ	3276
DisGeNETⁱ	3276
GeneCardsⁱ	PRMT1
HGNCⁱ	HGNC:5187, PRMT1
HPAⁱ	ENSG00000126457, Low tissue specificity
MIMⁱ	602950, gene
neXtProtⁱ	NX_Q99873
OpenTargetsⁱ	ENSG00000126457
PharmGKBⁱ	PA29461
VEuPathDBⁱ	HostDB:ENSG00000126457
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1499, Eukaryota
GeneTreeⁱ	ENSGT00940000154700
InParanoidⁱ	Q99873
OMAⁱ	TTDRMEV
OrthoDBⁱ	840669at2759
PhylomeDBⁱ	Q99873
TreeFamⁱ	TF300608

Enzyme and pathway databases

BRENDAⁱ	2.1.1.319, 2681
PathwayCommonsⁱ	Q99873
Reactomeⁱ	R-HSA-3214858, RMTs methylate histone arginines R-HSA-6804114, TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest R-HSA-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-HSA-9009391, Extra-nuclear estrogen signaling R-HSA-9018519, Estrogen-dependent gene expression R-HSA-9694631, Maturation of nucleoprotein
SABIO-RKⁱ	Q99873
SignaLinkⁱ	Q99873
SIGNORⁱ	Q99873

Miscellaneous databases

BioGRID-ORCSⁱ	3276, 777 hits in 1100 CRISPR screens
ChiTaRSⁱ	PRMT1, human
GeneWikiⁱ	PRMT1
GenomeRNAiⁱ	3276
Pharosⁱ	Q99873, Tchem
Protein Ontology More...PROⁱ	PR:Q99873
RNActⁱ	Q99873, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000126457, Expressed in embryo and 231 other tissues
ExpressionAtlasⁱ	Q99873, baseline and differential
Genevisibleⁱ	Q99873, HS

Family and domain databases

Gene3Dⁱ	3.40.50.150, 1 hit
InterProⁱ	View protein in InterPro IPR025799, Arg_MeTrfase IPR041698, Methyltransf_25 IPR029063, SAM-dependent_MTases
PANTHERⁱ	PTHR11006, PTHR11006, 1 hit
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
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ANM1_HUMAN
Accessionⁱ	Q99873Primary (citable) accession number: Q99873 Secondary accession number(s): A0A087X1W2 Q9NZ06
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	March 28, 2018
	Last modified:	May 25, 2022
	This is version 193 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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, Reference proteome

Documents

Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

Annotation systems

Supporting data

UniProtKB - Q99873 (ANM1_HUMAN)

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Protein arginine N-methyltransferase 1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoplasm and Cytosol

Nucleus

Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ