Q9UBU8 (MO4L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA damage DNA recombination DNA repair Growth regulation Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Chromatin regulator
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	NuA4 histone acetyltransferase complex Inferred from direct assay Ref.18. Source: UniProtKB Sin3 complex Inferred from direct assay Ref.18. 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 362

362

Mortality factor 4-like protein 1

PRO_0000088764

Regions

Domain

191 – 362

172

MRG

Region

26 – 62

37

Interaction with KAT8

Region

133 – 266

134

Sufficient for interaction with SIN3A

Region

164 – 230

67

Interaction with RB1-1

Region

188 – 342

155

Sufficient for interaction with PHF12

Region

323 – 344

22

Interaction with RB1-2

Motif

135 – 146

12

Nuclear localization signal Potential

Amino acid modifications

Modified residue

143

1

N6-acetyllysine Ref.20

Natural variations

Alternative sequence

1 – 127

127

Missing in isoform 3.

VSP_046016

Alternative sequence

52 – 91

40

KSAVR…LLTSS → N in isoform 2.

VSP_012889

Experimental info

Mutagenesis

208

1

V → E: Abolishes binding to MRFAP1. Ref.24

Mutagenesis

234

1

E → R: No effect on MRFAP1 binding. Ref.24

Mutagenesis

251

1

Y → A: No effect on MRFAP1 binding. Ref.24

Mutagenesis

254

1

N → C: Reduces binding to MRFAP1. Ref.24

Sequence conflict

224

1

P → R in AAH67826. Ref.11

Sequence conflict

261

1

K → KK in CAB70879. Ref.6

Secondary structure

1

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362

Helix Strand Turn

Details...

Beta strand

16 – 36

21

Beta strand

39 – 46

8

Beta strand

47 – 49

3

Beta strand

94 – 97

4

Helix

98 – 100

3

Beta strand

101 – 105

5

Helix

106 – 125

20

Helix

201 – 203

3

Helix

204 – 215

12

Beta strand

219 – 221

3

Beta strand

226 – 228

3

Helix

229 – 241

13

Beta strand

244 – 246

3

Helix

252 – 271

20

Helix

275 – 277

3

Helix

278 – 287

10

Helix

293 – 296

4

Helix

299 – 313

15

Helix

320 – 339

20

Helix

341 – 344

4

Helix

347 – 349

3

Beta strand

350 – 352

3

Helix

355 – 358

4

Turn

359 – 361

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 15, 2005. Version 2. Checksum: 96B76BCA801F1187	FASTA	362	41,474
	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
	Isoform 2 [UniParc]. Checksum: 33CDBEC7D9CF513F	FASTA	323	37,231
	10 20 30 40 50 60 MAPKQDPKPK FQEGERVLCF HGPLLYEAKC VKVAIKDKQV KYFIHYSGWN KNWDEWVPES 70 80 90 100 110 120 RVLKYVDTNL QKQRELQKAN QEQYAEGKMR GAAPGKKTSG LQQKNVEVKT KKNKQKTPGN 130 140 150 160 170 180 GDGGSTSETP QPPRKKRARV DPTVENEETF MNRVEVKVKI PEELKPWLVD DWDLITRQKQ 190 200 210 220 230 240 LFYLPAKKNV DSILEDYANY KKSRGNTDNK EYAVNEVVAG IKEYFNVMLG TQLLYKFERP 250 260 270 280 290 300 QYAEILADHP DAPMSQVYGA PHLLRLFVRI GAMLAYTPLD EKSLALLLNY LHDFLKYLAK 310 320 NSATLFSASD YEVAPPEYHR KAV
	Isoform 3 [UniParc]. Checksum: 04AA4B2175DF583E	FASTA	235	26,750
	10 20 30 40 50 60 MRGAAPGKKT SGLQQKNVEV KTKKNKQKTP GNGDGGSTSE TPQPPRKKRA RVDPTVENEE 70 80 90 100 110 120 TFMNRVEVKV KIPEELKPWL VDDWDLITRQ KQLFYLPAKK NVDSILEDYA NYKKSRGNTD 130 140 150 160 170 180 NKEYAVNEVV AGIKEYFNVM LGTQLLYKFE RPQYAEILAD HPDAPMSQVY GAPHLLRLFV 190 200 210 220 230 RIGAMLAYTP LDEKSLALLL NYLHDFLKYL AKNSATLFSA SDYEVAPPEY HRKAV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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. , 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. , 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, MASS SPECTROMETRY.
[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.

IPI

IPI00409675.
IPI00930346.

PIR

T46285.

RefSeq

NP_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.

UniGene

Hs.374503.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AQL	X-ray	2.30	A/B	190-362	[»]
2EFI	NMR	-	A	1-51	[»]
2F5J	X-ray	2.20	A/B	190-362	[»]
2F5K	X-ray	2.20	A/B/C/D/E/F	1-129	[»]
2LKM	NMR	-	B	194-362	[»]

ProteinModelPortal

Q9UBU8.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29017N.

IntAct

Q9UBU8. 12 interactions.

MINT

MINT-1472718.

STRING

9606.ENSP00000331310.

PTM databases

PhosphoSite

Q9UBU8.

Polymorphism databases

DMDM

59803121.

Proteomic databases

PaxDb

Q9UBU8.

PRIDE

Q9UBU8.

Protocols and materials databases

DNASU

10933.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331268; ENSP00000331310; ENSG00000185787.
ENST00000426013; ENSP00000408880; ENSG00000185787.
ENST00000558502; ENSP00000452808; ENSG00000185787.
ENST00000559345; ENSP00000452717; ENSG00000185787.

GeneID

10933.

KEGG

hsa:10933.

UCSC

uc002bel.3. human.
uc002bem.3. human.

Organism-specific databases

CTD

10933.

GeneCards

GC15P079102.

HGNC

HGNC:16989. MORF4L1.

HPA

HPA042360.

MIM

607303. gene.

neXtProt

NX_Q9UBU8.

PharmGKB

PA134895182.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG238705.

HOVERGEN

HBG052487.

InParanoid

Q9UBU8.

KO

K11339.

OrthoDB

EOG4WH8M6.

PhylomeDB

Q9UBU8.

Gene expression databases

ArrayExpress

Q9UBU8.

Bgee

Q9UBU8.

CleanEx

HS_MORF4L1.

Genevestigator

Q9UBU8.

GermOnline

ENSG00000185787. Homo sapiens.

Family and domain databases

InterPro

IPR016197. Chromodomain-like.
IPR017398. EAF3/MRG15.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]

PANTHER

PTHR10880. PTHR10880. 1 hit.

Pfam

PF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]

PIRSF

PIRSF038133. HAT_Nua4_EAF3/MRG15. 1 hit.

SUPFAM

SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS51640. MRG. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9UBU8.

GenomeRNAi

10933.

NextBio

41527.

SOURCE

Search...

Entry information

Entry name

MO4L1_HUMAN

Accession

Primary (citable) accession number: Q9UBU8
Secondary accession number(s): B4DKN6 , 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:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.