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Q8IYT2 (CMTR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2

EC=2.1.1.-
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 names
Name:CMTR2
Synonyms:AFT, FTSJD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length770 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

S-adenosyl-L-methionine + m7G(5')pppRmpN-RNA = S-adenosyl-L-homocysteine + m7G(5')pppRmpNm-RNA. Ref.6

Subcellular location

Nucleus. Cytoplasm. Membrane; Single-pass membrane protein Potential Ref.6.

Sequence similarities

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

Sequence caution

The sequence AAM49718.1 differs from that shown. Reason: Frameshift at position 337.

The sequence BAA91058.1 differs from that shown. Reason: Frameshift at position 739.

The sequence BAB14452.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Inferred from direct assay Ref.6. Source: UniProtKB

cap2 mRNA methylation

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionmRNA (nucleoside-2'-O-)-methyltransferase activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 770770Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2
PRO_0000326180

Regions

Transmembrane642 – 66221Helical; Potential
Domain109 – 322214Adrift-type SAM-dependent 2'-O-MTase

Sites

Active site2751Proton acceptor Probable
Binding site1481S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1671S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site2351S-adenosyl-L-methionine By similarity

Natural variations

Natural variant601L → F. Ref.1 Ref.3
Corresponds to variant rs3096380 [ dbSNP | Ensembl ].
VAR_039998
Natural variant1631F → Y. Ref.4
Corresponds to variant rs17853360 [ dbSNP | Ensembl ].
VAR_039999
Natural variant4161N → S. Ref.1
Corresponds to variant rs3803704 [ dbSNP | Ensembl ].
VAR_040000
Natural variant6081T → K.
Corresponds to variant rs3096381 [ dbSNP | Ensembl ].
VAR_040001
Natural variant7531F → L.
Corresponds to variant rs16970857 [ dbSNP | Ensembl ].
VAR_040002

Experimental info

Mutagenesis1171K → A: Abolishes catalytic activity. Ref.6
Mutagenesis2351D → A: Abolishes catalytic activity. Ref.6
Mutagenesis2751K → A: Abolishes catalytic activity. Ref.6
Sequence conflict271F → L in AAM49718. Ref.5
Sequence conflict531F → Y in AAM49718. Ref.5
Sequence conflict561D → E in AAM49718. Ref.5
Sequence conflict751N → K in AAM49718. Ref.5
Sequence conflict85 – 862WH → LD in AAM49718. Ref.5
Sequence conflict201 – 2022YF → HL in AAM49718. Ref.5
Sequence conflict2221F → I in AAM49718. Ref.5
Sequence conflict3171C → S in AAM49718. Ref.5
Sequence conflict6831C → S in BAA92047. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8IYT2 [UniParc].

Last modified November 24, 2009. Version 2.
Checksum: E5BE4A2B31AE3580

FASTA77088,120
        10         20         30         40         50         60 
MSKCRKTPVQ QLASPASFSP DILADIFELF AKNFSYGKPL NNEWQLPDPS EIFTCDHTEL 

        70         80         90        100        110        120 
NAFLDLKNSL NEVKNLLSDK KLDEWHEHTA FTNKAGKIIS HVRKSVNAEL CTQAWCKFHE 

       130        140        150        160        170        180 
ILCSFPLIPQ EAFQNGKLNS LHLCEAPGAF IASLNHYLKS HRFPCHWSWV ANTLNPYHEA 

       190        200        210        220        230        240 
NDDLMMIMDD RLIANTLHWW YFGPDNTGDI MTLKFLTGLQ NFISSMATVH LVTADGSFDC 

       250        260        270        280        290        300 
QGNPGEQEAL VSSLHYCEVV TALTTLGNGG SFVLKMFTMF EHCSINLMYL LNCCFDQVHV 

       310        320        330        340        350        360 
FKPATSKAGN SEVYVVCLHY KGREAIHPLL SKMTLNFGTE MKRKALFPHH VIPDSFLKRH 

       370        380        390        400        410        420 
EECCVFFHKY QLETISENIR LFECMGKAEQ EKLNNLRDCA IQYFMQKFQL KHLSRNNWLV 

       430        440        450        460        470        480 
KKSSIGCSTN TKWFGQRNKY FKTYNERKML EALSWKDKVA KGYFNSWAEE HGVYHPGQSS 

       490        500        510        520        530        540 
ILEGTASNLE CHLWHILEGK KLPKVKCSPF CNGEILKTLN EAIEKSLGGA FNLDSKFRPK 

       550        560        570        580        590        600 
QQYSCSCHVF SEELIFSELC SLTECLQDEQ VVVPSNQIKC LLVGFSTLRN IKMHIPLEVR 

       610        620        630        640        650        660 
LLESAELTTF SCSLLHDGDP TYQRLFLDCL LHSLRELHTG DVMILPVLSC FTRFMAGLIF 

       670        680        690        700        710        720 
VLHSCFRFIT FVCPTSSDPL RTCAVLLCVG YQDLPNPVFR YLQSVNELLS TLLNSDSPQQ 

       730        740        750        760        770 
VLQFVPMEVL LKGALLDFLW DLNAAIAKRH LHFIIQRERE EIINSLQLQN 

« Hide

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], 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001093112.1. NM_001099642.1.
NP_060818.4. NM_018348.5.
XP_005256103.1. XM_005256046.1.
XP_005256104.1. XM_005256047.1.
UniGeneHs.72782.

3D structure databases

ProteinModelPortalQ8IYT2.
SMRQ8IYT2. Positions 110-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120897. 2 interactions.
STRING9606.ENSP00000337512.

PTM databases

PhosphoSiteQ8IYT2.

Polymorphism databases

DMDM269849596.

Proteomic databases

PaxDbQ8IYT2.
PRIDEQ8IYT2.

Protocols and materials databases

DNASU55783.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338099; ENSP00000337512; ENSG00000180917.
ENST00000434935; ENSP00000411148; ENSG00000180917.
GeneID55783.
KEGGhsa:55783.
UCSCuc002ezy.4. human.

Organism-specific databases

CTD55783.
GeneCardsGC16M071315.
HGNCHGNC:25635. CMTR2.
HPAHPA041700.
HPA048265.
neXtProtNX_Q8IYT2.
PharmGKBPA162389041.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311388.
HOVERGENHBG098139.
InParanoidQ8IYT2.
KOK14590.
OMALQFVPME.
OrthoDBEOG7H1JJX.
PhylomeDBQ8IYT2.
TreeFamTF314897.

Gene expression databases

ArrayExpressQ8IYT2.
BgeeQ8IYT2.
CleanExHS_FTSJD1.
GenevestigatorQ8IYT2.

Family and domain databases

InterProIPR025807. Adrift_MeTrfase.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
[Graphical view]
PfamPF01728. FtsJ. 1 hit.
[Graphical view]
PROSITEPS51614. SAM_MT_ADRIFT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFTSJD1. human.
GenomeRNAi55783.
NextBio60871.
PROQ8IYT2.

Entry information

Entry nameCMTR2_HUMAN
AccessionPrimary (citable) accession number: Q8IYT2
Secondary accession number(s): B2RCD5 expand/collapse secondary AC list , D3DWS1, Q8NE77, Q8NFR5, Q9H8Z4, Q9NUS3, Q9NXF5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 24, 2009
Last modified: February 19, 2014
This is version 77 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

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 16

Human chromosome 16: entries, gene names and cross-references to MIM