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Q9H867 (MT21D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-lysine methyltransferase METTL21D

EC=2.1.1.-
Alternative name(s):
Methyltransferase-like protein 21D
VCP lysine methyltransferase
Short name=VCP-KMT
Valosin-containing protein lysine methyltransferase
Gene names
Name:VCPKMT
Synonyms:C14orf138, METTL21D
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein-lysine N-methyltransferase that specifically trimethylates 'Lys-315' of VCP/p97; this modification may decrease VCP ATPase activity. Ref.5 Ref.7

Subunit structure

Interacts with ALKBH6. Interacts with ASPSCR1 and UBXN6; interaction with ASPSCR1, but not with UBXN6, enhances VCP methylation. Ref.5 Ref.7

Subcellular location

Cytoplasm Ref.7.

Sequence similarities

Belongs to the methyltransferase superfamily. METTL21 family.

Sequence caution

The sequence CAD62329.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-lysine trimethylation

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein-lysine N-methyltransferase activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: Q9H867-4)

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.
Isoform 1 (identifier: Q9H867-1)

The sequence of this isoform differs from the canonical sequence as follows:
     123-144: VLKWGEEIEGFPSPPDFILMAD → GGRNRRLSFSTRLHTDGRLHIL
     145-229: Missing.
Isoform 2 (identifier: Q9H867-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: MADTLESSLE...AVGLMAATLG → MWGRLLQAFPPVPTPQSTLFYR
     191-229: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9H867-3)

The sequence of this isoform differs from the canonical sequence as follows:
     90-229: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9H867-5)

The sequence of this isoform differs from the canonical sequence as follows:
     191-225: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 229228Protein-lysine methyltransferase METTL21D
PRO_0000089937

Regions

Region75 – 773S-adenosyl-L-methionine binding By similarity

Sites

Binding site431S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site961S-adenosyl-L-methionine By similarity
Binding site1261S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1431S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.6

Natural variations

Alternative sequence1 – 8989MADTL…AATLG → MWGRLLQAFPPVPTPQSTLF YR in isoform 2.
VSP_008814
Alternative sequence90 – 229140Missing in isoform 3.
VSP_008815
Alternative sequence123 – 14422VLKWG…ILMAD → GGRNRRLSFSTRLHTDGRLH IL in isoform 1.
VSP_026586
Alternative sequence145 – 22985Missing in isoform 1.
VSP_026587
Alternative sequence191 – 22939Missing in isoform 2.
VSP_008816
Alternative sequence191 – 22535Missing in isoform 5.
VSP_043258
Natural variant631A → D.
Corresponds to variant rs11157729 [ dbSNP | Ensembl ].
VAR_059621

Experimental info

Mutagenesis731E → Q: Loss of methyltransferase activity. Ref.7
Mutagenesis961D → A or V: Loss of methyltransferase activity. Ref.5
Mutagenesis1441D → V: Loss of methyltransferase activity. Ref.5

Secondary structure

.............................................. 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 73B22FC1D14F12C7

FASTA22925,807
        10         20         30         40         50         60 
MADTLESSLE DPLRSFVRVL EKRDGTVLRL QQYSSGGVGC VVWDAAIVLS KYLETPEFSG 

        70         80         90        100        110        120 
DGAHALSRRS VLELGSGTGA VGLMAATLGA DVVVTDLEEL QDLLKMNINM NKHLVTGSVQ 

       130        140        150        160        170        180 
AKVLKWGEEI EGFPSPPDFI LMADCIYYEE SLEPLLKTLK DISGFETCII CCYEQRTMGK 

       190        200        210        220 
NPEIEKKYFE LLQLDFDFEK IPLEKHDEEY RSEDIHIIYI RKKKSKFPS 

« Hide

Isoform 1 [UniParc].

Checksum: A9570313CE131B75
Show »

FASTA14415,565
Isoform 2 [UniParc].

Checksum: 879E819E309F8610
Show »

FASTA12314,211
Isoform 3 [UniParc].

Checksum: 1E7A543768BB6488
Show »

FASTA899,371
Isoform 5 [UniParc].

Checksum: 34E94BD4A4DB2EE7
Show »

FASTA19421,435

References

« Hide 'large scale' references
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Prostate and Retinoblastoma.
[2]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: T-cell.
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1; 4 AND 5).
Tissue: Brain and Testis.
[5]"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, CATALYTIC ACTIVITY, INTERACTION WITH ALKBH6, MUTAGENESIS OF ASP-96 AND ASP-144.
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"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: FUNCTION, INTERACTION WITH ASPSCR1 AND UBXN6, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-73.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK023982 mRNA. Translation: BAB14752.1.
AK129564 mRNA. Translation: BAC85183.1.
BX247997 mRNA. Translation: CAD62329.1. Different initiation.
AL109758 Genomic DNA. No translation available.
BC027585 mRNA. No translation available.
BC105118 mRNA. Translation: AAI05119.1.
BC143673 mRNA. Translation: AAI43674.1.
BC143674 mRNA. Translation: AAI43675.1.
RefSeqNP_001035752.1. NM_001040662.1.
NP_078834.2. NM_024558.2.
UniGeneHs.558541.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LG1X-ray1.80A/B/C7-229[»]
ProteinModelPortalQ9H867.
SMRQ9H867. Positions 11-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122744. 15 interactions.
STRING9606.ENSP00000379201.

PTM databases

PhosphoSiteQ9H867.

Polymorphism databases

DMDM152031572.

Proteomic databases

PaxDbQ9H867.
PRIDEQ9H867.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395859; ENSP00000379200; ENSG00000100483. [Q9H867-5]
ENST00000395860; ENSP00000379201; ENSG00000100483. [Q9H867-4]
ENST00000491402; ENSP00000437113; ENSG00000100483. [Q9H867-1]
GeneID79609.
KEGGhsa:79609.
UCSCuc001wxo.1. human. [Q9H867-4]
uc001wxp.1. human. [Q9H867-5]

Organism-specific databases

CTD79609.
GeneCardsGC14M050577.
HGNCHGNC:20352. VCPKMT.
HPAHPA001146.
MIM615260. gene.
neXtProtNX_Q9H867.
PharmGKBPA134866014.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHOG000007089.
HOVERGENHBG054931.
InParanoidQ9H867.
OMAETCIICC.
OrthoDBEOG7RJPT0.
PhylomeDBQ9H867.
TreeFamTF352990.

Gene expression databases

BgeeQ9H867.
CleanExHS_C14orf138.
GenevestigatorQ9H867.

Family and domain databases

InterProIPR019410. Nicotinamide_N-MeTfrase-like.
[Graphical view]
PfamPF10294. Methyltransf_16. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi79609.
NextBio68654.
PROQ9H867.
SOURCESearch...

Entry information

Entry nameMT21D_HUMAN
AccessionPrimary (citable) accession number: Q9H867
Secondary accession number(s): B7ZLA3 expand/collapse secondary AC list , B7ZLA4, Q2M2X3, Q86T12
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM