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O60678

- ANM3_HUMAN

UniProt

O60678 - ANM3_HUMAN

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Protein

Protein arginine N-methyltransferase 3

Gene
PRMT3, HRMT1L3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.

Enzyme regulationi

Inhibited by N-ethylmaleimide and high concentrations of zinc chloride By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei87 – 871Not phosphorylated
Binding sitei230 – 2301S-adenosyl-L-methionine By similarity
Binding sitei239 – 2391S-adenosyl-L-methionine
Binding sitei263 – 2631S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei285 – 2851S-adenosyl-L-methionine
Binding sitei314 – 3141S-adenosyl-L-methionine
Active sitei329 – 3291 By similarity
Active sitei338 – 3381 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri48 – 7124C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. histone-arginine N-methyltransferase activity Source: RefGenome
  2. metal ion binding Source: UniProtKB-KW
  3. methyltransferase activity Source: UniProtKB
  4. modified amino acid binding Source: Ensembl
  5. protein-arginine N-methyltransferase activity Source: UniProtKB
  6. protein-arginine omega-N asymmetric methyltransferase activity Source: RefGenome
  7. protein binding Source: UniProtKB

GO - Biological processi

  1. histone arginine methylation Source: RefGenome
  2. negative regulation of protein ubiquitination Source: UniProtKB
  3. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: RefGenome
  4. regulation of transcription, DNA-templated Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

SABIO-RKO60678.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 3 (EC:2.1.1.-)
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
Gene namesi
Name:PRMT3
Synonyms:HRMT1L3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:30163. PRMT3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
  3. ribosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 871Y → C: Markedly reduced affinity for RPS2. 1 Publication
Mutagenesisi87 – 871Y → E: Markedly reduced affinity for RPS2. 1 Publication
Mutagenesisi87 – 871Y → F: No effect on interaction with RPS2. 1 Publication

Organism-specific databases

PharmGKBiPA29462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 531530Protein arginine N-methyltransferase 3PRO_0000212326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteine3 Publications
Modified residuei25 – 251Phosphoserine4 Publications
Modified residuei27 – 271Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO60678.
PaxDbiO60678.
PRIDEiO60678.

PTM databases

PhosphoSiteiO60678.

Expressioni

Gene expression databases

ArrayExpressiO60678.
BgeeiO60678.
CleanExiHS_PRMT3.
GenevestigatoriO60678.

Organism-specific databases

HPAiCAB022083.
HPA007832.

Interactioni

Subunit structurei

Monomer or homodimer By similarity. Interacts with EPB41L3; this inhibits methylation of target proteins. Interacts with the 40S ribosomal protein RPS2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SCN5AQ145242EBI-2809009,EBI-726858

Protein-protein interaction databases

BioGridi115491. 31 interactions.
IntActiO60678. 5 interactions.
MINTiMINT-6803908.
STRINGi9606.ENSP00000331879.

Structurei

Secondary structure

1
531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi223 – 2253
Helixi227 – 2348
Helixi237 – 24913
Helixi251 – 2533
Turni254 – 2563
Beta strandi258 – 2636
Helixi268 – 2758
Beta strandi279 – 2879
Helixi289 – 29911
Turni303 – 3053
Beta strandi306 – 3116
Turni313 – 3153
Beta strandi319 – 3213
Beta strandi323 – 3286
Turni336 – 3383
Helixi340 – 35112
Beta strandi352 – 3609
Beta strandi362 – 3709
Helixi373 – 3797
Helixi381 – 3844
Helixi392 – 3943
Helixi395 – 3984
Beta strandi403 – 4053
Helixi409 – 4113
Beta strandi417 – 4237
Turni424 – 4263
Helixi429 – 4324
Beta strandi433 – 44210
Beta strandi446 – 45914
Beta strandi467 – 4704
Beta strandi482 – 49312
Beta strandi498 – 50710
Beta strandi514 – 5218
Beta strandi524 – 5307

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FYTX-ray2.00A211-531[»]
3SMQX-ray2.00A211-531[»]
4HSGX-ray2.30A211-531[»]
ProteinModelPortaliO60678.
SMRiO60678. Positions 43-147, 221-531.

Miscellaneous databases

EvolutionaryTraceiO60678.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini217 – 531315SAM-dependent MTase PRMT-typeAdd
BLAST

Domaini

The zinc-finger is responsible for substrate specificity By similarity.

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri48 – 7124C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0500.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
KOiK11436.
OMAiAQDFVMH.
OrthoDBiEOG7S7SDJ.
PhylomeDBiO60678.
TreeFamiTF323587.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR010456. Ribosomal-L11_MeTrfase_PrmA.
IPR029063. SAM-dependent_MTases-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF06325. PrmA. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60678-1) [UniParc]FASTAAdd to Basket

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

MCSLASGATG GRGAVENEED LPELSDSGDE AAWEDEDDAD LPHGKQQTPC    50
LFCNRLFTSA EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN 100
PTVEYMNSIY NPVPWEKEEY LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN 150
GLSENTSVVE KLKHMEARAL SAEAALARAR EDLQKMKQFA QDFVMHTDVR 200
TCSSSTSVIA DLQEDEDGVY FSSYGHYGIH EEMLKDKIRT ESYRDFIYQN 250
PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN 300
KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK 350
YLAKGGSVYP DICTISLVAV SDVNKHADRI AFWDDVYGFK MSCMKKAVIP 400
EAVVEVLDPK TLISEPCGIK HIDCHTTSIS DLEFSSDFTL KITRTSMCTA 450
IAGYFDIYFE KNCHNRVVFS TGPQSTKTHW KQTVFLLEKP FSVKAGEALK 500
GKVTVHKSKK DPRSLTVTLT LNNSTQTYGL Q 531
Length:531
Mass (Da):59,876
Last modified:January 11, 2011 - v3
Checksum:iD02159E2BEDBE7B9
GO
Isoform 2 (identifier: O60678-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     11-99: GRGAVENEED...IKLINFIRLK → YSHLLKKHFHTVSLSISLILTAWFINM

Note: No experimental confirmation available.

Show »
Length:469
Mass (Da):52,875
Checksum:i4A67AC40A78A7B01
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti440 – 4401L → V.
Corresponds to variant rs3758805 [ dbSNP | Ensembl ].
VAR_024584
Natural varianti470 – 4701S → C.
Corresponds to variant rs11025585 [ dbSNP | Ensembl ].
VAR_030943
Natural varianti508 – 5081S → N.3 Publications
Corresponds to variant rs6483700 [ dbSNP | Ensembl ].
VAR_024585

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei11 – 9989GRGAV…FIRLK → YSHLLKKHFHTVSLSISLIL TAWFINM in isoform 2. VSP_040330Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211L → E in AAC39837. 1 Publication
Sequence conflicti103 – 1031V → F in BAG62289. 1 Publication
Sequence conflicti510 – 5101K → R in BAG62289. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK300591 mRNA. Translation: BAG62289.1.
AC025972 Genomic DNA. No translation available.
AC108005 Genomic DNA. No translation available.
BC037544 mRNA. Translation: AAH37544.1.
BC064831 mRNA. Translation: AAH64831.1.
AF059531 mRNA. Translation: AAC39837.1.
CCDSiCCDS44554.1. [O60678-2]
CCDS7853.1. [O60678-1]
RefSeqiNP_005779.1. NM_005788.3.
UniGeneiHs.152337.

Genome annotation databases

EnsembliENST00000331079; ENSP00000331879; ENSG00000185238. [O60678-1]
ENST00000437750; ENSP00000397766; ENSG00000185238. [O60678-2]
GeneIDi10196.
KEGGihsa:10196.
UCSCiuc001mqb.3. human. [O60678-1]
uc010rdn.2. human. [O60678-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK300591 mRNA. Translation: BAG62289.1 .
AC025972 Genomic DNA. No translation available.
AC108005 Genomic DNA. No translation available.
BC037544 mRNA. Translation: AAH37544.1 .
BC064831 mRNA. Translation: AAH64831.1 .
AF059531 mRNA. Translation: AAC39837.1 .
CCDSi CCDS44554.1. [O60678-2 ]
CCDS7853.1. [O60678-1 ]
RefSeqi NP_005779.1. NM_005788.3.
UniGenei Hs.152337.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FYT X-ray 2.00 A 211-531 [» ]
3SMQ X-ray 2.00 A 211-531 [» ]
4HSG X-ray 2.30 A 211-531 [» ]
ProteinModelPortali O60678.
SMRi O60678. Positions 43-147, 221-531.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115491. 31 interactions.
IntActi O60678. 5 interactions.
MINTi MINT-6803908.
STRINGi 9606.ENSP00000331879.

Chemistry

BindingDBi O60678.
ChEMBLi CHEMBL5891.
GuidetoPHARMACOLOGYi 1254.

PTM databases

PhosphoSitei O60678.

Proteomic databases

MaxQBi O60678.
PaxDbi O60678.
PRIDEi O60678.

Protocols and materials databases

DNASUi 10196.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331079 ; ENSP00000331879 ; ENSG00000185238 . [O60678-1 ]
ENST00000437750 ; ENSP00000397766 ; ENSG00000185238 . [O60678-2 ]
GeneIDi 10196.
KEGGi hsa:10196.
UCSCi uc001mqb.3. human. [O60678-1 ]
uc010rdn.2. human. [O60678-2 ]

Organism-specific databases

CTDi 10196.
GeneCardsi GC11P020373.
HGNCi HGNC:30163. PRMT3.
HPAi CAB022083.
HPA007832.
MIMi 603190. gene.
neXtProti NX_O60678.
PharmGKBi PA29462.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0500.
HOGENOMi HOG000198521.
HOVERGENi HBG001793.
KOi K11436.
OMAi AQDFVMH.
OrthoDBi EOG7S7SDJ.
PhylomeDBi O60678.
TreeFami TF323587.

Enzyme and pathway databases

SABIO-RK O60678.

Miscellaneous databases

EvolutionaryTracei O60678.
GeneWikii PRMT3.
GenomeRNAii 10196.
NextBioi 38588.
PROi O60678.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60678.
Bgeei O60678.
CleanExi HS_PRMT3.
Genevestigatori O60678.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025799. Arg_MeTrfase.
IPR010456. Ribosomal-L11_MeTrfase_PrmA.
IPR029063. SAM-dependent_MTases-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view ]
PANTHERi PTHR11006. PTHR11006. 1 hit.
Pfami PF06325. PrmA. 1 hit.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 2), VARIANT ASN-508.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1), VARIANT ASN-508.
    Tissue: Brain.
  4. "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation."
    Tang J., Gary J.D., Clarke S., Herschman H.R.
    J. Biol. Chem. 273:16935-16945(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-531 (ISOFORM 1), VARIANT ASN-508.
  5. "DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo."
    Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A., Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.
    Oncogene 23:7761-7771(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPB41L3.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)."
    Handrkova H., Petrak J., Halada P., Pospisilova D., Cmejla R.
    Biochim. Biophys. Acta 1814:277-282(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-25 AND SER-27, MUTAGENESIS OF TYR-87, ABSENCE OF PHOSPHORYLATION AT TYR-87, INTERACTION WITH RPS2.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "The crystal structure of human HMT1 HNRNP methyltransferase-like 3 in complex with SAH."
    Structural genomics consortium (SGC)
    Submitted (MAR-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 211-531 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.

Entry informationi

Entry nameiANM3_HUMAN
AccessioniPrimary (citable) accession number: O60678
Secondary accession number(s): B4DUC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 126 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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