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Q56NI9 (ESCO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence 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.8 Ref.9

Subcellular location

Nucleus. Chromosome Ref.8.

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. ECO subfamily.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentChromosome
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitotic cell cycle

Traceable author statement. Source: Reactome

post-translational protein acetylation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

regulation of DNA replication

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

chromatin

Inferred from direct assay Ref.8. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionmetal 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601N-acetyltransferase ESCO2
PRO_0000074542

Regions

Zinc finger387 – 41125CCHH-type

Amino acid modifications

Modified residue291Phosphoserine Ref.4
Modified residue751Phosphoserine Ref.6 Ref.10
Modified residue2441Phosphoserine Ref.6 Ref.10

Natural variations

Natural variant801A → V.
Corresponds to variant rs4732748 [ dbSNP | Ensembl ].
VAR_033840
Natural variant3591Q → P.
Corresponds to variant rs57479434 [ dbSNP | Ensembl ].
VAR_060994
Natural variant5391W → G in RBS. Ref.1
VAR_022649

Sequences

Sequence LengthMass (Da)Tools
Q56NI9 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: A3D10BFD486572AE

FASTA60168,307
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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.
[9]"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.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY882862 mRNA. Translation: AAX68677.1.
AK124215 mRNA. Translation: BAG54021.1.
CCDSCCDS34872.1.
RefSeqNP_001017420.1. NM_001017420.2.
XP_006716360.1. XM_006716297.1.
UniGeneHs.99480.

3D structure databases

ProteinModelPortalQ56NI9.
SMRQ56NI9. Positions 532-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127605. 11 interactions.
IntActQ56NI9. 1 interaction.
STRING9606.ENSP00000306999.

PTM databases

PhosphoSiteQ56NI9.

Polymorphism databases

DMDM67460434.

Proteomic databases

MaxQBQ56NI9.
PaxDbQ56NI9.
PRIDEQ56NI9.

Protocols and materials databases

DNASU157570.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305188; ENSP00000306999; ENSG00000171320.
GeneID157570.
KEGGhsa:157570.
UCSCuc003xgg.3. human.

Organism-specific databases

CTD157570.
GeneCardsGC08P027632.
GeneReviewsESCO2.
H-InvDBHIX0168881.
HGNCHGNC:27230. ESCO2.
HPAHPA053679.
MIM268300. phenotype.
269000. phenotype.
609353. gene.
neXtProtNX_Q56NI9.
Orphanet3103. Roberts syndrome.
PharmGKBPA134891970.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301368.
HOGENOMHOG000294103.
HOVERGENHBG081482.
InParanoidQ56NI9.
KOK11268.
OMAKIKPQVT.
OrthoDBEOG7J9VQQ.
PhylomeDBQ56NI9.
TreeFamTF314027.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ56NI9.
BgeeQ56NI9.
CleanExHS_ESCO2.
GenevestigatorQ56NI9.

Family and domain databases

InterProIPR028005. AcTrfase_ESCO_Znf_dom.
IPR028009. ESCO_Acetyltransf_dom.
[Graphical view]
PfamPF13880. Acetyltransf_13. 1 hit.
PF13878. zf-C2H2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiESCO2.
GenomeRNAi157570.
NextBio87487.
PROQ56NI9.
SOURCESearch...

Entry information

Entry nameESCO2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM