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Protein

Protein-glutamate O-methyltransferase

Gene

ARMT1

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

Functioni

O-methyltransferase that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Methylates PCNA, suggesting it is involved in the DNA damage response.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei258 – 2581S-adenosyl-L-methionine1 Publication
Binding sitei291 – 2911S-adenosyl-L-methionine1 Publication

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein carboxyl O-methyltransferase activity Source: UniProtKB
  • S-adenosylmethionine-dependent methyltransferase activity Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB-KW
  • methylation Source: UniProtKB
  • regulation of response to DNA damage stimulus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

DNA damage

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-glutamate O-methyltransferaseCurated (EC:2.1.1.-1 Publication)
Alternative name(s):
Acidic residue methyltransferase 11 Publication
Gene namesi
Name:ARMT11 PublicationImported
Synonyms:C6orf211Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:17872. ARMT1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134870747.

Polymorphism and mutation databases

BioMutaiC6orf211.
DMDMi74752737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 441440Protein-glutamate O-methyltransferasePRO_0000230795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei40 – 401N6-acetyllysineCombined sources
Modified residuei102 – 1021PhosphoserineCombined sources

Post-translational modificationi

Automethylated.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ9H993.
MaxQBiQ9H993.
PaxDbiQ9H993.
PeptideAtlasiQ9H993.
PRIDEiQ9H993.

PTM databases

iPTMnetiQ9H993.
PhosphoSiteiQ9H993.

Expressioni

Gene expression databases

BgeeiQ9H993.
CleanExiHS_C6orf211.
ExpressionAtlasiQ9H993. baseline and differential.
GenevisibleiQ9H993. HS.

Organism-specific databases

HPAiHPA003004.
HPA005819.

Interactioni

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122754. 28 interactions.
IntActiQ9H993. 3 interactions.
STRINGi9606.ENSP00000356263.

Structurei

3D structure databases

ProteinModelPortaliQ9H993.
SMRiQ9H993. Positions 4-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARMT1 family.Curated

Phylogenomic databases

eggNOGiKOG3870. Eukaryota.
ENOG410XPAF. LUCA.
GeneTreeiENSGT00530000064023.
HOGENOMiHOG000172710.
HOVERGENiHBG054833.
InParanoidiQ9H993.
OMAiQGKDFMN.
OrthoDBiEOG7XSTDB.
PhylomeDBiQ9H993.
TreeFamiTF314853.

Family and domain databases

InterProiIPR002791. DUF89.
[Graphical view]
PfamiPF01937. DUF89. 1 hit.
[Graphical view]
SUPFAMiSSF111321. SSF111321. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9H993-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVVPASLSG QDVGSFAYLT IKDRIPQILT KVIDTLHRHK SEFFEKHGEE
60 70 80 90 100
GVEAEKKAIS LLSKLRNELQ TDKPFIPLVE KFVDTDIWNQ YLEYQQSLLN
110 120 130 140 150
ESDGKSRWFY SPWLLVECYM YRRIHEAIIQ SPPIDYFDVF KESKEQNFYG
160 170 180 190 200
SQESIIALCT HLQQLIRTIE DLDENQLKDE FFKLLQISLW GNKCDLSLSG
210 220 230 240 250
GESSSQNTNV LNSLEDLKPF ILLNDMEHLW SLLSNCKKTR EKASATRVYI
260 270 280 290 300
VLDNSGFELV TDLILADFLL SSELATEVHF YGKTIPWFVS DTTIHDFNWL
310 320 330 340 350
IEQVKHSNHK WMSKCGADWE EYIKMGKWVY HNHIFWTLPH EYCAMPQVAP
360 370 380 390 400
DLYAELQKAH LILFKGDLNY RKLTGDRKWE FSVPFHQALN GFHPAPLCTI
410 420 430 440
RTLKAEIQVG LQPGQGEQLL ASEPSWWTTG KYGIFQYDGP L
Length:441
Mass (Da):51,172
Last modified:March 1, 2001 - v1
Checksum:i3BE4D15528FDFC4E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1212MY → ID in AAH11348 (PubMed:15489334).Curated
Sequence conflicti148 – 1481F → S in CAB53692 (PubMed:17974005).Curated
Sequence conflicti173 – 1731D → Y in AAH11348 (PubMed:15489334).Curated
Sequence conflicti220 – 2201F → Y in CAB53692 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731K → N.
Corresponds to variant rs35036943 [ dbSNP | Ensembl ].
VAR_053090
Natural varianti77 – 771P → R.1 Publication
Corresponds to variant rs17850732 [ dbSNP | Ensembl ].
VAR_025791
Natural varianti150 – 1501G → E.
Corresponds to variant rs35734927 [ dbSNP | Ensembl ].
VAR_053091
Natural varianti154 – 1541S → A.
Corresponds to variant rs34437617 [ dbSNP | Ensembl ].
VAR_053092
Natural varianti161 – 1611H → P.
Corresponds to variant rs36037706 [ dbSNP | Ensembl ].
VAR_053093
Natural varianti264 – 2641I → V.
Corresponds to variant rs35989216 [ dbSNP | Ensembl ].
VAR_053094
Natural varianti317 – 3171A → T.
Corresponds to variant rs35972078 [ dbSNP | Ensembl ].
VAR_053095

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022972 mRNA. Translation: BAB14339.1.
AL590543 Genomic DNA. Translation: CAI10942.1.
BC011348 mRNA. Translation: AAH11348.1.
AL110241 mRNA. Translation: CAB53692.2.
CCDSiCCDS5233.1.
PIRiT14772.
RefSeqiNP_001273491.1. NM_001286562.1.
NP_078849.1. NM_024573.2.
UniGeneiHs.15929.

Genome annotation databases

EnsembliENST00000367294; ENSP00000356263; ENSG00000146476.
GeneIDi79624.
KEGGihsa:79624.
UCSCiuc003qok.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022972 mRNA. Translation: BAB14339.1.
AL590543 Genomic DNA. Translation: CAI10942.1.
BC011348 mRNA. Translation: AAH11348.1.
AL110241 mRNA. Translation: CAB53692.2.
CCDSiCCDS5233.1.
PIRiT14772.
RefSeqiNP_001273491.1. NM_001286562.1.
NP_078849.1. NM_024573.2.
UniGeneiHs.15929.

3D structure databases

ProteinModelPortaliQ9H993.
SMRiQ9H993. Positions 4-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122754. 28 interactions.
IntActiQ9H993. 3 interactions.
STRINGi9606.ENSP00000356263.

PTM databases

iPTMnetiQ9H993.
PhosphoSiteiQ9H993.

Polymorphism and mutation databases

BioMutaiC6orf211.
DMDMi74752737.

Proteomic databases

EPDiQ9H993.
MaxQBiQ9H993.
PaxDbiQ9H993.
PeptideAtlasiQ9H993.
PRIDEiQ9H993.

Protocols and materials databases

DNASUi79624.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367294; ENSP00000356263; ENSG00000146476.
GeneIDi79624.
KEGGihsa:79624.
UCSCiuc003qok.3. human.

Organism-specific databases

CTDi79624.
GeneCardsiARMT1.
H-InvDBHIX0006300.
HGNCiHGNC:17872. ARMT1.
HPAiHPA003004.
HPA005819.
MIMi616332. gene.
neXtProtiNX_Q9H993.
PharmGKBiPA134870747.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3870. Eukaryota.
ENOG410XPAF. LUCA.
GeneTreeiENSGT00530000064023.
HOGENOMiHOG000172710.
HOVERGENiHBG054833.
InParanoidiQ9H993.
OMAiQGKDFMN.
OrthoDBiEOG7XSTDB.
PhylomeDBiQ9H993.
TreeFamiTF314853.

Miscellaneous databases

GenomeRNAii79624.
PROiQ9H993.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H993.
CleanExiHS_C6orf211.
ExpressionAtlasiQ9H993. baseline and differential.
GenevisibleiQ9H993. HS.

Family and domain databases

InterProiIPR002791. DUF89.
[Graphical view]
PfamiPF01937. DUF89. 1 hit.
[Graphical view]
SUPFAMiSSF111321. SSF111321. 1 hit.
ProtoNetiSearch...

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].
    Tissue: Teratocarcinoma.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    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], VARIANT ARG-77.
    Tissue: Lymph.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238.
    Tissue: Fetal kidney.
  5. "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 ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase that targets PCNA and is linked to the DNA damage response."
    Perry J.J., Ballard G.D., Albert A.E., Dobrolecki L.E., Malkas L.H., Hoelz D.J.
    Cell Rep. 10:1288-1296(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, METHYLATION.

Entry informationi

Entry nameiARMT1_HUMAN
AccessioniPrimary (citable) accession number: Q9H993
Secondary accession number(s): Q96FC6, Q9UFY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 109 of the entry and version 1 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 6
    Human chromosome 6: 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
  6. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.