Q9UBW7 (ZMYM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger MYM-type protein 2

Alternative name(s):
Fused in myeloproliferative disorders protein
Rearranged in atypical myeloproliferative disorder protein
Zinc finger protein 198

Gene names

Name:	ZMYM2
Synonyms:	FIM, RAMP, ZNF198

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	1377 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as a transcription factor.
Subunit structure	May be a component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Ref.12
Subcellular location	Nucleus Potential.
Involvement in disease	A chromosomal aberration involving ZMYM2 may be a cause of stem cell leukemia lymphoma syndrome (SCLL). Translocation t(8;13)(p11;q12) with FGFR1. SCLL usually presents as lymphoblastic lymphoma in association with a myeloproliferative disorder, often accompanied by pronounced peripheral eosinophilia and/or prominent eosinophilic infiltrates in the affected bone marrow.
Sequence similarities	Contains 9 MYM-type zinc fingers.
Sequence caution	The sequence AAB88464.1 differs from that shown. Reason: Frameshift at positions 330, 966, 1009 and 1017. The sequence AAC23591.1 differs from that shown. Reason: Frameshift at position 330. The sequence CAA73875.1 differs from that shown. Reason: Frameshift at positions 388, 403, 406, 409 and 418.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from direct assay PubMed 17027752. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular_function	zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9UBW7-1)

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: Q9UBW7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     165-251: Missing.
     529-549: KYGKLTTCTGCRTQCRFFDMT → VSRNVNGVQGLNIFEHCYYCH
     550-1377: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1377	1377	Zinc finger MYM-type protein 2		PRO_0000191382
Regions
	Zinc finger	352 – 386	35	MYM-type 1
	Zinc finger	398 – 436	39	MYM-type 2
	Zinc finger	445 – 480	36	MYM-type 3
	Zinc finger	491 – 549	59	MYM-type 4
	Zinc finger	559 – 597	39	MYM-type 5
	Zinc finger	605 – 652	48	MYM-type 6
	Zinc finger	660 – 694	35	MYM-type 7
	Zinc finger	701 – 740	40	MYM-type 8
	Zinc finger	747 – 781	35	MYM-type 9
Sites
	Site	913 – 914	2	Breakpoint for translocation to form ZMYM2-FGFR1
Amino acid modifications
	Modified residue	303	1	Phosphoserine Ref.17
	Modified residue	305	1	Phosphoserine Ref.14 Ref.17
	Modified residue	838	1	Phosphoserine Ref.13 Ref.17
	Modified residue	958	1	Phosphoserine Ref.17
	Modified residue	1376	1	Phosphothreonine Ref.13 Ref.14
Natural variations
	Alternative sequence	165 – 251	87	Missing in isoform 2.		VSP_039065
	Alternative sequence	529 – 549	21	KYGKL…FFDMT → VSRNVNGVQGLNIFEHCYYC H in isoform 2.		VSP_039066
	Alternative sequence	550 – 1377	828	Missing in isoform 2.		VSP_039067
Experimental info
	Sequence conflict	102	1	S → P in CAH56193. Ref.4
	Sequence conflict	110	1	K → E in AAH36372. Ref.7
	Sequence conflict	304	1	L → V in CAB66556. Ref.4
	Sequence conflict	330	1	T → S in CAB66556. Ref.4
	Sequence conflict	411 – 412	2	DK → EQ in CAA73875. Ref.1
	Sequence conflict	424	1	R → G in CAB66556. Ref.4
	Sequence conflict	657 – 659	3	NKV → ASL in CAH70133. Ref.5
	Sequence conflict	657 – 659	3	NKV → ASL in CAH71822. Ref.5
	Sequence conflict	736	1	K → G in CAA73875. Ref.1
	Sequence conflict	766 – 767	2	Missing in CAH70133. Ref.5
	Sequence conflict	766 – 767	2	Missing in CAH71822. Ref.5
	Sequence conflict	856	1	T → I in AAH36372. Ref.7
	Sequence conflict	967	1	Missing in AAB88464. Ref.9
	Sequence conflict	1009 – 1010	2	DF → IS in AAB88464. Ref.9
	Sequence conflict	1016	1	Missing in AAB88464. Ref.9
	Sequence conflict	1259	1	C → R in AAH36372. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 2652D4C766492FF9	FASTA	1,377	154,911
	10 20 30 40 50 60 MDTSSVGGLE LTDQTPVLLG STAMATSLTN VGNSFSGPAN PLVSRSNKFQ NSSVEDDDDV 70 80 90 100 110 120 VFIEPVQPPP PSVPVVADQR TITFTSSKNE ELQGNDSKIT PSSKELASQK GSVSETIVID 130 140 150 160 170 180 DEEDMETNQG QEKNSSNFIE RRPPETKNRT NDVDFSTSSF SRSKVNAGMG NSGITTEPDS 190 200 210 220 230 240 EIQIANVTTL ETGVSSVNDG QLENTDGRDM NLMITHVTSL QNTNLGDVSN GLQSSNFGVN 250 260 270 280 290 300 IQTYTPSLTS QTKTGVGPFN PGRMNVAGDV FQNGESATHH NPDSWISQSA SFPRNQKQPG 310 320 330 340 350 360 VDSLSPVASL PKQIFQPSVQ QQPTKPVKVT CANCKKPLQK GQTAYQRKGS AHLFCSTTCL 370 380 390 400 410 420 SSFSHKPAPK KLCVMCKKDI TTMKGTIVAQ VDSSESFQEF CSTSCLSLYE DKQNPTKGAL 430 440 450 460 470 480 NKSRCTICGK LTEIRHEVSF KNMTHKLCSD HCFNRYRMAN GLIMNCCEQC GEYLPSKGAG 490 500 510 520 530 540 NNVLVIDGQQ KRFCCQSCVS EYKQVGSHPS FLKEVRDHMQ DSFLMQPEKY GKLTTCTGCR 550 560 570 580 590 600 TQCRFFDMTQ CIGPNGYMEP YCSTACMNSH KTKYAKSQSL GIICHFCKRN SLPQYQATMP 610 620 630 640 650 660 DGKLYNFCNS SCVAKFQALS MQSSPNGQFV APSDIQLKCN YCKNSFCSKP EILEWENKVH 670 680 690 700 710 720 QFCSKTCSDD YKKLHCIVTY CEYCQEEKTL HETVNFSGVK RPFCSEGCKL LYKQDFARRL 730 740 750 760 770 780 GLRCVTCNYC SQLCKKGATK ELDGVVRDFC SEDCCKKFQD WYYKAARCDC CKSQGTLKER 790 800 810 820 830 840 VQWRGEMKHF CDQHCLLRFY CQQNEPNMTT QKGPENLHYD QGCQTSRTKM TGSAPPPSPT 850 860 870 880 890 900 PNKEMKNKAV LCKPLTMTKA TYCKPHMQTK SCQTDDTWRT EYVPVPIPVP VYIPVPMHMY 910 920 930 940 950 960 SQNIPVPTTV PVPVPVPVFL PAPLDSSEKI PAAIEELKSK VSSDALDTEL LTMTDMMSED 970 980 990 1000 1010 1020 EGKTETTNIN SVIIETDIIG SDLLKNSDPE TQSSMPDVPY EPDLDIEIDF PRAAEELDME 1030 1040 1050 1060 1070 1080 NEFLLPPVFG EEYEEQPRPR SKKKGAKRKA VSGYQSHDDS SDNSECSFPF KYTYGVNAWK 1090 1100 1110 1120 1130 1140 HWVKTRQLDE DLLVLDELKS SKSVKLKEDL LSHTTAELNY GLAHFVNEIR RPNGENYAPD 1150 1160 1170 1180 1190 1200 SIYYLCLGIQ EYLCGSNRKD NIFIDPGYQT FEQELNKILR SWQPSILPDG SIFSRVEEDY 1210 1220 1230 1240 1250 1260 LWRIKQLGSH SPVALLNTLF YFNTKYFGLK TVEQHLRLSF GTVFRHWKKN PLTMENKACL 1270 1280 1290 1300 1310 1320 RYQVSSLCGT DNEDKITTGK RKHEDDEPVF EQIENTANPS RCPVKMFECY LSKSPQNLNQ 1330 1340 1350 1360 1370 RMDVFYLQPE CSSSTDSPVW YTSTSLDRNT LENMLVRVLL VKDIYDKDNY ELDEDTD
	Isoform 2 [UniParc]. Checksum: E906383363CB8D65	FASTA	462	50,809
	10 20 30 40 50 60 MDTSSVGGLE LTDQTPVLLG STAMATSLTN VGNSFSGPAN PLVSRSNKFQ NSSVEDDDDV 70 80 90 100 110 120 VFIEPVQPPP PSVPVVADQR TITFTSSKNE ELQGNDSKIT PSSKELASQK GSVSETIVID 130 140 150 160 170 180 DEEDMETNQG QEKNSSNFIE RRPPETKNRT NDVDFSTSSF SRSKTKTGVG PFNPGRMNVA 190 200 210 220 230 240 GDVFQNGESA THHNPDSWIS QSASFPRNQK QPGVDSLSPV ASLPKQIFQP SVQQQPTKPV 250 260 270 280 290 300 KVTCANCKKP LQKGQTAYQR KGSAHLFCST TCLSSFSHKP APKKLCVMCK KDITTMKGTI 310 320 330 340 350 360 VAQVDSSESF QEFCSTSCLS LYEDKQNPTK GALNKSRCTI CGKLTEIRHE VSFKNMTHKL 370 380 390 400 410 420 CSDHCFNRYR MANGLIMNCC EQCGEYLPSK GAGNNVLVID GQQKRFCCQS CVSEYKQVGS 430 440 450 460 HPSFLKEVRD HMQDSFLMQP EVSRNVNGVQ GLNIFEHCYY CH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fibroblast growth factor receptor 1 is fused to FIM in stem-cell myeloproliferative disorder with t(8;13)(p12;q12)." Popovici C., Adelaide J., Ollendorff V., Chaffanet M., Guasch G., Jacrot M., Leroux D., Birnbaum D., Pebusque M.-J. Proc. Natl. Acad. Sci. U.S.A. 95:5712-5717(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Consistent fusion of ZNF198 to the fibroblast growth factor receptor-1 in the t(8;13)(p11;q12) myeloproliferative syndrome." Reiter A., Sohal J., Kulkarni S., Chase A., Macdonald D.H.C., Aguiar R.C.T., Goncalves C., Hernandez J.M., Jennings B.A., Goldman J.M., Cross N.C.P. Blood 92:1735-1742(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"The genomic structure of ZNF198 and location of breakpoints in the t(8;13) myeloproliferative syndrome." Kulkarni S., Reiter A.J., Smedley D., Goldman J.M., Cross N.C.P. Genomics 55:118-121(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[5]	"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 1). Tissue: Endometrial tumor.
[6]	"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].
[7]	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].
[8]	"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: Testis.
[9]	"The t(8;13) atypical myeloproliferative disorder: further analysis of the ZNF198 gene and lack of evidence for multiple genes disrupted on chromosome 13." Still I.H., Cowell J.K. Blood 92:1456-1458(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 152-1377 (ISOFORM 1).
[10]	"The t(8;13)(p11;q11-12) rearrangement associated with an atypical myeloproliferative disorder fuses the fibroblast growth factor receptor 1 gene to a novel gene RAMP." Smedley D., Hamoudi R., Clark J., Warren W., Abdul-Rauf M., Somers G., Venter D., Fagan K., Cooper C., Shipley J. Hum. Mol. Genet. 7:637-642(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 170-1020 (ISOFORM 1).
[11]	"FGFR1 is fused with a novel zinc-finger gene, ZNF198, in the t(8;13) leukaemia/lymphoma syndrome." Xiao S., Nalabolu S.R., Aster J.C., Ma J., Abruzzo L., Jaffe E.S., Stone R., Weissman S.M., Hudson T.J., Fletcher J.A. Nat. Genet. 18:84-87(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 621-1377 (ISOFORM 1).
[12]	"A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes." Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R. J. Biol. Chem. 278:7234-7239(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A; RCOR1; PHF21A; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[13]	"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-838 AND THR-1376, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-305 AND THR-1376, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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.
[16]	"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].
[17]	"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-303; SER-305; SER-838 AND SER-958, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y13472 mRNA. Translation: CAA73875.1. Frameshift. AJ224901 mRNA. Translation: CAA12204.1. AJ007676 , AJ007677, AJ007678, AJ007679, AJ007680, AJ007681, AJ007682, AJ007683, AJ007684, AJ007685, AJ007686, AJ007687, AJ007688, AJ007689, AJ007690, AJ007691, AJ007692, AJ007693, AJ007694, AJ007695, AJ007696 Genomic DNA. Translation: CAA07604.1. AL136621 mRNA. Translation: CAB66556.2. BX647944 mRNA. Translation: CAH56193.1. AL137119, AL138688 Genomic DNA. Translation: CAH70133.1. AL137119 Genomic DNA. Translation: CAH70134.1. AL138688, AL137119 Genomic DNA. Translation: CAH71822.1. CH471075 Genomic DNA. Translation: EAX08244.1. CH471075 Genomic DNA. Translation: EAX08247.1. BC036372 mRNA. Translation: AAH36372.1. AF060181 mRNA. Translation: AAC23591.1. Frameshift. AF035374 mRNA. Translation: AAB88464.1. Frameshift. AF012126 mRNA. Translation: AAC01561.1.
IPI	IPI00294603. IPI00646199.
PIR	T45119.
RefSeq	NP_001177893.1. NM_001190964.1. NP_001177894.1. NM_001190965.1. NP_003444.1. NM_003453.3. NP_932072.1. NM_197968.2.
UniGene	Hs.507433.
3D structure databases
ProteinModelPortal	Q9UBW7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBW7. 9 interactions.
MINT	MINT-267007.
PTM databases
PhosphoSite	Q9UBW7.
Polymorphism databases
DMDM	17369677.
Proteomic databases
PaxDb	Q9UBW7.
PRIDE	Q9UBW7.
Protocols and materials databases
DNASU	7750.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000382869; ENSP00000372322; ENSG00000121741. ENST00000382871; ENSP00000372324; ENSG00000121741. ENST00000382874; ENSP00000372327; ENSG00000121741. ENST00000382881; ENSP00000372334; ENSG00000121741. ENST00000456228; ENSP00000413744; ENSG00000121741.
GeneID	7750.
KEGG	hsa:7750.
UCSC	uc001umq.3. human. uc001umr.3. human.
Organism-specific databases
CTD	7750.
GeneCards	GC13P020532.
HGNC	HGNC:12989. ZMYM2.
HPA	HPA031765.
MIM	602221. gene.
neXtProt	NX_Q9UBW7.
PharmGKB	PA37569.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG86062.
HOVERGEN	HBG058385.
InParanoid	Q9UBW7.
OMA	PEVLEWE.
Enzyme and pathway databases
Reactome	REACT_116125. Disease.
Gene expression databases
ArrayExpress	Q9UBW7.
Bgee	Q9UBW7.
Genevestigator	Q9UBW7.
GermOnline	ENSG00000121741. Homo sapiens.
Family and domain databases
InterPro	IPR021893. DUF3504. IPR011017. TRASH_dom. IPR010507. Znf_MYM. [Graphical view]
Pfam	PF12012. DUF3504. 1 hit. PF06467. zf-FCS. 9 hits. [Graphical view]
SMART	SM00746. TRASH. 9 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ZMYM2. human.
GenomeRNAi	7750.
NextBio	29992.
SOURCE	Search...

Entry information

Entry name

ZMYM2_HUMAN

Accession

Primary (citable) accession number: Q9UBW7
Secondary accession number(s): A6NDG0 , A6NI02, O43212, O43434, O60898, Q5W0Q4, Q5W0T3, Q63HP0, Q8NE39, Q9H0V5, Q9H538, Q9UEU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 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.