Q7Z589 (EMSY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein EMSY

Gene names

Name:	EMSY
Synonyms:	C11orf30
ORF Names:	GL002

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin. Its interaction with BRCA2 suggests that it may play a central role in the DNA repair function of BRCA2. Ref.1
Subunit structure	Homodimer. Interacts with the transactivation domain of BRCA2. Interacts with the chromoshadow domain of CBX1 and with ZMYND11. Does not interact with CBX3 or CBX5. Ref.1 Ref.12
Subcellular location	Nucleus. Note: Localizes to DNA damage markers in irradiated cells, suggesting that it participates in DNA repair process. Ref.1
Miscellaneous	Defects in EMSY may be a cause of sporadic breast cancer and higher-grade ovarian cancers. Overexpressed through amplification almost exclusively in sporadic breast cancer (13%) and higher-grade ovarian cancer (17%). Amplification is associated with worse survival, particularly in node-negative breast cancer, suggesting that it may be of prognostic value. Was named EMSY by Ref.1 because the protein sequence contains the word 'SISTER', after the first author's sister, who is a breast cancer nurse.
Sequence similarities	Contains 1 ENT (EMSY N-terminal) domain.
Sequence caution	The sequence AAF86947.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH29375.1 differs from that shown. Reason: Erroneous initiation. The sequence AAL65260.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB14627.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Chromatin regulator Repressor
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification 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	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7Z589-1)

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: Q7Z589-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1091-1257: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q7Z589-3)

The sequence of this isoform differs from the canonical sequence as follows:
     82-82: N → K
     83-1322: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1322

1322

Protein EMSY

PRO_0000086968

Regions

Domain

16 – 100

85

ENT

Region

1 – 478

478

Interaction with BRCA2

Region

104 – 108

5

Interaction with ZMYND11

Compositional bias

209 – 213

5

Poly-Ser

Compositional bias

326 – 391

66

Ser-rich

Compositional bias

395 – 464

70

Gln-rich

Compositional bias

496 – 636

141

Thr-rich

Compositional bias

719 – 723

5

Poly-Ser

Compositional bias

945 – 1099

155

Gln-rich

Amino acid modifications

Modified residue

207

1

Phosphothreonine Ref.10

Modified residue

209

1

Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10

Modified residue

213

1

Phosphoserine Ref.9

Modified residue

238

1

Phosphoserine Ref.6 Ref.9

Modified residue

262

1

Phosphothreonine Ref.7

Modified residue

273

1

Phosphothreonine Ref.7

Modified residue

274

1

Phosphothreonine Ref.7

Modified residue

1130

1

Phosphoserine Ref.8 Ref.9

Modified residue

1136

1

Phosphoserine Ref.6 Ref.8 Ref.9

Glycosylation

228

1

O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence

82

1

N → K in isoform 3.

VSP_020774

Alternative sequence

83 – 1322

1240

Missing in isoform 3.

VSP_020775

Alternative sequence

1091 – 1257

167

Missing in isoform 2.

VSP_010431

Experimental info

Mutagenesis

100 – 102

3

VPL → APA: Abolishes interaction with CBX1. Ref.1

Mutagenesis

106

1

L → A: Abolishes interaction with ZMYND11. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1322

Helix Strand Turn

Details...

Helix

7 – 9

3

Helix

13 – 38

26

Helix

43 – 55

13

Helix

60 – 71

12

Helix

74 – 84

11

Helix

90 – 97

8

Helix

108 – 110

3

Beta strand

112 – 116

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 24, 2004. Version 2. Checksum: 7F8C95E8BA0FC9F0	FASTA	1,322	141,468
	10 20 30 40 50 60 MPVVWPTLLD LSRDECKRIL RKLELEAYAG VISALRAQGD LTKEKKDLLG ELSKVLSIST 70 80 90 100 110 120 ERHRAEVRRA VNDERLTTIA HNMSGPNSSS EWSIEGRRLV PLMPRLVPQT AFTVTANAVA 130 140 150 160 170 180 NAAIQHNASL PVPAETGSKE VVCYSYTSTT STPTSTPVPS GSIATVKSPR PASPASNVVV 190 200 210 220 230 240 LPSGSTVYVK SVSCSDEDEK PRKRRRTNSS SSSPVVLKEV PKAVVPVSKT ITVPVSGSPK 250 260 270 280 290 300 MSNIMQSIAN SLPPHMSPVK ITFTKPSTQT TNTTTQKVII VTTSPSSTFV PNILSKSHNY 310 320 330 340 350 360 AAVTKLVPTS VIASTTQKPP VVITASQSSL VSNSSSGSSS STPSPIPNTV AVTAVVSSTP 370 380 390 400 410 420 SVVMSTVAQG VSTSAIKMAS TRLPSPKSLV SAPTQILAQF PKQHQQSPKQ QLYQVQQQTQ 430 440 450 460 470 480 QQVAQPSPVS HQQQPQQSPL PPGIKPTIQI KQESGVKIIT QQVQPSKILP KPVTATLPTS 490 500 510 520 530 540 SNSPIMVVSS NGAIMTTKLV TTPTGTQATY TRPTVSPSIG RMAATPGAAT YVKTTSGSII 550 560 570 580 590 600 TVVPKSLATL GGKIISSNIV SGTTTKITTI PMTSKPNVIV VQKTTGKGTT IQGLPGKNVV 610 620 630 640 650 660 TTLLNAGGEK TIQTVPTGAK PAILTATRPI TKMIVTQPKG IGSTVQPAAK IIPTKIVYGQ 670 680 690 700 710 720 QGKTQVLIKP KPVTFQATVV SEQTRQLVTE TLQQASRVAE AGNSSIQEGK EEPQNYTDSS 730 740 750 760 770 780 SSSTESSQSS QDSQPVVHVI ASRRQDWSEH EIAMETSPTI IYQDVSSESQ SATSTIKALL 790 800 810 820 830 840 ELQQTTVKEK LESKPRQPTI DLSQMAVPIQ MTQEKRHSPE SPSIAVVESE LVAEYITTER 850 860 870 880 890 900 TDEGTEVAFP LLVSHRSQPQ QPSQPQRTLL QHVAQSQTAT QTSVVVKSIP ASSPGAITHI 910 920 930 940 950 960 MQQALSSHTA FTKHSEELGT EEGEVEEMDT LDPQTGLFYR SALTQSQSAK QQKLSQPPLE 970 980 990 1000 1010 1020 QTQLQVKTLQ CFQTKQKQTI HLQADQLQHK LPQMPQLSIR HQKLTPLQQE QAQPKPDVQH 1030 1040 1050 1060 1070 1080 TQHPMVAKDR QLPTLMAQPP QTVVQVLAVK TTQQLPKLQQ APNQPKIYVQ PQTPQSQMSL 1090 1100 1110 1120 1130 1140 PASSEKQTAS QVEQPIITQG SSVTKITFEG RQPPTVTKIT GGSSVPKLTS PVTSISPIQA 1150 1160 1170 1180 1190 1200 SEKTAVSDIL KMSLMEAQID TNVEHMIVDP PKKALATSML TGEAGSLPST HMVVAGMANS 1210 1220 1230 1240 1250 1260 TPQQQKCRES CSSPSTVGSS LTTRKIDPPA VPATGQFMRI QNVGQKKAEE SPAEIIIQAI 1270 1280 1290 1300 1310 1320 PQYAIPCHSS SNVVVEPSGL LELNNFTSQQ LDDEETAMEQ DIDSSTEDGT EPSPSQSSAE RS
	Isoform 2 [UniParc]. Checksum: BF3921D979C50121	FASTA	1,155	123,915
	10 20 30 40 50 60 MPVVWPTLLD LSRDECKRIL RKLELEAYAG VISALRAQGD LTKEKKDLLG ELSKVLSIST 70 80 90 100 110 120 ERHRAEVRRA VNDERLTTIA HNMSGPNSSS EWSIEGRRLV PLMPRLVPQT AFTVTANAVA 130 140 150 160 170 180 NAAIQHNASL PVPAETGSKE VVCYSYTSTT STPTSTPVPS GSIATVKSPR PASPASNVVV 190 200 210 220 230 240 LPSGSTVYVK SVSCSDEDEK PRKRRRTNSS SSSPVVLKEV PKAVVPVSKT ITVPVSGSPK 250 260 270 280 290 300 MSNIMQSIAN SLPPHMSPVK ITFTKPSTQT TNTTTQKVII VTTSPSSTFV PNILSKSHNY 310 320 330 340 350 360 AAVTKLVPTS VIASTTQKPP VVITASQSSL VSNSSSGSSS STPSPIPNTV AVTAVVSSTP 370 380 390 400 410 420 SVVMSTVAQG VSTSAIKMAS TRLPSPKSLV SAPTQILAQF PKQHQQSPKQ QLYQVQQQTQ 430 440 450 460 470 480 QQVAQPSPVS HQQQPQQSPL PPGIKPTIQI KQESGVKIIT QQVQPSKILP KPVTATLPTS 490 500 510 520 530 540 SNSPIMVVSS NGAIMTTKLV TTPTGTQATY TRPTVSPSIG RMAATPGAAT YVKTTSGSII 550 560 570 580 590 600 TVVPKSLATL GGKIISSNIV SGTTTKITTI PMTSKPNVIV VQKTTGKGTT IQGLPGKNVV 610 620 630 640 650 660 TTLLNAGGEK TIQTVPTGAK PAILTATRPI TKMIVTQPKG IGSTVQPAAK IIPTKIVYGQ 670 680 690 700 710 720 QGKTQVLIKP KPVTFQATVV SEQTRQLVTE TLQQASRVAE AGNSSIQEGK EEPQNYTDSS 730 740 750 760 770 780 SSSTESSQSS QDSQPVVHVI ASRRQDWSEH EIAMETSPTI IYQDVSSESQ SATSTIKALL 790 800 810 820 830 840 ELQQTTVKEK LESKPRQPTI DLSQMAVPIQ MTQEKRHSPE SPSIAVVESE LVAEYITTER 850 860 870 880 890 900 TDEGTEVAFP LLVSHRSQPQ QPSQPQRTLL QHVAQSQTAT QTSVVVKSIP ASSPGAITHI 910 920 930 940 950 960 MQQALSSHTA FTKHSEELGT EEGEVEEMDT LDPQTGLFYR SALTQSQSAK QQKLSQPPLE 970 980 990 1000 1010 1020 QTQLQVKTLQ CFQTKQKQTI HLQADQLQHK LPQMPQLSIR HQKLTPLQQE QAQPKPDVQH 1030 1040 1050 1060 1070 1080 TQHPMVAKDR QLPTLMAQPP QTVVQVLAVK TTQQLPKLQQ APNQPKIYVQ PQTPQSQMSL 1090 1100 1110 1120 1130 1140 PASSEKQTAS QAIPQYAIPC HSSSNVVVEP SGLLELNNFT SQQLDDEETA MEQDIDSSTE 1150 DGTEPSPSQS SAERS
	Isoform 3 [UniParc]. Checksum: 61ECFDD214DF46A5	FASTA	82	9,352
	10 20 30 40 50 60 MPVVWPTLLD LSRDECKRIL RKLELEAYAG VISALRAQGD LTKEKKDLLG ELSKVLSIST 70 80 ERHRAEVRRA VNDERLTTIA HK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer." Hughes-Davies L., Huntsman D., Ruas M., Fuks F., Bye J., Chin S.-F., Milner J., Brown L.A., Hsu F., Gilks B., Nielsen T., Schulzer M., Chia S., Ragaz J., Cahn A., Linger L., Ozdag H., Cattaneo E. , Jordanova E.S., Schuuring E., Yu D.S., Venkitaraman A., Ponder B., Doherty A., Aparicio S., Bentley D., Theillet C., Ponting C.P., Caldas C., Kouzarides T. Cell 115:523-535(2003) [PubMed: 14651845] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN CANCER, INTERACTION WITH BRCA2; CBX1 AND ZMYND11, MUTAGENESIS OF 100-VAL--LEU-102 AND LEU-106.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1082-1322 (ISOFORM 1). Tissue: Testis and Urinary bladder.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 861-1322 (ISOFORM 1). Tissue: Placenta.
[4]	Guo J.H., Zan Q., Yu L. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 861-1322 (ISOFORM 2). Tissue: Brain.
[5]	"A novel gene expressed in human liver non-tumor tissues." Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1115-1322 (ISOFORM 1). Tissue: Liver.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-238 AND SER-1136, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262; THR-273 AND THR-274, 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-1130 AND SER-1136, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-213; SER-238; SER-1130 AND SER-1136, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207 AND SER-209, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Binding of EMSY to HP1beta: implications for recruitment of HP1beta and BS69." Ekblad C.M.S., Chavali G.B., Basu B.P., Freund S.M.V., Veprintsev D., Hughes-Davies L., Kouzarides T., Doherty A.J., Itzhaki L.S. EMBO Rep. 6:675-680(2005) [PubMed: 15947784] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-108.
[12]	"Crystal structure of the ENT domain of human EMSY." Chavali G.B., Ekblad C.M., Basu B.P., Brissett N.C., Veprintsev D., Hughes-Davies L., Kouzarides T., Itzhaki L.S., Doherty A.J. J. Mol. Biol. 350:964-973(2005) [PubMed: 15978617] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 1-100, SUBUNIT.
[13]	"Crystal structure of the HP1-EMSY complex reveals an unusual mode of HP1 binding." Huang Y., Myers M.P., Xu R.-M. Structure 14:703-712(2006) [PubMed: 16615912] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 9-139 IN COMPLEX WITH CBX1.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ430203 mRNA. Translation: CAD22881.1.
BC029375 mRNA. Translation: AAH29375.1. Different initiation.
BC033404 mRNA. Translation: AAH33404.1.
AK023651 mRNA. Translation: BAB14627.1. Different initiation.
AY070433 mRNA. Translation: AAL65260.1. Different initiation.
AF226047 mRNA. Translation: AAF86947.1. Different initiation.

IPI

IPI00413757.
IPI00787382.
IPI00872314.

RefSeq

NP_064578.2. NM_020193.3.

UniGene

Hs.352588.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UTU	X-ray	2.00	A/B	1-108	[»]
1UZ3	X-ray	1.10	A/B	1-100	[»]
2FMM	X-ray	1.80	E	9-139	[»]

ProteinModelPortal

Q7Z589.

SMR

Q7Z589. Positions 9-112.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29099N.

STRING

Q7Z589.

PTM databases

PhosphoSite

Q7Z589.

Polymorphism databases

DMDM

47605660.

Proteomic databases

PRIDE

Q7Z589.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334736; ENSP00000334130; ENSG00000158636.

GeneID

56946.

KEGG

hsa:56946.

UCSC

uc001oxj.2. human.
uc001oxl.1. human.

Organism-specific databases

CTD

56946.

GeneCards

GC11P076156.

H-InvDB

HIX0009960.

HGNC

HGNC:18071. C11orf30.

HPA

CAB012234.

MIM

608574. gene.

neXtProt

NX_Q7Z589.

PharmGKB

PA134904392.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000009554.

HOVERGEN

HBG051476.

PhylomeDB

Q7Z589.

Gene expression databases

ArrayExpress

Q7Z589.

Bgee

Q7Z589.

CleanEx

HS_C11orf30.

Genevestigator

Q7Z589.

GermOnline

ENSG00000158636. Homo sapiens.

Family and domain databases

InterPro

IPR005491. ENT_N.
[Graphical view]

Pfam

PF03735. ENT. 1 hit.
[Graphical view]

PROSITE

PS51138. ENT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

62533.

SOURCE

Search...

Entry information

Entry name

EMSY_HUMAN

Accession

Primary (citable) accession number: Q7Z589
Secondary accession number(s): Q4G109 , Q8NBU6, Q8TE50, Q9H8I9, Q9NRH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	January 25, 2012
This is version 89 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.