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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-Experimental evidence at protein leveli

Functioni

Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri29 – 7749AtypicalAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-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

HGNCiHGNC:25663. SAP30L.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi88 – 892RK → KS: Impairs nuclear localization. 1 Publication
Mutagenesisi120 – 1278RRYKRHYK → AAAAAAAA: Abolishes nucleolar localization. 1 Publication

Organism-specific databases

PharmGKBiPA144596386.

Polymorphism and mutation databases

BioMutaiSAP30L.
DMDMi74734226.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Histone deacetylase complex subunit SAP30LPRO_0000309500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei92 – 921PhosphothreonineCombined sources
Modified residuei93 – 931PhosphoserineBy similarity
Modified residuei99 – 991PhosphoserineCombined sources
Modified residuei104 – 1041PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9HAJ7.
MaxQBiQ9HAJ7.
PaxDbiQ9HAJ7.
PRIDEiQ9HAJ7.

PTM databases

iPTMnetiQ9HAJ7.
PhosphoSiteiQ9HAJ7.

Expressioni

Tissue specificityi

Expressed in all tissues tested with highest levels in testis.

Inductioni

Up-regulated by TGFB1.1 Publication

Gene expression databases

BgeeiQ9HAJ7.
CleanExiHS_SAP30L.
GenevisibleiQ9HAJ7. HS.

Interactioni

Subunit structurei

Interacts with components of the histone deacetylase complex SIN3A, HDAC1 and HDAC2. Interacts with FEZ1.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi122808. 15 interactions.
IntActiQ9HAJ7. 6 interactions.
STRINGi9606.ENSP00000297109.

Structurei

Secondary structure

1
183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Beta strandi41 – 466Combined sources
Helixi51 – 566Combined sources
Beta strandi61 – 644Combined sources
Turni66 – 694Combined sources
Beta strandi72 – 743Combined sources
Helixi75 – 839Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2N1UNMR-A25-92[»]
ProteinModelPortaliQ9HAJ7.
SMRiQ9HAJ7. Positions 26-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SAP30 family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri29 – 7749AtypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IHMG. Eukaryota.
ENOG4111GVC. LUCA.
GeneTreeiENSGT00390000006633.
HOGENOMiHOG000007811.
HOVERGENiHBG057907.
InParanoidiQ9HAJ7.
OMAiFYGQSCC.
OrthoDBiEOG7P5T35.
PhylomeDBiQ9HAJ7.
TreeFamiTF324135.

Family and domain databases

InterProiIPR024145. His_deAcase_SAP30/SAP30L.
IPR025718. SAP30_Sin3-bd.
IPR025717. SAP30_zn-finger.
[Graphical view]
PANTHERiPTHR13286. PTHR13286. 1 hit.
PfamiPF13867. SAP30_Sin3_bdg. 1 hit.
PF13866. zf-SAP30. 1 hit.
[Graphical view]

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.

Note: No experimental confirmation available.
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.

Note: No experimental confirmation available.
Show »
Length:142
Mass (Da):16,039
Checksum:iB769D2CD6DC31A4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311L → R in AI199517 (Ref. 7) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 11346Missing in isoform 2. 1 PublicationVSP_046221Add
BLAST
Alternative sequencei68 – 10841Missing in isoform 3. 1 PublicationVSP_046860Add
BLAST

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

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]
UniGeneiHs.592566.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2N1UNMR-A25-92[»]
ProteinModelPortaliQ9HAJ7.
SMRiQ9HAJ7. Positions 26-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122808. 15 interactions.
IntActiQ9HAJ7. 6 interactions.
STRINGi9606.ENSP00000297109.

PTM databases

iPTMnetiQ9HAJ7.
PhosphoSiteiQ9HAJ7.

Polymorphism and mutation databases

BioMutaiSAP30L.
DMDMi74734226.

Proteomic databases

EPDiQ9HAJ7.
MaxQBiQ9HAJ7.
PaxDbiQ9HAJ7.
PRIDEiQ9HAJ7.

Protocols and materials databases

DNASUi79685.
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

CTDi79685.
GeneCardsiSAP30L.
HGNCiHGNC:25663. SAP30L.
MIMi610398. gene.
neXtProtiNX_Q9HAJ7.
PharmGKBiPA144596386.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHMG. Eukaryota.
ENOG4111GVC. LUCA.
GeneTreeiENSGT00390000006633.
HOGENOMiHOG000007811.
HOVERGENiHBG057907.
InParanoidiQ9HAJ7.
OMAiFYGQSCC.
OrthoDBiEOG7P5T35.
PhylomeDBiQ9HAJ7.
TreeFamiTF324135.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSAP30L. human.
GenomeRNAii79685.
PROiQ9HAJ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAJ7.
CleanExiHS_SAP30L.
GenevisibleiQ9HAJ7. HS.

Family and domain databases

InterProiIPR024145. His_deAcase_SAP30/SAP30L.
IPR025718. SAP30_Sin3-bd.
IPR025717. SAP30_zn-finger.
[Graphical view]
PANTHERiPTHR13286. PTHR13286. 1 hit.
PfamiPF13867. SAP30_Sin3_bdg. 1 hit.
PF13866. zf-SAP30. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TGF-beta induces the expression of SAP30L, a novel nuclear protein."
    Lindfors K., Viiri K.M., Niittynen M., Heinonen T.Y., Maki M., Kainulainen H.
    BMC Genomics 4:53-53(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, MUTAGENESIS OF 88-ARG-LYS-89, INDUCTION.
    Tissue: Heart.
  2. "Homo sapiens gene 2 transactivated by nonstructural protein 4A of hepatitis C virus (NS4ATP2) mRNA."
    Liu Y., Yang Y., Cheng J., Ji D., Li L., Zhang L., Chen J.
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryo.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  7. The Cancer Genome Anatomy Project (CGAP) at the National Cancer Institute
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-135 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-137 (ISOFORM 3).
    Tissue: Chronic myeloid leukemia cell and Oligodendroglioma.
  8. "FEZ1 dimerization and interaction with transcription regulatory proteins involves its coiled-coil region."
    Assmann E.M., Alborghetti M.R., Camargo M.E.R., Kobarg J.
    J. Biol. Chem. 281:9869-9881(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FEZ1.
  9. "SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus."
    Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O.
    Nucleic Acids Res. 34:3288-3298(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIN3A; HDAC1 AND HDAC2, MUTAGENESIS OF 120-ARG--LYS-127.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSP30L_HUMAN
AccessioniPrimary (citable) accession number: Q9HAJ7
Secondary accession number(s): E9PAU7, E9PAY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [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

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.