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

Q96GJ1 (TRM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (uracil(54)-C(5))-methyltransferase homolog

EC=2.1.1.35
Alternative name(s):
TRM2 homolog
Gene names
Name:TRMT2B
Synonyms:CXorf34
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation By similarity.

Catalytic activity

S-adenosyl-L-methionine + uracil54 in tRNA = S-adenosyl-L-homocysteine + 5-methyluracil54 in tRNA.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.

Ontologies

Keywords
   Biological processtRNA processing
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionS-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96GJ1-1)

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.
Isoform 2 (identifier: Q96GJ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     464-504: LCCPPDPAKKLLGEPFVLQQAVPVDLFPHTPHCELVLLFTR → RSLILLECSGMVSAHCSLHLPGSSDSPASAS
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96GJ1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-146: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504tRNA (uracil(54)-C(5))-methyltransferase homolog
PRO_0000311932

Sites

Active site4511Nucleophile By similarity
Active site4971Proton acceptor By similarity
Binding site3231S-adenosyl-L-methionine By similarity
Binding site3731S-adenosyl-L-methionine By similarity
Binding site4231S-adenosyl-L-methionine By similarity

Natural variations

Alternative sequence102 – 14645Missing in isoform 3.
VSP_029643
Alternative sequence464 – 50441LCCPP…LLFTR → RSLILLECSGMVSAHCSLHL PGSSDSPASAS in isoform 2.
VSP_029644
Natural variant121S → R.
Corresponds to variant rs7064613 [ dbSNP | Ensembl ].
VAR_037355

Experimental info

Sequence conflict2381H → R in BAB14223. Ref.1
Sequence conflict4511C → R in CAI46112. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D7A28E168AC9C366

FASTA50456,476
        10         20         30         40         50         60 
MAGLKRRVPL HSLRYFISMV GLFSKPGLLP WYARNPPGWS QLFLGTVCKG DFTRVIATKC 

        70         80         90        100        110        120 
QKGQKSQKKP SHLGPLDGSW QERLADVVTP LWRLSYEEQL KVKFAAQKKI LQRLESYIQM 

       130        140        150        160        170        180 
LNGVSVTTAV PKSERLSCLL HPIIPSPVIN GYRNKSTFSV NRGPDGNPKT VGFYLGTWRD 

       190        200        210        220        230        240 
GNVVCVQSNH LKNIPEKHSQ VAQYYEVFLR QSPLEPCLVF HEGGYWRELT VRTNSQGHTM 

       250        260        270        280        290        300 
AIITFHPQKL SQEELHVQKE IVKEFFIRGP GAACGLTSLY FQESTMTRCS HQQSPYQLLF 

       310        320        330        340        350        360 
GEPYIFEELL SLKIRISPDA FFQINTAGAE MLYRTVGELT GVNSDTILLD ICCGTGVIGL 

       370        380        390        400        410        420 
SLAQHTSRVL GIELLEQAVE DARWTAAFNG ITNSEFHTGQ AEKILPGLLK SKEDGQSIVA 

       430        440        450        460        470        480 
VVNPARAGLH YKVIQAIRNF RAIHTLVFVS CKLHGESTRN VIELCCPPDP AKKLLGEPFV 

       490        500 
LQQAVPVDLF PHTPHCELVL LFTR 

« Hide

Isoform 2 [UniParc].

Checksum: 22B3CD7F012C136F
Show »

FASTA49455,006
Isoform 3 [UniParc].

Checksum: 2000E09C0715483C
Show »

FASTA45951,485

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] (ISOFORM 1).
Tissue: Teratocarcinoma.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Lymph node.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (JUL-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] (ISOFORMS 1 AND 2).
Tissue: Brain, Colon, Lymph, Placenta and Skin.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK022749 mRNA. Translation: BAB14223.1.
AL832849 mRNA. Translation: CAI46112.1.
AL133275, AL109952, Z97985 Genomic DNA. Translation: CAI42155.1.
AL133275, AL109952, Z97985 Genomic DNA. Translation: CAI42156.1.
Z97985, AL109952, AL133275 Genomic DNA. Translation: CAI42658.1.
Z97985, AL109952, AL133275 Genomic DNA. Translation: CAI42657.1.
AL109952, AL133275, Z97985 Genomic DNA. Translation: CAI42997.1.
AL109952, AL133275, Z97985 Genomic DNA. Translation: CAI42998.1.
CH471115 Genomic DNA. Translation: EAX02831.1.
CH471115 Genomic DNA. Translation: EAX02837.1.
BC007526 mRNA. Translation: AAH07526.1.
BC008067 mRNA. Translation: AAH08067.2.
BC009437 mRNA. Translation: AAH09437.1.
BC020116 mRNA. Translation: AAH20116.1.
BC034272 mRNA. Translation: AAH34272.1.
RefSeqNP_001161442.1. NM_001167970.1.
NP_001161443.1. NM_001167971.1.
NP_001161444.1. NM_001167972.1.
NP_079193.2. NM_024917.5.
XP_005262252.1. XM_005262195.1.
XP_005262253.1. XM_005262196.1.
UniGeneHs.496501.

3D structure databases

ProteinModelPortalQ96GJ1.
SMRQ96GJ1. Positions 295-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123044. 2 interactions.

PTM databases

PhosphoSiteQ96GJ1.

Polymorphism databases

DMDM74762656.

Proteomic databases

PaxDbQ96GJ1.
PRIDEQ96GJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338687; ENSP00000340970; ENSG00000188917. [Q96GJ1-3]
ENST00000372935; ENSP00000362026; ENSG00000188917. [Q96GJ1-1]
ENST00000372936; ENSP00000362027; ENSG00000188917. [Q96GJ1-1]
ENST00000372939; ENSP00000362030; ENSG00000188917. [Q96GJ1-3]
ENST00000545398; ENSP00000438134; ENSG00000188917. [Q96GJ1-1]
GeneID79979.
KEGGhsa:79979.
UCSCuc004egq.3. human. [Q96GJ1-1]
uc004egv.3. human. [Q96GJ1-3]

Organism-specific databases

CTD79979.
GeneCardsGC0XM100264.
H-InvDBHIX0016920.
HIX0029044.
HGNCHGNC:25748. TRMT2B.
HPAHPA035120.
neXtProtNX_Q96GJ1.
PharmGKBPA164726782.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2265.
HOVERGENHBG108599.
InParanoidQ96GJ1.
KOK15331.
OMAHEGGYWR.
OrthoDBEOG7327N9.
PhylomeDBQ96GJ1.
TreeFamTF352239.

Gene expression databases

ArrayExpressQ96GJ1.
BgeeQ96GJ1.
CleanExHS_TRMT2B.
GenevestigatorQ96GJ1.

Family and domain databases

InterProIPR025714. Methyltranfer_dom.
IPR025823. tRNA_(uracil-5-)_MeTrfase_met.
[Graphical view]
PfamPF13847. Methyltransf_31. 1 hit.
[Graphical view]
PROSITEPS51687. SAM_MT_RNA_M5U. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRMT2B. human.
GenomeRNAi79979.
NextBio70009.
PROQ96GJ1.

Entry information

Entry nameTRM2_HUMAN
AccessionPrimary (citable) accession number: Q96GJ1
Secondary accession number(s): A6NDG5 expand/collapse secondary AC list , A6NEI9, A6NMG6, Q5JPF0, Q5JVY6, Q96HU7, Q96IH9, Q9H9K2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 111 of the entry and version 1 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 X

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