Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acetyltransferase ESCO1

Gene

ESCO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 SMC3.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri617 – 64125CCHH-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • mitotic cell cycle Source: Reactome
  • post-translational protein acetylation Source: UniProtKB
  • regulation of DNA replication Source: UniProtKB
  • sister chromatid cohesion Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-2468052. Establishment of Sister Chromatid Cohesion.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ESCO1
Synonyms:EFO1, KIAA1911
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:24645. ESCO1.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

  • Note: Nuclear at interphase, associated with chromosomes during mitosis (PubMed:15958495).

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi622 – 6221C → G: No effect on association with chromosomes. 1 Publication

Organism-specific databases

PharmGKBiPA134924215.

Polymorphism and mutation databases

BioMutaiESCO1.
DMDMi116241355.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 840840N-acetyltransferase ESCO1PRO_0000074539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei200 – 2001PhosphoserineCombined sources
Cross-linki332 – 332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei412 – 4121PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated during mitosis.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5FWF5.
MaxQBiQ5FWF5.
PaxDbiQ5FWF5.
PRIDEiQ5FWF5.

PTM databases

iPTMnetiQ5FWF5.
PhosphoSiteiQ5FWF5.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, brain, liver, placenta, lung, kidney and pancreas. Highly expressed in muscle.1 Publication

Gene expression databases

BgeeiQ5FWF5.
CleanExiHS_ESCO1.
ExpressionAtlasiQ5FWF5. baseline and differential.
GenevisibleiQ5FWF5. HS.

Organism-specific databases

HPAiHPA042497.

Interactioni

Protein-protein interaction databases

BioGridi125360. 22 interactions.
IntActiQ5FWF5. 14 interactions.
STRINGi9606.ENSP00000269214.

Structurei

Secondary structure

1
840
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi658 – 6614Combined sources
Beta strandi663 – 6708Combined sources
Helixi676 – 68914Combined sources
Beta strandi707 – 7137Combined sources
Beta strandi717 – 72610Combined sources
Beta strandi728 – 73912Combined sources
Beta strandi752 – 76413Combined sources
Beta strandi766 – 7749Combined sources
Helixi776 – 7783Combined sources
Beta strandi780 – 7823Combined sources
Helixi783 – 79412Combined sources
Beta strandi805 – 8106Combined sources
Helixi813 – 82311Combined sources
Beta strandi827 – 8337Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MXEX-ray2.60A/B654-836[»]
ProteinModelPortaliQ5FWF5.
SMRiQ5FWF5. Positions 654-836.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal region seems to be responsible for the association with chromosomes, thus excluding any involvement of the Zn finger in this process.

Sequence similaritiesi

Belongs to the acetyltransferase family. ECO subfamily.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri617 – 64125CCHH-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3014. Eukaryota.
ENOG410XTJX. LUCA.
GeneTreeiENSGT00390000008335.
HOVERGENiHBG081483.
InParanoidiQ5FWF5.
KOiK11268.
OMAiNSNWTKI.
OrthoDBiEOG7J9VQQ.
PhylomeDBiQ5FWF5.
TreeFamiTF314027.

Family and domain databases

InterProiIPR026656. AcTrfase_ESCO1.
IPR028005. AcTrfase_ESCO_Znf_dom.
IPR028009. ESCO_Acetyltransf_dom.
[Graphical view]
PANTHERiPTHR11076:SF26. PTHR11076:SF26. 1 hit.
PfamiPF13880. Acetyltransf_13. 1 hit.
PF13878. zf-C2H2_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5FWF5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MMSIQEKSKE NSSKVTKKSD DKNSETEIQD SQKNLAKKSG PKETIKSQAK
60 70 80 90 100
SSSESKINQP ELETRMSTRS SKAASNDKAT KSINKNTVTV RGYSQESTKK
110 120 130 140 150
KLSQKKLVHE NPKANEQLNR RSQRLQQLTE VSRRSLRSRE IQGQVQAVKQ
160 170 180 190 200
SLPPTKKEQC SSTQSKSNKT SQKHVKRKVL EVKSDSKEDE NLVINEVINS
210 220 230 240 250
PKGKKRKVEH QTACACSSQC TQGSEKCPQK TTRRDETKPV PVTSEVKRSK
260 270 280 290 300
MATSVVPKKN EMKKSVHTQV NTNTTLPKSP QPSVPEQSDN ELEQAGKSKR
310 320 330 340 350
GSILQLCEEI AGEIESDNVE VKKESSQMES VKEEKPTEIK LEETSVERQI
360 370 380 390 400
LHQKETNQDV QCNRFFPSRK TKPVKCILNG INSSAKKNSN WTKIKLSKFN
410 420 430 440 450
SVQHNKLDSQ VSPKLGLLRT SFSPPALEMH HPVTQSTFLG TKLHDRNITC
460 470 480 490 500
QQEKMKEINS EEVKINDITV EINKTTERAP ENCHLANEIK PSDPPLDNQM
510 520 530 540 550
KHSFDSASNK NFSQCLESKL ENSPVENVTA ASTLLSQAKI DTGENKFPGS
560 570 580 590 600
APQQHSILSN QTSKSSDNRE TPRNHSLPKC NSHLEITIPK DLKLKEAEKT
610 620 630 640 650
DEKQLIIDAG QKRFGAVSCN VCGMLYTASN PEDETQHLLF HNQFISAVKY
660 670 680 690 700
VGWKKERILA EYPDGRIIMV LPEDPKYALK KVDEIREMVD NDLGFQQAPL
710 720 730 740 750
MCYSRTKTLL FISNDKKVVG CLIAEHIQWG YRVIEEKLPV IRSEEEKVRF
760 770 780 790 800
ERQKAWCCST LPEPAICGIS RIWVFSMMRR KKIASRMIEC LRSNFIYGSY
810 820 830 840
LSKEEIAFSD PTPDGKLFAT QYCGTGQFLV YNFINGQNST
Length:840
Mass (Da):94,983
Last modified:October 17, 2006 - v3
Checksum:iA36BE0EC1BE3EDF2
GO
Isoform 2 (identifier: Q5FWF5-2) [UniParc]FASTAAdd to basket

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. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:701
Mass (Da):78,987
Checksum:iEA85A22EAD7134C0
GO

Sequence cautioni

The sequence AAH36943.1 differs from that shown.Wrong choice of frame.Curated
The sequence BAB67804.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC03483.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti384 – 3841S → L in BAB67804 (PubMed:11572484).Curated
Sequence conflicti432 – 4321P → S in CAH10682 (PubMed:17974005).Curated
Sequence conflicti805 – 8051E → A in BAC03483 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911N → S.
Corresponds to variant rs35087820 [ dbSNP | Ensembl ].
VAR_048167
Natural varianti221 – 2211T → M.1 Publication
Corresponds to variant rs13381941 [ dbSNP | Ensembl ].
VAR_022648

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei652 – 70150GWKKE…QAPLM → VLLINHHECGSEEEFITSLF LSMFNFRYTQRSFSFPIRFL EGLEERKNSG in isoform 2. 2 PublicationsVSP_014029Add
BLAST
Alternative sequencei702 – 840139Missing in isoform 2. 2 PublicationsVSP_014030Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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. Sequence problems.
BC089426 mRNA. Translation: AAH89426.1.
AK090579 mRNA. Translation: BAC03483.1. Different initiation.
BK001617 mRNA. Translation: DAA02068.1.
CCDSiCCDS32800.1. [Q5FWF5-1]
RefSeqiNP_443143.2. NM_052911.2. [Q5FWF5-1]
XP_011524100.1. XM_011525798.1. [Q5FWF5-1]
UniGeneiHs.464733.

Genome annotation databases

EnsembliENST00000269214; ENSP00000269214; ENSG00000141446. [Q5FWF5-1]
ENST00000383276; ENSP00000372763; ENSG00000141446. [Q5FWF5-2]
GeneIDi114799.
KEGGihsa:114799.
UCSCiuc002kth.2. human. [Q5FWF5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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. Sequence problems.
BC089426 mRNA. Translation: AAH89426.1.
AK090579 mRNA. Translation: BAC03483.1. Different initiation.
BK001617 mRNA. Translation: DAA02068.1.
CCDSiCCDS32800.1. [Q5FWF5-1]
RefSeqiNP_443143.2. NM_052911.2. [Q5FWF5-1]
XP_011524100.1. XM_011525798.1. [Q5FWF5-1]
UniGeneiHs.464733.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MXEX-ray2.60A/B654-836[»]
ProteinModelPortaliQ5FWF5.
SMRiQ5FWF5. Positions 654-836.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125360. 22 interactions.
IntActiQ5FWF5. 14 interactions.
STRINGi9606.ENSP00000269214.

PTM databases

iPTMnetiQ5FWF5.
PhosphoSiteiQ5FWF5.

Polymorphism and mutation databases

BioMutaiESCO1.
DMDMi116241355.

Proteomic databases

EPDiQ5FWF5.
MaxQBiQ5FWF5.
PaxDbiQ5FWF5.
PRIDEiQ5FWF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269214; ENSP00000269214; ENSG00000141446. [Q5FWF5-1]
ENST00000383276; ENSP00000372763; ENSG00000141446. [Q5FWF5-2]
GeneIDi114799.
KEGGihsa:114799.
UCSCiuc002kth.2. human. [Q5FWF5-1]

Organism-specific databases

CTDi114799.
GeneCardsiESCO1.
H-InvDBHIX0019345.
HGNCiHGNC:24645. ESCO1.
HPAiHPA042497.
MIMi609674. gene.
neXtProtiNX_Q5FWF5.
PharmGKBiPA134924215.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3014. Eukaryota.
ENOG410XTJX. LUCA.
GeneTreeiENSGT00390000008335.
HOVERGENiHBG081483.
InParanoidiQ5FWF5.
KOiK11268.
OMAiNSNWTKI.
OrthoDBiEOG7J9VQQ.
PhylomeDBiQ5FWF5.
TreeFamiTF314027.

Enzyme and pathway databases

ReactomeiR-HSA-2468052. Establishment of Sister Chromatid Cohesion.

Miscellaneous databases

ChiTaRSiESCO1. human.
GenomeRNAii114799.
NextBioi79238.
PROiQ5FWF5.
SOURCEiSearch...

Gene expression databases

BgeeiQ5FWF5.
CleanExiHS_ESCO1.
ExpressionAtlasiQ5FWF5. baseline and differential.
GenevisibleiQ5FWF5. HS.

Family and domain databases

InterProiIPR026656. AcTrfase_ESCO1.
IPR028005. AcTrfase_ESCO_Znf_dom.
IPR028009. ESCO_Acetyltransf_dom.
[Graphical view]
PANTHERiPTHR11076:SF26. PTHR11076:SF26. 1 hit.
PfamiPF13880. Acetyltransf_13. 1 hit.
PF13878. zf-C2H2_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. 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. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-840 (ISOFORM 2), 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH CHROMOSOMES, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF CYS-622.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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.
  12. "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-200 AND SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiESCO1_HUMAN
AccessioniPrimary (citable) accession number: Q5FWF5
Secondary accession number(s): B0YJ11
, B0YJ12, Q69YG4, Q69YS3, Q6IMD7, Q8N3Z5, Q8NBG2, Q96PX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 17, 2006
Last modified: April 13, 2016
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.