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Protein

Protein N-lysine methyltransferase METTL21A

Gene

Mettl21A

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members. Contributes to the in vivo trimethylation of Lys residues in HSPA1 and HSPA8. In vitro methylates 'Lys-561' in HSPA1, 'Lys-564' in HSPA2, 'Lys-585' in HSPA5, 'Lys-563' in HSPA6 and 'Lys-561' in HSPA8 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471S-adenosyl-L-methionine; via amide nitrogenBy similarity
Binding sitei94 – 941S-adenosyl-L-methionineBy similarity
Binding sitei125 – 1251S-adenosyl-L-methionine; via amide nitrogenBy similarity
Binding sitei143 – 1431S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein N-lysine methyltransferase METTL21A (EC:2.1.1.-)
Alternative name(s):
Methyltransferase-like protein 21A
Gene namesi
Name:Mettl21A
Synonyms:Fam119a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1914349. Mettl21a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Protein N-lysine methyltransferase METTL21APRO_0000292034Add
BLAST

Proteomic databases

EPDiQ9CQL0.
MaxQBiQ9CQL0.
PaxDbiQ9CQL0.
PeptideAtlasiQ9CQL0.
PRIDEiQ9CQL0.

PTM databases

PhosphoSiteiQ9CQL0.

Expressioni

Gene expression databases

BgeeiQ9CQL0.
GenevisibleiQ9CQL0. MM.

Interactioni

Subunit structurei

Interacts with heat shock 70 family members; these proteins probably are methylation substrates.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050424.

Structurei

3D structure databases

ProteinModelPortaliQ9CQL0.
SMRiQ9CQL0. Positions 15-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 753S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2793. Eukaryota.
ENOG4111IJ0. LUCA.
GeneTreeiENSGT00550000074572.
HOVERGENiHBG059353.
InParanoidiQ9CQL0.
OMAiHIYKAQR.
OrthoDBiEOG7RJPT0.
PhylomeDBiQ9CQL0.
TreeFamiTF313206.

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.

Q9CQL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALVPYEESA AIGLQKFHKP LATFSFANHT IQIRQDWRQL GVAAVVWDAA
60 70 80 90 100
VVLSMYLEMG AVELRGCSAV ELGAGTGLVG IVAALLGAQV TITDRKVALE
110 120 130 140 150
FLKSNVEANL PPHIQPKAVV KELTWGQNLE SFSPGEFDLI LGADVIYLED
160 170 180 190 200
TFTDLLQTLG HLCSNNSVIL LACRIRYERD SNFLTMLERQ FTVSKVHYDP
210
EKDVHIYKAQ KRNQREDL
Length:218
Mass (Da):24,286
Last modified:June 1, 2001 - v1
Checksum:i7CAFEA691B90195A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861L → P in AAH26952 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009673 mRNA. Translation: BAB26430.1.
AK009675 mRNA. Translation: BAB26431.1.
AK009678 mRNA. Translation: BAB26434.1.
AK009679 mRNA. Translation: BAB26435.1.
AK009680 mRNA. Translation: BAB26436.1.
AK009682 mRNA. Translation: BAB26437.1.
AK011433 mRNA. Translation: BAB27618.1.
AK033578 mRNA. Translation: BAC28371.1.
BC026952 mRNA. Translation: AAH26952.1.
CCDSiCCDS15006.1.
RefSeqiNP_080240.1. NM_025964.3.
XP_006496266.1. XM_006496203.2.
XP_006496267.1. XM_006496204.2.
UniGeneiMm.46394.

Genome annotation databases

EnsembliENSMUST00000053469; ENSMUSP00000050424; ENSMUSG00000025956.
ENSMUST00000114079; ENSMUSP00000109713; ENSMUSG00000025956.
GeneIDi67099.
KEGGimmu:67099.
UCSCiuc007bgu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009673 mRNA. Translation: BAB26430.1.
AK009675 mRNA. Translation: BAB26431.1.
AK009678 mRNA. Translation: BAB26434.1.
AK009679 mRNA. Translation: BAB26435.1.
AK009680 mRNA. Translation: BAB26436.1.
AK009682 mRNA. Translation: BAB26437.1.
AK011433 mRNA. Translation: BAB27618.1.
AK033578 mRNA. Translation: BAC28371.1.
BC026952 mRNA. Translation: AAH26952.1.
CCDSiCCDS15006.1.
RefSeqiNP_080240.1. NM_025964.3.
XP_006496266.1. XM_006496203.2.
XP_006496267.1. XM_006496204.2.
UniGeneiMm.46394.

3D structure databases

ProteinModelPortaliQ9CQL0.
SMRiQ9CQL0. Positions 15-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050424.

PTM databases

PhosphoSiteiQ9CQL0.

Proteomic databases

EPDiQ9CQL0.
MaxQBiQ9CQL0.
PaxDbiQ9CQL0.
PeptideAtlasiQ9CQL0.
PRIDEiQ9CQL0.

Protocols and materials databases

DNASUi67099.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053469; ENSMUSP00000050424; ENSMUSG00000025956.
ENSMUST00000114079; ENSMUSP00000109713; ENSMUSG00000025956.
GeneIDi67099.
KEGGimmu:67099.
UCSCiuc007bgu.1. mouse.

Organism-specific databases

CTDi151194.
MGIiMGI:1914349. Mettl21a.

Phylogenomic databases

eggNOGiKOG2793. Eukaryota.
ENOG4111IJ0. LUCA.
GeneTreeiENSGT00550000074572.
HOVERGENiHBG059353.
InParanoidiQ9CQL0.
OMAiHIYKAQR.
OrthoDBiEOG7RJPT0.
PhylomeDBiQ9CQL0.
TreeFamiTF313206.

Miscellaneous databases

PROiQ9CQL0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQL0.
GenevisibleiQ9CQL0. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum and Tongue.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiMT21A_MOUSE
AccessioniPrimary (citable) accession number: Q9CQL0
Secondary accession number(s): Q8R2Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.