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Q01105 (SET_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SET
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with CHTOP By similarity. Headphone-shaped homodimer. Isoform 1 and isoform 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, which also contains ANP32A, APEX1, HMGB2 and NME1, but not NME2. Within this complex, directly interacts with NME1 and with HMGB2. Interacts with SETBP1. Interacts with SGOL1. Interacts with APBB1. Ref.15 Ref.16 Ref.21 Ref.24 Ref.29

Subcellular location

Cytoplasmcytosol. Endoplasmic reticulum. Nucleusnucleoplasm. Note: In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. Following CTL attack, 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. The SET complex is associated with the endoplasmic reticulum. Ref.17 Ref.19

Tissue specificity

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

Domain

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. Ref.29

Post-translational modification

Isoform 2 is phosphorylated on Ser-15 and Thr-23.

Isoform 2 is acetylated on Lys-11. Ref.14

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.

Involvement in disease

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.

Sequence similarities

Belongs to the nucleosome assembly protein (NAP) family.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   LigandDNA-binding
   Molecular functionChaperone
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Traceable author statement Ref.3. Source: ProtInc

RNA metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of catalytic activity

Traceable author statement Ref.4. Source: GOC

negative regulation of histone acetylation

Traceable author statement PubMed 11555662. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 18374643. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.24. Source: UniProtKB

nucleocytoplasmic transport

Non-traceable author statement PubMed 11555662. Source: UniProtKB

nucleosome assembly

Traceable author statement Ref.1. Source: ProtInc

nucleosome disassembly

Traceable author statement PubMed 11555662. Source: UniProtKB

regulation of catalytic activity

Traceable author statement PubMed 11555662. Source: GOC

   Cellular_componentcytoplasm

Inferred from direct assay Ref.16Ref.19. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from direct assay PubMed 11555662Ref.19. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11555662. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 11555662Ref.19. Source: UniProtKB

protein complex

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone binding

Traceable author statement PubMed 11555662. Source: UniProtKB

protein phosphatase inhibitor activity

Traceable author statement Ref.4. Source: ProtInc

protein phosphatase type 2A regulator activity

Traceable author statement PubMed 11555662. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01105-1)

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.
Isoform 2 (identifier: Q01105-2)

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.
Isoform 3 (identifier: Q01105-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-37: APKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MPRSHQPPPPPH
Isoform 4 (identifier: Q01105-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2-37: APKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MGCRDLLPSLKPTLL
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 290289Protein SET
PRO_0000185662

Regions

Region31 – 7848Dimerization
Region79 – 225147Earmuff domain
Compositional bias239 – 29052Asp/Glu-rich (highly acidic)

Sites

Site283 – 2842Breakpoint for translocation to form SET-CAN oncogene

Amino acid modifications

Modified residue21N,N,N-trimethylalanine By similarity
Modified residue71Phosphoserine Ref.20 Ref.22 Ref.26
Modified residue681N6-acetyllysine By similarity
Modified residue1321N6-acetyllysine Ref.25
Modified residue1461Phosphotyrosine By similarity
Modified residue1501N6-acetyllysine Ref.25
Modified residue1721N6-acetyllysine Ref.25
Cross-link154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence2 – 3736APKRQ…LPKKG → MSAPAAKVSKKELNSNHDGA DETS in isoform 2.
VSP_009868
Alternative sequence2 – 3736APKRQ…LPKKG → MPRSHQPPPPPH in isoform 3.
VSP_045175
Alternative sequence2 – 3736APKRQ…LPKKG → MGCRDLLPSLKPTLL in isoform 4.
VSP_046741
Isoform 2:
Natural variant41A → Q.
Corresponds to variant rs1141138 [ dbSNP | Ensembl ].

Secondary structure

.......................... 290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TAF-I alpha) [UniParc].

Last modified April 13, 2004. Version 3.
Checksum: F4664118171EF230

FASTA29033,489
        10         20         30         40         50         60 
MAPKRQSPLP PQKKKPRPPP ALGPEETSAS AGLPKKGEKE QQEAIEHIDE VQNEIDRLNE 

        70         80         90        100        110        120 
QASEEILKVE QKYNKLRQPF FQKRSELIAK IPNFWVTTFV NHPQVSALLG EEDEEALHYL 

       130        140        150        160        170        180 
TRVEVTEFED IKSGYRIDFY FDENPYFENK VLSKEFHLNE SGDPSSKSTE IKWKSGKDLT 

       190        200        210        220        230        240 
KRSSQTQNKA SRKRQHEEPE SFFTWFTDHS DAGADELGEV IKDDIWPNPL QYYLVPDMDD 

       250        260        270        280        290 
EEGEGEEDDD DDEEEEGLED IDEEGDEDEG EEDEDDDEGE EGEEDEGEDD 

« Hide

Isoform 2 (TAF-I beta) [UniParc].

Checksum: CB8FB882987E38F7
Show »

FASTA27832,234
Isoform 3 [UniParc].

Checksum: A9A076FE734F8EC4
Show »

FASTA26631,124
Isoform 4 [UniParc].

Checksum: 5D51BD1DC837D602
Show »

FASTA26931,404

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
[17]"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: NME1 INHIBITION, SUBCELLULAR LOCATION, DESCRIPTION OF THE SET COMPLEX.
[18]Erratum
Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
Cell 115:241-241(2003)
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4."
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.
PLoS ONE 4:E5071-E5071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APBB1.
[25]"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].
[26]"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.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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].
[29]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA45018. A57984.
I59377.
RefSeqNP_001116293.1. NM_001122821.1.
NP_001234929.1. NM_001248000.1.
NP_001234930.1. NM_001248001.1.
NP_003002.2. NM_003011.3.
UniGeneHs.436687.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E50X-ray2.30A/B/P/Q38-238[»]
ProteinModelPortalQ01105.
SMRQ01105. Positions 38-236.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112316. 103 interactions.
DIPDIP-33561N.
IntActQ01105. 74 interactions.
MINTMINT-4990855.
STRING9606.ENSP00000361777.

PTM databases

PhosphoSiteQ01105.

Polymorphism databases

DMDM46397790.

Proteomic databases

PaxDbQ01105.
PeptideAtlasQ01105.
PRIDEQ01105.

Protocols and materials databases

DNASU6418.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322030; ENSP00000318012; ENSG00000119335. [Q01105-2]
ENST00000372686; ENSP00000361771; ENSG00000119335. [Q01105-3]
ENST00000372688; ENSP00000361773; ENSG00000119335.
ENST00000372692; ENSP00000361777; ENSG00000119335. [Q01105-1]
ENST00000409104; ENSP00000387321; ENSG00000119335. [Q01105-4]
GeneID6418.
KEGGhsa:6418.
UCSCuc004bvt.4. human. [Q01105-1]
uc004bvu.4. human. [Q01105-2]
uc011mbj.2. human.

Organism-specific databases

CTD6418.
GeneCardsGC09P131445.
HGNCHGNC:10760. SET.
HPACAB005232.
MIM600960. gene.
neXtProtNX_Q01105.
PharmGKBPA35678.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260846.
HOGENOMHOG000232096.
HOVERGENHBG014779.
InParanoidQ01105.
KOK11290.
OMAFEIENGG.
PhylomeDBQ01105.
TreeFamTF313386.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ01105.
BgeeQ01105.
CleanExHS_SET.
GenevestigatorQ01105.

Family and domain databases

InterProIPR002164. NAP_family.
[Graphical view]
PANTHERPTHR11875. PTHR11875. 1 hit.
PfamPF00956. NAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSET. human.
EvolutionaryTraceQ01105.
GeneWikiProtein_SET.
GenomeRNAi6418.
NextBio24926.
PROQ01105.
SOURCESearch...

Entry information

Entry nameSET_HUMAN
AccessionPrimary (citable) accession number: Q01105
Secondary accession number(s): A5A5H4 expand/collapse secondary AC list , A6NGV1, B4DUE2, Q15541, Q5VXV1, Q5VXV2, Q6FHZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 13, 2004
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM