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Q8N1G2

- CMTR1_HUMAN

UniProt

Q8N1G2 - CMTR1_HUMAN

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Protein

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1

Gene

CMTR1

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

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m7GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m7GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway.3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei281 – 2811S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei311 – 3111S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei364 – 3641S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei404 – 4041Proton acceptor1 Publication

GO - Molecular functioni

  1. mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB
  2. nucleic acid binding Source: InterPro

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: UniProtKB
  2. cap1 mRNA methylation Source: UniProtKB
  3. 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

BioCyciMetaCyc:ENSG00000137200-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC:2.1.1.57)
Alternative name(s):
Cap methyltransferase 1
Cap1 2'O-ribose methyltransferase 1
Short name:
MTr1
Short name:
hMTr1
FtsJ methyltransferase domain-containing protein 2
Interferon-stimulated gene 95 kDa protein
Short name:
ISG95
Gene namesi
Name:CMTR1
Synonyms:FTSJD2, KIAA0082, MTR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:21077. CMTR1.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi239 – 2391K → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi364 – 3641D → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi404 – 4041K → A: Abolishes catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA162389052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 835835Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1PRO_0000251239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei108 – 1081N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8N1G2.
PaxDbiQ8N1G2.
PeptideAtlasiQ8N1G2.
PRIDEiQ8N1G2.

PTM databases

PhosphoSiteiQ8N1G2.

Expressioni

Inductioni

By interferons alpha and beta, and by Vaccinia virus infection.3 Publications

Gene expression databases

BgeeiQ8N1G2.
CleanExiHS_FTSJD2.
ExpressionAtlasiQ8N1G2. baseline and differential.
GenevestigatoriQ8N1G2.

Organism-specific databases

HPAiHPA029954.
HPA029979.
HPA029980.

Interactioni

Subunit structurei

Interacts with POLR2A (via C-terminus).1 Publication

Protein-protein interaction databases

BioGridi116703. 3 interactions.
IntActiQ8N1G2. 2 interactions.
STRINGi9606.ENSP00000362550.

Structurei

Secondary structure

1
835
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi143 – 1464Combined sources
Turni168 – 1747Combined sources
Beta strandi176 – 1794Combined sources
Helixi184 – 1863Combined sources
Beta strandi189 – 1913Combined sources
Helixi193 – 20412Combined sources
Helixi205 – 2084Combined sources
Helixi211 – 22111Combined sources
Helixi225 – 2273Combined sources
Turni228 – 2314Combined sources
Beta strandi232 – 2343Combined sources
Helixi235 – 24612Combined sources
Turni247 – 2526Combined sources
Helixi265 – 2673Combined sources
Beta strandi271 – 2777Combined sources
Helixi282 – 29110Combined sources
Beta strandi293 – 3008Combined sources
Helixi310 – 3123Combined sources
Turni313 – 3164Combined sources
Turni318 – 3203Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi326 – 3283Combined sources
Helixi329 – 3313Combined sources
Helixi339 – 35113Combined sources
Turni352 – 3554Combined sources
Beta strandi358 – 3636Combined sources
Turni370 – 3723Combined sources
Helixi373 – 3753Combined sources
Helixi376 – 3794Combined sources
Helixi381 – 39414Combined sources
Beta strandi395 – 40511Combined sources
Helixi411 – 42313Combined sources
Beta strandi424 – 4307Combined sources
Beta strandi442 – 4498Combined sources
Helixi454 – 47017Combined sources
Beta strandi473 – 4819Combined sources
Helixi483 – 4875Combined sources
Helixi490 – 51930Combined sources
Helixi528 – 53912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4N48X-ray2.70A/B126-550[»]
4N49X-ray1.90A126-550[»]
4N4AX-ray2.35A126-550[»]
ProteinModelPortaliQ8N1G2.
SMRiQ8N1G2. Positions 141-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 13347G-patchPROSITE-ProRule annotationAdd
BLAST
Domaini231 – 450220RrmJ-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd
BLAST
Domaini752 – 78635WWAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni727 – 835109Interaction with POLR2AAdd
BLAST

Sequence similaritiesi

Contains 1 G-patch domain.PROSITE-ProRule annotation
Contains 1 RrmJ-type SAM-dependent 2'-O-MTase domain.PROSITE-ProRule annotation
Contains 1 WW domain.Curated

Phylogenomic databases

eggNOGiNOG319576.
GeneTreeiENSGT00530000063742.
HOGENOMiHOG000021970.
HOVERGENiHBG057271.
KOiK14589.
OMAiSRLFWEW.
OrthoDBiEOG78D7JK.
PhylomeDBiQ8N1G2.
TreeFamiTF314897.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025816. Cap_mRNA_MeTrfase_1.
IPR000467. G_patch_dom.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases-like.
IPR001202. WW_dom.
[Graphical view]
PfamiPF01728. FtsJ. 1 hit.
PF01585. G-patch. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS50174. G_PATCH. 1 hit.
PS51613. SAM_MT_RRMJ. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N1G2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRRTDPECT APIKKQKKRV AELALSLSST SDDEPPSSVS HGAKASTTSL
60 70 80 90 100
SGSDSETEGK QHSSDSFDDA FKADSLVEGT SSRYSMYNSV SQKLMAKMGF
110 120 130 140 150
REGEGLGKYS QGRKDIVEAS SQKGRRGLGL TLRGFDQELN VDWRDEPEPS
160 170 180 190 200
ACEQVSWFPE CTTEIPDTQE MSDWMVVGKR KMIIEDETEF CGEELLHSVL
210 220 230 240 250
QCKSVFDVLD GEEMRRARTR ANPYEMIRGV FFLNRAAMKM ANMDFVFDRM
260 270 280 290 300
FTNPRDSYGK PLVKDREAEL LYFADVCAGP GGFSEYVLWR KKWHAKGFGM
310 320 330 340 350
TLKGPNDFKL EDFYSASSEL FEPYYGEGGI DGDGDITRPE NISAFRNFVL
360 370 380 390 400
DNTDRKGVHF LMADGGFSVE GQENLQEILS KQLLLCQFLM ALSIVRTGGH
410 420 430 440 450
FICKTFDLFT PFSVGLVYLL YCCFERVCLF KPITSRPANS ERYVVCKGLK
460 470 480 490 500
VGIDDVRDYL FAVNIKLNQL RNTDSDVNLV VPLEVIKGDH EFTDYMIRSN
510 520 530 540 550
ESHCSLQIKA LAKIHAFVQD TTLSEPRQAE IRKECLRLWG IPDQARVAPS
560 570 580 590 600
SSDPKSKFFE LIQGTEIDIF SYKPTLLTSK TLEKIRPVFD YRCMVSGSEQ
610 620 630 640 650
KFLIGLGKSQ IYTWDGRQSD RWIKLDLKTE LPRDTLLSVE IVHELKGEGK
660 670 680 690 700
AQRKISAIHI LDVLVLNGTD VREQHFNQRI QLAEKFVKAV SKPSRPDMNP
710 720 730 740 750
IRVKEVYRLE EMEKIFVRLE MKIIKGSSGT PKLSYTGRDD RHFVPMGLYI
760 770 780 790 800
VRTVNEPWTM GFSKSFKKKF FYNKKTKDST FDLPADSIAP FHICYYGRLF
810 820 830
WEWGDGIRVH DSQKPQDQDK LSKEDVLSFI QMHRA
Length:835
Mass (Da):95,321
Last modified:October 1, 2002 - v1
Checksum:i03919512A73C30FB
GO

Sequence cautioni

The sequence BAA07893.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti795 – 7951Y → H in BAF85253. (PubMed:14702039)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D43949 mRNA. Translation: BAA07893.2. Different initiation.
AK292564 mRNA. Translation: BAF85253.1.
AL353597 Genomic DNA. Translation: CAI19603.1.
BC010731 mRNA. Translation: AAH10731.2.
BC031890 mRNA. Translation: AAH31890.1.
CCDSiCCDS4835.1.
RefSeqiNP_055865.1. NM_015050.2.
UniGeneiHs.520102.

Genome annotation databases

EnsembliENST00000373451; ENSP00000362550; ENSG00000137200.
GeneIDi23070.
KEGGihsa:23070.
UCSCiuc003ons.3. human.

Polymorphism databases

DMDMi74750894.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D43949 mRNA. Translation: BAA07893.2 . Different initiation.
AK292564 mRNA. Translation: BAF85253.1 .
AL353597 Genomic DNA. Translation: CAI19603.1 .
BC010731 mRNA. Translation: AAH10731.2 .
BC031890 mRNA. Translation: AAH31890.1 .
CCDSi CCDS4835.1.
RefSeqi NP_055865.1. NM_015050.2.
UniGenei Hs.520102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4N48 X-ray 2.70 A/B 126-550 [» ]
4N49 X-ray 1.90 A 126-550 [» ]
4N4A X-ray 2.35 A 126-550 [» ]
ProteinModelPortali Q8N1G2.
SMRi Q8N1G2. Positions 141-547.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116703. 3 interactions.
IntActi Q8N1G2. 2 interactions.
STRINGi 9606.ENSP00000362550.

PTM databases

PhosphoSitei Q8N1G2.

Polymorphism databases

DMDMi 74750894.

Proteomic databases

MaxQBi Q8N1G2.
PaxDbi Q8N1G2.
PeptideAtlasi Q8N1G2.
PRIDEi Q8N1G2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373451 ; ENSP00000362550 ; ENSG00000137200 .
GeneIDi 23070.
KEGGi hsa:23070.
UCSCi uc003ons.3. human.

Organism-specific databases

CTDi 23070.
GeneCardsi GC06P037506.
HGNCi HGNC:21077. CMTR1.
HPAi HPA029954.
HPA029979.
HPA029980.
neXtProti NX_Q8N1G2.
PharmGKBi PA162389052.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG319576.
GeneTreei ENSGT00530000063742.
HOGENOMi HOG000021970.
HOVERGENi HBG057271.
KOi K14589.
OMAi SRLFWEW.
OrthoDBi EOG78D7JK.
PhylomeDBi Q8N1G2.
TreeFami TF314897.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000137200-MONOMER.

Miscellaneous databases

GenomeRNAii 23070.
NextBioi 44167.
PROi Q8N1G2.

Gene expression databases

Bgeei Q8N1G2.
CleanExi HS_FTSJD2.
ExpressionAtlasi Q8N1G2. baseline and differential.
Genevestigatori Q8N1G2.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025816. Cap_mRNA_MeTrfase_1.
IPR000467. G_patch_dom.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases-like.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF01728. FtsJ. 1 hit.
PF01585. G-patch. 1 hit.
[Graphical view ]
SMARTi SM00443. G_patch. 1 hit.
SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS50174. G_PATCH. 1 hit.
PS51613. SAM_MT_RRMJ. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. Ohara O., Nagase T., Kikuno R., Nomura N.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "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].
    Tissue: Testis.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain and Lung.
  6. "Gene expression profiling of the cellular transcriptional network regulated by alpha/beta interferon and its partial attenuation by the hepatitis C virus nonstructural 5A protein."
    Geiss G.K., Carter V.S., He Y., Kwieciszewski B.K., Holzman T., Korth M.J., Lazaro C.A., Fausto N., Bumgarner R.E., Katze M.G.
    J. Virol. 77:6367-6375(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY INTERFERONS ALPHA AND BETA.
  7. "Cellular gene expression survey of vaccinia virus infection of human HeLa cells."
    Guerra S., Lopez-Fernandez L.A., Pascual-Montano A., Munoz M., Harshman K., Esteban M.
    J. Virol. 77:6493-6506(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY VIRAL INFECTION.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "The human interferon-regulated ISG95 protein interacts with RNA polymerase II and shows methyltransferase activity."
    Haline-Vaz T., Silva T.C.L., Zanchin N.I.T.
    Biochem. Biophys. Res. Commun. 372:719-724(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POLR2A, SUBCELLULAR LOCATION, INDUCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Characterization of hMTr1, a human Cap1 2'-O-Ribose methyltransferase."
    Belanger F., Stepinski J., Darzynkiewicz E., Pelletier J.
    J. Biol. Chem. 285:33037-33044(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-239; ASP-364 AND LYS-404.

Entry informationi

Entry nameiCMTR1_HUMAN
AccessioniPrimary (citable) accession number: Q8N1G2
Secondary accession number(s): A8K949, Q14670, Q96FJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 1, 2002
Last modified: November 26, 2014
This is version 101 of the entry and version 1 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3