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Protein

Histone deacetylase complex subunit SAP30L

Gene

SAP30L

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

Functioni

Isoform 1: Functions as transcription repressor, probably via its interaction with histone deacetylase complexes (PubMed:16820529, PubMed:18070604). Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus (PubMed:16820529). Binds DNA, apparently without sequence-specificity, and bends bound double-stranded DNA (PubMed:19015240). Binds phosphoinositol phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate) via the same basic sequence motif that mediates DNA binding and nuclear import (PubMed:19015240, PubMed:26609676).4 Publications
Isoform 2: Functions as transcription repressor; isoform 2 has lower transcription repressor activity than isoform 1 and isoform 3.1 Publication
Isoform 3: Functions as transcription repressor; its activity is marginally lower than that of isoform 1.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 77Atypical1 PublicationAdd BLAST49

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • histone deacetylase activity Source: GO_Central
  • non-sequence-specific DNA binding, bending Source: UniProtKB
  • nucleosome binding Source: UniProtKB
  • phosphatidylinositol-3-phosphate binding Source: UniProtKB
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB
  • phosphatidylinositol-5-phosphate binding Source: UniProtKB
  • transcription coregulator activity Source: GO_Central
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandLipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3214815 HDACs deacetylate histones
R-HSA-427413 NoRC negatively regulates rRNA expression

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase complex subunit SAP30L
Alternative name(s):
HCV non-structural protein 4A-transactivated protein 2
Sin3 corepressor complex subunit SAP30L
Sin3-associated protein p30-like
Gene namesi
Name:SAP30L
Synonyms:NS4ATP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000164576.11
HGNCiHGNC:25663 SAP30L
MIMi610398 gene
neXtProtiNX_Q9HAJ7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi88 – 90RKR → AAA: Strongly reduces affinity for DNA and for phosphoinositides. 1 Publication3
Mutagenesisi88 – 89RK → KS: Impairs nuclear localization. 1 Publication2
Mutagenesisi109 – 113Missing : Reduces transcriptional repressor activity, reduces localization in nucleoli, but has no effect on association with histone deacylase complexes. 1 Publication5
Mutagenesisi120 – 127RRYKRHYK → AAAAAAAA: Abolishes nucleolar localization. 1 Publication8

Organism-specific databases

DisGeNETi79685
OpenTargetsiENSG00000164576
PharmGKBiPA144596386

Polymorphism and mutation databases

BioMutaiSAP30L
DMDMi74734226

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003095001 – 183Histone deacetylase complex subunit SAP30LAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Disulfide bondi29 ↔ 30Redox-active1 Publication
Disulfide bondi38 ↔ 74Redox-active1 Publication
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei92PhosphothreonineCombined sources1
Modified residuei93PhosphoserineBy similarity1
Modified residuei99PhosphoserineCombined sources1
Modified residuei104PhosphothreonineCombined sources1
Cross-linki155Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9HAJ7
MaxQBiQ9HAJ7
PaxDbiQ9HAJ7
PeptideAtlasiQ9HAJ7
PRIDEiQ9HAJ7
ProteomicsDBi81408

PTM databases

iPTMnetiQ9HAJ7
PhosphoSitePlusiQ9HAJ7

Expressioni

Tissue specificityi

Detected in brain and ovary, and at lower levels in heart, small intestine, lung, kidney, skeletal muscle, stomach and spleen (at protein level) (PubMed:18070604). Ubiquitous; expressed in all tissues tested with highest levels in testis (PubMed:14680513).2 Publications

Inductioni

Up-regulated by TGFB1.1 Publication

Gene expression databases

BgeeiENSG00000164576
CleanExiHS_SAP30L
GenevisibleiQ9HAJ7 HS

Organism-specific databases

HPAiHPA048665

Interactioni

Subunit structurei

Interacts with components of the histone deacetylase complex SIN3A, HDAC1 and HDAC2 (PubMed:16820529). Binds histones and nucleosomes (PubMed:19015240). Interacts with FEZ1 (PubMed:16484223).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HMBOX1Q6NT763EBI-2340040,EBI-2549423

GO - Molecular functioni

  • histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122808, 18 interactors
IntActiQ9HAJ7, 9 interactors
MINTiQ9HAJ7
STRINGi9606.ENSP00000297109

Structurei

Secondary structure

1183
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 33Combined sources3
Beta strandi41 – 46Combined sources6
Helixi51 – 56Combined sources6
Beta strandi61 – 64Combined sources4
Turni66 – 69Combined sources4
Beta strandi72 – 74Combined sources3
Helixi75 – 83Combined sources9

3D structure databases

ProteinModelPortaliQ9HAJ7
SMRiQ9HAJ7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni88 – 90Important for DNA and phosphoinositide binding1 Publication3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi86 – 91Nuclear localization signal (NLS)1 Publication6

Domaini

The zinc-finger domain mediates direct interaction with DNA and phosphoinositol phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate) (PubMed:26609676). In vitro oxydation causes reversible disulfide bond formation between Cys residues in the zinc-finger domain and reversible loss of zinc ion binding (PubMed:26609676).1 Publication

Sequence similaritiesi

Belongs to the SAP30 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 77Atypical1 PublicationAdd BLAST49

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IHMG Eukaryota
ENOG4111GVC LUCA
GeneTreeiENSGT00390000006633
HOGENOMiHOG000007811
HOVERGENiHBG057907
InParanoidiQ9HAJ7
OMAiFYGQSCC
OrthoDBiEOG091G0PSQ
PhylomeDBiQ9HAJ7
TreeFamiTF324135

Family and domain databases

Gene3Di1.10.720.110, 1 hit
InterProiView protein in InterPro
IPR024145 His_deAcase_SAP30/SAP30L
IPR038291 SAP30_C_sf
IPR025718 SAP30_Sin3-bd
IPR025717 SAP30_zn-finger
PANTHERiPTHR13286 PTHR13286, 1 hit
PfamiView protein in Pfam
PF13867 SAP30_Sin3_bdg, 1 hit
PF13866 zf-SAP30, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HAJ7-1) [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
MNGFSTEEDS REGPPAAPAA AAPGYGQSCC LIEDGERCVR PAGNASFSKR
60 70 80 90 100
VQKSISQKKL KLDIDKSVRH LYICDFHKNF IQSVRNKRKR KTSDDGGDSP
110 120 130 140 150
EHDTDIPEVD LFQLQVNTLR RYKRHYKLQT RPGFNKAQLA ETVSRHFRNI
160 170 180
PVNEKETLAY FIYMVKSNKS RLDQKSEGGK QLE
Length:183
Mass (Da):20,877
Last modified:March 1, 2001 - v1
Checksum:iEB19E448C6A1FA45
GO
Isoform 2 (identifier: Q9HAJ7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-113: Missing.

Show »
Length:137
Mass (Da):15,437
Checksum:iCCC8C6263BFFE497
GO
Isoform 3 (identifier: Q9HAJ7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-108: Missing.

Show »
Length:142
Mass (Da):16,039
Checksum:iB769D2CD6DC31A4B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31L → R in AI199517 (Ref. 7) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04622168 – 113Missing in isoform 2. 1 Publication1 PublicationAdd BLAST46
Alternative sequenceiVSP_04686068 – 108Missing in isoform 3. 1 Publication1 PublicationAdd BLAST41

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY341060 mRNA Translation: AAQ16562.1
AY846876 mRNA Translation: AAX54477.1
AK021588 mRNA Translation: BAB13848.1
AC008625 Genomic DNA No translation available.
CH471062 Genomic DNA Translation: EAW61637.1
BC009829 mRNA Translation: AAH09829.1
AI199517 mRNA No translation available.
AI436556 mRNA No translation available.
CCDSiCCDS4326.1 [Q9HAJ7-1]
CCDS47321.1 [Q9HAJ7-3]
CCDS47322.1 [Q9HAJ7-2]
RefSeqiNP_001124534.1, NM_001131062.1 [Q9HAJ7-3]
NP_001124535.1, NM_001131063.1 [Q9HAJ7-2]
NP_078908.1, NM_024632.5 [Q9HAJ7-1]
UniGeneiHs.592566

Genome annotation databases

EnsembliENST00000297109; ENSP00000297109; ENSG00000164576 [Q9HAJ7-1]
ENST00000426761; ENSP00000416393; ENSG00000164576 [Q9HAJ7-2]
ENST00000440364; ENSP00000390927; ENSG00000164576 [Q9HAJ7-3]
GeneIDi79685
KEGGihsa:79685
UCSCiuc003lvk.4 human [Q9HAJ7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSP30L_HUMAN
AccessioniPrimary (citable) accession number: Q9HAJ7
Secondary accession number(s): E9PAU7, E9PAY2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2001
Last modified: July 18, 2018
This is version 135 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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