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Protein

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2

Gene

CMTR2

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

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m7GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m7GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N7 methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-(mRNA) = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-(mRNA).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei148 – 1481S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei167 – 1671S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei235 – 2351S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei275 – 2751Proton acceptor1 Publication

GO - Molecular functioni

  • mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: UniProtKB
  • cap2 mRNA methylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.296. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC:2.1.1.296)
Alternative name(s):
Cap methyltransferase 2
Cap2 2'O-ribose methyltransferase 2
Short name:
HMTr2
Short name:
MTr2
FtsJ methyltransferase domain-containing protein 1
Protein adrift homolog
Gene namesi
Name:CMTR2
Synonyms:AFT, FTSJD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25635. CMTR2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei642 – 66221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi117 – 1171K → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi235 – 2351D → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi275 – 2751K → A: Abolishes catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA162389041.

Polymorphism and mutation databases

BioMutaiFTSJD1.
DMDMi269849596.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 770770Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2PRO_0000326180Add
BLAST

Proteomic databases

MaxQBiQ8IYT2.
PaxDbiQ8IYT2.
PRIDEiQ8IYT2.

PTM databases

PhosphoSiteiQ8IYT2.

Expressioni

Gene expression databases

BgeeiQ8IYT2.
CleanExiHS_FTSJD1.
ExpressionAtlasiQ8IYT2. baseline and differential.
GenevisibleiQ8IYT2. HS.

Organism-specific databases

HPAiHPA041700.
HPA048265.

Interactioni

Protein-protein interaction databases

BioGridi120897. 1 interaction.
STRINGi9606.ENSP00000337512.

Structurei

3D structure databases

ProteinModelPortaliQ8IYT2.
SMRiQ8IYT2. Positions 208-317, 623-730.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 322214Adrift-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Adrift-type SAM-dependent 2'-O-MTase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG311388.
GeneTreeiENSGT00530000063742.
HOVERGENiHBG098139.
InParanoidiQ8IYT2.
KOiK14590.
OMAiLQFVPME.
OrthoDBiEOG7H1JJX.
PhylomeDBiQ8IYT2.
TreeFamiTF314897.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025807. Adrift-typ_MeTrfase.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51614. SAM_MT_ADRIFT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IYT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKCRKTPVQ QLASPASFSP DILADIFELF AKNFSYGKPL NNEWQLPDPS
60 70 80 90 100
EIFTCDHTEL NAFLDLKNSL NEVKNLLSDK KLDEWHEHTA FTNKAGKIIS
110 120 130 140 150
HVRKSVNAEL CTQAWCKFHE ILCSFPLIPQ EAFQNGKLNS LHLCEAPGAF
160 170 180 190 200
IASLNHYLKS HRFPCHWSWV ANTLNPYHEA NDDLMMIMDD RLIANTLHWW
210 220 230 240 250
YFGPDNTGDI MTLKFLTGLQ NFISSMATVH LVTADGSFDC QGNPGEQEAL
260 270 280 290 300
VSSLHYCEVV TALTTLGNGG SFVLKMFTMF EHCSINLMYL LNCCFDQVHV
310 320 330 340 350
FKPATSKAGN SEVYVVCLHY KGREAIHPLL SKMTLNFGTE MKRKALFPHH
360 370 380 390 400
VIPDSFLKRH EECCVFFHKY QLETISENIR LFECMGKAEQ EKLNNLRDCA
410 420 430 440 450
IQYFMQKFQL KHLSRNNWLV KKSSIGCSTN TKWFGQRNKY FKTYNERKML
460 470 480 490 500
EALSWKDKVA KGYFNSWAEE HGVYHPGQSS ILEGTASNLE CHLWHILEGK
510 520 530 540 550
KLPKVKCSPF CNGEILKTLN EAIEKSLGGA FNLDSKFRPK QQYSCSCHVF
560 570 580 590 600
SEELIFSELC SLTECLQDEQ VVVPSNQIKC LLVGFSTLRN IKMHIPLEVR
610 620 630 640 650
LLESAELTTF SCSLLHDGDP TYQRLFLDCL LHSLRELHTG DVMILPVLSC
660 670 680 690 700
FTRFMAGLIF VLHSCFRFIT FVCPTSSDPL RTCAVLLCVG YQDLPNPVFR
710 720 730 740 750
YLQSVNELLS TLLNSDSPQQ VLQFVPMEVL LKGALLDFLW DLNAAIAKRH
760 770
LHFIIQRERE EIINSLQLQN
Length:770
Mass (Da):88,120
Last modified:November 24, 2009 - v2
Checksum:iE5BE4A2B31AE3580
GO

Sequence cautioni

The sequence AAM49718.1 differs from that shown. Reason: Frameshift at position 337. Curated
The sequence BAA91058.1 differs from that shown. Reason: Frameshift at position 739. Curated
The sequence BAB14452.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271F → L in AAM49718 (Ref. 5) Curated
Sequence conflicti53 – 531F → Y in AAM49718 (Ref. 5) Curated
Sequence conflicti56 – 561D → E in AAM49718 (Ref. 5) Curated
Sequence conflicti75 – 751N → K in AAM49718 (Ref. 5) Curated
Sequence conflicti85 – 862WH → LD in AAM49718 (Ref. 5) Curated
Sequence conflicti201 – 2022YF → HL in AAM49718 (Ref. 5) Curated
Sequence conflicti222 – 2221F → I in AAM49718 (Ref. 5) Curated
Sequence conflicti317 – 3171C → S in AAM49718 (Ref. 5) Curated
Sequence conflicti683 – 6831C → S in BAA92047 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601L → F.2 Publications
Corresponds to variant rs3096380 [ dbSNP | Ensembl ].
VAR_039998
Natural varianti163 – 1631F → Y.1 Publication
Corresponds to variant rs17853360 [ dbSNP | Ensembl ].
VAR_039999
Natural varianti416 – 4161N → S.1 Publication
Corresponds to variant rs3803704 [ dbSNP | Ensembl ].
VAR_040000
Natural varianti608 – 6081T → K.
Corresponds to variant rs3096381 [ dbSNP | Ensembl ].
VAR_040001
Natural varianti753 – 7531F → L.
Corresponds to variant rs16970857 [ dbSNP | Ensembl ].
VAR_040002

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000289 mRNA. Translation: BAA91058.1. Frameshift.
AK002033 mRNA. Translation: BAA92047.1.
AK023183 mRNA. Translation: BAB14452.1. Different initiation.
AK315056 mRNA. Translation: BAG37532.1.
AC106736 Genomic DNA. No translation available.
CH471166 Genomic DNA. Translation: EAW59246.1.
CH471166 Genomic DNA. Translation: EAW59247.1.
BC034468 mRNA. Translation: AAH34468.1.
BC035005 mRNA. Translation: AAH35005.1.
AF458590 mRNA. Translation: AAM49718.1. Frameshift.
CCDSiCCDS10898.1.
RefSeqiNP_001093112.1. NM_001099642.1.
NP_060818.4. NM_018348.5.
XP_005256103.1. XM_005256046.2.
XP_005256104.1. XM_005256047.2.
UniGeneiHs.72782.

Genome annotation databases

EnsembliENST00000338099; ENSP00000337512; ENSG00000180917.
ENST00000434935; ENSP00000411148; ENSG00000180917.
GeneIDi55783.
KEGGihsa:55783.
UCSCiuc002ezy.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000289 mRNA. Translation: BAA91058.1. Frameshift.
AK002033 mRNA. Translation: BAA92047.1.
AK023183 mRNA. Translation: BAB14452.1. Different initiation.
AK315056 mRNA. Translation: BAG37532.1.
AC106736 Genomic DNA. No translation available.
CH471166 Genomic DNA. Translation: EAW59246.1.
CH471166 Genomic DNA. Translation: EAW59247.1.
BC034468 mRNA. Translation: AAH34468.1.
BC035005 mRNA. Translation: AAH35005.1.
AF458590 mRNA. Translation: AAM49718.1. Frameshift.
CCDSiCCDS10898.1.
RefSeqiNP_001093112.1. NM_001099642.1.
NP_060818.4. NM_018348.5.
XP_005256103.1. XM_005256046.2.
XP_005256104.1. XM_005256047.2.
UniGeneiHs.72782.

3D structure databases

ProteinModelPortaliQ8IYT2.
SMRiQ8IYT2. Positions 208-317, 623-730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120897. 1 interaction.
STRINGi9606.ENSP00000337512.

PTM databases

PhosphoSiteiQ8IYT2.

Polymorphism and mutation databases

BioMutaiFTSJD1.
DMDMi269849596.

Proteomic databases

MaxQBiQ8IYT2.
PaxDbiQ8IYT2.
PRIDEiQ8IYT2.

Protocols and materials databases

DNASUi55783.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338099; ENSP00000337512; ENSG00000180917.
ENST00000434935; ENSP00000411148; ENSG00000180917.
GeneIDi55783.
KEGGihsa:55783.
UCSCiuc002ezy.4. human.

Organism-specific databases

CTDi55783.
GeneCardsiGC16M071315.
HGNCiHGNC:25635. CMTR2.
HPAiHPA041700.
HPA048265.
MIMi616190. gene.
neXtProtiNX_Q8IYT2.
PharmGKBiPA162389041.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG311388.
GeneTreeiENSGT00530000063742.
HOVERGENiHBG098139.
InParanoidiQ8IYT2.
KOiK14590.
OMAiLQFVPME.
OrthoDBiEOG7H1JJX.
PhylomeDBiQ8IYT2.
TreeFamiTF314897.

Enzyme and pathway databases

BRENDAi2.1.1.296. 2681.

Miscellaneous databases

ChiTaRSiCMTR2. human.
GenomeRNAii55783.
NextBioi60871.
PROiQ8IYT2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IYT2.
CleanExiHS_FTSJD1.
ExpressionAtlasiQ8IYT2. baseline and differential.
GenevisibleiQ8IYT2. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025807. Adrift-typ_MeTrfase.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51614. SAM_MT_ADRIFT. 1 hit.
[Graphical view]
ProtoNetiSearch...

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], VARIANTS PHE-60 AND SER-416.
    Tissue: Placenta and Trachea.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-60.
  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], VARIANT TYR-163.
    Tissue: Testis.
  5. Zan Q., Guo J.H., Yu L.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-343.
    Tissue: Testis.
  6. "2'-O-ribose methylation of cap2 in human: function and evolution in a horizontally mobile family."
    Werner M., Purta E., Kaminska K.H., Cymerman I.A., Campbell D.A., Mittra B., Zamudio J.R., Sturm N.R., Jaworski J., Bujnicki J.M.
    Nucleic Acids Res. 39:4756-4768(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-117; ASP-235 AND LYS-275.

Entry informationi

Entry nameiCMTR2_HUMAN
AccessioniPrimary (citable) accession number: Q8IYT2
Secondary accession number(s): B2RCD5
, D3DWS1, Q8NE77, Q8NFR5, Q9H8Z4, Q9NUS3, Q9NXF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 24, 2009
Last modified: June 24, 2015
This is version 87 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. 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.