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Protein

Protein-lysine methyltransferase METTL21C

Gene

METTL21C

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

Functioni

Protein-lysine methyltransferase.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921S-adenosyl-L-methionine; via amide nitrogen1 Publication
Binding sitei141 – 1411S-adenosyl-L-methionine1 Publication
Binding sitei172 – 1721S-adenosyl-L-methionine; via amide nitrogen1 Publication
Binding sitei193 – 1931S-adenosyl-L-homocysteine; via carbonyl oxygen1 Publication

GO - Molecular functioni

  • protein-lysine N-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • peptidyl-lysine methylation Source: GOC
  • protein methylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-lysine methyltransferase METTL21C (EC:2.1.1.-)
Alternative name(s):
Methyltransferase-like protein 21C
Gene namesi
Name:METTL21C
Synonyms:C13orf39
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:33717. METTL21C.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi141 – 1411D → A: Abolishes methyltransferase activity. 1 Publication

Organism-specific databases

PharmGKBiPA162378126.

Polymorphism and mutation databases

DMDMi74757117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Protein-lysine methyltransferase METTL21CPRO_0000319590Add
BLAST

Proteomic databases

MaxQBiQ5VZV1.
PaxDbiQ5VZV1.
PRIDEiQ5VZV1.

PTM databases

iPTMnetiQ5VZV1.
PhosphoSiteiQ5VZV1.

Expressioni

Gene expression databases

BgeeiQ5VZV1.
CleanExiHS_C13orf39.
GenevisibleiQ5VZV1. HS.

Organism-specific databases

HPAiHPA040083.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
TCEB1Q153693EBI-10236049,EBI-301231

Protein-protein interaction databases

BioGridi128220. 17 interactions.
IntActiQ5VZV1. 1 interaction.
STRINGi9606.ENSP00000267273.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi52 – 565Combined sources
Beta strandi67 – 737Combined sources
Beta strandi76 – 827Combined sources
Helixi87 – 893Combined sources
Helixi93 – 10917Combined sources
Beta strandi115 – 1206Combined sources
Helixi125 – 1328Combined sources
Beta strandi136 – 1416Combined sources
Turni143 – 1453Combined sources
Helixi146 – 15712Combined sources
Turni158 – 1603Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi166 – 1694Combined sources
Helixi176 – 1794Combined sources
Turni182 – 1843Combined sources
Beta strandi188 – 1947Combined sources
Beta strandi197 – 1993Combined sources
Helixi202 – 21211Combined sources
Beta strandi218 – 2247Combined sources
Helixi228 – 24013Combined sources
Beta strandi241 – 2499Combined sources
Turni250 – 2534Combined sources
Beta strandi254 – 2618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MTLX-ray1.65A/B22-264[»]
ProteinModelPortaliQ5VZV1.
SMRiQ5VZV1. Positions 45-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1223S-adenosyl-L-methionine binding1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2793. Eukaryota.
COG0500. LUCA.
GeneTreeiENSGT00550000074572.
HOVERGENiHBG107723.
InParanoidiQ5VZV1.
OMAiSYTQEHY.
OrthoDBiEOG7RJPT0.
PhylomeDBiQ5VZV1.
TreeFamiTF354267.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q5VZV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVCLSSAQQ PGRRGEGLSS PGGWLEAEKK GAPQKDSTGG VLEESNKIEP
60 70 80 90 100
SLHSLQKFVP TDYASYTQEH YRFAGKEIVI QESIESYGAV VWPGAMALCQ
110 120 130 140 150
YLEEHAEELN FQDAKILEIG AGPGLVSIVA SILGAQVTAT DLPDVLGNLQ
160 170 180 190 200
YNLLKNTLQC TAHLPEVKEL VWGEDLDKNF PKSAFYYDYV LASDVVYHHY
210 220 230 240 250
FLDKLLTTMV YLSQPGTVLL WANKFRFSTD YEFLDKFKQV FDTTLLAEYP
260
ESSVKLFKGI LKWD
Length:264
Mass (Da):29,565
Last modified:December 7, 2004 - v1
Checksum:i239B4B24D62DC1D0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151G → R.
Corresponds to variant rs45462291 [ dbSNP | Ensembl ].
VAR_062229
Natural varianti46 – 461N → S.
Corresponds to variant rs16960383 [ dbSNP | Ensembl ].
VAR_039013

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL158063 Genomic DNA. Translation: CAH72181.1.
BC132748 mRNA. Translation: AAI32749.1.
BC132750 mRNA. Translation: AAI32751.1.
CCDSiCCDS32003.1.
RefSeqiNP_001010977.1. NM_001010977.2.
UniGeneiHs.508623.

Genome annotation databases

EnsembliENST00000267273; ENSP00000267273; ENSG00000139780.
GeneIDi196541.
KEGGihsa:196541.
UCSCiuc001vpj.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL158063 Genomic DNA. Translation: CAH72181.1.
BC132748 mRNA. Translation: AAI32749.1.
BC132750 mRNA. Translation: AAI32751.1.
CCDSiCCDS32003.1.
RefSeqiNP_001010977.1. NM_001010977.2.
UniGeneiHs.508623.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MTLX-ray1.65A/B22-264[»]
ProteinModelPortaliQ5VZV1.
SMRiQ5VZV1. Positions 45-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128220. 17 interactions.
IntActiQ5VZV1. 1 interaction.
STRINGi9606.ENSP00000267273.

PTM databases

iPTMnetiQ5VZV1.
PhosphoSiteiQ5VZV1.

Polymorphism and mutation databases

DMDMi74757117.

Proteomic databases

MaxQBiQ5VZV1.
PaxDbiQ5VZV1.
PRIDEiQ5VZV1.

Protocols and materials databases

DNASUi196541.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267273; ENSP00000267273; ENSG00000139780.
GeneIDi196541.
KEGGihsa:196541.
UCSCiuc001vpj.5. human.

Organism-specific databases

CTDi196541.
GeneCardsiMETTL21C.
HGNCiHGNC:33717. METTL21C.
HPAiHPA040083.
MIMi615259. gene.
neXtProtiNX_Q5VZV1.
PharmGKBiPA162378126.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2793. Eukaryota.
COG0500. LUCA.
GeneTreeiENSGT00550000074572.
HOVERGENiHBG107723.
InParanoidiQ5VZV1.
OMAiSYTQEHY.
OrthoDBiEOG7RJPT0.
PhylomeDBiQ5VZV1.
TreeFamiTF354267.

Miscellaneous databases

GenomeRNAii196541.
NextBioi89529.
PROiQ5VZV1.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VZV1.
CleanExiHS_C13orf39.
GenevisibleiQ5VZV1. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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].
  3. "Lysine methylation of VCP by a member of a novel human protein methyltransferase family."
    Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S., Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.
    Nat. Commun. 3:1038-1038(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-141.
  4. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP70 FAMILY MEMBERS, SUBCELLULAR LOCATION.
  5. "Human methyltransferase-like protein 21C."
    Hong B.S., Tempel W., Dong A., Li Y., Arrowsmith C.H., Bountra C., Edwards A.M., Brown P.J.
    Submitted (SEP-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 22-264 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.

Entry informationi

Entry nameiMT21C_HUMAN
AccessioniPrimary (citable) accession number: Q5VZV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 7, 2004
Last modified: March 16, 2016
This is version 103 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 13
    Human chromosome 13: 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

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.