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Q9H0E3

- SP130_HUMAN

UniProt

Q9H0E3 - SP130_HUMAN

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Protein

Histone deacetylase complex subunit SAP130

Gene

SAP130

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes.1 Publication

GO - Molecular functioni

  1. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone H3 acetylation Source: UniProtKB
  3. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.
REACT_200856. NoRC negatively regulates rRNA expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase complex subunit SAP130
Alternative name(s):
130 kDa Sin3-associated polypeptide
Sin3-associated polypeptide p130
Gene namesi
Name:SAP130
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:29813. SAP130.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: HPA
  2. STAGA complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10481048Histone deacetylase complex subunit SAP130PRO_0000283736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei355 – 3551Phosphothreonine2 Publications
Modified residuei442 – 4421Phosphoserine2 Publications
Modified residuei855 – 8551Phosphoserine1 Publication
Modified residuei856 – 8561Phosphothreonine2 Publications
Modified residuei875 – 8751Phosphoserine1 Publication

Post-translational modificationi

Acetylated.1 Publication
Sumoylated with SUMO1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9H0E3.
PaxDbiQ9H0E3.
PRIDEiQ9H0E3.

PTM databases

PhosphoSiteiQ9H0E3.

Expressioni

Tissue specificityi

Expressed in various cancer cell ines.1 Publication

Gene expression databases

BgeeiQ9H0E3.
CleanExiHS_SAP130.
ExpressionAtlasiQ9H0E3. baseline and differential.
GenevestigatoriQ9H0E3.

Organism-specific databases

HPAiHPA034664.

Interactioni

Subunit structurei

Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts (released by dead or dying cells) with CLEC4E (By similarity).By similarity

Protein-protein interaction databases

BioGridi122735. 31 interactions.
IntActiQ9H0E3. 5 interactions.
MINTiMINT-1185872.
STRINGi9606.ENSP00000259235.

Structurei

3D structure databases

ProteinModelPortaliQ9H0E3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni836 – 1047212Interactions with SIN3A and HDAC1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi81 – 855Poly-Ser
Compositional biasi124 – 16946Pro-richAdd
BLAST
Compositional biasi234 – 2385Poly-Ala
Compositional biasi709 – 836128Pro-richAdd
BLAST

Domaini

The N-terminus may interact with a transcriptional coactivator.
The C-terminus may interact with HDAC-dependent and HDAC-independent corepressors.

Sequence similaritiesi

Belongs to the SAP130 family.Curated

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00440000037733.
HOGENOMiHOG000081804.
HOVERGENiHBG106600.
InParanoidiQ9H0E3.
OMAiVSAREHM.
OrthoDBiEOG7V1FPT.
PhylomeDBiQ9H0E3.
TreeFamiTF332685.

Family and domain databases

InterProiIPR024137. His_deAcase_cplx_SAP130.
[Graphical view]
PANTHERiPTHR13497. PTHR13497. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H0E3-1) [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
MGPPRHPQAG EIEAGGAGGG RRLQVEMSSQ QFPRLGAPST GLSQAPSQIA
60 70 80 90 100
NSGSAGLINP AATVNDESGR DSEVSAREHM SSSSSLQSRE EKQEPVVVRP
110 120 130 140 150
YPQVQMLSTH HAVASATPVA VTAPPAHLTP AVPLSFSEGL MKPPPKPTMP
160 170 180 190 200
SRPIAPAPPS TLSLPPKVPG QVTVTMESSI PQASAIPVAT ISGQQGHPSN
210 220 230 240 250
LHHIMTTNVQ MSIIRSNAPG PPLHIGASHL PRGAAAAAVM SSSKVTTVLR
260 270 280 290 300
PTSQLPNAAT AQPAVQHIIH QPIQSRPPVT TSNAIPPAVV ATVSATRAQS
310 320 330 340 350
PVITTTAAHA TDSALSRPTL SIQHPPSAAI SIQRPAQSRD VTTRITLPSH
360 370 380 390 400
PALGTPKQQL HTMAQKTIFS TGTPVAAATV APILATNTIP SATTAGSVSH
410 420 430 440 450
TQAPTSTIVT MTVPSHSSHA TAVTTSNIPV AKVVPQQITH TSPRIQPDYP
460 470 480 490 500
AERSSLIPIS GHRASPNPVA METRSDNRPS VPVQFQYFLP TYPPSAYPLA
510 520 530 540 550
AHTYTPITSS VSTIRQYPVS AQAPNSAITA QTGVGVASTV HLNPMQLMTV
560 570 580 590 600
DASHARHIQG IQPAPISTQG IQPAPIGTPG IQPAPLGTQG IHSATPINTQ
610 620 630 640 650
GLQPAPMGTQ QPQPEGKTSA VVLADGATIV ANPISNPFSA APAATTVVQT
660 670 680 690 700
HSQSASTNAP AQGSSPRPSI LRKKPATDGA KPKSEIHVSM ATPVTVSMET
710 720 730 740 750
VSNQNNDQPT IAVPPTAQQP PPTIPTMIAA ASPPSQPAVA LSTIPGAVPI
760 770 780 790 800
TPPITTIAAA PPPSVTVGGS LSSVLGPPVP EIKVKEEVEP MDIMRPVSAV
810 820 830 840 850
PPLATNTVSP SLALLANNLS MPTSDLPPGA SPRKKPRKQQ HVISTEEGDM
860 870 880 890 900
METNSTDDEK STAKSLLVKA EKRKSPPKEY IDEEGVRYVP VRPRPPITLL
910 920 930 940 950
RHYRNPWKAA YHHFQRYSDV RVKEEKKAML QEIANQKGVS CRAQGWKVHL
960 970 980 990 1000
CAAQLLQLTN LEHDVYERLT NLQEGIIPKK KAATDDDLHR INELIQGNMQ
1010 1020 1030 1040
RCKLVMDQIS EARDSMLKVL DHKDRVLKLL NKNGTVKKVS KLKRKEKV
Length:1,048
Mass (Da):110,324
Last modified:March 1, 2001 - v1
Checksum:iEB4E74E35BA07AEE
GO
Isoform 2 (identifier: Q9H0E3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-470: Missing.
     678-678: D → DGMAVRKTLIPPQPPDVASPRVESSMRSTSGSPRPA

Show »
Length:613
Mass (Da):65,689
Checksum:i6392B91A2F6FCDF5
GO
Isoform 3 (identifier: Q9H0E3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     678-678: D → DGMAVRKTLIPPQPPDVASPRVESSMRSTSGSPRPA

Note: No experimental confirmation available.

Show »
Length:1,083
Mass (Da):113,967
Checksum:i25C99C93FF72BF0E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 470470Missing in isoform 2. 1 PublicationVSP_024355Add
BLAST
Alternative sequencei678 – 6781D → DGMAVRKTLIPPQPPDVASP RVESSMRSTSGSPRPA in isoform 2 and isoform 3. 2 PublicationsVSP_024356

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY220791 mRNA. Translation: AAO63591.1.
AL136833 mRNA. Translation: CAB66767.1.
AK022823 mRNA. Translation: BAB14261.1.
AC118060 Genomic DNA. Translation: AAX88975.1.
AC012306 Genomic DNA. Translation: AAY14878.1.
BC017453 mRNA. Translation: AAH17453.2.
BC117255 mRNA. Translation: AAI17256.1.
BC143898 mRNA. Translation: AAI43899.1.
CCDSiCCDS2153.1. [Q9H0E3-1]
CCDS54397.1. [Q9H0E3-3]
RefSeqiNP_001139400.1. NM_001145928.1. [Q9H0E3-3]
NP_078821.2. NM_024545.3. [Q9H0E3-1]
UniGeneiHs.32995.

Genome annotation databases

EnsembliENST00000259235; ENSP00000259235; ENSG00000136715. [Q9H0E3-1]
ENST00000357702; ENSP00000350333; ENSG00000136715. [Q9H0E3-3]
GeneIDi79595.
KEGGihsa:79595.
UCSCiuc002tpp.2. human. [Q9H0E3-1]
uc002tpq.1. human. [Q9H0E3-3]

Polymorphism databases

DMDMi74717977.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY220791 mRNA. Translation: AAO63591.1 .
AL136833 mRNA. Translation: CAB66767.1 .
AK022823 mRNA. Translation: BAB14261.1 .
AC118060 Genomic DNA. Translation: AAX88975.1 .
AC012306 Genomic DNA. Translation: AAY14878.1 .
BC017453 mRNA. Translation: AAH17453.2 .
BC117255 mRNA. Translation: AAI17256.1 .
BC143898 mRNA. Translation: AAI43899.1 .
CCDSi CCDS2153.1. [Q9H0E3-1 ]
CCDS54397.1. [Q9H0E3-3 ]
RefSeqi NP_001139400.1. NM_001145928.1. [Q9H0E3-3 ]
NP_078821.2. NM_024545.3. [Q9H0E3-1 ]
UniGenei Hs.32995.

3D structure databases

ProteinModelPortali Q9H0E3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122735. 31 interactions.
IntActi Q9H0E3. 5 interactions.
MINTi MINT-1185872.
STRINGi 9606.ENSP00000259235.

Chemistry

ChEMBLi CHEMBL1229012.

PTM databases

PhosphoSitei Q9H0E3.

Polymorphism databases

DMDMi 74717977.

Proteomic databases

MaxQBi Q9H0E3.
PaxDbi Q9H0E3.
PRIDEi Q9H0E3.

Protocols and materials databases

DNASUi 79595.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259235 ; ENSP00000259235 ; ENSG00000136715 . [Q9H0E3-1 ]
ENST00000357702 ; ENSP00000350333 ; ENSG00000136715 . [Q9H0E3-3 ]
GeneIDi 79595.
KEGGi hsa:79595.
UCSCi uc002tpp.2. human. [Q9H0E3-1 ]
uc002tpq.1. human. [Q9H0E3-3 ]

Organism-specific databases

CTDi 79595.
GeneCardsi GC02M128792.
HGNCi HGNC:29813. SAP130.
HPAi HPA034664.
MIMi 609697. gene.
neXtProti NX_Q9H0E3.
PharmGKBi PA143485608.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00440000037733.
HOGENOMi HOG000081804.
HOVERGENi HBG106600.
InParanoidi Q9H0E3.
OMAi VSAREHM.
OrthoDBi EOG7V1FPT.
PhylomeDBi Q9H0E3.
TreeFami TF332685.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.
REACT_200856. NoRC negatively regulates rRNA expression.

Miscellaneous databases

ChiTaRSi SAP130. human.
GeneWikii SAP130.
GenomeRNAii 79595.
NextBioi 68614.
PROi Q9H0E3.
SOURCEi Search...

Gene expression databases

Bgeei Q9H0E3.
CleanExi HS_SAP130.
ExpressionAtlasi Q9H0E3. baseline and differential.
Genevestigatori Q9H0E3.

Family and domain databases

InterProi IPR024137. His_deAcase_cplx_SAP130.
[Graphical view ]
PANTHERi PTHR13497. PTHR13497. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of three new components of the mSin3A corepressor complex."
    Fleischer T.C., Yun U.J., Ayer D.E.
    Mol. Cell. Biol. 23:3456-3467(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, ACETYLATION, IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  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 2).
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 3).
  6. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
    Gocke C.B., Yu H., Kang J.
    J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION WITH SUMO1, SUBCELLULAR LOCATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-355; SER-442 AND SER-875, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-355; SER-442; SER-855 AND THR-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSP130_HUMAN
AccessioniPrimary (citable) accession number: Q9H0E3
Secondary accession number(s): B7ZLM3
, C9K0X9, Q4ZFV4, Q53T46, Q8WVW4, Q9H9G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 98 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3