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Q9UBP6

- TRMB_HUMAN

UniProt

Q9UBP6 - TRMB_HUMAN

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Protein

tRNA (guanine-N(7)-)-methyltransferase

Gene

METTL1

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

Functioni

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.1 PublicationUniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841S-adenosyl-L-methionine; via carbonyl oxygen1 PublicationUniRule annotation
Binding sitei160 – 1601S-adenosyl-L-methionine; via carbonyl oxygen1 PublicationUniRule annotation
Active sitei163 – 1631UniRule annotation

GO - Molecular functioni

  1. tRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB
  2. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. RNA (guanine-N7)-methylation Source: GOC
  2. tRNA modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine, tRNA-binding

Enzyme and pathway databases

UniPathwayiUPA00989.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine-N(7)-)-methyltransferaseUniRule annotation (EC:2.1.1.33UniRule annotation)
Alternative name(s):
Methyltransferase-like protein 1UniRule annotation
tRNA (guanine(46)-N(7))-methyltransferaseUniRule annotation
tRNA(m7G46)-methyltransferaseUniRule annotation
Gene namesi
Name:METTL1UniRule annotation
Synonyms:C12orf1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7030. METTL1.

Subcellular locationi

Nucleus 1 PublicationUniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271S → A: Able to complement a trm8-delta mutant yeast. 1 Publication
Mutagenesisi27 – 271S → D or E: Abolishes ability to complement a trm8-delta mutant yeast. 1 Publication

Organism-specific databases

PharmGKBiPA30766.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 276275tRNA (guanine-N(7)-)-methyltransferasePRO_0000171431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei27 – 271Phosphoserine; by PKB and RPS6KA31 PublicationUniRule annotation

Post-translational modificationi

Phosphorylation at Ser-27 inactivates its catalytic activity but does not affect the interaction with WDR4.1 PublicationUniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UBP6.
PaxDbiQ9UBP6.
PRIDEiQ9UBP6.

PTM databases

PhosphoSiteiQ9UBP6.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9UBP6.
CleanExiHS_METTL1.
ExpressionAtlasiQ9UBP6. baseline and differential.
GenevestigatoriQ9UBP6.

Organism-specific databases

HPAiHPA020914.
HPA050450.

Interactioni

Subunit structurei

Forms a complex with WDR4.1 PublicationUniRule annotation

Protein-protein interaction databases

BioGridi110392. 32 interactions.
IntActiQ9UBP6. 1 interaction.
MINTiMINT-1440834.
STRINGi9606.ENSP00000314441.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 433Combined sources
Turni47 – 493Combined sources
Beta strandi78 – 836Combined sources
Helixi89 – 946Combined sources
Helixi95 – 973Combined sources
Beta strandi101 – 1088Combined sources
Helixi110 – 12516Combined sources
Beta strandi134 – 1385Combined sources
Turni141 – 1433Combined sources
Helixi145 – 1484Combined sources
Beta strandi154 – 1618Combined sources
Helixi178 – 18710Combined sources
Beta strandi188 – 19912Combined sources
Helixi201 – 21212Combined sources
Beta strandi217 – 2204Combined sources
Helixi222 – 2254Combined sources
Helixi231 – 2333Combined sources
Turni234 – 2363Combined sources
Helixi239 – 2468Combined sources
Beta strandi252 – 2587Combined sources
Turni262 – 2643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CKKX-ray1.55A32-265[»]
ProteinModelPortaliQ9UBP6.
SMRiQ9UBP6. Positions 37-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBP6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1082S-adenosyl-L-methionine binding
Regioni140 – 1412S-adenosyl-L-methionine binding
Regioni238 – 2403S-adenosyl-L-methionine binding

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0220.
GeneTreeiENSGT00390000017840.
HOGENOMiHOG000260965.
HOVERGENiHBG044569.
InParanoidiQ9UBP6.
KOiK03439.
OMAiRAHSNPI.
OrthoDBiEOG7PS1GC.
PhylomeDBiQ9UBP6.
TreeFamiTF314083.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_03055. tRNA_methyltr_TrmB_euk.
InterProiIPR029063. SAM-dependent_MTases-like.
IPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UBP6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAETRNVAG AEAPPPQKRY YRQRAHSNPM ADHTLRYPVK PEEMDWSELY
60 70 80 90 100
PEFFAPLTQN QSHDDPKDKK EKRAQAQVEF ADIGCGYGGL LVELSPLFPD
110 120 130 140 150
TLILGLEIRV KVSDYVQDRI RALRAAPAGG FQNIACLRSN AMKHLPNFFY
160 170 180 190 200
KGQLTKMFFL FPDPHFKRTK HKWRIISPTL LAEYAYVLRV GGLVYTITDV
210 220 230 240 250
LELHDWMCTH FEEHPLFERV PLEDLSEDPV VGHLGTSTEE GKKVLRNGGK
260 270
NFPAIFRRIQ DPVLQAVTSQ TSLPGH
Length:276
Mass (Da):31,471
Last modified:May 1, 2000 - v1
Checksum:i715AE85A18632892
GO
Isoform 2 (identifier: Q9UBP6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     92-155: VELSPLFPDT...PNFFYKGQLT → ADKDVLPLPR...VHSFRRAPTV
     156-276: Missing.

Note: No experimental confirmation available.

Show »
Length:155
Mass (Da):17,423
Checksum:iCFC2A730BA85E8D4
GO

Sequence cautioni

The sequence CAA65470.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181K → R in BAD96922. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei92 – 15564VELSP…KGQLT → ADKDVLPLPRPTFQADKAQV ANHQSHPASRICLRAKSWGA GVYHNRCAGATRLDVHSFRR APTV in isoform 2. 1 PublicationVSP_044671Add
BLAST
Alternative sequencei156 – 276121Missing in isoform 2. 1 PublicationVSP_044672Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18643 mRNA. Translation: CAA77239.1.
Y18642 Genomic DNA. Translation: CAA77238.1.
X96698 mRNA. Translation: CAA65470.1. Different initiation.
AK314851 mRNA. Translation: BAG37368.1.
AK223202 mRNA. Translation: BAD96922.1.
AC025165 Genomic DNA. No translation available.
BC000550 mRNA. Translation: AAH00550.1.
CCDSiCCDS8955.3. [Q9UBP6-1]
CCDS8956.1. [Q9UBP6-2]
RefSeqiNP_005362.3. NM_005371.5. [Q9UBP6-1]
NP_075422.3. NM_023033.3. [Q9UBP6-2]
UniGeneiHs.42957.

Genome annotation databases

EnsembliENST00000257848; ENSP00000257848; ENSG00000037897. [Q9UBP6-2]
ENST00000324871; ENSP00000314441; ENSG00000037897. [Q9UBP6-1]
GeneIDi4234.
KEGGihsa:4234.
UCSCiuc010ssd.2. human. [Q9UBP6-1]

Polymorphism databases

DMDMi32171926.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18643 mRNA. Translation: CAA77239.1 .
Y18642 Genomic DNA. Translation: CAA77238.1 .
X96698 mRNA. Translation: CAA65470.1 . Different initiation.
AK314851 mRNA. Translation: BAG37368.1 .
AK223202 mRNA. Translation: BAD96922.1 .
AC025165 Genomic DNA. No translation available.
BC000550 mRNA. Translation: AAH00550.1 .
CCDSi CCDS8955.3. [Q9UBP6-1 ]
CCDS8956.1. [Q9UBP6-2 ]
RefSeqi NP_005362.3. NM_005371.5. [Q9UBP6-1 ]
NP_075422.3. NM_023033.3. [Q9UBP6-2 ]
UniGenei Hs.42957.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CKK X-ray 1.55 A 32-265 [» ]
ProteinModelPortali Q9UBP6.
SMRi Q9UBP6. Positions 37-265.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110392. 32 interactions.
IntActi Q9UBP6. 1 interaction.
MINTi MINT-1440834.
STRINGi 9606.ENSP00000314441.

PTM databases

PhosphoSitei Q9UBP6.

Polymorphism databases

DMDMi 32171926.

Proteomic databases

MaxQBi Q9UBP6.
PaxDbi Q9UBP6.
PRIDEi Q9UBP6.

Protocols and materials databases

DNASUi 4234.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257848 ; ENSP00000257848 ; ENSG00000037897 . [Q9UBP6-2 ]
ENST00000324871 ; ENSP00000314441 ; ENSG00000037897 . [Q9UBP6-1 ]
GeneIDi 4234.
KEGGi hsa:4234.
UCSCi uc010ssd.2. human. [Q9UBP6-1 ]

Organism-specific databases

CTDi 4234.
GeneCardsi GC12M058174.
HGNCi HGNC:7030. METTL1.
HPAi HPA020914.
HPA050450.
MIMi 604466. gene.
neXtProti NX_Q9UBP6.
PharmGKBi PA30766.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0220.
GeneTreei ENSGT00390000017840.
HOGENOMi HOG000260965.
HOVERGENi HBG044569.
InParanoidi Q9UBP6.
KOi K03439.
OMAi RAHSNPI.
OrthoDBi EOG7PS1GC.
PhylomeDBi Q9UBP6.
TreeFami TF314083.

Enzyme and pathway databases

UniPathwayi UPA00989 .

Miscellaneous databases

ChiTaRSi METTL1. human.
EvolutionaryTracei Q9UBP6.
GeneWikii METTL1.
GenomeRNAii 4234.
NextBioi 16693.
PROi Q9UBP6.
SOURCEi Search...

Gene expression databases

Bgeei Q9UBP6.
CleanExi HS_METTL1.
ExpressionAtlasi Q9UBP6. baseline and differential.
Genevestigatori Q9UBP6.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
HAMAPi MF_03055. tRNA_methyltr_TrmB_euk.
InterProi IPR029063. SAM-dependent_MTases-like.
IPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view ]
Pfami PF02390. Methyltransf_4. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
TIGRFAMsi TIGR00091. TIGR00091. 1 hit.
PROSITEi PS51625. SAM_MT_TRMB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular analysis of METTL1, a novel human methyltransferase-like gene with a high degree of phylogenetic conservation."
    Bahr A., Hankeln T., Fiedler T., Hegemann J., Schmidt E.R.
    Genomics 57:424-428(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "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] (ISOFORM 1).
  3. 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] (ISOFORM 2).
    Tissue: Kidney proximal tubule.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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] (ISOFORM 1).
    Tissue: Brain.
  6. "Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA."
    Alexandrov A., Martzen M.R., Phizicky E.M.
    RNA 8:1253-1266(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH WDR4.
  7. "The tRNA methylase METTL1 is phosphorylated and inactivated by PKB and RSK in vitro and in cells."
    Cartlidge R.A., Knebel A., Peggie M., Alexandrov A., Phizicky E.M., Cohen P.
    EMBO J. 24:1696-1705(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WDR4, PHOSPHORYLATION AT SER-27, MUTAGENESIS OF SER-27.
  8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human methyltransferase-like protein 1."
    Structural genomics consortium (SGC)
    Submitted (APR-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 32-265 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

Entry informationi

Entry nameiTRMB_HUMAN
AccessioniPrimary (citable) accession number: Q9UBP6
Secondary accession number(s): B2RBX1
, H7BXF2, Q14105, Q53FS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 117 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3