O55128 (SAP18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase complex subunit SAP18

Alternative name(s):
18 kDa Sin3-associated polypeptide
Sin3-associated polypeptide p18

Gene names

Name:

Sap18

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism By similarity.
Subunit structure	Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and THOC4. Found in a heterotrimeric complex with ACIN1, RNPS1 and SAP18. Forms a complex with SIN3A and HDAC1 By similarity.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: Shuttles between the nucleus and the cytoplasm By similarity.
Tissue specificity	Expressed in all tissues tested; highest levels in the brain, kidney and muscle; lowest levels in lung spleen, liver, intestine and testis, and moderate levels in salivary gland and heart. Ref.1
Sequence similarities	Belongs to the SAP18 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Molecular function	Repressor
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sufu	Q9Z0P7	6	EBI-3508332,EBI-3508336

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 153	152	Histone deacetylase complex subunit SAP18		PRO_0000220976
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O55128 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 68FE63E6EAD04E6F	FASTA	153	17,595
	10 20 30 40 50 60 MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN VPSSELQIYT 70 80 90 100 110 120 WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFMDLKRPG YRVKEIGSTM SGRKGTDDSM 130 140 150 TLQSQKFQIG DYLDIAITPP NRAPPSSGRM RPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the murine transcriptional corepressor component SAP18 and differential expression of its mRNA in the hematopoietic hierarchy." Boehmelt G., Antonio L., Iscove N.N. Gene 207:267-275(1998) [PubMed: 9511770] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Spleen.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum, Heart and Testis.
[3]	"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]. Strain: FVB/N. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z97062 mRNA. Translation: CAB09797.1. AK005189 mRNA. Translation: BAB23871.1. AK006647 mRNA. Translation: BAB24687.1. AK085992 mRNA. Translation: BAC39588.1. BC006625 mRNA. Translation: AAH06625.1.
IPI	IPI00115831.
RefSeq	NP_033145.2. NM_009119.3.
UniGene	Mm.30173. Mm.344671.
3D structure databases
ProteinModelPortal	O55128.
SMR	O55128. Positions 6-149.
ModBase	Search...
Protein-protein interaction databases
IntAct	O55128. 4 interactions.
PTM databases
PhosphoSite	O55128.
Proteomic databases
PRIDE	O55128.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000022533; ENSMUSP00000022533; ENSMUSG00000021963.
GeneID	20220.
KEGG	mmu:20220.
Organism-specific databases
CTD	10284.
MGI	MGI:1277978. Sap18.
Phylogenomic databases
eggNOG	roNOG05542.
HOGENOM	HBG745731.
HOVERGEN	HBG003465.
InParanoid	O55128.
OMA	DISITPP.
OrthoDB	EOG44MXTB.
PhylomeDB	O55128.
Gene expression databases
ArrayExpress	O55128.
Bgee	O55128.
CleanEx	MM_SAP18.
Genevestigator	O55128.
GermOnline	ENSMUSG00000021963. Mus musculus. ENSMUSG00000061104. Mus musculus.
Family and domain databases
InterPro	IPR017250. Hist_deAcase_cplx_SAP18. IPR010516. SAP18. [Graphical view]
KO	K14324.
PANTHER	PTHR13082. SAP18. 1 hit.
Pfam	PF06487. SAP18. 1 hit. [Graphical view]
PIRSF	PIRSF037637. HDAC_SAP18. 1 hit.
ProtoNet	Search...
Other
NextBio	452506.
SOURCE	Search...

Entry information

Entry name

SAP18_MOUSE

Accession

Primary (citable) accession number: O55128
Secondary accession number(s): Q545L4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	November 16, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program