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Protein

N-acetyltransferase ESCO2

Gene

Esco2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri384 – 40825CCHH-typeAdd
BLAST

GO - Molecular functioni

  • lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • chromosome segregation Source: MGI
  • double-strand break repair Source: MGI
  • hematopoietic progenitor cell differentiation Source: MGI
  • post-translational protein acetylation Source: MGI
  • protein localization to chromatin Source: MGI
  • regulation of DNA replication Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_326853. Establishment of Sister Chromatid Cohesion.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyltransferase ESCO2 (EC:2.3.1.-)
Alternative name(s):
Establishment of cohesion 1 homolog 2
Short name:
ECO1 homolog 2
Gene namesi
Name:Esco2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1919238. Esco2.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • chromocenter Source: MGI
  • Golgi apparatus Source: MGI
  • nuclear pericentric heterochromatin Source: MGI
  • nucleus Source: MGI
  • site of double-strand break Source: MGI
  • XY body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592N-acetyltransferase ESCO2PRO_0000074543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411PhosphoserineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8CIB9.
PRIDEiQ8CIB9.

PTM databases

PhosphoSiteiQ8CIB9.

Expressioni

Gene expression databases

BgeeiQ8CIB9.
GenevisibleiQ8CIB9. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022613.

Structurei

3D structure databases

ProteinModelPortaliQ8CIB9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetyltransferase family. ECO subfamily.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri384 – 40825CCHH-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG301368.
GeneTreeiENSGT00390000008335.
HOGENOMiHOG000294103.
HOVERGENiHBG081482.
InParanoidiQ8CIB9.
KOiK11268.
OMAiFISDEKR.
OrthoDBiEOG7J9VQQ.
PhylomeDBiQ8CIB9.
TreeFamiTF314027.

Family and domain databases

InterProiIPR028005. AcTrfase_ESCO_Znf_dom.
IPR028009. ESCO_Acetyltransf_dom.
[Graphical view]
PfamiPF13880. Acetyltransf_13. 1 hit.
PF13878. zf-C2H2_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CIB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMATCTPRKR KRYTLNADND DSLLTDISSS KLRCAENLFP SPNKKHNYQS
60 70 80 90 100
SVQKEDKSCS HQLHFPSSPL KTTENSRFSF ANHSSLFKPA MSTVSFYSKE
110 120 130 140 150
KYYLNPLERK LIRECRSICL ATESGDKPIP SVTENIQRKP VCTKKNKKKQ
160 170 180 190 200
KSLTAKYQPN YKHIKSKSRN LKNSKPNQVT YKPVVDQENS CFPAKNYPNS
210 220 230 240 250
PPRVLSQKIK PQVTLQGGAA FFVRKRNSLK KLPLEDKPLL LQKNLPEVPE
260 270 280 290 300
GAPEAKQIPK SLLVDEKSSV KVQNARSKNE EKLRKNPSGA VVSSKECNLD
310 320 330 340 350
KHDFPSENSL DENKTISPES VYPIFNVSSV NTKRPEEQSS VGSTACTNFL
360 370 380 390 400
KQTNVPKNIN SRDTNKGGKD QLVIDAGQKH FGTTVCKSCG MIYTASNPED
410 420 430 440 450
EIQHLQHHHR FLEGIKFVGW KRERVVAEFW DGKIVLVLPR DPSYAIKKVE
460 470 480 490 500
DVQELVDLEL GFQQTVPVCP DKTKTFLFID EKRVVGCLIA EPIKQAFRVL
510 520 530 540 550
SEPSASKECS RAWRCSDVPE PAICGISRIW VFRLKRRKRI ARRLVDTVRN
560 570 580 590
CFMFGCFLST NEIAFSDPTP DGKLFATKYC NTPNFLVYNF HN
Length:592
Mass (Da):67,273
Last modified:June 7, 2005 - v3
Checksum:iF1067E8D3D1ED7CF
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 552KE → RK in AAH33303 (PubMed:15489334).Curated
Sequence conflicti494 – 4941K → E in BAB26905 (PubMed:16141072).Curated
Sequence conflicti585 – 5851F → Y in BAB26905 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27216.1.
RefSeqiNP_082315.3. NM_028039.2.
UniGeneiMm.249280.

Genome annotation databases

EnsembliENSMUST00000022613; ENSMUSP00000022613; ENSMUSG00000022034.
GeneIDi71988.
KEGGimmu:71988.
UCSCiuc007ujp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27216.1.
RefSeqiNP_082315.3. NM_028039.2.
UniGeneiMm.249280.

3D structure databases

ProteinModelPortaliQ8CIB9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022613.

PTM databases

PhosphoSiteiQ8CIB9.

Proteomic databases

MaxQBiQ8CIB9.
PRIDEiQ8CIB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022613; ENSMUSP00000022613; ENSMUSG00000022034.
GeneIDi71988.
KEGGimmu:71988.
UCSCiuc007ujp.2. mouse.

Organism-specific databases

CTDi157570.
MGIiMGI:1919238. Esco2.

Phylogenomic databases

eggNOGiNOG301368.
GeneTreeiENSGT00390000008335.
HOGENOMiHOG000294103.
HOVERGENiHBG081482.
InParanoidiQ8CIB9.
KOiK11268.
OMAiFISDEKR.
OrthoDBiEOG7J9VQQ.
PhylomeDBiQ8CIB9.
TreeFamiTF314027.

Enzyme and pathway databases

ReactomeiREACT_326853. Establishment of Sister Chromatid Cohesion.

Miscellaneous databases

NextBioi335142.
PROiQ8CIB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CIB9.
GenevisibleiQ8CIB9. MM.

Family and domain databases

InterProiIPR028005. AcTrfase_ESCO_Znf_dom.
IPR028009. ESCO_Acetyltransf_dom.
[Graphical view]
PfamiPF13880. Acetyltransf_13. 1 hit.
PF13878. zf-C2H2_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiESCO2_MOUSE
AccessioniPrimary (citable) accession number: Q8CIB9
Secondary accession number(s): Q3UMT6
, Q6IQX5, Q8BNG9, Q8BQF8, Q9CRI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 22, 2015
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.