Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidine protein methyltransferase 1 homolog

Gene

METTL18

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probable histidine methyltransferase.By similarity

GO - Molecular functioni

  1. protein methyltransferase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine protein methyltransferase 1 homolog (EC:2.1.1.-)
Alternative name(s):
Arsenic-transactivated protein 2
Short name:
AsTP2
Methyltransferase-like protein 18
Gene namesi
Name:METTL18
Synonyms:ASTP2, C1orf156
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28793. METTL18.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672407.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Histidine protein methyltransferase 1 homologPRO_0000247199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721Phosphoserine1 Publication
Modified residuei77 – 771Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95568.
PaxDbiO95568.
PRIDEiO95568.

PTM databases

PhosphoSiteiO95568.

Expressioni

Gene expression databases

BgeeiO95568.
CleanExiHS_C1orf156.
ExpressionAtlasiO95568. baseline and differential.
GenevestigatoriO95568.

Organism-specific databases

HPAiHPA035314.

Interactioni

Subunit structurei

Interacts with GRWD1, RPL3 and members of the heat shock protein 90 and 70 families; these proteins may possibly be methylation substrates for the enzyme.1 Publication

Protein-protein interaction databases

BioGridi124936. 45 interactions.
IntActiO95568. 4 interactions.
MINTiMINT-3003072.
STRINGi9606.ENSP00000307077.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi86 – 883Combined sources
Beta strandi92 – 943Combined sources
Beta strandi101 – 1033Combined sources
Helixi109 – 1135Combined sources
Beta strandi116 – 1205Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi162 – 1643Combined sources
Helixi170 – 18112Combined sources
Beta strandi190 – 1945Combined sources
Helixi200 – 2078Combined sources
Beta strandi211 – 2188Combined sources
Helixi220 – 2256Combined sources
Helixi227 – 2337Combined sources
Helixi257 – 2626Combined sources
Beta strandi263 – 2686Combined sources
Helixi270 – 2789Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi287 – 2948Combined sources
Helixi299 – 3013Combined sources
Helixi302 – 31211Combined sources
Beta strandi313 – 32614Combined sources
Turni328 – 3303Combined sources
Helixi334 – 34411Combined sources
Beta strandi346 – 35510Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi361 – 3688Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RFQX-ray2.40A63-372[»]
ProteinModelPortaliO95568.
SMRiO95568. Positions 69-369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG274683.
GeneTreeiENSGT00390000000464.
HOVERGENiHBG053309.
InParanoidiO95568.
OMAiEWSEFCK.
OrthoDBiEOG7VQJF8.
PhylomeDBiO95568.
TreeFamiTF320884.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR019410. Nicotinamide_N-MeTfrase-like.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF10294. Methyltransf_16. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

O95568-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFQFNFTIE DHLENELTPI RDGALTLDSS KELSVSESQK GEERDRKCSA
60 70 80 90 100
EQFDLPQDHL WEHKSMENAA PSQDTDSPLS AASSSRNLEP HGKQPSLRAA
110 120 130 140 150
KEHAMPKDLK KMLENKVIET LPGFQHVKLS VVKTILLKEN FPGENIVSKS
160 170 180 190 200
FSSHSDLITG VYEGGLKIWE CTFDLLAYFT KAKVKFAGKK VLDLGCGSGL
210 220 230 240 250
LGITAFKGGS KEIHFQDYNS MVIDEVTLPN VVANSTLEDE ENDVNEPDVK
260 270 280 290 300
RCRKPKVTQL YKCRFFSGEW SEFCKLVLSS EKLFVKYDLI LTSETIYNPD
310 320 330 340 350
YYSNLHQTFL RLLSKNGRVL LASKAHYFGV GGGVHLFQKF VEERDVFKTR
360 370
ILKIIDEGLK RFIIEITFKF PG
Length:372
Mass (Da):42,148
Last modified:May 1, 1999 - v1
Checksum:i3F0C1599035BA8B1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101E → D.
Corresponds to variant rs10489177 [ dbSNP | Ensembl ].
VAR_027087
Natural varianti309 – 3091F → L.
Corresponds to variant rs34396097 [ dbSNP | Ensembl ].
VAR_054050
Natural varianti318 – 3181R → H.
Corresponds to variant rs35984232 [ dbSNP | Ensembl ].
VAR_054051
Natural varianti325 – 3251A → V.
Corresponds to variant rs16862686 [ dbSNP | Ensembl ].
VAR_027088
Natural varianti360 – 3601K → M.
Corresponds to variant rs13375701 [ dbSNP | Ensembl ].
VAR_027089

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY744366 mRNA. Translation: AAU95377.1.
AL035369 mRNA. Translation: CAA23019.1.
CR450330 mRNA. Translation: CAG29326.1.
AK313909 mRNA. Translation: BAG36632.1.
AL021940 Genomic DNA. Translation: CAI19361.1.
CH471067 Genomic DNA. Translation: EAW90861.1.
BC008679 mRNA. Translation: AAH08679.1.
CCDSiCCDS1284.1.
RefSeqiNP_219486.1. NM_033418.2.
XP_005245663.1. XM_005245606.2.
XP_006711690.1. XM_006711627.1.
UniGeneiHs.33922.

Genome annotation databases

EnsembliENST00000303469; ENSP00000307077; ENSG00000171806.
ENST00000310392; ENSP00000307975; ENSG00000171806.
GeneIDi92342.
KEGGihsa:92342.
UCSCiuc001ggn.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY744366 mRNA. Translation: AAU95377.1.
AL035369 mRNA. Translation: CAA23019.1.
CR450330 mRNA. Translation: CAG29326.1.
AK313909 mRNA. Translation: BAG36632.1.
AL021940 Genomic DNA. Translation: CAI19361.1.
CH471067 Genomic DNA. Translation: EAW90861.1.
BC008679 mRNA. Translation: AAH08679.1.
CCDSiCCDS1284.1.
RefSeqiNP_219486.1. NM_033418.2.
XP_005245663.1. XM_005245606.2.
XP_006711690.1. XM_006711627.1.
UniGeneiHs.33922.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RFQX-ray2.40A63-372[»]
ProteinModelPortaliO95568.
SMRiO95568. Positions 69-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124936. 45 interactions.
IntActiO95568. 4 interactions.
MINTiMINT-3003072.
STRINGi9606.ENSP00000307077.

PTM databases

PhosphoSiteiO95568.

Proteomic databases

MaxQBiO95568.
PaxDbiO95568.
PRIDEiO95568.

Protocols and materials databases

DNASUi92342.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303469; ENSP00000307077; ENSG00000171806.
ENST00000310392; ENSP00000307975; ENSG00000171806.
GeneIDi92342.
KEGGihsa:92342.
UCSCiuc001ggn.4. human.

Organism-specific databases

CTDi92342.
GeneCardsiGC01M169762.
HGNCiHGNC:28793. METTL18.
HPAiHPA035314.
MIMi615255. gene.
neXtProtiNX_O95568.
PharmGKBiPA142672407.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG274683.
GeneTreeiENSGT00390000000464.
HOVERGENiHBG053309.
InParanoidiO95568.
OMAiEWSEFCK.
OrthoDBiEOG7VQJF8.
PhylomeDBiO95568.
TreeFamiTF320884.

Miscellaneous databases

GenomeRNAii92342.
NextBioi77711.
PROiO95568.
SOURCEiSearch...

Gene expression databases

BgeeiO95568.
CleanExiHS_C1orf156.
ExpressionAtlasiO95568. baseline and differential.
GenevestigatoriO95568.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR019410. Nicotinamide_N-MeTfrase-like.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF10294. Methyltransf_16. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and identification of human AsTP2 gene transactivated by arsenic trioxide."
    Wu S.-H., Cheng J., Zheng Y.-J., Liu Y., Zhang Y.-X.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Rhodes S.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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 (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Subthalamic nucleus.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
    Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
    PLoS Genet. 9:E1003210-E1003210(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRWD1; RPL3; HSP70 AND HSP90 FAMILY MEMBERS.

Entry informationi

Entry nameiMET18_HUMAN
AccessioniPrimary (citable) accession number: O95568
Secondary accession number(s): B2R9T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 1, 1999
Last modified: April 1, 2015
This is version 105 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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 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.