Q5FWF5 (ESCO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetyltransferase ESCO1
EC=2.3.1.-

Alternative name(s):
CTF7 homolog 1
Establishment factor-like protein 1
Short name=EFO1p
Short name=hEFO1
Establishment of cohesion 1 homolog 1
Short name=ECO1 homolog 1
Short name=ESO1 homolog 1

Gene names

Name:	ESCO1
Synonyms:	EFO1, KIAA1911

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

General annotation (Comments)

Function	Acetyltransferase required for the establishment of sister chromatid cohesion and couple 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 S phase. Acts by mediating the acetylation of cohesin component SMC3. Ref.7 Ref.8 Ref.11 Ref.12
Subcellular location	Nucleus. Chromosome. Note: Nuclear at interphase, associated with chromosomes during mitosis. Ref.7 Ref.8 Ref.12
Tissue specificity	Widely expressed. Expressed in heart, brain, liver, placenta, lung, kidney and pancreas. Highly expressed in muscle. Ref.7
Domain	The N-terminal region seems to be responsible for the association with chromosomes, thus excluding any involvement of the Zn finger in this process.
Post-translational modification	Phosphorylated during mitosis. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the acetyltransferase family. GCN5 subfamily.
Caution	It is uncertain whether Met-1 or Met-2 is the initiator.
Sequence caution	The sequence BAB67804.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC03483.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
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. Source: UniProtKB regulation of DNA replication Inferred from mutant phenotype Ref.12. Source: UniProtKB
Cellular component	chromatin Inferred from direct assay Ref.12. 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...

Alternative products

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

Isoform 1 (identifier: Q5FWF5-1)

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: Q5FWF5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     652-701: GWKKERILAE...DLGFQQAPLM → VLLINHHECG...EGLEERKNSG
     702-840: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q5FWF5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-668: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 840	840	N-acetyltransferase ESCO1		PRO_0000074539
Regions
	Zinc finger	617 – 641	25	CCHH-type
Amino acid modifications
	Modified residue	31	1	Phosphoserine Ref.9
	Modified residue	200	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1 – 668	668	Missing in isoform 3.		VSP_014028
	Alternative sequence	652 – 701	50	GWKKE…QAPLM → VLLINHHECGSEEEFITSLF LSMFNFRYTQRSFSFPIRFL EGLEERKNSG in isoform 2.		VSP_014029
	Alternative sequence	702 – 840	139	Missing in isoform 2.		VSP_014030
	Natural variant	191	1	N → S. Corresponds to variant rs35087820 [ dbSNP | Ensembl ].		VAR_048167
	Natural variant	221	1	T → M. Ref.5 Corresponds to variant rs13381941 [ dbSNP | Ensembl ].		VAR_022648
Experimental info
	Mutagenesis	622	1	C → G: No effect on association with chromosomes. Ref.8
	Sequence conflict	384	1	S → L in BAB67804. Ref.1
	Sequence conflict	432	1	P → S in CAH10682. Ref.2
	Sequence conflict	805	1	E → A in BAC03483. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: A36BE0EC1BE3EDF2	FASTA	840	94,983
	10 20 30 40 50 60 MMSIQEKSKE NSSKVTKKSD DKNSETEIQD SQKNLAKKSG PKETIKSQAK SSSESKINQP 70 80 90 100 110 120 ELETRMSTRS SKAASNDKAT KSINKNTVTV RGYSQESTKK KLSQKKLVHE NPKANEQLNR 130 140 150 160 170 180 RSQRLQQLTE VSRRSLRSRE IQGQVQAVKQ SLPPTKKEQC SSTQSKSNKT SQKHVKRKVL 190 200 210 220 230 240 EVKSDSKEDE NLVINEVINS PKGKKRKVEH QTACACSSQC TQGSEKCPQK TTRRDETKPV 250 260 270 280 290 300 PVTSEVKRSK MATSVVPKKN EMKKSVHTQV NTNTTLPKSP QPSVPEQSDN ELEQAGKSKR 310 320 330 340 350 360 GSILQLCEEI AGEIESDNVE VKKESSQMES VKEEKPTEIK LEETSVERQI LHQKETNQDV 370 380 390 400 410 420 QCNRFFPSRK TKPVKCILNG INSSAKKNSN WTKIKLSKFN SVQHNKLDSQ VSPKLGLLRT 430 440 450 460 470 480 SFSPPALEMH HPVTQSTFLG TKLHDRNITC QQEKMKEINS EEVKINDITV EINKTTERAP 490 500 510 520 530 540 ENCHLANEIK PSDPPLDNQM KHSFDSASNK NFSQCLESKL ENSPVENVTA ASTLLSQAKI 550 560 570 580 590 600 DTGENKFPGS APQQHSILSN QTSKSSDNRE TPRNHSLPKC NSHLEITIPK DLKLKEAEKT 610 620 630 640 650 660 DEKQLIIDAG QKRFGAVSCN VCGMLYTASN PEDETQHLLF HNQFISAVKY VGWKKERILA 670 680 690 700 710 720 EYPDGRIIMV LPEDPKYALK KVDEIREMVD NDLGFQQAPL MCYSRTKTLL FISNDKKVVG 730 740 750 760 770 780 CLIAEHIQWG YRVIEEKLPV IRSEEEKVRF ERQKAWCCST LPEPAICGIS RIWVFSMMRR 790 800 810 820 830 840 KKIASRMIEC LRSNFIYGSY LSKEEIAFSD PTPDGKLFAT QYCGTGQFLV YNFINGQNST
	Isoform 2 [UniParc]. Checksum: EA85A22EAD7134C0	FASTA	701	78,987
	10 20 30 40 50 60 MMSIQEKSKE NSSKVTKKSD DKNSETEIQD SQKNLAKKSG PKETIKSQAK SSSESKINQP 70 80 90 100 110 120 ELETRMSTRS SKAASNDKAT KSINKNTVTV RGYSQESTKK KLSQKKLVHE NPKANEQLNR 130 140 150 160 170 180 RSQRLQQLTE VSRRSLRSRE IQGQVQAVKQ SLPPTKKEQC SSTQSKSNKT SQKHVKRKVL 190 200 210 220 230 240 EVKSDSKEDE NLVINEVINS PKGKKRKVEH QTACACSSQC TQGSEKCPQK TTRRDETKPV 250 260 270 280 290 300 PVTSEVKRSK MATSVVPKKN EMKKSVHTQV NTNTTLPKSP QPSVPEQSDN ELEQAGKSKR 310 320 330 340 350 360 GSILQLCEEI AGEIESDNVE VKKESSQMES VKEEKPTEIK LEETSVERQI LHQKETNQDV 370 380 390 400 410 420 QCNRFFPSRK TKPVKCILNG INSSAKKNSN WTKIKLSKFN SVQHNKLDSQ VSPKLGLLRT 430 440 450 460 470 480 SFSPPALEMH HPVTQSTFLG TKLHDRNITC QQEKMKEINS EEVKINDITV EINKTTERAP 490 500 510 520 530 540 ENCHLANEIK PSDPPLDNQM KHSFDSASNK NFSQCLESKL ENSPVENVTA ASTLLSQAKI 550 560 570 580 590 600 DTGENKFPGS APQQHSILSN QTSKSSDNRE TPRNHSLPKC NSHLEITIPK DLKLKEAEKT 610 620 630 640 650 660 DEKQLIIDAG QKRFGAVSCN VCGMLYTASN PEDETQHLLF HNQFISAVKY VVLLINHHEC 670 680 690 700 GSEEEFITSL FLSMFNFRYT QRSFSFPIRF LEGLEERKNS G
	Isoform 3 [UniParc]. Checksum: 695316F9D35CB49B	FASTA	172	19,927
	10 20 30 40 50 60 MVLPEDPKYA LKKVDEIREM VDNDLGFQQA PLMCYSRTKT LLFISNDKKV VGCLIAEHIQ 70 80 90 100 110 120 WGYRVIEEKL PVIRSEEEKV RFERQKAWCC STLPEPAICG ISRIWVFSMM RRKKIASRMI 130 140 150 160 170 ECLRSNFIYG SYLSKEEIAF SDPTPDGKLF ATQYCGTGQF LVYNFINGQN ST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins." Nagase T., Kikuno R., Ohara O. DNA Res. 8:179-187(2001) [PubMed: 11572484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Bone marrow and Melanoma.
[3]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORMS 1 AND 3), VARIANT MET-221. Tissue: Lymph and Mammary gland.
[6]	"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 437-840 (ISOFORM 1).
[7]	"Human EFO1p exhibits acetyltransferase activity and is a unique combination of linker histone and Ctf7p/Eco1p chromatid cohesion establishment domains." Bellows A.M., Kenna M.A., Cassimeris L., Skibbens R.V. Nucleic Acids Res. 31:6334-6343(2003) [PubMed: 14576321] [Abstract] Cited for: IDENTIFICATION (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"Two human orthologues of Eco1/Ctf7 acetyltransferases are both required for proper sister-chromatid cohesion." Hou F., Zou H. Mol. Biol. Cell 16:3908-3918(2005) [PubMed: 15958495] [Abstract] Cited for: FUNCTION, ASSOCIATION WITH CHROMOSOMES, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF CYS-622.
[9]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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-200, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Acetylation of Smc3 by Eco1 is required for S phase sister chromatid cohesion in both human and yeast." Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X., Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J. Mol. Cell 31:143-151(2008) [PubMed: 18614053] [Abstract] Cited for: FUNCTION.
[12]	"Cohesin acetylation speeds the replication fork." Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V. Nature 462:231-234(2009) [PubMed: 19907496] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB067498 mRNA. Translation: BAB67804.1. Different initiation. AL832041 mRNA. Translation: CAH10584.1. AL834200 mRNA. Translation: CAH10682.1. EF444976 Genomic DNA. Translation: ACA05989.1. EF444976 Genomic DNA. Translation: ACA05990.1. CH471088 Genomic DNA. Translation: EAX01128.1. CH471088 Genomic DNA. Translation: EAX01127.1. BC036943 mRNA. Translation: AAH36943.1. BC089426 mRNA. Translation: AAH89426.1. AK090579 mRNA. Translation: BAC03483.1. Different initiation. BK001617 mRNA. Translation: DAA02068.1.
IPI	IPI00289838. IPI00552279. IPI00604608.
RefSeq	NP_443143.2. NM_052911.2.
UniGene	Hs.464733.
3D structure databases
ProteinModelPortal	Q5FWF5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5FWF5. 1 interaction.
STRING	Q5FWF5.
PTM databases
PhosphoSite	Q5FWF5.
Polymorphism databases
DMDM	116241355.
Proteomic databases
PRIDE	Q5FWF5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000269214; ENSP00000269214; ENSG00000141446.
GeneID	114799.
KEGG	hsa:114799.
NMPDR	fig|9606.3.peg.14850.
UCSC	uc002kth.1. human.
Organism-specific databases
CTD	114799.
GeneCards	GC18M019109.
H-InvDB	HIX0019345.
HGNC	HGNC:24645. ESCO1.
HPA	HPA042497.
MIM	609674. gene.
neXtProt	NX_Q5FWF5.
PharmGKB	PA134924215.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05231.
GeneTree	ENSGT00390000008335.
HOVERGEN	HBG081483.
InParanoid	Q5FWF5.
OMA	SKINQPE.
OrthoDB	EOG45TCP1.
PhylomeDB	Q5FWF5.
Gene expression databases
ArrayExpress	Q5FWF5.
Bgee	Q5FWF5.
CleanEx	HS_ESCO1.
Genevestigator	Q5FWF5.
GermOnline	ENSG00000141446. Homo sapiens.
Family and domain databases
KO	K11268.
ProtoNet	Search...
Other
NextBio	79238.
SOURCE	Search...

Entry information

Entry name

ESCO1_HUMAN

Accession

Primary (citable) accession number: Q5FWF5
Secondary accession number(s): B0YJ11 , B0YJ12, Q69YG4, Q69YS3, Q6IMD7, Q8N3Z5, Q8NBG2, Q96PX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 70 of the entry and version 3 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.