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Q8CIB9 (ESCO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Nucleus By similarity. Chromosome By similarity.

Sequence similarities

Belongs to the acetyltransferase family. ECO subfamily.

Sequence caution

The sequence BAB26905.1 differs from that shown. Reason: Erroneous termination at position 481. Translated as Glu.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentChromosome
Nucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome segregation

Inferred from mutant phenotype PubMed 22101327. Source: MGI

double-strand break repair

Inferred from mutant phenotype PubMed 22614755. Source: MGI

hematopoietic progenitor cell differentiation

Inferred from genetic interaction PubMed 24029230. Source: MGI

post-translational protein acetylation

Inferred from electronic annotation. Source: Ensembl

protein localization to chromatin

Inferred from mutant phenotype PubMed 22101327. Source: MGI

regulation of DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentXY body

Inferred from direct assay PubMed 22699483. Source: MGI

chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

chromocenter

Inferred from direct assay PubMed 22101327. Source: MGI

nuclear centromeric heterochromatin

Inferred from direct assay PubMed 22101327. Source: MGI

site of double-strand break

Inferred from direct assay PubMed 22614755PubMed 22699483. Source: MGI

   Molecular_functionlysine N-acetyltransferase activity

Inferred from mutant phenotype PubMed 22101327. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592N-acetyltransferase ESCO2
PRO_0000074543

Regions

Zinc finger384 – 40825CCHH-type

Amino acid modifications

Modified residue411Phosphoserine By similarity
Modified residue851Phosphoserine By similarity

Experimental info

Sequence conflict54 – 552KE → RK in AAH33303. Ref.2
Sequence conflict4941K → E in BAB26905. Ref.1
Sequence conflict5851F → Y in BAB26905. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8CIB9 [UniParc].

Last modified June 7, 2005. Version 3.
Checksum: F1067E8D3D1ED7CF

FASTA59267,273
        10         20         30         40         50         60 
MMATCTPRKR KRYTLNADND DSLLTDISSS KLRCAENLFP SPNKKHNYQS SVQKEDKSCS 

        70         80         90        100        110        120 
HQLHFPSSPL KTTENSRFSF ANHSSLFKPA MSTVSFYSKE KYYLNPLERK LIRECRSICL 

       130        140        150        160        170        180 
ATESGDKPIP SVTENIQRKP VCTKKNKKKQ KSLTAKYQPN YKHIKSKSRN LKNSKPNQVT 

       190        200        210        220        230        240 
YKPVVDQENS CFPAKNYPNS PPRVLSQKIK PQVTLQGGAA FFVRKRNSLK KLPLEDKPLL 

       250        260        270        280        290        300 
LQKNLPEVPE GAPEAKQIPK SLLVDEKSSV KVQNARSKNE EKLRKNPSGA VVSSKECNLD 

       310        320        330        340        350        360 
KHDFPSENSL DENKTISPES VYPIFNVSSV NTKRPEEQSS VGSTACTNFL KQTNVPKNIN 

       370        380        390        400        410        420 
SRDTNKGGKD QLVIDAGQKH FGTTVCKSCG MIYTASNPED EIQHLQHHHR FLEGIKFVGW 

       430        440        450        460        470        480 
KRERVVAEFW DGKIVLVLPR DPSYAIKKVE DVQELVDLEL GFQQTVPVCP DKTKTFLFID 

       490        500        510        520        530        540 
EKRVVGCLIA EPIKQAFRVL SEPSASKECS RAWRCSDVPE PAICGISRIW VFRLKRRKRI 

       550        560        570        580        590 
ARRLVDTVRN CFMFGCFLST NEIAFSDPTP DGKLFATKYC NTPNFLVYNF HN 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Lung.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Embryo and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010391 mRNA. Translation: BAB26905.1. Sequence problems.
AK050845 mRNA. Translation: BAC34431.1.
AK144685 mRNA. Translation: BAE26012.1.
BC033303 mRNA. Translation: AAH33303.2.
BC071275 mRNA. Translation: AAH71275.1.
CCDSCCDS27216.1.
RefSeqNP_082315.3. NM_028039.2.
UniGeneMm.249280.

3D structure databases

ProteinModelPortalQ8CIB9.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8CIB9.

Proteomic databases

PRIDEQ8CIB9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022613; ENSMUSP00000022613; ENSMUSG00000022034.
GeneID71988.
KEGGmmu:71988.
UCSCuc007ujp.2. mouse.

Organism-specific databases

CTD157570.
MGIMGI:1919238. Esco2.

Phylogenomic databases

eggNOGNOG301368.
GeneTreeENSGT00390000008335.
HOGENOMHOG000294103.
HOVERGENHBG081482.
InParanoidQ8CIB9.
KOK11268.
OMAKIKPQVT.
OrthoDBEOG7J9VQQ.
PhylomeDBQ8CIB9.
TreeFamTF314027.

Gene expression databases

BgeeQ8CIB9.
GenevestigatorQ8CIB9.

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

NextBio335142.
PROQ8CIB9.
SOURCESearch...

Entry information

Entry nameESCO2_MOUSE
AccessionPrimary (citable) accession number: Q8CIB9
Secondary accession number(s): Q3UMT6 expand/collapse secondary AC list , Q6IQX5, Q8BNG9, Q8BQF8, Q9CRI8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot