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E5RFP7

- E5RFP7_HUMAN

UniProt

E5RFP7 - E5RFP7_HUMAN

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Protein
Submitted name:

N-acetyltransferase ESCO2

Gene

ESCO2

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: Ensembl

GO - Biological processi

  1. chromosome segregation Source: Ensembl
  2. double-strand break repair Source: Ensembl
  3. hematopoietic progenitor cell differentiation Source: Ensembl
  4. protein localization to chromatin Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
N-acetyltransferase ESCO2Imported
Gene namesi
Name:ESCO2Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:27230. ESCO2.

Subcellular locationi

GO - Cellular componenti

  1. chromocenter Source: Ensembl
  2. Golgi apparatus Source: HPA
  3. nuclear pericentric heterochromatin Source: Ensembl
  4. nucleus Source: HPA
  5. site of double-strand break Source: Ensembl
  6. XY body Source: Ensembl
Complete GO annotation...

Expressioni

Gene expression databases

BgeeiE5RFP7.
ExpressionAtlasiE5RFP7. baseline and differential.

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00390000008335.

Sequencei

Sequence statusi: Fragment.

E5RFP7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAALTPRKRK QDSLKCDSLL HFTENLFPSP NKKHCFYQNS DKNEENLHCS
60 70 80 90 100
QQEHFVLSAL KTTEINRLPS ANQGSPFKSA LSTVSFYNQN KWYLNPLERK
110 120 130
LIKESRSTCL KTNDEDKSFP IVTEKMQGKP VCS
Length:133
Mass (Da):15,325
Last modified:February 8, 2011 - v1
Checksum:i38DC58CF6770D4FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei133 – 1331Imported

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC104997 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000519637; ENSP00000428027; ENSG00000171320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC104997 Genomic DNA. No translation available.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000519637 ; ENSP00000428027 ; ENSG00000171320 .

Organism-specific databases

HGNCi HGNC:27230. ESCO2.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00390000008335.

Miscellaneous databases

NextBioi 35497812.

Gene expression databases

Bgeei E5RFP7.
ExpressionAtlasi E5RFP7. baseline and differential.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  2. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Glockner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiE5RFP7_HUMAN
AccessioniPrimary (citable) accession number: E5RFP7
Entry historyi
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: October 29, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3