Q99873 (ANM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein arginine N-methyltransferase 1
EC=2.1.1.-

Alternative name(s):
Histone-arginine N-methyltransferase PRMT1
EC=2.1.1.125
Interferon receptor 1-bound protein 4

Gene names

Name:	PRMT1
Synonyms:	HMT2, HRMT1L2, IR1B4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional acivity. Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Catalytic activity	S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. Ref.11 Ref.12 Ref.18
Enzyme regulation	By BTG1, BTG2 and ILF3.
Subunit structure	Homodimer and heterodimer with PRMT8. Individual homodimers can associate to form a homohexamer. Interacts with BTG1, BTG2, NFATC2IP and IFNAR1 By similarity. Interacts with and methylates CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex By similarity. 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. Ref.9 Ref.10 Ref.13 Ref.15 Ref.17
Subcellular location	Nucleus. Nucleus › nucleoplasm By similarity. Cytoplasm › cytosol By similarity. Note: Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction By similarity. Ref.20
Tissue specificity	Widely expressed. Ref.3
Sequence similarities	Belongs to the protein arginine N-methyltransferase family.
Biophysicochemical properties	Kinetic parameters: KM=1 µM for AdoMet Ref.18 KM=4.2 µM for H4 Vmax=1.2 nmol/min/mg enzyme toward AdoMet Vmax=1.24 nmol/min/mg enzyme toward H4

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell surface receptor signaling pathway Traceable author statement PubMed 9029147. Source: ProtInc in utero embryonic development Inferred from electronic annotation. Source: Compara negative regulation of megakaryocyte differentiation Inferred from direct assay Ref.21. Source: UniProtKB neuron projection development Inferred from mutant phenotype Ref.16. Source: UniProtKB
Cellular_component	cytoplasm Traceable author statement PubMed 9029147. Source: ProtInc cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.9. Source: MGI protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	[cytochrome c]-arginine N-methyltransferase activity Inferred from electronic annotation. Source: Compara histone methyltransferase activity (H4-R3 specific) Inferred from direct assay Ref.11. Source: UniProtKB protein-arginine omega-N asymmetric methyltransferase activity Inferred from electronic annotation. Source: Compara protein-arginine omega-N monomethyltransferase activity Inferred from electronic annotation. Source: Compara snoRNP binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHTOP	Q9Y3Y2	2	EBI-78738,EBI-347794
DHX9	Q08211	2	EBI-78738,EBI-352022
gag	P04591	2	EBI-78738,EBI-6179727	From a different organism.
HABP4	Q5JVS0	2	EBI-78738,EBI-523625
ILF3	Q12906	2	EBI-78738,EBI-78756

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99873-1)

Also known as: V2;

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.

Isoform 2 (identifier: Q99873-2)

Also known as: V3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MENFVATLANGMSLQPPLE → MVGVA

Isoform 3 (identifier: Q99873-3)

Also known as: V1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MENFVATLANGMSLQPPLE → M

Isoform 4 (identifier: Q99873-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MENFVATLANGMSLQPPLE → MAAAEAANCIM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	Protein arginine N-methyltransferase 1		PRO_0000212321
Sites
	Active site	152	1	By similarity
	Active site	161	1	By similarity
	Binding site	53	1	S-adenosyl-L-methionine By similarity
	Binding site	62	1	S-adenosyl-L-methionine By similarity
	Binding site	86	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	108	1	S-adenosyl-L-methionine By similarity
	Binding site	137	1	S-adenosyl-L-methionine By similarity
Natural variations
	Alternative sequence	1 – 19	19	MENFV…QPPLE → MVGVA in isoform 2.		VSP_005208
	Alternative sequence	1 – 19	19	MENFV…QPPLE → M in isoform 3.		VSP_005209
	Alternative sequence	1 – 19	19	MENFV…QPPLE → MAAAEAANCIM in isoform 4.		VSP_046334
	Natural variant	78	1	K → M. Corresponds to variant rs1804486 [ dbSNP | Ensembl ].		VAR_037501
	Natural variant	158	1	L → F. Corresponds to variant rs11673683 [ dbSNP | Ensembl ].		VAR_037502
Experimental info
	Mutagenesis	82	1	V → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. Ref.15
	Mutagenesis	83	1	L → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. Ref.15
	Mutagenesis	84	1	D → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. Ref.15
	Sequence conflict	108	1	E → V in CAA71763. Ref.1
	Sequence conflict	108	1	E → V in CAA71764. Ref.1
	Sequence conflict	108	1	E → V in CAA71765. Ref.1
	Sequence conflict	108	1	E → V in BAA11029. Ref.2
	Sequence conflict	147 – 175	29	DIIIS…RDKWL → ASSSASGWATASSTSPCSTP CSMPGTSV in BAA11029. Ref.2
	Sequence conflict	202	1	K → E in BAG65435. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (V2) [UniParc]. Last modified December 4, 2007. Version 2. Checksum: A286D99B5AFC1860	FASTA	361	41,516
	10 20 30 40 50 60 MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF GIHEEMLKDE 70 80 90 100 110 120 VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG ARKVIGIECS SISDYAVKIV 130 140 150 160 170 180 KANKLDHVVT IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVLYA RDKWLAPDGL 190 200 210 220 230 240 IFPDRATLYV TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVTNAC 250 260 270 280 290 300 LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG FSTSPESPYT 310 320 330 340 350 360 HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC ELSCSTDYRM R
	Isoform 2 (V3) [UniParc]. Checksum: 2546A25EF744E265	FASTA	347	39,929
	10 20 30 40 50 60 MVGVAEVSCG QAESSEKPNA EDMTSKDYYF DSYAHFGIHE EMLKDEVRTL TYRNSMFHNR 70 80 90 100 110 120 HLFKDKVVLD VGSGTGILCM FAAKAGARKV IGIECSSISD YAVKIVKANK LDHVVTIIKG 130 140 150 160 170 180 KVEEVELPVE KVDIIISEWM GYCLFYESML NTVLYARDKW LAPDGLIFPD RATLYVTAIE 190 200 210 220 230 240 DRQYKDYKIH WWENVYGFDM SCIKDVAIKE PLVDVVDPKQ LVTNACLIKE VDIYTVKVED 250 260 270 280 290 300 LTFTSPFCLQ VKRNDYVHAL VAYFNIEFTR CHKRTGFSTS PESPYTHWKQ TVFYMEDYLT 310 320 330 340 VKTGEEIFGT IGMRPNAKNN RDLDFTIDLD FKGQLCELSC STDYRMR
	Isoform 3 (V1) [UniParc]. Checksum: DFC413AC52F49754	FASTA	343	39,602
	10 20 30 40 50 60 MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN SMFHNRHLFK 70 80 90 100 110 120 DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV VTIIKGKVEE 130 140 150 160 170 180 VELPVEKVDI IISEWMGYCL FYESMLNTVL YARDKWLAPD GLIFPDRATL YVTAIEDRQY 190 200 210 220 230 240 KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY TVKVEDLTFT 250 260 270 280 290 300 SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY MEDYLTVKTG 310 320 330 340 EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR
	Isoform 4 [UniParc]. Checksum: 1704BA3762F3E264	FASTA	353	40,548
	10 20 30 40 50 60 MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN 70 80 90 100 110 120 SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV 130 140 150 160 170 180 VTIIKGKVEE VELPVEKVDI IISEWMGYCL FYESMLNTVL YARDKWLAPD GLIFPDRATL 190 200 210 220 230 240 YVTAIEDRQY KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY 250 260 270 280 290 300 TVKVEDLTFT SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY 310 320 330 340 350 MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)." Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A., Henry M.F. Genomics 48:330-340(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[2]	"Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant." Nikawa J., Nakano H., Ohi N. Gene 171:107-111(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Glial cell.
[3]	"Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene." Scorilas A., Black M.H., Talieri M., Diamandis E.P. Biochem. Biophys. Res. Commun. 278:349-359(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Uterus.
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] (ISOFORMS 3 AND 4). Tissue: Lung.
[9]	"Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3." Tang J., Kao P.N., Herschman H.R. J. Biol. Chem. 275:19866-19876(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ILF3.
[10]	"The structure and oligomerization of the yeast arginine methyltransferase, Hmt1." Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A., Hogle J.M. Nat. Struct. Biol. 7:1165-1171(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[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.
[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.
[13]	"Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties." Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B. Mol. Cell 11:1055-1066(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SUPT5H.
[14]	"Regulation of estrogen rapid signaling through arginine methylation by PRMT1." Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L. Mol. Cell 31:212-221(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt." Yamagata K., Daitoku H., Takahashi Y., Namiki K., Hisatake K., Kako K., Mukai H., Kasuya Y., Fukamizu A. Mol. Cell 32:221-231(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FOXO1, MUTAGENESIS OF VAL-82; LEU-83 AND ASP-84.
[16]	"PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells." Miyata S., Mori Y., Tohyama M. Neurosci. Lett. 445:162-165(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state." Pahlich S., Zakaryan R.P., Gehring H. Proteins 72:1125-1137(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EWS AND PRMT8.
[18]	"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.
[19]	"PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function." Jobert L., Argentini M., Tora L. Exp. Cell Res. 315:1273-1286(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling." Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M. Genes Dev. 23:118-132(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[21]	"Protein-arginine methyltransferase 1 suppresses megakaryocytic differentiation via modulation of the p38 MAPK pathway in K562 cells." Chang Y.I., Hua W.K., Yao C.L., Hwang S.M., Hung Y.C., Kuan C.J., Leou J.S., Lin W.J. J. Biol. Chem. 285:20595-20606(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y10805 mRNA. Translation: CAA71763.1. Y10806 mRNA. Translation: CAA71764.1. Y10807 mRNA. Translation: CAA71765.1. D66904 mRNA. Translation: BAA11029.1. AF222689 Genomic DNA. Translation: AAF62893.1. AF222689 Genomic DNA. Translation: AAF62894.1. AF222689 Genomic DNA. Translation: AAF62895.1. AK304660 mRNA. Translation: BAG65435.1. CR407608 mRNA. Translation: CAG28536.1. AC011495 Genomic DNA. No translation available. CH471177 Genomic DNA. Translation: EAW52521.1. BC019268 mRNA. Translation: AAH19268.2. BC109282 mRNA. Translation: AAI09283.2. BC109283 mRNA. Translation: AAI09284.2.
IPI	IPI00382516. IPI01014546. IPI01018101.
RefSeq	NP_001527.3. NM_001536.5. NP_938074.2. NM_198318.4.
UniGene	Hs.20521.
3D structure databases
ProteinModelPortal	Q99873.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-30878N.
IntAct	Q99873. 32 interactions.
MINT	MINT-4861475.
PTM databases
PhosphoSite	Q99873.
Polymorphism databases
DMDM	161789011.
Proteomic databases
PaxDb	Q99873.
PRIDE	Q99873.
Protocols and materials databases
DNASU	3276.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000391851; ENSP00000375724; ENSG00000126457.
GeneID	3276.
KEGG	hsa:3276.
UCSC	uc010enf.2. human. uc021uxu.1. human.
Organism-specific databases
CTD	3276.
GeneCards	GC19P050181.
HGNC	HGNC:5187. PRMT1.
HPA	CAB022550.
MIM	602950. gene.
neXtProt	NX_Q99873.
PharmGKB	PA29461.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0500.
HOVERGEN	HBG001793.
InParanoid	Q99873.
KO	K11434.
OrthoDB	EOG434W66.
PhylomeDB	Q99873.
Enzyme and pathway databases
SABIO-RK	Q99873.
Gene expression databases
ArrayExpress	Q99873.
Bgee	Q99873.
CleanEx	HS_PRMT1.
Genevestigator	Q99873.
GermOnline	ENSG00000126457. Homo sapiens.
Family and domain databases
InterPro	IPR025799. Arg_MeTrfase. IPR025714. Methyltranfer_dom. [Graphical view]
PANTHER	PTHR11006. PTHR11006. 1 hit.
Pfam	PF13847. Methyltransf_31. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q99873.
ChEMBL	CHEMBL5524.
ChiTaRS	PRMT1. human.
GenomeRNAi	3276.
NextBio	13013.
SOURCE	Search...

Entry information

Entry name

ANM1_HUMAN

Accession

Primary (citable) accession number: Q99873
Secondary accession number(s): B4E3C3 , G5E9B6, Q15529, Q2VP93, Q6LEU5, Q8WUW5, Q99872, Q99874, Q9NZ04, Q9NZ05, Q9NZ06

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 4, 2007
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.