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
Submitted name:

Histone deacetylase complex subunit SAP18

Gene

SAP18

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Submitted name:
Histone deacetylase complex subunit SAP18Imported
Gene namesi
Name:SAP18Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:10530. SAP18.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

EPDiX6RAL5.
MaxQBiX6RAL5.
PaxDbiX6RAL5.

Expressioni

Gene expression databases

ExpressionAtlasiX6RAL5. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000371973.

Structurei

3D structure databases

ProteinModelPortaliX6RAL5.
SMRiX6RAL5. Positions 25-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiKOG3391. Eukaryota.
ENOG4111FBB. LUCA.
GeneTreeiENSGT00390000003152.
KOiK14324.
OMAiITPPNRM.
PhylomeDBiX6RAL5.

Family and domain databases

InterProiIPR017250. Hist_deAcase_cplx_SAP18.
IPR010516. SAP18.
[Graphical view]
PANTHERiPTHR13082. PTHR13082. 1 hit.
PfamiPF06487. SAP18. 1 hit.
[Graphical view]
PIRSFiPIRSF037637. HDAC_SAP18. 1 hit.

Sequencei

Sequence statusi: Complete.

X6RAL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAAGVGGQG ERLAGRRRKM AVESRVTQEE IKKEPEKPID REKTCPLLLR
60 70 80 90 100
VFTTNNGRHH RMDEFSRGNV PSSELQIYTW MDATLKELTS LVKEVYPEAR
110 120 130 140 150
KKGTHFNFAI VFTDVKRPGY RVKEIGSTMS GRKGTDDSMT LQSQKFQIGD
160 170
YLDIAITPPN RAPPPSGRMR PY
Length:172
Mass (Da):19,526
Last modified:June 11, 2014 - v1
Checksum:i0E990E2DC0C24C90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL158032 Genomic DNA. No translation available.
RefSeqiNP_005861.2. NM_005870.4.
UniGeneiHs.524899.

Genome annotation databases

EnsembliENST00000382533; ENSP00000371973; ENSG00000150459.
ENST00000621421; ENSP00000481842; ENSG00000150459.
GeneIDi10284.
KEGGihsa:10284.
UCSCiuc001uns.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL158032 Genomic DNA. No translation available.
RefSeqiNP_005861.2. NM_005870.4.
UniGeneiHs.524899.

3D structure databases

ProteinModelPortaliX6RAL5.
SMRiX6RAL5. Positions 25-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000371973.

Proteomic databases

EPDiX6RAL5.
MaxQBiX6RAL5.
PaxDbiX6RAL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382533; ENSP00000371973; ENSG00000150459.
ENST00000621421; ENSP00000481842; ENSG00000150459.
GeneIDi10284.
KEGGihsa:10284.
UCSCiuc001uns.4. human.

Organism-specific databases

CTDi10284.
HGNCiHGNC:10530. SAP18.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3391. Eukaryota.
ENOG4111FBB. LUCA.
GeneTreeiENSGT00390000003152.
KOiK14324.
OMAiITPPNRM.
PhylomeDBiX6RAL5.

Miscellaneous databases

ChiTaRSiSAP18. human.
GenomeRNAii10284.

Gene expression databases

ExpressionAtlasiX6RAL5. baseline and differential.

Family and domain databases

InterProiIPR017250. Hist_deAcase_cplx_SAP18.
IPR010516. SAP18.
[Graphical view]
PANTHERiPTHR13082. PTHR13082. 1 hit.
PfamiPF06487. SAP18. 1 hit.
[Graphical view]
PIRSFiPIRSF037637. HDAC_SAP18. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (APR-2014) to UniProtKB
    Cited for: IDENTIFICATION.
  6. Ensembl
    Submitted (SEP-2014) to UniProtKB
    Cited for: IDENTIFICATION.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiX6RAL5_HUMAN
AccessioniPrimary (citable) accession number: X6RAL5
Entry historyi
Integrated into UniProtKB/TrEMBL: June 11, 2014
Last sequence update: June 11, 2014
Last modified: April 13, 2016
This is version 18 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, Proteomics identificationCombined sources, Reference proteomeImported

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.