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Q99873

- ANM1_HUMAN

UniProt

Q99873 - ANM1_HUMAN

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Protein

Protein arginine N-methyltransferase 1

Gene

PRMT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity.10 Publications

Catalytic activityi

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].3 Publications

Enzyme regulationi

By BTG1, BTG2 and ILF3.

Kineticsi

  1. KM=1 µM for AdoMet1 Publication
  2. KM=4.2 µM for H41 Publication

Vmax=1.2 nmol/min/mg enzyme toward AdoMet1 Publication

Vmax=1.24 nmol/min/mg enzyme toward H41 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531S-adenosyl-L-methionineBy similarity
Binding sitei62 – 621S-adenosyl-L-methionineBy similarity
Binding sitei86 – 861S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei108 – 1081S-adenosyl-L-methionineBy similarity
Binding sitei137 – 1371S-adenosyl-L-methionineBy similarity
Active sitei152 – 1521By similarity
Active sitei161 – 1611By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cell surface receptor signaling pathway Source: ProtInc
  2. histone H4-R3 methylation Source: UniProtKB
  3. histone methylation Source: UniProtKB
  4. negative regulation of megakaryocyte differentiation Source: UniProtKB
  5. neuron projection development Source: UniProtKB
  6. peptidyl-arginine methylation Source: UniProtKB
  7. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: RefGenome
  8. protein methylation Source: ProtInc
  9. regulation of transcription, DNA-templated Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_228108. RMTs methylate histone arginines.
SABIO-RKQ99873.
SignaLinkiQ99873.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 1 (EC:2.1.1.-)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT1 (EC:2.1.1.125)
Interferon receptor 1-bound protein 4
Gene namesi
Name:PRMT1
Synonyms:HMT2, HRMT1L2, IR1B4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:5187. PRMT1.

Subcellular locationi

Nucleus 1 Publication. Nucleusnucleoplasm By similarity. Cytoplasmcytosol By similarity
Note: Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: RefGenome
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi82 – 821V → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication
Mutagenesisi83 – 831L → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication
Mutagenesisi84 – 841D → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication

Organism-specific databases

PharmGKBiPA29461.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Protein arginine N-methyltransferase 1PRO_0000212321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241N6-succinyllysineBy similarity

Proteomic databases

MaxQBiQ99873.
PaxDbiQ99873.
PRIDEiQ99873.

PTM databases

PhosphoSiteiQ99873.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ99873.
CleanExiHS_PRMT1.
ExpressionAtlasiQ99873. baseline and differential.
GenevestigatoriQ99873.

Organism-specific databases

HPAiCAB022550.

Interactioni

Subunit structurei

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.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-78738,EBI-78738
CHTOPQ9Y3Y22EBI-78738,EBI-347794
DCAF8Q5TAQ92EBI-78738,EBI-740686
DHX9Q082112EBI-78738,EBI-352022
EWSR1Q018442EBI-78738,EBI-739737
FAM9AQ8IZU12EBI-78738,EBI-8468186
gagP045912EBI-78738,EBI-6179727From a different organism.
HABP4Q5JVS02EBI-78738,EBI-523625
HNRNPKP619783EBI-78738,EBI-304185
ILF3Q129062EBI-78738,EBI-78756
NRIP1P485524EBI-78738,EBI-746484
OFCC1Q8IZS52EBI-78738,EBI-8477661
PRMT8Q9NR223EBI-78738,EBI-745545
SCN5AQ145242EBI-78738,EBI-726858
SPSB1Q96BD62EBI-78738,EBI-2659201
SPSB2Q996192EBI-78738,EBI-2323209
SYNCRIPO605062EBI-78738,EBI-1024357
VHLP403372EBI-78738,EBI-301246

Protein-protein interaction databases

BioGridi109512. 129 interactions.
DIPiDIP-30878N.
IntActiQ99873. 72 interactions.
MINTiMINT-4861475.

Structurei

3D structure databases

ProteinModelPortaliQ99873.
SMRiQ99873. Positions 49-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 361322SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00550000074406.
HOVERGENiHBG001793.
InParanoidiQ99873.
KOiK11434.
PhylomeDBiQ99873.

Family and domain databases

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

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99873-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF
60 70 80 90 100
GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG
110 120 130 140 150
ARKVIGIECS SISDYAVKIV KANKLDHVVT IIKGKVEEVE LPVEKVDIII
160 170 180 190 200
SEWMGYCLFY ESMLNTVLYA RDKWLAPDGL IFPDRATLYV TAIEDRQYKD
210 220 230 240 250
YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVTNAC LIKEVDIYTV
260 270 280 290 300
KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG FSTSPESPYT
310 320 330 340 350
HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC
360
ELSCSTDYRM R
Length:361
Mass (Da):41,516
Last modified:December 4, 2007 - v2
Checksum:iA286D99B5AFC1860
GO
Isoform 2 (identifier: Q99873-2) [UniParc]FASTAAdd to Basket

Also known as: V3

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

Show »
Length:347
Mass (Da):39,929
Checksum:i2546A25EF744E265
GO
Isoform 3 (identifier: Q99873-3) [UniParc]FASTAAdd to Basket

Also known as: V1

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

Show »
Length:343
Mass (Da):39,602
Checksum:iDFC413AC52F49754
GO
Isoform 4 (identifier: Q99873-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:353
Mass (Da):40,548
Checksum:i1704BA3762F3E264
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081E → V in CAA71763. (PubMed:9545638)Curated
Sequence conflicti108 – 1081E → V in CAA71764. (PubMed:9545638)Curated
Sequence conflicti108 – 1081E → V in CAA71765. (PubMed:9545638)Curated
Sequence conflicti108 – 1081E → V in BAA11029. (PubMed:8675017)Curated
Sequence conflicti147 – 17529DIIIS…RDKWL → ASSSASGWATASSTSPCSTP CSMPGTSV in BAA11029. (PubMed:8675017)CuratedAdd
BLAST
Sequence conflicti202 – 2021K → E in BAG65435. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti78 – 781K → M.
Corresponds to variant rs1804486 [ dbSNP | Ensembl ].
VAR_037501
Natural varianti158 – 1581L → F.
Corresponds to variant rs11673683 [ dbSNP | Ensembl ].
VAR_037502

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1919MENFV…QPPLE → MVGVA in isoform 2. 1 PublicationVSP_005208Add
BLAST
Alternative sequencei1 – 1919MENFV…QPPLE → M in isoform 3. 1 PublicationVSP_005209Add
BLAST
Alternative sequencei1 – 1919MENFV…QPPLE → MAAAEAANCIM in isoform 4. 2 PublicationsVSP_046334Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS42592.1. [Q99873-4]
RefSeqiNP_001527.3. NM_001536.5.
NP_938074.2. NM_198318.4. [Q99873-4]
UniGeneiHs.20521.

Genome annotation databases

EnsembliENST00000391851; ENSP00000375724; ENSG00000126457. [Q99873-4]
GeneIDi3276.
KEGGihsa:3276.
UCSCiuc002ppe.3. human.
uc021uxu.1. human. [Q99873-2]

Polymorphism databases

DMDMi161789011.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS42592.1. [Q99873-4 ]
RefSeqi NP_001527.3. NM_001536.5.
NP_938074.2. NM_198318.4. [Q99873-4 ]
UniGenei Hs.20521.

3D structure databases

ProteinModelPortali Q99873.
SMRi Q99873. Positions 49-361.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109512. 129 interactions.
DIPi DIP-30878N.
IntActi Q99873. 72 interactions.
MINTi MINT-4861475.

Chemistry

BindingDBi Q99873.
ChEMBLi CHEMBL5524.
GuidetoPHARMACOLOGYi 1252.

PTM databases

PhosphoSitei Q99873.

Polymorphism databases

DMDMi 161789011.

Proteomic databases

MaxQBi Q99873.
PaxDbi Q99873.
PRIDEi Q99873.

Protocols and materials databases

DNASUi 3276.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000391851 ; ENSP00000375724 ; ENSG00000126457 . [Q99873-4 ]
GeneIDi 3276.
KEGGi hsa:3276.
UCSCi uc002ppe.3. human.
uc021uxu.1. human. [Q99873-2 ]

Organism-specific databases

CTDi 3276.
GeneCardsi GC19P050181.
HGNCi HGNC:5187. PRMT1.
HPAi CAB022550.
MIMi 602950. gene.
neXtProti NX_Q99873.
PharmGKBi PA29461.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0500.
GeneTreei ENSGT00550000074406.
HOVERGENi HBG001793.
InParanoidi Q99873.
KOi K11434.
PhylomeDBi Q99873.

Enzyme and pathway databases

Reactomei REACT_228108. RMTs methylate histone arginines.
SABIO-RK Q99873.
SignaLinki Q99873.

Miscellaneous databases

ChiTaRSi PRMT1. human.
GeneWikii PRMT1.
GenomeRNAii 3276.
NextBioi 13013.
PROi Q99873.
SOURCEi Search...

Gene expression databases

Bgeei Q99873.
CleanExi HS_PRMT1.
ExpressionAtlasi Q99873. baseline and differential.
Genevestigatori Q99873.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiANM1_HUMAN
AccessioniPrimary (citable) accession number: Q99873
Secondary accession number(s): B4E3C3
, G5E9B6, Q15529, Q2VP93, Q6LEU5, Q8WUW5, Q99872, Q99874, Q9NZ04, Q9NZ05, Q9NZ06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 4, 2007
Last modified: November 26, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3