Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9HC36 (RMTL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA methyltransferase-like protein 1

EC=2.1.1.-
Gene names
Name:RNMTL1
ORF Names:HC90
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable RNA methyltransferase By similarity.

Tissue specificity

Expressed at same level in normal liver and hepatocarcinoma. Ref.6

Sequence similarities

Belongs to the RNA methyltransferase TrmH family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA methyltransferase activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420RNA methyltransferase-like protein 1
PRO_0000311301

Sites

Binding site3561S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3801S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity
Binding site3891S-adenosyl-L-methionine; via amide nitrogen By similarity

Natural variations

Natural variant81A → S. Ref.5
Corresponds to variant rs2273454 [ dbSNP | Ensembl ].
VAR_037217
Natural variant451G → E.
Corresponds to variant rs2249542 [ dbSNP | Ensembl ].
VAR_037218
Natural variant1851I → V. Ref.5
Corresponds to variant rs17854653 [ dbSNP | Ensembl ].
VAR_037219
Natural variant3261E → Q.
Corresponds to variant rs35780267 [ dbSNP | Ensembl ].
VAR_037220

Experimental info

Sequence conflict2471A → V in BAD96620. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9HC36 [UniParc].

Last modified June 1, 2002. Version 2.
Checksum: CC06C27489A89FC3

FASTA42047,020
        10         20         30         40         50         60 
MAALVRPARF VVRPLLQVVQ AWDLDARRWV RALRRSPVKV VFPSGEVVEQ KRAPGKQPRK 

        70         80         90        100        110        120 
APSEASAQEQ REKQPLEESA SRAPSTWEES GLRYDKAYPG DRRLSSVMTI VKSRPFREKQ 

       130        140        150        160        170        180 
GKILLEGRRL ISDALKAGAV PKMFFFSRLE YLKELPVDKL KGVSLIKVKF EDIKDWSDLV 

       190        200        210        220        230        240 
TPQGIMGIFA KPDHVKMTYP KTQLQHSLPL LLICDNLRDP GNLGTILRSA AGAGCSKVLL 

       250        260        270        280        290        300 
TKGCVDAWEP KVLRAGMGAH FRMPIINNLE WETVPNYLPP DTRVYVADNC GLYAQAEMSN 

       310        320        330        340        350        360 
KASDHGWVCD QRVMKFHKYE EEEDVETGAS QDWLPHVEVQ SYDSDWTEAP AAVVIGGETY 

       370        380        390        400        410        420 
GVSLESLQLA ESTGGKRLLI PVVPGVDSLN SAMAASILLF EGKRQLRGRA EDLSRDRSYH 

« 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].
Tissue: Teratocarcinoma.
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Homo sapiens P579 chromosome 17p DNA sequence fragment."
Gu J.R., Zhao X.T., Wan D.F., Jiang H.Q., Huang Y., He Y.H., Qin W.X., Han L.W., Zhang P.P., Qiu X.K., He L.P.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]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].
[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], VARIANTS SER-8 AND VAL-185.
Tissue: Brain and Skin.
[6]"The ATF/CREB site is the key element for transcription of the human RNA methyltransferase like 1(RNMTL1) gene, a newly discovered 17p13.3 gene."
Xu J., De Zhu J., Ni M., Wan F., Gu J.R.
Cell Res. 12:177-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001443 mRNA. Translation: BAA91694.1.
AK222900 mRNA. Translation: BAD96620.1.
AF177344 mRNA. Translation: AAG17988.2.
CH471108 Genomic DNA. Translation: EAW90642.1.
BC011550 mRNA. Translation: AAH11550.1.
BC050614 mRNA. Translation: AAH50614.1.
CCDSCCDS10997.1.
RefSeqNP_060616.1. NM_018146.2.
UniGeneHs.182729.

3D structure databases

ProteinModelPortalQ9HC36.
SMRQ9HC36. Positions 103-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120477. 19 interactions.
IntActQ9HC36. 2 interactions.
MINTMINT-8052394.
STRING9606.ENSP00000306080.

PTM databases

PhosphoSiteQ9HC36.

Polymorphism databases

DMDM74734265.

Proteomic databases

MaxQBQ9HC36.
PaxDbQ9HC36.
PRIDEQ9HC36.

Protocols and materials databases

DNASU55178.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304478; ENSP00000306080; ENSG00000171861.
GeneID55178.
KEGGhsa:55178.
UCSCuc002frw.3. human.

Organism-specific databases

CTD55178.
GeneCardsGC17P000685.
HGNCHGNC:18485. RNMTL1.
HPAHPA022534.
HPA023031.
HPA023292.
MIM612600. gene.
neXtProtNX_Q9HC36.
PharmGKBPA38341.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0566.
HOGENOMHOG000154151.
HOVERGENHBG108411.
InParanoidQ9HC36.
OMARYDKAFP.
OrthoDBEOG7MSMPJ.
PhylomeDBQ9HC36.
TreeFamTF323420.

Gene expression databases

ArrayExpressQ9HC36.
BgeeQ9HC36.
CleanExHS_RNMTL1.
GenevestigatorQ9HC36.

Family and domain databases

Gene3D3.30.1330.30. 1 hit.
3.40.1280.10. 2 hits.
InterProIPR029028. Alpha/beta_knot_MTases.
IPR029064. L30e-like.
IPR001537. SpoU_MeTrfase.
IPR013123. SpoU_subst-bd.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamPF00588. SpoU_methylase. 1 hit.
PF08032. SpoU_sub_bind. 1 hit.
[Graphical view]
SMARTSM00967. SpoU_sub_bind. 1 hit.
[Graphical view]
SUPFAMSSF55315. SSF55315. 1 hit.
SSF75217. SSF75217. 2 hits.
ProtoNetSearch...

Other

ChiTaRSRNMTL1. human.
GeneWikiRNMTL1.
GenomeRNAi55178.
NextBio58983.
PROQ9HC36.
SOURCESearch...

Entry information

Entry nameRMTL1_HUMAN
AccessionPrimary (citable) accession number: Q9HC36
Secondary accession number(s): Q53GN1 expand/collapse secondary AC list , Q86VC3, Q96F76, Q9NVQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 98 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM