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Protein

7SK snRNA methylphosphate capping enzyme

Gene

Mepce

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei558 – 5581S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

  • negative regulation of chromatin binding Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of G1/S transition of mitotic cell cycle Source: MGI
  • RNA methylation Source: UniProtKB
  • snRNA metabolic process Source: UniProtKB
  • snRNA modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
7SK snRNA methylphosphate capping enzyme (EC:2.1.1.-)
Short name:
MePCE
Gene namesi
Name:Mepce
Synonyms:Bcdin3, Bipl1, D5Wsu46e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:106477. Mepce.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6666667SK snRNA methylphosphate capping enzymePRO_0000289263Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei57 – 571PhosphoserineBy similarity
Modified residuei126 – 1261PhosphoserineBy similarity
Modified residuei150 – 1501PhosphoserineBy similarity
Modified residuei154 – 1541PhosphoserineBy similarity
Modified residuei188 – 1881PhosphothreonineCombined sources
Modified residuei191 – 1911PhosphoserineBy similarity
Modified residuei192 – 1921PhosphoserineCombined sources
Modified residuei229 – 2291PhosphoserineBy similarity
Modified residuei268 – 2681PhosphothreonineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei321 – 3211PhosphoserineBy similarity
Modified residuei368 – 3681PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8K3A9.
MaxQBiQ8K3A9.
PaxDbiQ8K3A9.
PRIDEiQ8K3A9.

PTM databases

iPTMnetiQ8K3A9.

Expressioni

Gene expression databases

BgeeiQ8K3A9.
CleanExiMM_MEPCE.
ExpressionAtlasiQ8K3A9. baseline and differential.
GenevisibleiQ8K3A9. MM.

Interactioni

Subunit structurei

Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, MEPCE/BCDIN3, SART3 proteins and 7SK and U6 snRNAs.By similarity

Protein-protein interaction databases

IntActiQ8K3A9. 1 interaction.
STRINGi10090.ENSMUSP00000031740.

Structurei

3D structure databases

ProteinModelPortaliQ8K3A9.
SMRiQ8K3A9. Positions 408-662.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini408 – 663256Bin3-type SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni428 – 4303S-adenosyl-L-methionine bindingBy similarity
Regioni451 – 4522S-adenosyl-L-methionine bindingBy similarity
Regioni536 – 5372S-adenosyl-L-methionine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi25 – 135111Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the methyltransferase superfamily.Curated
Contains 1 Bin3-type SAM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2899. Eukaryota.
ENOG410XZ7T. LUCA.
GeneTreeiENSGT00390000015611.
HOGENOMiHOG000113562.
HOVERGENiHBG099856.
InParanoidiQ8K3A9.
KOiK15190.
OMAiHGEGTTQ.
OrthoDBiEOG78M02C.
PhylomeDBiQ8K3A9.
TreeFamiTF324061.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR010675. Bin3_C.
IPR024160. BIN3_SAM-bd_dom.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF06859. Bin3. 1 hit.
PF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51515. BIN3_SAM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K3A9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEMAAEKEP FLVPAPPPPL KDESGGGGGP EVQSHQEAAS GELRDGTEHG
60 70 80 90 100
PGPRAHSAGA AASGGGGPQA QAHGEPHGRA AAPADVGEER RGGGGTDLGP
110 120 130 140 150
PAPPRPRNGY QPHRPPGGGG GKRRNSCNVG GGSGGSFKHP AFKRRRRVNS
160 170 180 190 200
DCDSVLPSNF LLGGNIFDPL NLNSLLDEEV SRALNAETPK SSPLPAKGRD
210 220 230 240 250
PVEILIPKDI TDPLSLNTCT DEAHVVLASP LKIGRKRHRH RGPHHQQQQQ
260 270 280 290 300
ASGGNDSNAA VLPTDPLTPS LHGEGATQQQ QNRGQNRDAP QPYELNTAIN
310 320 330 340 350
CRDEVVSPLP SALQGSSGSL SAPPAASVTS APSTSSSSRH RKRRRTSSKS
360 370 380 390 400
EAGARGGSQG SKEKGRGSGG GRHHHHPLPA TGFKKQQLKF QYGNYCKYYG
410 420 430 440 450
YRNPSCEDVR LRVLKPEWFQ GRDVLDLGCN VGHLTLSIAC KWGPARMVGL
460 470 480 490 500
DIDPRLIHSA RQNIRHYLSE ELRLQAQTSE GDPGTEGEEG TITVRKRSCF
510 520 530 540 550
PASLTASRGP IAAPQVPLDG ADTSVFPNNV VFVTGNYVLD RDELVDAQRP
560 570 580 590 600
EYDVVLCFSL TKWVHLNWGD EGLKRMFRRI YRHLRPGGIL VLEPQPWSSY
610 620 630 640 650
CKRKSLTETI YKNYFRIQLK PEQFSSYLTS PEVGFSSYEL VATPNNTSRG
660
FQRPVYLFHK ARSPSH
Length:666
Mass (Da):72,050
Last modified:May 29, 2007 - v2
Checksum:i872F17A84E049AD9
GO

Sequence cautioni

The sequence AAH17157.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAX39492.1 differs from that shown. Reason: Frameshift at positions 17, 60 and 78. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801Missing in AAX39492 (PubMed:16926269).Curated
Sequence conflicti246 – 2461Missing in AAH26876 (PubMed:15489334).Curated
Sequence conflicti441 – 4411K → M in AAH17157 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY823670 Genomic DNA. Translation: AAX39492.1. Frameshift.
AK139731 mRNA. Translation: BAE24116.1.
AK154415 mRNA. Translation: BAE32569.1.
BC017157 mRNA. Translation: AAH17157.2. Different initiation.
BC026876 mRNA. Translation: AAH26876.1.
CCDSiCCDS39337.1.
RefSeqiNP_659162.3. NM_144913.3.
UniGeneiMm.61193.

Genome annotation databases

EnsembliENSMUST00000031740; ENSMUSP00000031740; ENSMUSG00000029726.
GeneIDi231803.
KEGGimmu:231803.
UCSCiuc009ady.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY823670 Genomic DNA. Translation: AAX39492.1. Frameshift.
AK139731 mRNA. Translation: BAE24116.1.
AK154415 mRNA. Translation: BAE32569.1.
BC017157 mRNA. Translation: AAH17157.2. Different initiation.
BC026876 mRNA. Translation: AAH26876.1.
CCDSiCCDS39337.1.
RefSeqiNP_659162.3. NM_144913.3.
UniGeneiMm.61193.

3D structure databases

ProteinModelPortaliQ8K3A9.
SMRiQ8K3A9. Positions 408-662.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K3A9. 1 interaction.
STRINGi10090.ENSMUSP00000031740.

PTM databases

iPTMnetiQ8K3A9.

Proteomic databases

EPDiQ8K3A9.
MaxQBiQ8K3A9.
PaxDbiQ8K3A9.
PRIDEiQ8K3A9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031740; ENSMUSP00000031740; ENSMUSG00000029726.
GeneIDi231803.
KEGGimmu:231803.
UCSCiuc009ady.1. mouse.

Organism-specific databases

CTDi56257.
MGIiMGI:106477. Mepce.

Phylogenomic databases

eggNOGiKOG2899. Eukaryota.
ENOG410XZ7T. LUCA.
GeneTreeiENSGT00390000015611.
HOGENOMiHOG000113562.
HOVERGENiHBG099856.
InParanoidiQ8K3A9.
KOiK15190.
OMAiHGEGTTQ.
OrthoDBiEOG78M02C.
PhylomeDBiQ8K3A9.
TreeFamiTF324061.

Miscellaneous databases

NextBioi380757.
PROiQ8K3A9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K3A9.
CleanExiMM_MEPCE.
ExpressionAtlasiQ8K3A9. baseline and differential.
GenevisibleiQ8K3A9. MM.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR010675. Bin3_C.
IPR024160. BIN3_SAM-bd_dom.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF06859. Bin3. 1 hit.
PF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51515. BIN3_SAM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comparative analysis of the paired immunoglobulin-like receptor (PILR) locus in six mammalian genomes: duplication, conversion, and the birth of new genes."
    Wilson M.D., Cheung J., Martindale D.W., Scherer S.W., Koop B.F.
    Physiol. Genomics 27:201-218(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Egg.
  3. "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].
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor and Salivary gland.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMEPCE_MOUSE
AccessioniPrimary (citable) accession number: Q8K3A9
Secondary accession number(s): Q2YFS5
, Q3U465, Q3UT64, Q91W35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: March 16, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.