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Q9H867

- MT21D_HUMAN

UniProt

Q9H867 - MT21D_HUMAN

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Protein

Protein-lysine methyltransferase METTL21D

Gene

VCPKMT

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

Functioni

Protein-lysine N-methyltransferase that specifically trimethylates 'Lys-315' of VCP/p97; this modification may decrease VCP ATPase activity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431S-adenosyl-L-methionine; via amide nitrogen1 Publication
Binding sitei96 – 961S-adenosyl-L-methionine1 Publication
Binding sitei126 – 1261S-adenosyl-L-methionine; via amide nitrogen1 Publication
Binding sitei143 – 1431S-adenosyl-L-methionine; via carbonyl oxygen1 Publication
Binding sitei148 – 1481S-adenosyl-L-methionine1 Publication

GO - Molecular functioni

  1. protein-lysine N-methyltransferase activity Source: UniProtKB

GO - Biological processi

  1. peptidyl-lysine trimethylation 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 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 namesi
Name:VCPKMT
Synonyms:C14orf138, METTL21D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:20352. VCPKMT.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731E → Q: Loss of methyltransferase activity. 1 Publication
Mutagenesisi96 – 961D → A or V: Loss of methyltransferase activity. 1 Publication
Mutagenesisi144 – 1441D → V: Loss of methyltransferase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134866014.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 229228Protein-lysine methyltransferase METTL21DPRO_0000089937Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9H867.
PaxDbiQ9H867.
PRIDEiQ9H867.

PTM databases

PhosphoSiteiQ9H867.

Expressioni

Gene expression databases

BgeeiQ9H867.
CleanExiHS_C14orf138.
GenevestigatoriQ9H867.

Organism-specific databases

HPAiHPA001146.

Interactioni

Subunit structurei

Interacts with ALKBH6. Interacts with ASPSCR1 and UBXN6; interaction with ASPSCR1, but not with UBXN6, enhances VCP methylation.2 Publications

Protein-protein interaction databases

BioGridi122744. 15 interactions.
STRINGi9606.ENSP00000379201.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 165Combined sources
Beta strandi17 – 215Combined sources
Beta strandi27 – 337Combined sources
Helixi44 – 5310Combined sources
Helixi56 – 594Combined sources
Beta strandi61 – 633Combined sources
Turni65 – 684Combined sources
Beta strandi70 – 756Combined sources
Helixi80 – 867Combined sources
Turni87 – 893Combined sources
Beta strandi91 – 966Combined sources
Helixi98 – 1003Combined sources
Helixi101 – 11010Combined sources
Helixi112 – 1143Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi138 – 1447Combined sources
Helixi149 – 1513Combined sources
Helixi153 – 16210Combined sources
Beta strandi168 – 1747Combined sources
Helixi181 – 19212Combined sources
Turni193 – 1953Combined sources
Beta strandi196 – 2005Combined sources
Helixi203 – 2053Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi215 – 2228Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LG1X-ray1.80A/B/C7-229[»]
ProteinModelPortaliQ9H867.
SMRiQ9H867. Positions 11-228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 773S-adenosyl-L-methionine binding1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00550000074572.
HOGENOMiHOG000007089.
HOVERGENiHBG054931.
InParanoidiQ9H867.
OMAiETCIICC.
OrthoDBiEOG7RJPT0.
PhylomeDBiQ9H867.
TreeFamiTF352990.

Family and domain databases

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

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 4 (identifier: Q9H867-4) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MADTLESSLE DPLRSFVRVL EKRDGTVLRL QQYSSGGVGC VVWDAAIVLS
60 70 80 90 100
KYLETPEFSG DGAHALSRRS VLELGSGTGA VGLMAATLGA DVVVTDLEEL
110 120 130 140 150
QDLLKMNINM NKHLVTGSVQ AKVLKWGEEI EGFPSPPDFI LMADCIYYEE
160 170 180 190 200
SLEPLLKTLK DISGFETCII CCYEQRTMGK NPEIEKKYFE LLQLDFDFEK
210 220
IPLEKHDEEY RSEDIHIIYI RKKKSKFPS
Length:229
Mass (Da):25,807
Last modified:July 10, 2007 - v2
Checksum:i73B22FC1D14F12C7
GO
Isoform 1 (identifier: Q9H867-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-144: VLKWGEEIEGFPSPPDFILMAD → GGRNRRLSFSTRLHTDGRLHIL
     145-229: Missing.

Show »
Length:144
Mass (Da):15,565
Checksum:iA9570313CE131B75
GO
Isoform 2 (identifier: Q9H867-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:123
Mass (Da):14,211
Checksum:i879E819E309F8610
GO
Isoform 3 (identifier: Q9H867-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-229: Missing.

Note: No experimental confirmation available.

Show »
Length:89
Mass (Da):9,371
Checksum:i1E7A543768BB6488
GO
Isoform 5 (identifier: Q9H867-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     191-225: Missing.

Note: No experimental confirmation available.

Show »
Length:194
Mass (Da):21,435
Checksum:i34E94BD4A4DB2EE7
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631A → D.
Corresponds to variant rs11157729 [ dbSNP | Ensembl ].
VAR_059621

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989MADTL…AATLG → MWGRLLQAFPPVPTPQSTLF YR in isoform 2. 1 PublicationVSP_008814Add
BLAST
Alternative sequencei90 – 229140Missing in isoform 3. 1 PublicationVSP_008815Add
BLAST
Alternative sequencei123 – 14422VLKWG…ILMAD → GGRNRRLSFSTRLHTDGRLH IL in isoform 1. 2 PublicationsVSP_026586Add
BLAST
Alternative sequencei145 – 22985Missing in isoform 1. 2 PublicationsVSP_026587Add
BLAST
Alternative sequencei191 – 22939Missing in isoform 2. 1 PublicationVSP_008816Add
BLAST
Alternative sequencei191 – 22535Missing in isoform 5. 1 PublicationVSP_043258Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41951.1. [Q9H867-5]
CCDS9696.2. [Q9H867-4]
RefSeqiNP_001035752.1. NM_001040662.1. [Q9H867-5]
NP_078834.2. NM_024558.2. [Q9H867-4]
XP_006720317.1. XM_006720254.1. [Q9H867-1]
UniGeneiHs.558541.

Genome annotation databases

EnsembliENST00000395859; ENSP00000379200; ENSG00000100483. [Q9H867-5]
ENST00000395860; ENSP00000379201; ENSG00000100483. [Q9H867-4]
ENST00000491402; ENSP00000437113; ENSG00000100483. [Q9H867-1]
GeneIDi79609.
KEGGihsa:79609.
UCSCiuc001wxo.1. human. [Q9H867-4]
uc001wxp.1. human. [Q9H867-5]

Polymorphism databases

DMDMi152031572.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS41951.1. [Q9H867-5 ]
CCDS9696.2. [Q9H867-4 ]
RefSeqi NP_001035752.1. NM_001040662.1. [Q9H867-5 ]
NP_078834.2. NM_024558.2. [Q9H867-4 ]
XP_006720317.1. XM_006720254.1. [Q9H867-1 ]
UniGenei Hs.558541.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LG1 X-ray 1.80 A/B/C 7-229 [» ]
ProteinModelPortali Q9H867.
SMRi Q9H867. Positions 11-228.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122744. 15 interactions.
STRINGi 9606.ENSP00000379201.

PTM databases

PhosphoSitei Q9H867.

Polymorphism databases

DMDMi 152031572.

Proteomic databases

MaxQBi Q9H867.
PaxDbi Q9H867.
PRIDEi Q9H867.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000395859 ; ENSP00000379200 ; ENSG00000100483 . [Q9H867-5 ]
ENST00000395860 ; ENSP00000379201 ; ENSG00000100483 . [Q9H867-4 ]
ENST00000491402 ; ENSP00000437113 ; ENSG00000100483 . [Q9H867-1 ]
GeneIDi 79609.
KEGGi hsa:79609.
UCSCi uc001wxo.1. human. [Q9H867-4 ]
uc001wxp.1. human. [Q9H867-5 ]

Organism-specific databases

CTDi 79609.
GeneCardsi GC14M050577.
HGNCi HGNC:20352. VCPKMT.
HPAi HPA001146.
MIMi 615260. gene.
neXtProti NX_Q9H867.
PharmGKBi PA134866014.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0500.
GeneTreei ENSGT00550000074572.
HOGENOMi HOG000007089.
HOVERGENi HBG054931.
InParanoidi Q9H867.
OMAi ETCIICC.
OrthoDBi EOG7RJPT0.
PhylomeDBi Q9H867.
TreeFami TF352990.

Miscellaneous databases

GenomeRNAii 79609.
NextBioi 68654.
PROi Q9H867.
SOURCEi Search...

Gene expression databases

Bgeei Q9H867.
CleanExi HS_C14orf138.
Genevestigatori Q9H867.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR019410. Nicotinamide_N-MeTfrase-like.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF10294. Methyltransf_16. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
ProtoNeti Search...

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] (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.
    , 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. 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.
  8. "The crystal structure of human methyltransferase-like protein 21D in complex with SAM."
    Zeng H., Dong A., Fenner M., Bountra C., Arrowsmith C.H., Edwards A.M., Brown P.J., Wu H.
    Submitted (JUN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 7-229 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

Entry informationi

Entry nameiMT21D_HUMAN
AccessioniPrimary (citable) accession number: Q9H867
Secondary accession number(s): B7ZLA3
, B7ZLA4, Q2M2X3, Q86T12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: July 10, 2007
Last modified: November 26, 2014
This is version 100 of the entry and version 2 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 14
    Human chromosome 14: 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