Q56NI9 (ESCO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetyltransferase ESCO2
EC=2.3.1.-

Alternative name(s):
Establishment of cohesion 1 homolog 2
Short name=ECO1 homolog 2

Gene names

Name:

ESCO2

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

General annotation (Comments)

Function	Acetyltransferase required for the establishment of sister chromatid cohesion. Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during the S phase. Acetylates the cohesin component SMC3. Ref.1 Ref.7 Ref.8
Subcellular location	Nucleus. Chromosome Ref.7.
Tissue specificity	Widely expressed in fetal tissues. In adult, it is expressed in thymus, placenta and small intestine. Ref.1
Involvement in disease	Roberts syndrome (RBS) [MIM:268300]: Rare autosomal recessive disorder characterized by pre- and postnatal growth retardation, microcephaly, bilateral cleft lip and palate, and mesomelic symmetric limb reduction. Severely affected infants may be stillborn or die shortly after birth. RBS chromosomes have a lack of cohesion involving the heterochromatic C-banding regions around centromeres and the distal portion of the long arm of the Y chromosome (known as premature centromere separation, heterochromatin repulsion or puffing, or RS effect). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 SC phocomelia syndrome (SCPS) [MIM:269000]: Has a milder phenotype than RBS, with a lesser degree of symmetric limb reduction and additionally includes flexion contractures of various joints, midfacial hemangioma, hypoplastic cartilage of ears and nose, scant silvery-blond hair, and cloudy corneae. Although microcephaly is present, mental retardation may be mild and survival into adulthood is common. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3
Sequence similarities	Belongs to the acetyltransferase family. GCN5 subfamily.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Chromosome Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW post-translational protein acetylation Inferred from mutant phenotype Ref.8. Source: UniProtKB regulation of DNA replication Inferred from mutant phenotype Ref.7. Source: UniProtKB
Cellular_component	chromatin Inferred from direct assay Ref.7. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity, transferring acyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 601	601	N-acetyltransferase ESCO2		PRO_0000074542
Regions
	Zinc finger	387 – 411	25	CCHH-type
Amino acid modifications
	Modified residue	29	1	Phosphoserine Ref.4
	Modified residue	75	1	Phosphoserine Ref.6 Ref.9
	Modified residue	244	1	Phosphoserine Ref.6 Ref.9
Natural variations
	Natural variant	80	1	A → V. Corresponds to variant rs4732748 [ dbSNP | Ensembl ].		VAR_033840
	Natural variant	359	1	Q → P. Corresponds to variant rs57479434 [ dbSNP | Ensembl ].		VAR_060994
	Natural variant	539	1	W → G in RBS. Ref.1		VAR_022649

Sequences

	Sequence		Length	Mass (Da)
	Q56NI9 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: A3D10BFD486572AE	FASTA	601	68,307
	10 20 30 40 50 60 MAALTPRKRK QDSLKCDSLL HFTENLFPSP NKKHCFYQNS DKNEENLHCS QQEHFVLSAL 70 80 90 100 110 120 KTTEINRLPS ANQGSPFKSA LSTVSFYNQN KWYLNPLERK LIKESRSTCL KTNDEDKSFP 130 140 150 160 170 180 IVTEKMQGKP VCSKKNNKKP QKSLTAKYQP KYRHIKPVSR NSRNSKQNRV IYKPIVEKEN 190 200 210 220 230 240 NCHSAENNSN APRVLSQKIK PQVTLQGGAA FFVRKKSSLR KSSLENEPSL GRTQKSKSEV 250 260 270 280 290 300 IEDSDVETVS EKKTFATRQV PKCLVLEEKL KIGLLSASSK NKEKLIKDSS DDRVSSKEHK 310 320 330 340 350 360 VDKNEAFSSE DSLGENKTIS PKSTVYPIFS ASSVNSKRSL GEEQFSVGSV NFMKQTNIQK 370 380 390 400 410 420 NTNTRDTSKK TKDQLIIDAG QKHFGATVCK SCGMIYTASN PEDEMQHVQH HHRFLEGIKY 430 440 450 460 470 480 VGWKKERVVA EFWDGKIVLV LPHDPSFAIK KVEDVQELVD NELGFQQVVP KCPNKIKTFL 490 500 510 520 530 540 FISDEKRVVG CLIAEPIKQA FRVLSEPIGP ESPSSTECPR AWQCSDVPEP AVCGISRIWV 550 560 570 580 590 600 FRLKRRKRIA RRLVDTLRNC FMFGCFLSTD EIAFSDPTPD GKLFATKYCN TPNFLVYNFN S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Roberts syndrome is caused by mutations in ESCO2, a human homolog of yeast ECO1 that is essential for the establishment of sister chromatid cohesion." Vega H., Waisfisz Q., Gordillo M., Sakai N., Yanagihara I., Yamada M., van Gosliga D., Kayserili H., Xu C., Ozono K., Wang Jabs E., Inui K., Joenje H. Nat. Genet. 37:468-470(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT RBS GLY-539.
[2]	"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]. Tissue: Thymus.
[3]	"Inactivating mutations in ESCO2 cause SC phocomelia and Roberts syndrome: no phenotype-genotype correlation." Schuele B., Oviedo A., Johnston K., Pai S., Francke U. Am. J. Hum. Genet. 77:1117-1128(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SCPS.
[4]	"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-29, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"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-75 AND SER-244, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Cohesin acetylation speeds the replication fork." Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V. Nature 462:231-234(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"Sororin mediates sister chromatid cohesion by antagonizing wapl." Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A., Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M. Cell 143:737-749(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"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-75 AND SER-244, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY882862 mRNA. Translation: AAX68677.1. AK124215 mRNA. Translation: BAG54021.1.
IPI	IPI00087498.
RefSeq	NP_001017420.1. NM_001017420.2.
UniGene	Hs.99480.
3D structure databases
ProteinModelPortal	Q56NI9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q56NI9. 1 interaction.
STRING	9606.ENSP00000306999.
PTM databases
PhosphoSite	Q56NI9.
Polymorphism databases
DMDM	67460434.
Proteomic databases
PaxDb	Q56NI9.
PRIDE	Q56NI9.
Protocols and materials databases
DNASU	157570.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000305188; ENSP00000306999; ENSG00000171320.
GeneID	157570.
KEGG	hsa:157570.
UCSC	uc003xgg.3. human.
Organism-specific databases
CTD	157570.
GeneCards	GC08P027632.
H-InvDB	HIX0168881.
HGNC	HGNC:27230. ESCO2.
MIM	268300. phenotype. 269000. phenotype. 609353. gene.
neXtProt	NX_Q56NI9.
Orphanet	3103. Roberts syndrome.
PharmGKB	PA134891970.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG301368.
HOGENOM	HOG000294103.
HOVERGEN	HBG081482.
InParanoid	Q56NI9.
KO	K11268.
OMA	KIKPQVT.
OrthoDB	EOG4HQDJ3.
PhylomeDB	Q56NI9.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle.
Gene expression databases
ArrayExpress	Q56NI9.
Bgee	Q56NI9.
CleanEx	HS_ESCO2.
Genevestigator	Q56NI9.
GermOnline	ENSG00000171320. Homo sapiens.
Family and domain databases
InterPro	IPR026656. AcTrfase_ESCO. [Graphical view]
PANTHER	PTHR11076:SF1. PTHR11076:SF1. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	157570.
NextBio	87487.
SOURCE	Search...

Entry information

Entry name

ESCO2_HUMAN

Accession

Primary (citable) accession number: Q56NI9
Secondary accession number(s): B3KW59

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 75 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.