Q99549 (MPP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
M-phase phosphoprotein 8

Alternative name(s):
Two hybrid-associated protein 3 with RanBPM
Short name=Twa3

Gene names

Name:	MPHOSPH8
Synonyms:	MPP8

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	860 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in transcriptional regulation. Specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression. Ref.11
Subunit structure	Homodimer. Interacts (via chromo domain) with histone H3K9me3. Has the highest affinity for H3K9me3, and lesser affinity for H3K9me2 and H3K9me1. Interacts with DNMT3, EHMT1 and SETDB1. Ref.11 Ref.14 Ref.16
Subcellular location	Nucleus. Note: Detected on heterochromatin. Detected on nucleosomes. Ref.6 Ref.11
Domain	The chromo domain mediates interaction with methylated 'Lys-9' of histone H3 (H3K9me), with the highest affinity for the trimethylated form (H3K9me3). Ref.14 Ref.16
Post-translational modification	Phosphorylated in M (mitotic) phase. Ref.6
Sequence similarities	Contains 4 ANK repeats. Contains 1 chromo domain.
Sequence caution	The sequence AAH46214.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB71284.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAI46172.1 differs from that shown. Reason: Frameshift at positions 248, 255 and 731.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Non-traceable author statement Ref.6. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.11. Source: UniProtKB regulation of DNA methylation Inferred from mutant phenotype Ref.11. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.6. Source: UniProtKB nuclear heterochromatin Inferred from direct assay Ref.11. Source: UniProtKB nuclear nucleosome Inferred from direct assay Ref.11. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	methylated histone residue binding Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99549-1)

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: Q99549-2)

The sequence of this isoform differs from the canonical sequence as follows:
     820-860: DSHFVYSFSP...LIGAYRVQLQ → TGSRSVVQAG...GLKMHATTSG

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 860

860

M-phase phosphoprotein 8

PRO_0000080244

Regions

Domain

59 – 118

60

Chromo

Repeat

600 – 629

30

ANK 1

Repeat

633 – 662

30

ANK 2

Repeat

666 – 695

30

ANK 3

Repeat

699 – 728

30

ANK 4

Region

80 – 87

8

Histone H3K9me3 binding

Compositional bias

151 – 256

106

Lys-rich

Sites

Site

59

1

Interaction with histone H3K9me3

Amino acid modifications

Modified residue

51

1

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.12 Ref.13

Modified residue

85

1

Phosphoserine By similarity

Modified residue

136

1

Phosphoserine Ref.8 Ref.10 Ref.12 Ref.13

Modified residue

138

1

Phosphoserine Ref.8 Ref.10 Ref.12 Ref.13

Modified residue

149

1

Phosphoserine Ref.8 Ref.10

Modified residue

188

1

Phosphoserine Ref.10

Modified residue

189

1

Phosphoserine Ref.8 Ref.10

Modified residue

192

1

Phosphoserine Ref.10

Modified residue

272

1

Phosphoserine Potential

Modified residue

319

1

Phosphoserine Ref.7 Ref.13

Modified residue

334

1

Phosphothreonine Potential

Modified residue

385

1

Phosphothreonine Potential

Modified residue

392

1

Phosphoserine Ref.7 Ref.12 Ref.13

Modified residue

400

1

Phosphoserine Ref.12

Modified residue

403

1

Phosphoserine Ref.10 Ref.12 Ref.13

Modified residue

454

1

Phosphothreonine Ref.12

Natural variations

Alternative sequence

820 – 860

41

DSHFV…RVQLQ → TGSRSVVQAGVQWRGLQLTG VLTSQAQAILPPQPPNYLGL KMHATTSG in isoform 2.

VSP_031523

Experimental info

Mutagenesis

80

1

W → A: Abolishes interaction with histone H3K9me3. Ref.11

Sequence conflict

526 – 530

5

DGRQQ → GEFGI in CAA66912. Ref.6

Sequence conflict

860

1

Q → QPNRRDWAEFS in AAH46214. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

860

Helix Strand Turn

Details...

Beta strand

61 – 70

10

Beta strand

73 – 80

8

Helix

85 – 87

3

Beta strand

89 – 92

4

Helix

93 – 96

4

Helix

100 – 114

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 2005. Version 2. Checksum: DD75D14C3DBF5E95	FASTA	860	97,182
	10 20 30 40 50 60 MEQVAEGARV TAVPVSAADS TEELAEVEEG VGVVGEDNDA AARGAEAFGD SEEDGEDVFE 70 80 90 100 110 120 VEKILDMKTE GGKVLYKVRW KGYTSDDDTW EPEIHLEDCK EVLLEFRKKI AENKAKAVRK 130 140 150 160 170 180 DIQRLSLNND IFEANSDSDQ QSETKEDTSP KKKKKKLRQR EEKSPDDLKK KKAKAGKLKD 190 200 210 220 230 240 KSKPDLESSL ESLVFDLRTK KRISEAKEEL KESKKPKKDE VKETKELKKV KKGEIRDLKT 250 260 270 280 290 300 KTREDPKENR KTKKEKFVES QVESESSVLN DSPFPEDDSE GLHSDSREEK QNTKSARERA 310 320 330 340 350 360 GQDMGLEHGF EKPLDSAMSA EEDTDVRGRR KKKTPRKAED TRENRKLENK NAFLEKKTVP 370 380 390 400 410 420 KKQRNQDRSK SAAELEKLMP VSAQTPKGRR LSGEERGLWS TDSAEEDKET KRNESKEKYQ 430 440 450 460 470 480 KRHDSDKEEK GRKEPKGLKT LKEIRNAFDL FKLTPEEKND VSENNRKREE IPLDFKTIDD 490 500 510 520 530 540 HKTKENKQSL KERRNTRDET DTWAYIAAEG DQEVLDSVCQ ADENSDGRQQ ILSLGMDLQL 550 560 570 580 590 600 EWMKLEDFQK HLDGKDENFA ATDAIPSNVL RDAVKNGDYI TVKVALNSNE EYNLDQEDSS 610 620 630 640 650 660 GMTLVMLAAA GGQDDLLRLL ITKGAKVNGR QKNGTTALIH AAEKNFLTTV AILLEAGAFV 670 680 690 700 710 720 NVQQSNGETA LMKACKRGNS DIVRLVIECG ADCNILSKHQ NSALHFAKQS NNVLVYDLLK 730 740 750 760 770 780 NHLETLSRVA EETIKDYFEA RLALLEPVFP IACHRLCEGP DFSTDFNYKP PQNIPEGSGI 790 800 810 820 830 840 LLFIFHANFL GKEVIARLCG PCSVQAVVLN DKFQLPVFLD SHFVYSFSPV AGPNKLFIRL 850 860 TEAPSAKVKL LIGAYRVQLQ
	Isoform 2 [UniParc]. Checksum: 5638702150529EA3	FASTA	867	97,637
	10 20 30 40 50 60 MEQVAEGARV TAVPVSAADS TEELAEVEEG VGVVGEDNDA AARGAEAFGD SEEDGEDVFE 70 80 90 100 110 120 VEKILDMKTE GGKVLYKVRW KGYTSDDDTW EPEIHLEDCK EVLLEFRKKI AENKAKAVRK 130 140 150 160 170 180 DIQRLSLNND IFEANSDSDQ QSETKEDTSP KKKKKKLRQR EEKSPDDLKK KKAKAGKLKD 190 200 210 220 230 240 KSKPDLESSL ESLVFDLRTK KRISEAKEEL KESKKPKKDE VKETKELKKV KKGEIRDLKT 250 260 270 280 290 300 KTREDPKENR KTKKEKFVES QVESESSVLN DSPFPEDDSE GLHSDSREEK QNTKSARERA 310 320 330 340 350 360 GQDMGLEHGF EKPLDSAMSA EEDTDVRGRR KKKTPRKAED TRENRKLENK NAFLEKKTVP 370 380 390 400 410 420 KKQRNQDRSK SAAELEKLMP VSAQTPKGRR LSGEERGLWS TDSAEEDKET KRNESKEKYQ 430 440 450 460 470 480 KRHDSDKEEK GRKEPKGLKT LKEIRNAFDL FKLTPEEKND VSENNRKREE IPLDFKTIDD 490 500 510 520 530 540 HKTKENKQSL KERRNTRDET DTWAYIAAEG DQEVLDSVCQ ADENSDGRQQ ILSLGMDLQL 550 560 570 580 590 600 EWMKLEDFQK HLDGKDENFA ATDAIPSNVL RDAVKNGDYI TVKVALNSNE EYNLDQEDSS 610 620 630 640 650 660 GMTLVMLAAA GGQDDLLRLL ITKGAKVNGR QKNGTTALIH AAEKNFLTTV AILLEAGAFV 670 680 690 700 710 720 NVQQSNGETA LMKACKRGNS DIVRLVIECG ADCNILSKHQ NSALHFAKQS NNVLVYDLLK 730 740 750 760 770 780 NHLETLSRVA EETIKDYFEA RLALLEPVFP IACHRLCEGP DFSTDFNYKP PQNIPEGSGI 790 800 810 820 830 840 LLFIFHANFL GKEVIARLCG PCSVQAVVLN DKFQLPVFLT GSRSVVQAGV QWRGLQLTGV 850 860 LTSQAQAILP PQPPNYLGLK MHATTSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 619-860 (ISOFORM 1). Tissue: Placenta.
[2]	"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: Lymph node.
[3]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: Pancreas and PNS.
[6]	"Identification of novel M phase phosphoproteins by expression cloning." Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M. Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 228-532 (ISOFORMS 1/2), SUBCELLULAR LOCATION, PHOSPHORYLATION. Tissue: Lymphoblast.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-319 AND SER-392, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-138; SER-149 AND SER-189, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-136; SER-138; SER-149; SER-188; SER-189; SER-192 AND SER-403, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion." Kokura K., Sun L., Bedford M.T., Fang J. EMBO J. 29:3673-3687(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HISTONE H3K9ME3; DNMT3A; EHMT1 AND SETDB1, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-80.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-136; SER-138; SER-392; SER-400; SER-403 AND THR-454, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-136; SER-138; SER-319; SER-392 AND SER-403, MASS SPECTROMETRY.
[14]	"Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9: potential effect of phosphorylation on methyl-lysine binding." Chang Y., Horton J.R., Bedford M.T., Zhang X., Cheng X. J. Mol. Biol. 408:807-814(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 55-116 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE, DOMAIN CHROMO, SUBUNIT.
[15]	"MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a." Chang Y., Sun L., Kokura K., Horton J.R., Fukuda M., Espejo A., Izumi V., Koomen J.M., Bedford M.T., Zhang X., Shinkai Y., Fang J., Cheng X. Nat. Commun. 2:533-533(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 55-116 IN COMPLEX WITH DNMT3A.
[16]	"Structural basis for specific binding of human MPP8 chromodomain to histone H3 methylated at lysine 9." Li J., Li Z., Ruan J., Xu C., Tong Y., Pan P.W., Tempel W., Crombet L., Min J., Zang J. PLoS ONE 6:E25104-E25104(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 55-116 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE, DOMAIN CHROMO, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK056785 mRNA. Translation: BAB71284.1. Different initiation.
AK300258 mRNA. Translation: BAH13245.1.
AL832864 mRNA. Translation: CAI46172.1. Frameshift.
AL359457, AL354808 Genomic DNA. Translation: CAI16671.1.
AL354808, AL359457 Genomic DNA. Translation: CAI41002.1.
CH471075 Genomic DNA. Translation: EAX08228.1.
CH471075 Genomic DNA. Translation: EAX08230.1.
BC003542 mRNA. Translation: AAH03542.2.
BC046214 mRNA. Translation: AAH46214.1. Different initiation.
X98259 mRNA. Translation: CAA66912.1.

IPI

IPI00030408.
IPI00885104.

RefSeq

NP_059990.2. NM_017520.3.

UniGene

Hs.741282.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LWE	X-ray	2.05	A/B	55-116	[»]
3QO2	X-ray	2.49	A/B/C/D	55-116	[»]
3R93	X-ray	2.06	A/B/C/D	55-116	[»]
3SVM	X-ray	2.31	A	55-116	[»]

ProteinModelPortal

Q99549.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99549. 2 interactions.

MINT

MINT-6943098.

STRING

9606.ENSP00000355388.

PTM databases

PhosphoSite

Q99549.

Polymorphism databases

DMDM

93204602.

Proteomic databases

PaxDb

Q99549.

PeptideAtlas

Q99549.

PRIDE

Q99549.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361479; ENSP00000355388; ENSG00000196199.
ENST00000414242; ENSP00000414663; ENSG00000196199.

GeneID

54737.

KEGG

hsa:54737.

UCSC

uc001umg.3. human.
uc001umh.3. human.

Organism-specific databases

CTD

54737.

GeneCards

GC13P020208.

H-InvDB

HIX0171874.

HGNC

HGNC:29810. MPHOSPH8.

HPA

HPA039701.
HPA040035.

MIM

611626. gene.

neXtProt

NX_Q99549.

PharmGKB

PA162396090.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOGENOM

HOG000290641.

HOVERGEN

HBG052503.

InParanoid

Q99549.

OMA

REEKSPD.

OrthoDB

EOG44J2J7.

Gene expression databases

ArrayExpress

Q99549.

Bgee

Q99549.

CleanEx

HS_MPHOSPH8.

Genevestigator

Q99549.

GermOnline

ENSG00000196199. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]

Pfam

PF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00385. Chromo. 1 hit.
[Graphical view]

SMART

SM00248. ANK. 4 hits.
SM00298. CHROMO. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]

ProtoNet

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Other

ChEMBL

CHEMBL1741210.

ChiTaRS

MPHOSPH8. human.

EvolutionaryTrace

Q99549.

GenomeRNAi

54737.

NextBio

57325.

SOURCE

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Entry information

Entry name

MPP8_HUMAN

Accession

Primary (citable) accession number: Q99549
Secondary accession number(s): B7Z6F9 , Q5JPE5, Q5JTQ0, Q86TK3, Q96MK4, Q9BTP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 2005
Last modified:	May 29, 2013
This is version 103 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.