Q15326 (ZMY11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger MYND domain-containing protein 11

Alternative name(s):
Adenovirus 5 E1A-binding protein
Protein BS69

Gene names

Name:	ZMYND11
Synonyms:	BS69

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

General annotation (Comments)

Function	Corepressor of transcription Probable. May be involved in chromatin remodeling through association with several remodeling factors. Ref.2 Ref.6
Subunit structure	Interacts (via MYND-type zinc finger) with NCOR1. Interacts (via MYND-type zinc finger) with human adenovirus early E1A protein (via PXLXP motif); this interaction inhibits E1A mediated transactivation. Interacts (via MYND-type zinc finger) with Epstein-Barr virus EBNA2 protein (via PXLXP motif). Interacts (via MYND-type zinc finger) with EZH2. Interacts with E2F6. Ref.2 Ref.6 Ref.7
Subcellular location	Nucleus. Chromosome. Note: Associates with chromatin and mitotic chromosomes. Ref.2
Tissue specificity	Ubiquitous. Ref.2
Post-translational modification	Ubiquitinated, leading to proteasomal degradation. Ref.2
Sequence similarities	Contains 1 bromo domain. Contains 1 MYND-type zinc finger. Contains 1 PHD-type zinc finger. Contains 1 PWWP domain.
Sequence caution	The sequence BAG35465.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA60052.1 differs from that shown. Reason: Frameshift at positions 11 and 39.

Ontologies

Keywords
Biological process	Cell cycle Host-virus interaction Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement Ref.1. Source: ProtInc chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 20732415. Source: UniProtKB negative regulation of JNK cascade Inferred from mutant phenotype PubMed 20732415. Source: UniProtKB negative regulation of extrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 20732415. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LTBR	P36941	5	EBI-2799565,EBI-3509981

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15326-1)

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: Q15326-2)

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.

Isoform 3 (identifier: Q15326-3)

The sequence of this isoform differs from the canonical sequence as follows:
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

Isoform 4 (identifier: Q15326-4)

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

Isoform 5 (identifier: Q15326-5)

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
     173-203: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 602	602	Zinc finger MYND domain-containing protein 11		PRO_0000211218
Regions
	Domain	168 – 238	71	Bromo
	Domain	280 – 331	52	PWWP
	Zinc finger	100 – 148	49	PHD-type
	Zinc finger	563 – 598	36	MYND-type
	Region	452 – 572	121	Interaction with human adenovirus E1A
	Motif	394 – 400	7	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	421	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	93 – 146	54	Missing in isoform 2, isoform 4 and isoform 5.		VSP_044482
	Alternative sequence	173 – 203	31	Missing in isoform 5.		VSP_046246
	Alternative sequence	563 – 602	40	CYNCE…CRRKR → VNTSLF in isoform 3 and isoform 4.		VSP_044483
Experimental info
	Mutagenesis	563	1	C → S: Abrogates binding to EZH2. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2012. Version 2. Checksum: 3AD525B90574BDE8	FASTA	602	70,963
	10 20 30 40 50 60 MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV 70 80 90 100 110 120 KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD WYCFECHLPG EVLICDLCFR 130 140 150 160 170 180 VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG 190 200 210 220 230 240 KDNKHPMYRR LVHSAVDVPT IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI 250 260 270 280 290 300 ARMLYKDTCH ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ 310 320 330 340 350 360 KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL ELHQRFLREG 370 380 390 400 410 420 RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR NQSVEPKKEE PEPETEAVSS 430 440 450 460 470 480 SQEIPTMPQP IEKVSVSTQT KKLSASSPRM LHRSTQTTND GVCQSMCHDK YTKIFNDFKD 490 500 510 520 530 540 RMKSDHKRET ERVVREALEK LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV 550 560 570 580 590 600 EEIKKLATQH KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR KR
	Isoform 2 [UniParc]. Checksum: 5EDF3D170E2EDD11	FASTA	548	64,426
	10 20 30 40 50 60 MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV 70 80 90 100 110 120 KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EISIKKKNTN KQEMGTYLRF IVSRMKERAI 130 140 150 160 170 180 DLNKKGKDNK HPMYRRLVHS AVDVPTIQEK VNEGKYRSYE EFKADAQLLL HNTVIFYGAD 190 200 210 220 230 240 SEQADIARML YKDTCHELDE LQLCKNCFYL SNARPDNWFC YPCIPNHELV WAKMKGFGFW 250 260 270 280 290 300 PAKVMQKEDN QVDVRFFGHH HQRAWIPSEN IQDITVNIHR LHVKRSMGWK KACDELELHQ 310 320 330 340 350 360 RFLREGRFWK SKNEDRGEEE AESSISSTSN EQLKVTQEPR AKKGRRNQSV EPKKEEPEPE 370 380 390 400 410 420 TEAVSSSQEI PTMPQPIEKV SVSTQTKKLS ASSPRMLHRS TQTTNDGVCQ SMCHDKYTKI 430 440 450 460 470 480 FNDFKDRMKS DHKRETERVV REALEKLRSE MEEEKRQAVN KAVANMQGEM DRKCKQVKEK 490 500 510 520 530 540 CKEEFVEEIK KLATQHKQLI SQTKKKQWCY NCEEEAMYHC CWNTSYCSIK CQQEHWHAEH KRTCRRKR
	Isoform 3 [UniParc]. Checksum: 597E186F867E225B	FASTA	568	66,590
	10 20 30 40 50 60 MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV 70 80 90 100 110 120 KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD WYCFECHLPG EVLICDLCFR 130 140 150 160 170 180 VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG 190 200 210 220 230 240 KDNKHPMYRR LVHSAVDVPT IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI 250 260 270 280 290 300 ARMLYKDTCH ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ 310 320 330 340 350 360 KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL ELHQRFLREG 370 380 390 400 410 420 RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR NQSVEPKKEE PEPETEAVSS 430 440 450 460 470 480 SQEIPTMPQP IEKVSVSTQT KKLSASSPRM LHRSTQTTND GVCQSMCHDK YTKIFNDFKD 490 500 510 520 530 540 RMKSDHKRET ERVVREALEK LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV 550 560 EEIKKLATQH KQLISQTKKK QWVNTSLF
	Isoform 4 [UniParc]. Checksum: C20F5B606BAB0E2E	FASTA	514	60,053
	10 20 30 40 50 60 MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV 70 80 90 100 110 120 KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EISIKKKNTN KQEMGTYLRF IVSRMKERAI 130 140 150 160 170 180 DLNKKGKDNK HPMYRRLVHS AVDVPTIQEK VNEGKYRSYE EFKADAQLLL HNTVIFYGAD 190 200 210 220 230 240 SEQADIARML YKDTCHELDE LQLCKNCFYL SNARPDNWFC YPCIPNHELV WAKMKGFGFW 250 260 270 280 290 300 PAKVMQKEDN QVDVRFFGHH HQRAWIPSEN IQDITVNIHR LHVKRSMGWK KACDELELHQ 310 320 330 340 350 360 RFLREGRFWK SKNEDRGEEE AESSISSTSN EQLKVTQEPR AKKGRRNQSV EPKKEEPEPE 370 380 390 400 410 420 TEAVSSSQEI PTMPQPIEKV SVSTQTKKLS ASSPRMLHRS TQTTNDGVCQ SMCHDKYTKI 430 440 450 460 470 480 FNDFKDRMKS DHKRETERVV REALEKLRSE MEEEKRQAVN KAVANMQGEM DRKCKQVKEK 490 500 510 CKEEFVEEIK KLATQHKQLI SQTKKKQWVN TSLF
	Isoform 5 [UniParc]. Checksum: E8EA00DD12FA4FF8	FASTA	517	60,869
	10 20 30 40 50 60 MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV 70 80 90 100 110 120 KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EISIKKKNTN KQEMGTYLRF IVSRMKERKV 130 140 150 160 170 180 NEGKYRSYEE FKADAQLLLH NTVIFYGADS EQADIARMLY KDTCHELDEL QLCKNCFYLS 190 200 210 220 230 240 NARPDNWFCY PCIPNHELVW AKMKGFGFWP AKVMQKEDNQ VDVRFFGHHH QRAWIPSENI 250 260 270 280 290 300 QDITVNIHRL HVKRSMGWKK ACDELELHQR FLREGRFWKS KNEDRGEEEA ESSISSTSNE 310 320 330 340 350 360 QLKVTQEPRA KKGRRNQSVE PKKEEPEPET EAVSSSQEIP TMPQPIEKVS VSTQTKKLSA 370 380 390 400 410 420 SSPRMLHRST QTTNDGVCQS MCHDKYTKIF NDFKDRMKSD HKRETERVVR EALEKLRSEM 430 440 450 460 470 480 EEEKRQAVNK AVANMQGEMD RKCKQVKEKC KEEFVEEIKK LATQHKQLIS QTKKKQWCYN 490 500 510 CEEEAMYHCC WNTSYCSIKC QQEHWHAEHK RTCRRKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"BS69, a novel adenovirus E1A-associated protein that inhibits E1A transactivation." Hateboer G., Gennissen A., Ramos Y.F.M., Kerkhoven R.M., Sonntag-Buck V., Stunnenberg H.G., Bernards R. EMBO J. 14:3159-3169(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon carcinoma.
[2]	"New insights into BS69 functions." Velasco G., Grkovic S., Ansieau S. J. Biol. Chem. 281:16546-16550(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, UBIQUITINATION, INTERACTION WITH E2F6 AND EZH2, MUTAGENESIS OF CYS-563.
[3]	"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 5). Tissue: Amygdala and Brain.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton 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].
[6]	"The adenovirus E1A binding protein BS69 is a corepressor of transcription through recruitment of N-CoR." Masselink H., Bernards R. Oncogene 19:1538-1546(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NCOR1.
[7]	"The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif." Ansieau S., Leutz A. J. Biol. Chem. 277:4906-4910(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2 PROTEIN.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[9]	"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-421, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X86098 mRNA. Translation: CAA60052.1. Frameshift. DQ335452 mRNA. Translation: ABC72408.1. DQ335453 mRNA. Translation: ABC72409.1. DQ335454 mRNA. Translation: ABC72410.1. DQ335455 mRNA. Translation: ABC72411.1. AK294469 mRNA. Translation: BAH11779.1. AK312570 mRNA. Translation: BAG35465.1. Different initiation. AL589988, AL603831 Genomic DNA. Translation: CAH69845.1. AL603831, AL589988 Genomic DNA. Translation: CAI40899.1. AL713922 Genomic DNA. No translation available. AL731539 Genomic DNA. No translation available. CH471072 Genomic DNA. Translation: EAW86540.1. CH471072 Genomic DNA. Translation: EAW86541.1.
IPI	IPI00480004. IPI00556262. IPI00873394. IPI00878480. IPI00930718. IPI00967676.
PIR	S56145.
RefSeq	NP_001189393.1. NM_001202464.1. NP_001189394.1. NM_001202465.1. NP_001189396.1. NM_001202467.1. NP_001189397.1. NM_001202468.1. NP_006615.2. NM_006624.5.
UniGene	Hs.292265. Hs.740145.
3D structure databases
ProteinModelPortal	Q15326.
SMR	Q15326. Positions 98-239, 279-352, 560-600.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15326. 7 interactions.
MINT	MINT-156360.
STRING	9606.ENSP00000309992.
PTM databases
PhosphoSite	Q15326.
Polymorphism databases
DMDM	10719919.
Proteomic databases
PaxDb	Q15326.
PRIDE	Q15326.
Protocols and materials databases
DNASU	10771.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000309776; ENSP00000309992; ENSG00000015171. ENST00000381591; ENSP00000371003; ENSG00000015171. ENST00000381604; ENSP00000371017; ENSG00000015171. ENST00000397959; ENSP00000381050; ENSG00000015171. ENST00000397962; ENSP00000381053; ENSG00000015171. ENST00000565311; ENSP00000457248; ENSG00000260150.
GeneID	10771.
KEGG	hsa:10771.
UCSC	uc001ifk.3. human. uc001ifm.3. human. uc001ifn.3. human. uc009xhg.3. human. uc010pzw.2. human.
Organism-specific databases
CTD	10771.
GeneCards	GC10P000170.
H-InvDB	HIX0025946.
HGNC	HGNC:16966. ZMYND11.
HPA	HPA015816. HPA030553.
MIM	608668. gene.
neXtProt	NX_Q15326.
PharmGKB	PA128394578.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG265768.
HOGENOM	HOG000038026.
HOVERGEN	HBG054949.
InParanoid	Q15326.
OMA	TSDGVCQ.
Gene expression databases
ArrayExpress	Q15326.
Bgee	Q15326.
CleanEx	HS_ZMYND11.
Genevestigator	Q15326.
GermOnline	ENSG00000015171. Homo sapiens.
Family and domain databases
Gene3D	1.20.920.10. 1 hit. 3.30.40.10. 1 hit.
InterPro	IPR001487. Bromodomain. IPR000313. PWWP. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR002893. Znf_MYND. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF00439. Bromodomain. 1 hit. PF00855. PWWP. 1 hit. [Graphical view]
SMART	SM00297. BROMO. 1 hit. SM00249. PHD. 1 hit. SM00293. PWWP. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 1 hit. SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS50014. BROMODOMAIN_2. 1 hit. PS50812. PWWP. 1 hit. PS01360. ZF_MYND_1. 1 hit. PS50865. ZF_MYND_2. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ZMYND11. human.
GenomeRNAi	10771.
NextBio	40897.
SOURCE	Search...

Entry information

Entry name

ZMY11_HUMAN

Accession

Primary (citable) accession number: Q15326
Secondary accession number(s): B2R6G8 , B7Z293, Q2LD45, Q2LD46, Q2LD47, Q2LD48, Q5VUI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 28, 2012
Last modified:	May 29, 2013
This is version 120 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.