UniProtKB - Q6P2P2 (ANM9_HUMAN)

>sp|Q6P2P2|ANM9_HUMAN Protein arginine N-methyltransferase 9 OS=Homo sapiens OX=9606 GN=PRMT9 PE=1 SV=1
MSNSRPRSRRDAGGGAGAAGRDELVSRSLQSAEHCLGVQDFGTAYAHYLLVLSLAPELKH
DVKETFQYTLFRWAEELDALSRIQDLLGCYEQALELFPDDEVICNSMGEHLFRMGFRDEA
AGYFHKAVKLNPDFSDAKENFYRVANWLVERWHFIMLNDTKRNTIYNAAIQKAVCLGSKS
VLDIGAGTGILSMFAKKAGAHSVYACELSKTMYELACDVVAANKMEAGIKLLHTKSLDIE
IPKHIPERVSLVVTETVDAGLFGEGIVESLIHAWEHLLLQPKTKGESANCEKYGKVIPAS
AVIFGMAVECAEIRRHHRVGIKDIAGIHLPTNVKFQSPAYSSVDTEETIEPYTTEKMSRV
PGGYLALTECFEIMTVDFNNLQELKSLATKKPDKIGIPVIKEGILDAIMVWFVLQLDDEH
SLSTSPSEETCWEQAVYPVQDLADYWIKPGDHVMMEVSCQDCYLRIQSISVLGLECEMDV
AKSFTQNKDLLSLGNEAELCSALANLQTSKPDAVEQTCILESTEIALLNNIPYHEGFKMA
MSKVLSSLTPEKLYQTMDTHCQNEMSSGTGQSNTVQNILEPFYVLDVSEGFSVLPVIAGT
LGQVKPYSSVEKDQHRIALDLISEANHFPKETLEFWLRHVEDESAMLQRPKSDKLWSIII
LDVIEPSGLIQQEIMEKAAISRCLLQSGGKIFPQYVLMFGLLVESQTLLEENAVQGTERT
LGLNIAPFINQFQVPIRVFLDLSSLPCIPLSKPVELLRLDLMTPYLNTSNREVKVYVCKS
GRLTAIPFWYHMYLDEEIRLDTSSEASHWKQAAVVLDNPIQVEMGEELVLSIQHHKSNVS
ITVKQ

Entry version 145 (16 Oct 2019)
Sequence version 1 (05 Jul 2004)
Previous versions | rss

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Protein

Protein arginine N-methyltransferase 9

Gene

PRMT9

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of SF3B2. Involved in the regulation of alternative splicing of pre-mRNA (PubMed:25737013, PubMed:25979344).2 Publications

Caution

This protein should not be confused with FBXO11 (AC Q86XK2) that was initially erroneously named PRMT9.Curated

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.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145."
  Yang Y., Hadjikyriacou A., Xia Z., Gayatri S., Kim D., Zurita-Lopez C., Kelly R., Guo A., Li W., Clarke S.G., Bedford M.T.
  Nat. Commun. 6:6428-6428(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH SF3B2, CATALYTIC ACTIVITY, MUTAGENESIS OF 182-LEU--GLY-185.
- Ref.9
  "Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2."
  Hadjikyriacou A., Yang Y., Espejo A., Bedford M.T., Clarke S.G.
  J. Biol. Chem. 290:16723-16743(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-258 AND GLY-260, IDENTIFICATION IN A COMPLEX WITH PRMT9; SF3B2 AND SF3B4.
- Ref.10
  "Protein arginine methyltransferase product specificity is mediated by distinct active-site architectures."
  Jain K., Warmack R.A., Debler E.W., Hadjikyriacou A., Stavropoulos P., Clarke S.G.
  J. Biol. Chem. 291:18299-18308(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: MUTAGENESIS OF CYS-431, CATALYTIC ACTIVITY.
EC:
2.1.1.320
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145."
  Yang Y., Hadjikyriacou A., Xia Z., Gayatri S., Kim D., Zurita-Lopez C., Kelly R., Guo A., Li W., Clarke S.G., Bedford M.T.
  Nat. Commun. 6:6428-6428(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH SF3B2, CATALYTIC ACTIVITY, MUTAGENESIS OF 182-LEU--GLY-185.
- Ref.9
  "Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2."
  Hadjikyriacou A., Yang Y., Espejo A., Bedford M.T., Clarke S.G.
  J. Biol. Chem. 290:16723-16743(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-258 AND GLY-260, IDENTIFICATION IN A COMPLEX WITH PRMT9; SF3B2 AND SF3B4.
- Ref.10
  "Protein arginine methyltransferase product specificity is mediated by distinct active-site architectures."
  Jain K., Warmack R.A., Debler E.W., Hadjikyriacou A., Stavropoulos P., Clarke S.G.
  J. Biol. Chem. 291:18299-18308(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: MUTAGENESIS OF CYS-431, CATALYTIC ACTIVITY.
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

pH dependenceⁱ

Optimum pH is between is between 7.5 and 8.0.1 Publication

Temperature dependenceⁱ

Optimum temperature is 37 degrees Celsius.1 Publication

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

mRNA processing
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- Ref.8
  "PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145."
  Yang Y., Hadjikyriacou A., Xia Z., Gayatri S., Kim D., Zurita-Lopez C., Kelly R., Guo A., Li W., Clarke S.G., Bedford M.T.
  Nat. Commun. 6:6428-6428(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH SF3B2, CATALYTIC ACTIVITY, MUTAGENESIS OF 182-LEU--GLY-185.

Complete GO annotation on QuickGO ...

Keywordsⁱ

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

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Protein arginine N-methyltransferase 9 Alternative name(s): Protein arginine N-methyltransferase 10 (EC:2.1.1.3203 Publications)
Gene namesⁱ	Name:PRMT9Imported Synonyms:PRMT10
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 4

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:25099 PRMT9
MIMⁱ	616125 gene
neXtProtⁱ	NX_Q6P2P2

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	182 – 185	LDIG → AAAA: Loss of interaction with SF3B2; Abolishes enzymatic activity. 1 Publication	4
Mutagenesisⁱ	258	D → G: Abolishes enzymatic activity. 1 Publication	1
Mutagenesisⁱ	260	G → E: Abolishes enzymatic activity. 1 Publication	1
Mutagenesisⁱ	431	C → H: 8-fold increase in MMA production and almost complete elimination of sDMA production. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	90826
Open Targets More...OpenTargetsⁱ	ENSG00000164169
PharmGKBⁱ	PA165664476

Miscellaneous databases

Pharosⁱ	Q6P2P2

Pharosⁱ

Q6P2P2

Chemistry databases

ChEMBLⁱ	CHEMBL4105724

ChEMBLⁱ

CHEMBL4105724

Polymorphism and mutation databases

BioMutaⁱ	PRMT9
DMDMⁱ	74758248

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000325929	1 – 845	Protein arginine N-methyltransferase 9Add BLAST		845

Proteomic databases

EPDⁱ	Q6P2P2
jPOSTⁱ	Q6P2P2
MassIVEⁱ	Q6P2P2
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q6P2P2
PaxDbⁱ	Q6P2P2
PeptideAtlas More...PeptideAtlasⁱ	Q6P2P2
PRIDEⁱ	Q6P2P2
ProteomicsDBⁱ	3704 66914 [Q6P2P2-1] 66915 [Q6P2P2-2]

PTM databases

iPTMnetⁱ	Q6P2P2
PhosphoSitePlusⁱ	Q6P2P2

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000164169 Expressed in 188 organ(s), highest expression level in right ovary
ExpressionAtlasⁱ	Q6P2P2 baseline and differential
Genevisibleⁱ	Q6P2P2 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA036844 HPA042537

HPAⁱ

HPA036844
HPA042537

Interactionⁱ

Subunit structureⁱ

Found in a complex with PRMT9, SF3B2 and SF3B4 (PubMed:25737013).

Interacts with SF3B2 (PubMed:25737013).

1 Publication

Protein-protein interaction databases

BioGridⁱ	124766, 13 interactors
IntActⁱ	Q6P2P2, 10 interactors
STRINGⁱ	9606.ENSP00000314396

Structureⁱ

3D structure databases

ModBaseⁱ	Search...
SWISS-MODEL-Workspaceⁱ	Submit a new modelling project...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	25 – 58	TPR 1Add BLAST	34
Repeatⁱ	67 – 100	TPR 2Add BLAST	34
Repeatⁱ	101 – 134	TPR 3Add BLAST	34
Domainⁱ	137 – 466	SAM-dependent MTase PRMT-type 1PROSITE-ProRule annotationAdd BLAST	330
Domainⁱ	530 – 845	SAM-dependent MTase PRMT-type 2PROSITE-ProRule annotationAdd BLAST	316

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

Repeat, TPR repeat

Phylogenomic databases

eggNOGⁱ	ENOG410INRY Eukaryota ENOG410Y35C LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000158472
HOGENOMⁱ	HOG000285961
InParanoidⁱ	Q6P2P2
KEGG Orthology (KO) More...KOⁱ	K19737
OMAⁱ	HICKSGQ
Database of Orthologous Groups More...OrthoDBⁱ	519653at2759
PhylomeDBⁱ	Q6P2P2
TreeFamⁱ	TF315221

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR025799 Arg_MeTrfase IPR029063 SAM-dependent_MTases IPR013026 TPR-contain_dom IPR011990 TPR-like_helical_dom_sf IPR019734 TPR_repeat
SUPFAMⁱ	SSF48452 SSF48452, 1 hit SSF53335 SSF53335, 2 hits
PROSITEⁱ	View protein in PROSITE PS51678 SAM_MT_PRMT, 2 hits PS50005 TPR, 2 hits PS50293 TPR_REGION, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: Q6P2P2-1) [UniParc]FASTA Add to basket

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
MSNSRPRSRR DAGGGAGAAG RDELVSRSLQ SAEHCLGVQD FGTAYAHYLL 
        60         70         80         90        100
VLSLAPELKH DVKETFQYTL FRWAEELDAL SRIQDLLGCY EQALELFPDD 
       110        120        130        140        150
EVICNSMGEH LFRMGFRDEA AGYFHKAVKL NPDFSDAKEN FYRVANWLVE 
       160        170        180        190        200
RWHFIMLNDT KRNTIYNAAI QKAVCLGSKS VLDIGAGTGI LSMFAKKAGA 
       210        220        230        240        250
HSVYACELSK TMYELACDVV AANKMEAGIK LLHTKSLDIE IPKHIPERVS 
       260        270        280        290        300
LVVTETVDAG LFGEGIVESL IHAWEHLLLQ PKTKGESANC EKYGKVIPAS 
       310        320        330        340        350
AVIFGMAVEC AEIRRHHRVG IKDIAGIHLP TNVKFQSPAY SSVDTEETIE 
       360        370        380        390        400
PYTTEKMSRV PGGYLALTEC FEIMTVDFNN LQELKSLATK KPDKIGIPVI 
       410        420        430        440        450
KEGILDAIMV WFVLQLDDEH SLSTSPSEET CWEQAVYPVQ DLADYWIKPG 
       460        470        480        490        500
DHVMMEVSCQ DCYLRIQSIS VLGLECEMDV AKSFTQNKDL LSLGNEAELC 
       510        520        530        540        550
SALANLQTSK PDAVEQTCIL ESTEIALLNN IPYHEGFKMA MSKVLSSLTP 
       560        570        580        590        600
EKLYQTMDTH CQNEMSSGTG QSNTVQNILE PFYVLDVSEG FSVLPVIAGT 
       610        620        630        640        650
LGQVKPYSSV EKDQHRIALD LISEANHFPK ETLEFWLRHV EDESAMLQRP 
       660        670        680        690        700
KSDKLWSIII LDVIEPSGLI QQEIMEKAAI SRCLLQSGGK IFPQYVLMFG 
       710        720        730        740        750
LLVESQTLLE ENAVQGTERT LGLNIAPFIN QFQVPIRVFL DLSSLPCIPL 
       760        770        780        790        800
SKPVELLRLD LMTPYLNTSN REVKVYVCKS GRLTAIPFWY HMYLDEEIRL 
       810        820        830        840 
DTSSEASHWK QAAVVLDNPI QVEMGEELVL SIQHHKSNVS ITVKQ

Length:845

Mass (Da):94,501

Last modified:July 5, 2004 - v1

Checksum:ⁱ96C509E190D05A53

Isoform 2 (identifier: Q6P2P2-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-113: Missing.

« Hide

        10         20         30         40         50
MGFRDEAAGY FHKAVKLNPD FSDAKENFYR VANWLVERWH FIMLNDTKRN 
        60         70         80         90        100
TIYNAAIQKA VCLGSKSVLD IGAGTGILSM FAKKAGAHSV YACELSKTMY 
       110        120        130        140        150
ELACDVVAAN KMEAGIKLLH TKSLDIEIPK HIPERVSLVV TETVDAGLFG 
       160        170        180        190        200
EGIVESLIHA WEHLLLQPKT KGESANCEKY GKVIPASAVI FGMAVECAEI 
       210        220        230        240        250
RRHHRVGIKD IAGIHLPTNV KFQSPAYSSV DTEETIEPYT TEKMSRVPGG 
       260        270        280        290        300
YLALTECFEI MTVDFNNLQE LKSLATKKPD KIGIPVIKEG ILDAIMVWFV 
       310        320        330        340        350
LQLDDEHSLS TSPSEETCWE QAVYPVQDLA DYWIKPGDHV MMEVSCQDCY 
       360        370        380        390        400
LRIQSISVLG LECEMDVAKS FTQNKDLLSL GNEAELCSAL ANLQTSKPDA 
       410        420        430        440        450
VEQTCILEST EIALLNNIPY HEGFKMAMSK VLSSLTPEKL YQTMDTHCQN 
       460        470        480        490        500
EMSSGTGQSN TVQNILEPFY VLDVSEGFSV LPVIAGTLGQ VKPYSSVEKD 
       510        520        530        540        550
QHRIALDLIS EANHFPKETL EFWLRHVEDE SAMLQRPKSD KLWSIIILDV 
       560        570        580        590        600
IEPSGLIQQE IMEKAAISRC LLQSGGKIFP QYVLMFGLLV ESQTLLEENA 
       610        620        630        640        650
VQGTERTLGL NIAPFINQFQ VPIRVFLDLS SLPCIPLSKP VELLRLDLMT 
       660        670        680        690        700
PYLNTSNREV KVYVCKSGRL TAIPFWYHMY LDEEIRLDTS SEASHWKQAA 
       710        720        730 
VVLDNPIQVE MGEELVLSIQ HHKSNVSITV KQ

Show »

Length:732

Mass (Da):81,857

Checksum:ⁱEF627AD71327807F

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	D6REN0	D6REN0_HUMAN		Protein arginine N-methyltransferas... Protein arginine N-methyltransferase 9	PRMT9	66	Annotation score:

Sequence cautionⁱ

The sequence BAC87459 differs from that shown. Intron retention.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	504	A → P in AAH21250 (PubMed:15489334).Curated		1
Sequence conflictⁱ	805	E → G in BAF85593 (PubMed:14702039).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_039954	483	S → G. Corresponds to variant dbSNP:rs17023638Ensembl.		1
Natural variantⁱVAR_039955	747	C → Y. Corresponds to variant dbSNP:rs11557361Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_053972	1 – 113	Missing in isoform 2. 1 PublicationAdd BLAST		113

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK128483 mRNA Translation: BAC87459.1 Sequence problems. AK096703 mRNA Translation: BAG53354.1 AK292904 mRNA Translation: BAF85593.1 AC093835 Genomic DNA No translation available. CH471056 Genomic DNA Translation: EAX05013.1 BC004337 mRNA Translation: AAH04337.1 BC021250 mRNA Translation: AAH21250.2 BC064403 mRNA Translation: AAH64403.1 AL137452 mRNA Translation: CAB70744.1 CH471056 Genomic DNA Translation: EAX05011.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS3771.1 [Q6P2P2-1]
PIRⁱ	T46267
NCBI Reference Sequences More...RefSeqⁱ	NP_001291387.1, NM_001304458.1 [Q6P2P2-2] NP_612373.2, NM_138364.3 [Q6P2P2-1]

Genome annotation databases

Ensemblⁱ	ENST00000322396; ENSP00000314396; ENSG00000164169 [Q6P2P2-1]
GeneIDⁱ	90826
KEGGⁱ	hsa:90826
UCSC genome browser More...UCSCⁱ	uc003ilc.4 human [Q6P2P2-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q6P2P2	Isoform 2 of Protein arginine N-methyltransferase 9		HUMAN		732	UniRef100_Q6P2P2
UPI00001C0FFF		HUMAN		489
UPI0000EE2AED		HUMAN		540
UPI0009D78095		HUMAN		437

Protein	Similar proteins		Species	Score	Length	Source
Q6P2P2	Isoform 2 of Protein arginine N-methyltransferase 9		HUMAN		732	UniRef90_Q6P2P2
Uncharacterized protein (Fragment)		MONMO		973
Protein arginine methyltransferase 9		HORSE		846
Protein arginine		LYNPA		846
protein arginine N-methyltransferase 9		VULVU		846
+88

Protein	Similar proteins		Species	Score	Length	Source
Q6P2P2	Protein arginine N-methyltransferase 9		XENLA		827	UniRef50_Q6P2P2
Protein arginine N-methyltransferase 9		MOUSE		846
Isoform 2 of Protein arginine N-methyltransferase 9		HUMAN		732
Uncharacterized protein (Fragment)		MONMO		973
TPR_REGION domain-containing protein		SOUCH		846
+586

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK128483 mRNA Translation: BAC87459.1 Sequence problems. AK096703 mRNA Translation: BAG53354.1 AK292904 mRNA Translation: BAF85593.1 AC093835 Genomic DNA No translation available. CH471056 Genomic DNA Translation: EAX05013.1 BC004337 mRNA Translation: AAH04337.1 BC021250 mRNA Translation: AAH21250.2 BC064403 mRNA Translation: AAH64403.1 AL137452 mRNA Translation: CAB70744.1 CH471056 Genomic DNA Translation: EAX05011.1
CCDSⁱ	CCDS3771.1 [Q6P2P2-1]
PIRⁱ	T46267
RefSeqⁱ	NP_001291387.1, NM_001304458.1 [Q6P2P2-2] NP_612373.2, NM_138364.3 [Q6P2P2-1]

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
	6PDM	X-ray	2.45	A	127-845	[»]
ModBaseⁱ	Search...
SWISS-MODEL-Workspaceⁱ	Submit a new modelling project...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	124766, 13 interactors
IntActⁱ	Q6P2P2, 10 interactors
STRINGⁱ	9606.ENSP00000314396

Chemistry databases

ChEMBLⁱ	CHEMBL4105724

ChEMBLⁱ

CHEMBL4105724

PTM databases

iPTMnetⁱ	Q6P2P2
PhosphoSitePlusⁱ	Q6P2P2

Polymorphism and mutation databases

BioMutaⁱ	PRMT9
DMDMⁱ	74758248

Proteomic databases

EPDⁱ	Q6P2P2
jPOSTⁱ	Q6P2P2
MassIVEⁱ	Q6P2P2
MaxQBⁱ	Q6P2P2
PaxDbⁱ	Q6P2P2
PeptideAtlasⁱ	Q6P2P2
PRIDEⁱ	Q6P2P2
ProteomicsDBⁱ	3704 66914 [Q6P2P2-1] 66915 [Q6P2P2-2]

Genome annotation databases

Ensemblⁱ	ENST00000322396; ENSP00000314396; ENSG00000164169 [Q6P2P2-1]
GeneIDⁱ	90826
KEGGⁱ	hsa:90826
UCSCⁱ	uc003ilc.4 human [Q6P2P2-1]

Organism-specific databases

CTDⁱ	90826
DisGeNETⁱ	90826
GeneCardsⁱ	PRMT9
HGNCⁱ	HGNC:25099 PRMT9
HPAⁱ	HPA036844 HPA042537
MIMⁱ	616125 gene
neXtProtⁱ	NX_Q6P2P2
OpenTargetsⁱ	ENSG00000164169
PharmGKBⁱ	PA165664476
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410INRY Eukaryota ENOG410Y35C LUCA
GeneTreeⁱ	ENSGT00940000158472
HOGENOMⁱ	HOG000285961
InParanoidⁱ	Q6P2P2
KOⁱ	K19737
OMAⁱ	HICKSGQ
OrthoDBⁱ	519653at2759
PhylomeDBⁱ	Q6P2P2
TreeFamⁱ	TF315221

Miscellaneous databases

ChiTaRSⁱ	PRMT9 human
GenomeRNAiⁱ	90826
Pharosⁱ	Q6P2P2
Protein Ontology More...PROⁱ	PR:Q6P2P2
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000164169 Expressed in 188 organ(s), highest expression level in right ovary
ExpressionAtlasⁱ	Q6P2P2 baseline and differential
Genevisibleⁱ	Q6P2P2 HS

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR025799 Arg_MeTrfase IPR029063 SAM-dependent_MTases IPR013026 TPR-contain_dom IPR011990 TPR-like_helical_dom_sf IPR019734 TPR_repeat
SUPFAMⁱ	SSF48452 SSF48452, 1 hit SSF53335 SSF53335, 2 hits
PROSITEⁱ	View protein in PROSITE PS51678 SAM_MT_PRMT, 2 hits PS50005 TPR, 2 hits PS50293 TPR_REGION, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ANM9_HUMAN
Accessionⁱ	Q6P2P2Primary (citable) accession number: Q6P2P2 Secondary accession number(s): A8KA39 , B3KU92, Q6ZR58, Q8N383, Q9BT55, Q9NT98
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
	Last sequence update:	July 5, 2004
	Last modified:	October 16, 2019
	This is version 145 of the entry and version 1 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, Complete proteome, Reference proteome

Documents

Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations

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UniProtKB - Q6P2P2 (ANM9_HUMAN)

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Protein arginine N-methyltransferase 9

PRMT9

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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_section">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>pH dependencei

Temperature dependencei

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GO - Biological processi

<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

Other locations

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

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Organism-specific databases

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Chemistry databases

Polymorphism and mutation 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

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

Protein-protein interaction 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

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

Keywords - Domaini

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

Polymorphism and mutation databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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

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Functionⁱ

Catalytic activityⁱ

pH dependenceⁱ

Temperature dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ