Q01105 (SET_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

SET

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.25 Ref.30
Subcellular location	Cytoplasm › cytosol. Endoplasmic reticulum. Nucleus › nucleoplasm. 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.30
Post-translational modification	Isoform 2 is phosphorylated on Ser-15 and Thr-23. Isoform 2 is acetylated on Lys-11. 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 component	Cytoplasm Endoplasmic reticulum Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Ligand	DNA-binding
Molecular function	Chaperone
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Traceable author statement Ref.3. Source: ProtInc gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome 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-dependent Inferred from direct assay Ref.25. 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
Cellular_component	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 perinuclear region of cytoplasm Inferred from direct assay PubMed 11555662Ref.19. Source: UniProtKB protein complex Inferred from direct assay Ref.16. Source: UniProtKB
Molecular_function	DNA 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDM2	Q00987	2	EBI-1053182,EBI-389668
PRKAR1A	P10644	2	EBI-1053182,EBI-476431

Alternative products

This entry describes 3 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:
     1-37: MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MSAPAAKVSKKELNSNHDGADETS

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

Isoform 3 (identifier: Q01105-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MPRSHQPPPPPH

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 290

289

Protein SET

PRO_0000185662

Regions

Region

31 – 78

48

Dimerization

Region

79 – 225

147

Earmuff domain

Compositional bias

239 – 290

52

Asp/Glu-rich (highly acidic)

Sites

Site

283 – 284

2

Breakpoint for translocation to form SET-CAN oncogene

Amino acid modifications

Modified residue

2

1

N,N,N-trimethylalanine By similarity

Modified residue

7

1

Phosphoserine Ref.20 Ref.22 Ref.27

Modified residue

30

1

Phosphoserine By similarity

Modified residue

132

1

N6-acetyllysine Ref.26

Modified residue

146

1

Phosphotyrosine By similarity

Modified residue

150

1

N6-acetyllysine Ref.26

Modified residue

172

1

N6-acetyllysine Ref.26

Cross-link

154

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

Natural variations

Alternative sequence

1 – 37

37

MAPKR…LPKKG → MSAPAAKVSKKELNSNHDGA DETS in isoform 2.

VSP_009868

Alternative sequence

1 – 37

37

MAPKR…LPKKG → MPRSHQPPPPPH in isoform 3.

VSP_045175

Isoform 2:

Natural variant

4

1

P → Q.
Corresponds to variant rs1141138 [ dbSNP | Ensembl ].

Secondary structure

1

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290

Helix Strand Turn

Details...

Helix

38 – 88

51

Helix

94 – 100

7

Helix

103 – 106

4

Helix

111 – 116

6

Helix

117 – 119

3

Beta strand

120 – 127

8

Beta strand

135 – 141

7

Beta strand

145 – 148

4

Beta strand

150 – 156

7

Beta strand

166 – 168

3

Helix

203 – 206

4

Helix

215 – 223

9

Turn

224 – 227

4

Helix

230 – 233

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TAF-I alpha) [UniParc]. Last modified April 13, 2004. Version 3. Checksum: F4664118171EF230	FASTA	290	33,489
	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
	Isoform 2 (TAF-I beta) [UniParc]. Checksum: 52A6F516686010CE	FASTA	277	32,103
	10 20 30 40 50 60 MSAPAAKVSK KELNSNHDGA DETSEKEQQE AIEHIDEVQN EIDRLNEQAS EEILKVEQKY 70 80 90 100 110 120 NKLRQPFFQK RSELIAKIPN FWVTTFVNHP QVSALLGEED EEALHYLTRV EVTEFEDIKS 130 140 150 160 170 180 GYRIDFYFDE NPYFENKVLS KEFHLNESGD PSSKSTEIKW KSGKDLTKRS SQTQNKASRK 190 200 210 220 230 240 RQHEEPESFF TWFTDHSDAG ADELGEVIKD DIWPNPLQYY LVPDMDDEEG EGEEDDDDDE 250 260 270 EEEGLEDIDE EGDEDEGEED EDDDEGEEGE EDEGEDD
	Isoform 3 [UniParc]. Checksum: A9B69B63736E06F4	FASTA	265	30,993
	10 20 30 40 50 60 MPRSHQPPPP PHEKEQQEAI EHIDEVQNEI DRLNEQASEE ILKVEQKYNK LRQPFFQKRS 70 80 90 100 110 120 ELIAKIPNFW VTTFVNHPQV SALLGEEDEE ALHYLTRVEV TEFEDIKSGY RIDFYFDENP 130 140 150 160 170 180 YFENKVLSKE FHLNESGDPS SKSTEIKWKS GKDLTKRSSQ TQNKASRKRQ HEEPESFFTW 190 200 210 220 230 240 FTDHSDAGAD ELGEVIKDDI WPNPLQYYLV PDMDDEEGEG EEDDDDDEEE EGLEDIDEEG 250 260 DEDEGEEDED DDEGEEGEED EGEDD

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-154, MASS SPECTROMETRY.
[24]	"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.
[25]	"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.
[26]	"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), MASS SPECTROMETRY.
[27]	"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), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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].
[29]	"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), MASS SPECTROMETRY.
[30]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
AL359678 Genomic DNA. No translation available.
AL356481 Genomic DNA. Translation: CAH71410.1.
BC032749 mRNA. Translation: AAH32749.1.
EF534308 mRNA. Translation: ABP96841.1.

IPI

IPI00072377.
IPI00301311.

PIR

A45018. A57984.
I59377.

RefSeq

NP_001116293.1. NM_001122821.1.
NP_001234929.1. NM_001248000.1.
NP_001234930.1. NM_001248001.1.
NP_003002.2. NM_003011.3.

UniGene

Hs.436687.
Hs.596814.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E50	X-ray	2.30	A/B/P/Q	38-238	[»]

ProteinModelPortal

Q01105.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33561N.

IntAct

Q01105. 62 interactions.

MINT

MINT-4990855.

STRING

9606.ENSP00000361777.

PTM databases

PhosphoSite

Q01105.

Polymorphism databases

DMDM

46397790.

Proteomic databases

PaxDb

Q01105.

PeptideAtlas

Q01105.

PRIDE

Q01105.

Protocols and materials databases

DNASU

6418.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322030; ENSP00000318012; ENSG00000119335.
ENST00000372686; ENSP00000361771; ENSG00000119335.
ENST00000372688; ENSP00000361773; ENSG00000119335.
ENST00000372692; ENSP00000361777; ENSG00000119335.

GeneID

6418.

KEGG

hsa:6418.

UCSC

uc004bvt.4. human.
uc004bvu.4. human.
uc011mbj.2. human.

Organism-specific databases

CTD

6418.

GeneCards

GC09P131445.

HGNC

HGNC:10760. SET.

HPA

CAB005232.

MIM

600960. gene.

neXtProt

NX_Q01105.

PharmGKB

PA35678.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG260846.

HOGENOM

HOG000232096.

HOVERGEN

HBG014779.

InParanoid

Q01105.

KO

K11290.

OMA

TWFTDHA.

OrthoDB

EOG41RPV7.

PhylomeDB

Q01105.

Enzyme and pathway databases

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q01105.

Bgee

Q01105.

CleanEx

HS_SET.

Genevestigator

Q01105.

GermOnline

ENSG00000119335. Homo sapiens.

Family and domain databases

InterPro

IPR002164. NAP_family.
[Graphical view]

PANTHER

PTHR11875. PTHR11875. 1 hit.

Pfam

PF00956. NAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SET. human.

EvolutionaryTrace

Q01105.

GenomeRNAi

6418.

NextBio

24926.

SOURCE

Search...

Entry information

Entry name

SET_HUMAN

Accession

Primary (citable) accession number: Q01105
Secondary accession number(s): A5A5H4 , A6NGV1, B4DUE2, Q15541, Q5VXV1, Q6FHZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 13, 2004
Last modified:	May 29, 2013
This is version 141 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.