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Entry version 141 (08 May 2019)
Sequence version 1 (01 Mar 2001)
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Protein

Histone deacetylase complex subunit SAP30L

Gene

SAP30L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri29 – 77Atypical1 PublicationAdd BLAST49

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3214815 HDACs deacetylate histones
R-HSA-427413 NoRC negatively regulates rRNA expression

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SAP30L
Synonyms:NS4ATP2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:25663 SAP30L

Online Mendelian Inheritance in Man (OMIM)

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MIMi
610398 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9HAJ7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
79685

Open Targets

More...
OpenTargetsi
ENSG00000164576

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA144596386

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SAP30L

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74734226

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003095001 – 183Histone deacetylase complex subunit SAP30LAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi29 ↔ 30Redox-active1 Publication
Disulfide bondi38 ↔ 74Redox-active1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
Q9HAJ7

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9HAJ7

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9HAJ7

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9HAJ7

PeptideAtlas

More...
PeptideAtlasi
Q9HAJ7

PRoteomics IDEntifications database

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PRIDEi
Q9HAJ7

ProteomicsDB human proteome resource

More...
ProteomicsDBi
81408

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9HAJ7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9HAJ7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by TGFB1.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000164576 Expressed in 217 organ(s), highest expression level in testis

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9HAJ7 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA048665

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
122808, 22 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3321 SIN3A histone deacetylase complex
CPX-3322 SIN3B histone deacetylase complex
CPX-3323 SIN3A histone deacetylase complex, ES cell-specific variant

Protein interaction database and analysis system

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IntActi
Q9HAJ7, 9 interactors

Molecular INTeraction database

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MINTi
Q9HAJ7

STRING: functional protein association networks

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STRINGi
9606.ENSP00000297109

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1183
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N1UNMR-A25-92[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9HAJ7

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni88 – 90Important for DNA and phosphoinositide binding1 Publication3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi86 – 91Nuclear localization signal (NLS)1 Publication6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IHMG Eukaryota
ENOG4111GVC LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000006633

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000007811

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9HAJ7

Identification of Orthologs from Complete Genome Data

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OMAi
FYGQSCC

Database of Orthologous Groups

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OrthoDBi
1520155at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9HAJ7

TreeFam database of animal gene trees

More...
TreeFami
TF324135

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.720.110, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR024145 His_deAcase_SAP30/SAP30L
IPR038291 SAP30_C_sf
IPR025718 SAP30_Sin3-bd
IPR025717 SAP30_zn-finger

The PANTHER Classification System

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PANTHERi
PTHR13286 PTHR13286, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13867 SAP30_Sin3_bdg, 1 hit
PF13866 zf-SAP30, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti31L → R in AI199517 (Ref. 7) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4326.1 [Q9HAJ7-1]
CCDS47321.1 [Q9HAJ7-3]
CCDS47322.1 [Q9HAJ7-2]

NCBI Reference Sequences

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RefSeqi
NP_001124534.1, NM_001131062.1 [Q9HAJ7-3]
NP_001124535.1, NM_001131063.1 [Q9HAJ7-2]
NP_078908.1, NM_024632.5 [Q9HAJ7-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000297109; ENSP00000297109; ENSG00000164576 [Q9HAJ7-1]
ENST00000426761; ENSP00000416393; ENSG00000164576 [Q9HAJ7-2]
ENST00000440364; ENSP00000390927; ENSG00000164576 [Q9HAJ7-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
79685

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:79685

UCSC genome browser

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UCSCi
uc003lvk.4 human [Q9HAJ7-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N1UNMR-A25-92[»]
SMRiQ9HAJ7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122808, 22 interactors
ComplexPortaliCPX-3321 SIN3A histone deacetylase complex
CPX-3322 SIN3B histone deacetylase complex
CPX-3323 SIN3A histone deacetylase complex, ES cell-specific variant
IntActiQ9HAJ7, 9 interactors
MINTiQ9HAJ7
STRINGi9606.ENSP00000297109

PTM databases

iPTMnetiQ9HAJ7
PhosphoSitePlusiQ9HAJ7

Polymorphism and mutation databases

BioMutaiSAP30L
DMDMi74734226

Proteomic databases

EPDiQ9HAJ7
jPOSTiQ9HAJ7
MaxQBiQ9HAJ7
PaxDbiQ9HAJ7
PeptideAtlasiQ9HAJ7
PRIDEiQ9HAJ7
ProteomicsDBi81408

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
79685
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
79685
DisGeNETi79685

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SAP30L
HGNCiHGNC:25663 SAP30L
HPAiHPA048665
MIMi610398 gene
neXtProtiNX_Q9HAJ7
OpenTargetsiENSG00000164576
PharmGKBiPA144596386

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IHMG Eukaryota
ENOG4111GVC LUCA
GeneTreeiENSGT00390000006633
HOGENOMiHOG000007811
InParanoidiQ9HAJ7
OMAiFYGQSCC
OrthoDBi1520155at2759
PhylomeDBiQ9HAJ7
TreeFamiTF324135

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
SAP30L human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
79685

Protein Ontology

More...
PROi
PR:Q9HAJ7

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000164576 Expressed in 217 organ(s), highest expression level in testis
GenevisibleiQ9HAJ7 HS

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSP30L_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9HAJ7
Secondary accession number(s): E9PAU7, E9PAY2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2001
Last modified: May 8, 2019
This is version 141 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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