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Q9UBU8 (MO4L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. 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:
Mortality factor 4-like protein 1
Alternative name(s):
MORF-related gene 15 protein
Protein MSL3-1
Transcription factor-like protein MRG15
Gene names
Name:MORF4L1
Synonyms:MRG15
ORF Names:FWP006, HSPC008, HSPC061, PP368
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones 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. Required for homologous recombination repair (HRR) and resistance to mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and RAD51, but not BRCA1, to DNA-damage foci. Ref.18 Ref.21

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, VPS72/YL1 and MEAF6. 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 RB1 and KAT8. May also interact with PHF12 and one or more as yet undefined members of the TLE (transducin-like enhancer of split) family of transcriptional repressors. Interacts with the N-terminus of MRFAP1. Found in a complex composed of MORF4L1, MRFAP1 and RB1. Interacts with the entire BRCA complex, which contains BRCA1, PALB2, BRCA2 and RAD51. Interacts with PALB2. Forms a complex with MSL1 and NUPR1. Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.21 Ref.23

Subcellular location

Nucleus.

Sequence similarities

Contains 1 MRG domain.

Sequence caution

The sequence AAG17253.1 differs from that shown. Reason: Frameshift at positions 348 and 360.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Growth regulation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionChromatin regulator
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Ensembl

chromatin organization

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Inferred from direct assay Ref.21. Source: UniProtKB

histone H2A acetylation

Inferred from direct assay Ref.18. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay Ref.18. Source: UniProtKB

histone deacetylation

Inferred from direct assay Ref.18. Source: UniProtKB

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuA4 histone acetyltransferase complex

Inferred from direct assay Ref.18. Source: UniProtKB

Sin3 complex

Inferred from direct assay Ref.18. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

protein N-terminus binding

Inferred from physical interaction PubMed 17577209. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBU8-1)

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: Q9UBU8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     52-91: KSAVRPRRSEKSLKTHEDIVALFPVPEGAPSVHHPLLTSS → N
Isoform 3 (identifier: Q9UBU8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Mortality factor 4-like protein 1
PRO_0000088764

Regions

Domain191 – 362172MRG
Region26 – 6237Interaction with KAT8
Region133 – 266134Sufficient for interaction with SIN3A
Region164 – 23067Interaction with RB1-1
Region188 – 342155Sufficient for interaction with PHF12
Region323 – 34422Interaction with RB1-2
Motif135 – 14612Nuclear localization signal Potential

Amino acid modifications

Modified residue1431N6-acetyllysine Ref.20

Natural variations

Alternative sequence1 – 127127Missing in isoform 3.
VSP_046016
Alternative sequence52 – 9140KSAVR…LLTSS → N in isoform 2.
VSP_012889

Experimental info

Mutagenesis2081V → E: Abolishes binding to MRFAP1. Ref.24
Mutagenesis2341E → R: No effect on MRFAP1 binding. Ref.24
Mutagenesis2511Y → A: No effect on MRFAP1 binding. Ref.24
Mutagenesis2541N → C: Reduces binding to MRFAP1. Ref.24
Sequence conflict2241P → R in AAH67826. Ref.11
Sequence conflict2611K → KK in CAB70879. Ref.6

Secondary structure

........................................ 362
Helix Strand Turn

Details...

Sequences

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

Last modified February 15, 2005. Version 2.
Checksum: 96B76BCA801F1187

FASTA36241,474
        10         20         30         40         50         60 
MAPKQDPKPK FQEGERVLCF HGPLLYEAKC VKVAIKDKQV KYFIHYSGWN KKSAVRPRRS 

        70         80         90        100        110        120 
EKSLKTHEDI VALFPVPEGA PSVHHPLLTS SWDEWVPESR VLKYVDTNLQ KQRELQKANQ 

       130        140        150        160        170        180 
EQYAEGKMRG AAPGKKTSGL QQKNVEVKTK KNKQKTPGNG DGGSTSETPQ PPRKKRARVD 

       190        200        210        220        230        240 
PTVENEETFM NRVEVKVKIP EELKPWLVDD WDLITRQKQL FYLPAKKNVD SILEDYANYK 

       250        260        270        280        290        300 
KSRGNTDNKE YAVNEVVAGI KEYFNVMLGT QLLYKFERPQ YAEILADHPD APMSQVYGAP 

       310        320        330        340        350        360 
HLLRLFVRIG AMLAYTPLDE KSLALLLNYL HDFLKYLAKN SATLFSASDY EVAPPEYHRK 


AV 

« Hide

Isoform 2 [UniParc].

Checksum: 33CDBEC7D9CF513F
Show »

FASTA32337,231
Isoform 3 [UniParc].

Checksum: 04AA4B2175DF583E
Show »

FASTA23526,750

References

« Hide 'large scale' references
[1]"Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factor-like genes."
Bertram M.J., Berube N.G., Hang-Swanson X., Ran Q., Leung J.K., Bryce S., Spurgers K., Bick R.J., Baldini A., Ning Y., Clark L.J., Parkinson E.K., Barrett J.C., Smith J.R., Pereira-Smith O.M.
Mol. Cell. Biol. 19:1479-1485(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Two human homologs of the Drosophila dosage compensation gene msl-3 are located on the X chromosome."
D'Esposito M., Cocchia M., Matarazzo M.R., Macmillan S., Mazzarella R.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Cloning and identification of cellular senescence associated genes from fibroblasts 2BS."
Guo S., Tong T., Zhang Z.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lung.
[5]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Umbilical cord blood.
[6]Liu B., Zhao B., Wang X.Y., Xu Y.Y., Liu Y.Q., Song L., Ye J., Sheng H., Gao Y., Zhang C.L., Wei Y.J., Zhang J., Song L., Jiang Y.X., Zhao Z.W., Ding J.F., Liu L.S., Gao R.L. expand/collapse author list , Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Aorta.
[7]"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] (ISOFORMS 1 AND 3).
Tissue: Colon and Embryonic stem cell.
[8]"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 2).
Tissue: Kidney.
[9]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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].
[11]"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 2 AND 3).
Tissue: Embryonic stem cell, Skin and Testis.
[12]"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-29; 42-51; 118-127; 156-173; 179-192; 228-240; 244-261 AND 340-359, IDENTIFICATION IN NUA4 COMPLEX.
[13]Mei G., Yu W., Gibbs R.A.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-362 (ISOFORMS 1/2).
Tissue: Brain.
[14]"MRG15 activates the B-myb promoter through formation of a nuclear complex with the retinoblastoma protein and the novel protein PAM14."
Leung J.K., Berube N., Venable S., Ahmed S., Timchenko N., Pereira-Smith O.M.
J. Biol. Chem. 276:39171-39178(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MRFAP1 AND RB1.
[15]"MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation."
Pardo P.S., Leung J.K., Lucchesi J.C., Pereira-Smith O.M.
J. Biol. Chem. 277:50860-50866(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH RB1 AND MRFAP1, INTERACTION WITH RB1 AND KAT8.
[16]"Role for the mortality factors MORF4, MRGX, and MRG15 in transcriptional repression via associations with Pf1, mSin3A, and transducin-like enhancer of Split."
Yochum G.S., Ayer D.E.
Mol. Cell. Biol. 22:7868-7876(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHF12; SIN3A AND TLE FAMILY MEMBERS.
[17]"The highly conserved and multifunctional NuA4 HAT complex."
Doyon Y., Cote J.
Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON NUA4 COMPLEX.
[18]"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN SIN3A COMPLEX.
[19]"p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage."
Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M., Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C., Iovanna J.L.
J. Cell. Physiol. 221:594-602(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MSL1 AND NUPR1.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"MRG15 binds directly to PALB2 and stimulates homology-directed repair of chromosomal breaks."
Hayakawa T., Zhang F., Hayakawa N., Ohtani Y., Shinmyozu K., Nakayama J., Andreassen P.R.
J. Cell Sci. 123:1124-1130(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BRCA COMPLEX AND PALB2.
[22]"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].
[23]"The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14."
Zhang P., Zhao J., Wang B., Du J., Lu Y., Chen J., Ding J.
Protein Sci. 15:2423-2434(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 190-362, INTERACTION WITH MRFAP1.
[24]"Multipurpose MRG domain involved in cell senescence and proliferation exhibits structural homology to a DNA-interacting domain."
Bowman B.R., Moure C.M., Kirtane B.M., Welschhans R.L., Tominaga K., Pereira-Smith O.M., Quiocho F.A.
Structure 14:151-158(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 190-362, MUTAGENESIS OF VAL-208; GLU-234; TYR-251 AND ASN-254.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF100615 mRNA. Translation: AAD29872.1.
AF167173 mRNA. Translation: AAF80854.1.
AF218011 mRNA. Translation: AAG17253.1. Frameshift.
AY148481 mRNA. Translation: AAN65338.1.
AF070664 mRNA. Translation: AAD20970.1.
AF161546 mRNA. Translation: AAF29033.1.
AF109188 mRNA. Translation: AAQ13497.1.
AK296650 mRNA. Translation: BAG59248.1.
AK300789 mRNA. Translation: BAH13347.1.
AL137697 mRNA. Translation: CAB70879.2.
AC011944 Genomic DNA. No translation available.
AC022748 Genomic DNA. No translation available.
AC103975 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99145.1.
CH471136 Genomic DNA. Translation: EAW99144.1.
CH471136 Genomic DNA. Translation: EAW99146.1.
CH471136 Genomic DNA. Translation: EAW99147.1.
BC022845 mRNA. Translation: AAH22845.1.
BC002936 mRNA. Translation: AAH02936.1.
BC067826 mRNA. Translation: AAH67826.1.
CX165647 mRNA. No translation available.
AF131847 mRNA. Translation: AAD20058.1.
PIRT46285.
RefSeqNP_001252532.1. NM_001265603.1.
NP_001252533.1. NM_001265604.1.
NP_001252534.1. NM_001265605.1.
NP_006782.1. NM_006791.3.
NP_996670.1. NM_206839.2.
UniGeneHs.374503.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AQLX-ray2.30A/B190-362[»]
2EFINMR-A1-51[»]
2F5JX-ray2.20A/B190-362[»]
2F5KX-ray2.20A/B/C/D/E/F1-129[»]
2LKMNMR-B194-362[»]
ProteinModelPortalQ9UBU8.
SMRQ9UBU8. Positions 1-132, 194-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116134. 58 interactions.
DIPDIP-29017N.
IntActQ9UBU8. 18 interactions.
MINTMINT-1472718.
STRING9606.ENSP00000331310.

PTM databases

PhosphoSiteQ9UBU8.

Polymorphism databases

DMDM59803121.

Proteomic databases

PaxDbQ9UBU8.
PRIDEQ9UBU8.

Protocols and materials databases

DNASU10933.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331268; ENSP00000331310; ENSG00000185787. [Q9UBU8-1]
ENST00000426013; ENSP00000408880; ENSG00000185787. [Q9UBU8-2]
ENST00000558502; ENSP00000452808; ENSG00000185787. [Q9UBU8-3]
ENST00000559345; ENSP00000452717; ENSG00000185787. [Q9UBU8-3]
GeneID10933.
KEGGhsa:10933.
UCSCuc002bel.4. human. [Q9UBU8-1]
uc002bem.4. human. [Q9UBU8-2]

Organism-specific databases

CTD10933.
GeneCardsGC15P079102.
HGNCHGNC:16989. MORF4L1.
HPAHPA042360.
MIM607303. gene.
neXtProtNX_Q9UBU8.
PharmGKBPA134895182.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238705.
HOVERGENHBG052487.
InParanoidQ9UBU8.
KOK11339.
PhylomeDBQ9UBU8.
TreeFamTF323400.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.

Gene expression databases

ArrayExpressQ9UBU8.
BgeeQ9UBU8.
CleanExHS_MORF4L1.
GenevestigatorQ9UBU8.

Family and domain databases

InterProIPR016197. Chromodomain-like.
IPR017398. EAF3/MRG15.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERPTHR10880. PTHR10880. 1 hit.
PfamPF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
PIRSFPIRSF038133. HAT_Nua4_EAF3/MRG15. 1 hit.
SUPFAMSSF54160. SSF54160. 2 hits.
PROSITEPS51640. MRG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UBU8.
GeneWikiMORF4L1.
GenomeRNAi10933.
NextBio41527.
PROQ9UBU8.
SOURCESearch...

Entry information

Entry nameMO4L1_HUMAN
AccessionPrimary (citable) accession number: Q9UBU8
Secondary accession number(s): B4DKN6 expand/collapse secondary AC list , B7Z6R1, D3DW88, O95899, Q5QTS1, Q6NVX8, Q86YT7, Q9HBP6, Q9NSW5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 148 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM