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Q9R0Q4 (MO4L2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mortality factor 4-like protein 2
Alternative name(s):
MORF-related gene X protein
Sid 393
Transcription factor-like protein MRGX
Gene names
Name:Morf4l2
Synonyms:Kiaa0026, Sid393
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones By similarity.

Subunit structure

Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41 and VPS72/YL1. The NuA4 complex interacts with MYC and the adenovirus E1A protein. MORF4L1 may also participate in the formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit, but which include the SWI/SNF related protein SRCAP. Component of the MSIN3A histone deacetylase complex, which includes SIN3A, HDAC2, ARID4B, MORF4L1, RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with MRFAP1 and RB1. May also interact with one or more as yet undefined members of the TLE (transducin-like enhancer of split) family of transcriptional repressors By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 1 MRG domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288Mortality factor 4-like protein 2
PRO_0000088769

Regions

Domain117 – 288172MRG

Amino acid modifications

Modified residue711Phosphoserine By similarity

Experimental info

Sequence conflict371A → S in AAH75653. Ref.5
Sequence conflict1451Q → P in BAC36075. Ref.2
Sequence conflict1761E → D in BAC97848. Ref.3
Sequence conflict1861I → T in BAC41017. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9R0Q4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: DE371EDD3D4DF4E2

FASTA28832,184
        10         20         30         40         50         60 
MSSRKQASQT RGQQSAEEDN FKKPTRSNMQ RSKMRGAASG KKSAGSQPKN LDPALPGRWG 

        70         80         90        100        110        120 
GRSAENPPSG SVRKTRKNKQ KAPGNGDGGS TSEVPQPPRK KRARADPTVE SEEAFKSRME 

       130        140        150        160        170        180 
VKVKIPEELK PWLVEDWDLV TRQKQLFQLP AKKNVDAILE EYANCKKSQG NVDNKEYAVN 

       190        200        210        220        230        240 
EVVGGIKEYF NVMLGTQLLY KFERPQYAEI LLAHPDAPMS QIYGAPHLLR LFVRIGAMLA 

       250        260        270        280 
YTPLDEKSLA LLLGYLHDFL KYLAKNSASL FTASDYKVAS ADYHRKAL 

« Hide

References

« Hide 'large scale' references
[1]"Mouse homolog of KIAA0026."
Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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: C3H/HeJ, C57BL/6J and NOD.
Tissue: Bone marrow, Embryonic stem cell, Eye and Thymus.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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].
Strain: 129 and C57BL/6.
Tissue: Eye and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025049 mRNA. Translation: BAA84687.1.
AK075946 mRNA. Translation: BAC36075.1.
AK088849 mRNA. Translation: BAC40611.1.
AK089963 mRNA. Translation: BAC41017.1.
AK129038 mRNA. Translation: BAC97848.1.
AK131944 mRNA. Translation: BAE20890.1.
AK145686 mRNA. Translation: BAE26588.1.
AK150401 mRNA. Translation: BAE29527.1.
AK150670 mRNA. Translation: BAE29752.1.
AK151570 mRNA. Translation: BAE30512.1.
AK160012 mRNA. Translation: BAE35559.1.
AK161610 mRNA. Translation: BAE36491.1.
AK164433 mRNA. Translation: BAE37786.1.
AK166637 mRNA. Translation: BAE38909.1.
AL671887 Genomic DNA. Translation: CAM17215.1.
BC075653 mRNA. Translation: AAH75653.1.
BC088731 mRNA. Translation: AAH88731.1.
RefSeqNP_001161697.1. NM_001168225.1.
NP_001161698.1. NM_001168226.1.
NP_001161699.1. NM_001168227.1.
NP_001161700.1. NM_001168228.1.
NP_001161701.1. NM_001168229.1.
NP_001161702.1. NM_001168230.1.
NP_062742.4. NM_019768.4.
XP_006528647.1. XM_006528584.1.
UniGeneMm.27218.

3D structure databases

ProteinModelPortalQ9R0Q4.
SMRQ9R0Q4. Positions 117-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000108722.

PTM databases

PhosphoSiteQ9R0Q4.

Proteomic databases

PaxDbQ9R0Q4.
PRIDEQ9R0Q4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033797; ENSMUSP00000033797; ENSMUSG00000031422.
ENSMUST00000080411; ENSMUSP00000108722; ENSMUSG00000031422.
ENSMUST00000113097; ENSMUSP00000108720; ENSMUSG00000031422.
ENSMUST00000164609; ENSMUSP00000129774; ENSMUSG00000031422.
ENSMUST00000166478; ENSMUSP00000131909; ENSMUSG00000031422.
ENSMUST00000166930; ENSMUSP00000126363; ENSMUSG00000031422.
ENSMUST00000169418; ENSMUSP00000132643; ENSMUSG00000031422.
GeneID56397.
KEGGmmu:56397.
UCSCuc009uiu.3. mouse.

Organism-specific databases

CTD9643.
MGIMGI:1927167. Morf4l2.
RougeSearch...

Phylogenomic databases

eggNOGNOG317973.
GeneTreeENSGT00530000063018.
HOVERGENHBG052487.
InParanoidA2AEB2.
KOK11342.
OMARGNMQRS.
OrthoDBEOG7ZPNK7.
PhylomeDBQ9R0Q4.
TreeFamTF323400.

Gene expression databases

ArrayExpressQ9R0Q4.
BgeeQ9R0Q4.
CleanExMM_MORF4L2.
GenevestigatorQ9R0Q4.

Family and domain databases

InterProIPR008676. MRG.
IPR026541. MRG_dom.
[Graphical view]
PANTHERPTHR10880. PTHR10880. 1 hit.
PfamPF05712. MRG. 1 hit.
[Graphical view]
PROSITEPS51640. MRG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMORF4L2. mouse.
NextBio312500.
PROQ9R0Q4.
SOURCESearch...

Entry information

Entry nameMO4L2_MOUSE
AccessionPrimary (citable) accession number: Q9R0Q4
Secondary accession number(s): A2AEB2 expand/collapse secondary AC list , Q3UL62, Q6DIB1, Q6ZQK7, Q8C201, Q8C6C2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot