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Q01105

- SET_HUMAN

UniProt

Q01105 - SET_HUMAN

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Protein

Protein SET

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

Functioni

Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei283 – 2842Breakpoint for translocation to form SET-CAN oncogene

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. histone binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. protein phosphatase inhibitor activity Source: ProtInc
  5. protein phosphatase type 2A regulator activity Source: UniProtKB

GO - Biological processi

  1. DNA replication Source: ProtInc
  2. gene expression Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. negative regulation of catalytic activity Source: GOC
  6. negative regulation of histone acetylation Source: UniProtKB
  7. negative regulation of neuron apoptotic process Source: MGI
  8. negative regulation of transcription, DNA-templated Source: UniProtKB
  9. nucleocytoplasmic transport Source: UniProtKB
  10. nucleosome assembly Source: ProtInc
  11. nucleosome disassembly Source: UniProtKB
  12. regulation of catalytic activity Source: GOC
  13. RNA metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_172744. Condensation of Prophase Chromosomes.
REACT_25218. HuR stabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SET
Alternative name(s):
HLA-DR-associated protein II
Inhibitor of granzyme A-activated DNase
Short name:
IGAAD
PHAPII
Phosphatase 2A inhibitor I2PP2A
Short name:
I-2PP2A
Template-activating factor I
Short name:
TAF-I
Gene namesi
Name:SET
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:10760. SET.

Subcellular locationi

Cytoplasmcytosol. Endoplasmic reticulum. Nucleusnucleoplasm
Note: In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavage by GZMA, moves rapidly to the nucleus, where it is found in the nucleoplasm, avoiding the nucleolus. Similar translocation to the nucleus is also observed for lymphocyte-activated killer cells after the addition of calcium.4 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB-SubCell
  3. endoplasmic reticulum Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. perinuclear region of cytoplasm Source: UniProtKB
  7. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving SET is found in some cases of acute undifferentiated leukemia (AUL). Translocation t(6;9)(q21;q34.1) with NUP214/CAN.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA35678.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 290289Protein SETPRO_0000185662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N,N,N-trimethylalanine By similarity
Modified residuei7 – 71Phosphoserine3 Publications
Modified residuei68 – 681N6-acetyllysine By similarity
Modified residuei132 – 1321N6-acetyllysine1 Publication
Modified residuei146 – 1461Phosphotyrosine By similarity
Modified residuei150 – 1501N6-acetyllysine1 Publication
Cross-linki154 – 154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei172 – 1721N6-acetyllysine1 Publication

Post-translational modificationi

Isoform 2 is phosphorylated on Ser-15 and Thr-23.
Isoform 2 is acetylated on Lys-11.1 Publication
Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group By similarity.
N-terminus of isoform 1 is methylated by METTL11A/NTM1. Mainly trimethylated By similarity.
Isoform 2 is cleaved after Lys-176 by GZMA. The cleavage inhibits its nucelosome assembly activity and disrupts the inhibition on NME1.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ01105.
PaxDbiQ01105.
PeptideAtlasiQ01105.
PRIDEiQ01105.

PTM databases

PhosphoSiteiQ01105.

Expressioni

Tissue specificityi

Widely expressed. Low levels in quiescent cells during serum starvation, contact inhibition or differentiation. Highly expressed in Wilms' tumor.

Gene expression databases

ArrayExpressiQ01105.
BgeeiQ01105.
CleanExiHS_SET.
GenevestigatoriQ01105.

Organism-specific databases

HPAiCAB005232.

Interactioni

Subunit structurei

Headphone-shaped homodimer. Isoforms 1 and 2 interact directly with each other and with ANP32A within the tripartite INHAT (inhibitor of acetyltransferases) complex. Isoform 1 and isoform 2 interact also with histones. Isoform 2 is a component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1, but not NME2 or TREX2. Within this complex, directly interacts with ANP32A, NME1, HMGB2 and TREX1; the interaction with ANP32A is enhanced after cleavage. Interacts with APBB1, CHTOP, SETBP1, SGOL1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM2Q009872EBI-1053182,EBI-389668
PRKAR1AP106442EBI-1053182,EBI-476431
RAC1P630008EBI-1053182,EBI-413628
TAF1AQ155732EBI-1053182,EBI-2510647
TAF1BQ53T943EBI-1053182,EBI-1560239
TAF1CQ155724EBI-1053182,EBI-2510659
TBPP202264EBI-1053182,EBI-355371
UBTFP174804EBI-1053182,EBI-396235

Protein-protein interaction databases

BioGridi112316. 105 interactions.
DIPiDIP-33561N.
IntActiQ01105. 74 interactions.
MINTiMINT-4990855.
STRINGi9606.ENSP00000361777.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 8851
Helixi94 – 1007
Helixi103 – 1064
Helixi111 – 1166
Helixi117 – 1193
Beta strandi120 – 1278
Beta strandi135 – 1417
Beta strandi145 – 1484
Beta strandi150 – 1567
Beta strandi166 – 1683
Helixi203 – 2064
Helixi215 – 2239
Turni224 – 2274
Helixi230 – 2334

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E50X-ray2.30A/B/P/Q38-238[»]
ProteinModelPortaliQ01105.
SMRiQ01105. Positions 38-236.

Miscellaneous databases

EvolutionaryTraceiQ01105.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 7848DimerizationAdd
BLAST
Regioni79 – 225147Earmuff domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi239 – 29052Asp/Glu-rich (highly acidic)Add
BLAST

Domaini

A long alpha helix in the N-terminus mediates dimerization, while the earmuff domain is responsible for core histone and dsDNA binding. The C-terminal acidic domain mediates the inhibition of histone acetyltransferases and is required for the DNA replication stimulatory activity.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG260846.
HOGENOMiHOG000232096.
HOVERGENiHBG014779.
InParanoidiQ01105.
KOiK11290.
OMAiTWFTDHA.
PhylomeDBiQ01105.
TreeFamiTF313386.

Family and domain databases

InterProiIPR002164. NAP_family.
[Graphical view]
PANTHERiPTHR11875. PTHR11875. 1 hit.
PfamiPF00956. NAP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q01105-1) [UniParc]FASTAAdd to Basket

Also known as: TAF-I alpha

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

MAPKRQSPLP PQKKKPRPPP ALGPEETSAS AGLPKKGEKE QQEAIEHIDE    50
VQNEIDRLNE QASEEILKVE QKYNKLRQPF FQKRSELIAK IPNFWVTTFV 100
NHPQVSALLG EEDEEALHYL TRVEVTEFED IKSGYRIDFY FDENPYFENK 150
VLSKEFHLNE SGDPSSKSTE IKWKSGKDLT KRSSQTQNKA SRKRQHEEPE 200
SFFTWFTDHS DAGADELGEV IKDDIWPNPL QYYLVPDMDD EEGEGEEDDD 250
DDEEEEGLED IDEEGDEDEG EEDEDDDEGE EGEEDEGEDD 290
Length:290
Mass (Da):33,489
Last modified:April 13, 2004 - v3
Checksum:iF4664118171EF230
GO
Isoform 2 (identifier: Q01105-2) [UniParc]FASTAAdd to Basket

Also known as: TAF-I beta

The sequence of this isoform differs from the canonical sequence as follows:
     2-37: APKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MSAPAAKVSKKELNSNHDGADETS

Note: Contains a N6-acetyllysine at position 11. Contains a phosphoserine at position 15. Contains a phosphoserine at position 24.

Show »
Length:278
Mass (Da):32,234
Checksum:iCB8FB882987E38F7
GO
Isoform 3 (identifier: Q01105-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-37: APKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MPRSHQPPPPPH

Show »
Length:266
Mass (Da):31,124
Checksum:iA9A076FE734F8EC4
GO
Isoform 4 (identifier: Q01105-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-37: APKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MGCRDLLPSLKPTLL

Note: Gene prediction based on EST data.

Show »
Length:269
Mass (Da):31,404
Checksum:i5D51BD1DC837D602
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: Q01105-2)
Natural varianti4 – 41A → Q.
Corresponds to variant rs1141138 [ dbSNP | Ensembl ].

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 3736APKRQ…LPKKG → MSAPAAKVSKKELNSNHDGA DETS in isoform 2. VSP_009868Add
BLAST
Alternative sequencei2 – 3736APKRQ…LPKKG → MPRSHQPPPPPH in isoform 3. VSP_045175Add
BLAST
Alternative sequencei2 – 3736APKRQ…LPKKG → MGCRDLLPSLKPTLL in isoform 4. VSP_046741Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93651 mRNA. Translation: AAA60318.1.
X75091 mRNA. Translation: CAA52982.1.
D45198 mRNA. Translation: BAA08139.1.
U51924 mRNA. Translation: AAC50460.1.
AY349172 mRNA. Translation: AAQ79833.1.
CR536543 mRNA. Translation: CAG38780.1.
CR542050 mRNA. Translation: CAG46847.1.
AK223556 mRNA. Translation: BAD97276.1.
AK300609 mRNA. Translation: BAG62304.1.
AL356481 Genomic DNA. Translation: CAH71410.1.
AL359678 Genomic DNA. No translation available.
BC032749 mRNA. Translation: AAH32749.1.
EF534308 mRNA. Translation: ABP96841.1.
CCDSiCCDS48037.1. [Q01105-1]
CCDS59150.1. [Q01105-3]
PIRiA57984. A45018.
I59377.
RefSeqiNP_001116293.1. NM_001122821.1. [Q01105-1]
NP_001234929.1. NM_001248000.1.
NP_001234930.1. NM_001248001.1. [Q01105-3]
NP_003002.2. NM_003011.3.
UniGeneiHs.436687.

Genome annotation databases

EnsembliENST00000322030; ENSP00000318012; ENSG00000119335. [Q01105-2]
ENST00000372686; ENSP00000361771; ENSG00000119335. [Q01105-3]
ENST00000372688; ENSP00000361773; ENSG00000119335.
ENST00000372692; ENSP00000361777; ENSG00000119335. [Q01105-1]
ENST00000409104; ENSP00000387321; ENSG00000119335. [Q01105-4]
GeneIDi6418.
KEGGihsa:6418.
UCSCiuc004bvt.4. human. [Q01105-1]
uc004bvu.4. human. [Q01105-2]
uc011mbj.2. human.

Polymorphism databases

DMDMi46397790.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93651 mRNA. Translation: AAA60318.1 .
X75091 mRNA. Translation: CAA52982.1 .
D45198 mRNA. Translation: BAA08139.1 .
U51924 mRNA. Translation: AAC50460.1 .
AY349172 mRNA. Translation: AAQ79833.1 .
CR536543 mRNA. Translation: CAG38780.1 .
CR542050 mRNA. Translation: CAG46847.1 .
AK223556 mRNA. Translation: BAD97276.1 .
AK300609 mRNA. Translation: BAG62304.1 .
AL356481 Genomic DNA. Translation: CAH71410.1 .
AL359678 Genomic DNA. No translation available.
BC032749 mRNA. Translation: AAH32749.1 .
EF534308 mRNA. Translation: ABP96841.1 .
CCDSi CCDS48037.1. [Q01105-1 ]
CCDS59150.1. [Q01105-3 ]
PIRi A57984. A45018.
I59377.
RefSeqi NP_001116293.1. NM_001122821.1. [Q01105-1 ]
NP_001234929.1. NM_001248000.1.
NP_001234930.1. NM_001248001.1. [Q01105-3 ]
NP_003002.2. NM_003011.3.
UniGenei Hs.436687.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E50 X-ray 2.30 A/B/P/Q 38-238 [» ]
ProteinModelPortali Q01105.
SMRi Q01105. Positions 38-236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112316. 105 interactions.
DIPi DIP-33561N.
IntActi Q01105. 74 interactions.
MINTi MINT-4990855.
STRINGi 9606.ENSP00000361777.

PTM databases

PhosphoSitei Q01105.

Polymorphism databases

DMDMi 46397790.

Proteomic databases

MaxQBi Q01105.
PaxDbi Q01105.
PeptideAtlasi Q01105.
PRIDEi Q01105.

Protocols and materials databases

DNASUi 6418.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322030 ; ENSP00000318012 ; ENSG00000119335 . [Q01105-2 ]
ENST00000372686 ; ENSP00000361771 ; ENSG00000119335 . [Q01105-3 ]
ENST00000372688 ; ENSP00000361773 ; ENSG00000119335 .
ENST00000372692 ; ENSP00000361777 ; ENSG00000119335 . [Q01105-1 ]
ENST00000409104 ; ENSP00000387321 ; ENSG00000119335 . [Q01105-4 ]
GeneIDi 6418.
KEGGi hsa:6418.
UCSCi uc004bvt.4. human. [Q01105-1 ]
uc004bvu.4. human. [Q01105-2 ]
uc011mbj.2. human.

Organism-specific databases

CTDi 6418.
GeneCardsi GC09P131445.
HGNCi HGNC:10760. SET.
HPAi CAB005232.
MIMi 600960. gene.
neXtProti NX_Q01105.
PharmGKBi PA35678.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG260846.
HOGENOMi HOG000232096.
HOVERGENi HBG014779.
InParanoidi Q01105.
KOi K11290.
OMAi TWFTDHA.
PhylomeDBi Q01105.
TreeFami TF313386.

Enzyme and pathway databases

Reactomei REACT_172744. Condensation of Prophase Chromosomes.
REACT_25218. HuR stabilizes mRNA.

Miscellaneous databases

ChiTaRSi SET. human.
EvolutionaryTracei Q01105.
GeneWikii Protein_SET.
GenomeRNAii 6418.
NextBioi 24926.
PROi Q01105.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01105.
Bgeei Q01105.
CleanExi HS_SET.
Genevestigatori Q01105.

Family and domain databases

InterProi IPR002164. NAP_family.
[Graphical view ]
PANTHERi PTHR11875. PTHR11875. 1 hit.
Pfami PF00956. NAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene."
    von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A., Grosveld G.
    Mol. Cell. Biol. 12:3346-3355(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII."
    Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T., Zimmermann B., Kratzin H.D., Hilschmann N.
    Biol. Chem. Hoppe-Seyler 375:113-126(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
  3. "Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis."
    Nagata K., Kawase H., Handa H., Yano K., Yamasaki M., Ishimi Y., Okuda A., Kikuchi A., Matsumoto K.
    Proc. Natl. Acad. Sci. U.S.A. 92:4279-4283(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 14-35; 40-60; 75-90 AND 155-167, ACTIVATION OF DNA REPLICATION.
    Tissue: Cervix carcinoma.
  4. "The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A."
    Li M., Makkinje A., Damuni Z.
    J. Biol. Chem. 271:11059-11062(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Kidney.
  5. "Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau."
    Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.
    FEBS Lett. 579:363-372(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  8. "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 3).
  9. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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 2).
    Tissue: Testis.
  11. "Identification and characterization of SET, a nuclear phosphoprotein encoded by the translocation break point in acute undifferentiated leukemia."
    Adachi Y., Pavlaki G.N., Copeland T.D.
    J. Biol. Chem. 269:2258-2262(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
  12. "A relative factor in human rectum carcinoma."
    Wang L.C., Chen Y.
    Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-241 (ISOFORM 2).
  13. "Expression of SET, an inhibitor of protein phosphatase 2A, in renal development and Wilms' tumor."
    Carlson S.G., Eng E., Kim E.-G., Perlman E.J., Copeland T.D., Ballermann B.J.
    J. Am. Soc. Nephrol. 9:1873-1880(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPRESSION IN THE KIDNEY.
  14. "Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein."
    Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.
    Cell 104:119-130(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION OF HISTONE ACETYLATION.
  15. "Identification and characterization of SEB, a novel protein that binds to the acute undifferentiated leukemia-associated protein SET."
    Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D., Ueda K., Adachi Y.
    Eur. J. Biochem. 268:1340-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETBP1.
    Tissue: Cervix carcinoma.
  16. "Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks."
    Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J.
    J. Biol. Chem. 276:43285-43293(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AN32A, CLEAVAGE AT LYS-189, SUBCELLULAR LOCATION.
  17. "HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A."
    Fan Z., Beresford P.J., Zhang D., Lieberman J.
    Mol. Cell. Biol. 22:2810-2820(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HMGB2, IDENTIFICATION IN THE SET COMPLEX.
  18. "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
    Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
    Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NME1 INHIBITION, INTERACTION WITH NME1, SUBCELLULAR LOCATION, DESCRIPTION OF THE SET COMPLEX, CLEAVAGE BY GZMA.
  19. Erratum
    Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
    Cell 115:241-241(2003)
  20. "Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A."
    Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., Pommier Y., Lieberman J.
    Nat. Immunol. 4:145-153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  21. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
    Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
    Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TREX1, IDENTIFICATION IN THE SET COMPLEX, CLEAVAGE BY GZMA, SUBCELLULAR LOCATION.
  23. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
    Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
    Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGOL1.
  24. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: INTERACTION WITH APBB1.
  27. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-150 AND LYS-172, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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 SER-7, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "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 SER-15 AND SER-24 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity."
    Muto S., Senda M., Akai Y., Sato L., Suzuki T., Nagai R., Senda T., Horikoshi M.
    Proc. Natl. Acad. Sci. U.S.A. 104:4285-4290(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-238, DNA-BINDING, DOMAINS, SUBUNIT.

Entry informationi

Entry nameiSET_HUMAN
AccessioniPrimary (citable) accession number: Q01105
Secondary accession number(s): A5A5H4
, A6NGV1, B4DUE2, Q15541, Q5VXV1, Q5VXV2, Q6FHZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 13, 2004
Last modified: September 3, 2014
This is version 153 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

External Data

Dasty 3

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