O75446 (SAP30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase complex subunit SAP30

Alternative name(s):
30 kDa Sin3-associated polypeptide
Sin3 corepressor complex subunit SAP30
Sin3-associated polypeptide p30

Gene names

Name:

SAP30

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

General annotation (Comments)

Function	Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones. Ref.1 UniProtKB O88574
Subunit structure	Interacts with SIN3A, SIN3B, HDAC2 and NCOR1. Interacts with SAMS1 By similarity. Component of the histone deacetylase complex that includes at least SIN3A, HDAC1 and HDAC2. Interacts with HDAC1 and HCFC1. Ref.1 Ref.5
Subcellular location	Nucleus Ref.2.
Tissue specificity	Expressed in all tissues tested with highest levels in pancreas, ovary, PBL, spleen and thymus; lowest levels in brain, placenta, lung and kidney. Ref.2
Sequence similarities	Belongs to the SAP30 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	histone deacetylase complex Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.5Ref.1. Source: UniProtKB transcription corepressor activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 220

220

Histone deacetylase complex subunit SAP30

PRO_0000097582

Regions

Zinc finger

67 – 115

49

Atypical

Region

1 – 129

129

Interaction with NCOR1 By similarity

Region

130 – 220

91

Interaction with SIN3A By similarity

Compositional bias

15 – 59

45

Ala-rich

Amino acid modifications

Modified residue

104

1

N6-acetyllysine Ref.12

Modified residue

131

1

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

138

1

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

145

1

Phosphothreonine Ref.9

Modified residue

169

1

Phosphothreonine Ref.10

Experimental info

Mutagenesis

67

1

C → A: Abolishes zinc-binding. Ref.13

Mutagenesis

68

1

C → A: Retains zinc-binding. Ref.13

Mutagenesis

108

1

H → A: Retains zinc-binding. Ref.13

Mutagenesis

112

1

C → A: Abolishes zinc-binding. Ref.13

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

220

Helix Strand Turn

Details...

Beta strand

69 – 71

3

Helix

87 – 96

10

Beta strand

99 – 102

4

Helix

113 – 120

8

Beta strand

123 – 125

3

Sequences

	Sequence		Length	Mass (Da)
	O75446 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: FF84E06B17AFCAC2	FASTA	220	23,306
	10 20 30 40 50 60 MNGFTPDEMS RGGDAAAAVA AVVAAAAAAA SAGNGTGAGT GAEVPGAGAV SAAGPPGAAG 70 80 90 100 110 120 PGPGQLCCLR EDGERCGRAA GNASFSKRIQ KSISQKKVKI ELDKSARHLY ICDYHKNLIQ 130 140 150 160 170 180 SVRNRRKRKG SDDDGGDSPV QDIDTPEVDL YQLQVNTLRR YKRHFKLPTR PGLNKAQLVE 190 200 210 220 IVGCHFRSIP VNEKDTLTYF IYSVKNDKNK SDLKVDSGVH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex." Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P., Hampsey M., Reinberg D. Mol. Cell 1:1021-1031(1998) [PubMed: 9651585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HDAC1. Tissue: Cervix carcinoma.
[2]	"SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors." Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., Ayer D.E., Eisenman R.N. Mol. Cell 2:33-42(1998) [PubMed: 9702189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Brain.
[5]	"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1." Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W. Genes Dev. 17:896-911(2003) [PubMed: 12670868] [Abstract] Cited for: INTERACTION WITH HCFC1.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-131; SER-138 AND THR-145, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-138 AND THR-169, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104, MASS SPECTROMETRY.
[13]	"Solution structure of a novel zinc finger motif in the SAP30 polypeptide of the Sin3 corepressor complex and its potential role in nucleic acid recognition." He Y., Imhoff R., Sahu A., Radhakrishnan I. Nucleic Acids Res. 37:2142-2152(2009) [PubMed: 19223330] [Abstract] Cited for: STRUCTURE BY NMR OF 64-131, DNA-BINDING, ZINC-FINGER, MUTAGENESIS OF CYS-67; CYS-68; HIS-108 AND CYS-112.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF055993 mRNA. Translation: AAC33316.1.
CH471056 Genomic DNA. Translation: EAX04755.1.
CH471056 Genomic DNA. Translation: EAX04756.1.
BC016757 mRNA. Translation: AAH16757.1.

IPI

IPI00022019.

RefSeq

NP_003855.1. NM_003864.3.

UniGene

Hs.591715.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KDP	NMR	-	A	64-131	[»]

ProteinModelPortal

O75446.

SMR

O75446. Positions 62-220.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75446. 8 interactions.

STRING

O75446.

PTM databases

PhosphoSite

O75446.

Proteomic databases

PeptideAtlas

O75446.

PRIDE

O75446.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296504; ENSP00000296504; ENSG00000164105.

GeneID

8819.

KEGG

hsa:8819.

UCSC

uc003itd.1. human.

Organism-specific databases

CTD

8819.

GeneCards

GC04P174292.

H-InvDB

HIX0004639.

HGNC

HGNC:10532. SAP30.

MIM

603378. gene.

neXtProt

NX_O75446.

PharmGKB

PA34941.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08323.

GeneTree

ENSGT00390000006633.

HOGENOM

HBG279868.

HOVERGEN

HBG057907.

InParanoid

O75446.

OMA

FTPDEMS.

OrthoDB

EOG48PMMK.

PhylomeDB

O75446.

Enzyme and pathway databases

Pathway_Interaction_DB

hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

ArrayExpress

O75446.

Bgee

O75446.

CleanEx

HS_SAP30.

Genevestigator

O75446.

GermOnline

ENSG00000164105. Homo sapiens.

Family and domain databases

InterPro

IPR024145. His_deAcase_SAP30/SAP30L.
[Graphical view]

PANTHER

PTHR13286. PTHR13286. 1 hit.

ProtoNet

Search...

Other

NextBio

33082.

SOURCE

Search...

Entry information

Entry name

SAP30_HUMAN

Accession

Primary (citable) accession number: O75446
Secondary accession number(s): D3DP38

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 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.