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O15047

- SET1A_HUMAN

UniProt

O15047 - SET1A_HUMAN

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Protein
Histone-lysine N-methyltransferase SETD1A
Gene
SETD1A, KIAA0339, KMT2F, SET1, SET1A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
  3. nucleotide binding Source: InterPro
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. histone H3-K4 methylation Source: GOC
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.43. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETD1A (EC:2.1.1.43)
Alternative name(s):
Lysine N-methyltransferase 2F
SET domain-containing protein 1A
Short name:
hSET1A
Set1/Ash2 histone methyltransferase complex subunit SET1
Gene namesi
Name:SETD1A
Synonyms:KIAA0339, KMT2F, SET1, SET1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:29010. SETD1A.

Subcellular locationi

Nucleus speckle. Chromosome
Note: Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1B, suggesting that SETD1A and SETD1B each bind to a unique set of target genes.1 Publication

GO - Cellular componenti

  1. Set1C/COMPASS complex Source: UniProtKB
  2. chromosome Source: UniProtKB-SubCell
  3. histone methyltransferase complex Source: UniProtKB
  4. nuclear speck Source: UniProtKB-SubCell
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394556.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17071707Histone-lysine N-methyltransferase SETD1A
PRO_0000186056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei508 – 5081Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO15047.
PaxDbiO15047.
PRIDEiO15047.

PTM databases

PhosphoSiteiO15047.

Expressioni

Gene expression databases

ArrayExpressiO15047.
BgeeiO15047.
CleanExiHS_SETD1A.
GenevestigatoriO15047.

Organism-specific databases

HPAiHPA020646.

Interactioni

Subunit structurei

Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with HCFC1. Interacts with ASH2/ASH2L, CXXC1/CFP1, WDR5 and RBBP5. Interacts (via the RRM domain) with WDR82. Interacts (via the RRM domain) with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) only in the presence of WDR82. Binds specifically to CTD heptad repeats phosphorylated on 'Ser-5' of each heptad. Interacts with ZNF335. Interacts with SUPT6H.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HCFC1P516102EBI-540779,EBI-396176
RBBP5Q152913EBI-540779,EBI-592823

Protein-protein interaction databases

BioGridi115088. 18 interactions.
DIPiDIP-33494N.
IntActiO15047. 13 interactions.
STRINGi9606.ENSP00000262519.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi95 – 1006
Helixi107 – 1148
Turni115 – 1173
Beta strandi120 – 1278
Turni129 – 1313
Beta strandi134 – 14411
Helixi145 – 15511
Beta strandi166 – 1694
Helixi174 – 18411
Turni190 – 1923
Helixi1494 – 14974

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S8SX-ray1.30A89-197[»]
3UVNX-ray1.79B/D1492-1502[»]
4EWRX-ray1.50C1488-1501[»]
ProteinModelPortaliO15047.
SMRiO15047. Positions 89-195.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 17289RRM
Add
BLAST
Domaini1568 – 1685118SET
Add
BLAST
Domaini1691 – 170717Post-SET
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1415 – 145036Interaction with CFP1
Add
BLAST
Regioni1450 – 153788Interaction with ASH2L, RBBP5 and WDR5
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1299 – 13035HCFC1-binding motif (HBM)

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi244 – 362119Ser-rich
Add
BLAST
Compositional biasi383 – 654272Pro-rich
Add
BLAST
Compositional biasi899 – 1010112Glu-rich
Add
BLAST
Compositional biasi1011 – 106252Ser-rich
Add
BLAST
Compositional biasi1071 – 1194124Pro-rich
Add
BLAST
Compositional biasi1334 – 137542Glu-rich
Add
BLAST
Compositional biasi1403 – 141715Pro-rich
Add
BLAST

Sequence similaritiesi

Contains 1 post-SET domain.
Contains 1 SET domain.

Phylogenomic databases

eggNOGiCOG2940.
HOGENOMiHOG000154291.
HOVERGENiHBG067119.
InParanoidiO15047.
KOiK11422.
OMAiGYLRLTY.
OrthoDBiEOG7GQXTT.
PhylomeDBiO15047.
TreeFamiTF106436.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR024657. COMPASS_Set1_N-SET.
IPR012677. Nucleotide-bd_a/b_plait.
IPR003616. Post-SET_dom.
IPR000504. RRM_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF11764. N-SET. 1 hit.
PF00076. RRM_1. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00508. PostSET. 1 hit.
SM00360. RRM. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS50868. POST_SET. 1 hit.
PS50102. RRM. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15047-1 [UniParc]FASTAAdd to Basket

« Hide

MDQEGGGDGQ KAPSFQWRNY KLIVDPALDP ALRRPSQKVY RYDGVHFSVN     50
DSKYIPVEDL QDPRCHVRSK NRDFSLPVPK FKLDEFYIGQ IPLKEVTFAR 100
LNDNVRETFL KDMCRKYGEV EEVEILLHPR TRKHLGLARV LFTSTRGAKE 150
TVKNLHLTSV MGNIIHAQLD IKGQQRMKYY ELIVNGSYTP QTVPTGGKAL 200
SEKFQGSGAA TETAESRRRS SSDTAAYPAG TTAVGTPGNG TPCSQDTSFS 250
SSRQDTPSSF GQFTPQSSQG TPYTSRGSTP YSQDSAYSSS TTSTSFKPRR 300
SENSYQDAFS RRHFSASSAS TTASTAIAAT TAATASSSAS SSSLSSSSSS 350
SSSSSSSQFR SSDANYPAYY ESWNRYQRHT SYPPRRATRE EPPGAPFAEN 400
TAERFPPSYT SYLPPEPSRP TDQDYRPPAS EAPPPEPPEP GGGGGGGGPS 450
PEREEVRTSP RPASPARSGS PAPETTNESV PFAQHSSLDS RIEMLLKEQR 500
SKFSFLASDT EEEEENSSMV LGARDTGSEV PSGSGHGPCT PPPAPANFED 550
VAPTGSGEPG ATRESPKANG QNQASPCSSG DDMEISDDDR GGSPPPAPTP 600
PQQPPPPPPP PPPPPPYLAS LPLGYPPHQP AYLLPPRPDG PPPPEYPPPP 650
PPPPHIYDFV NSLELMDRLG AQWGGMPMSF QMQTQMLTRL HQLRQGKGLI 700
AASAGPPGGA FGEAFLPFPP PQEAAYGLPY ALYAQGQEGR GAYSREAYHL 750
PMPMAAEPLP SSSVSGEEAR LPPREEAELA EGKTLPTAGT VGRVLAMLVQ 800
EMKSIMQRDL NRKMVENVAF GAFDQWWESK EEKAKPFQNA AKQQAKEEDK 850
EKTKLKEPGL LSLVDWAKSG GTTGIEAFAF GSGLRGALRL PSFKVKRKEP 900
SEISEASEEK RPRPSTPAEE DEDDPEQEKE AGEPGRPGTK PPKRDEERGK 950
TQGKHRKSFA LDSEGEEASQ ESSSEKDEED DEEDEEDEDR EEAVDTTKKE 1000
TEVSDGEDEE SDSSSKCSLY ADSDGENDST SDSESSSSSS SSSSSSSSSS 1050
SSSSSSSSES SSEDEEEEER PAALPSASPP PREVPVPTPA PVEVPVPERV 1100
AGSPVTPLPE QEASPARPAG PTEESPPSAP LRPPEPPAGP PAPAPRPDER 1150
PSSPIPLLPP PKKRRKTVSF SAIEVVPAPE PPPATPPQAK FPGPASRKAP 1200
RGVERTIRNL PLDHASLVKS WPEEVSRGGR SRAGGRGRLT EEEEAEPGTE 1250
VDLAVLADLA LTPARRGLPA LPAVEDSEAT ETSDEAERPR PLLSHILLEH 1300
NYALAVKPTP PAPALRPPEP VPAPAALFSS PADEVLEAPE VVVAEAEEPK 1350
PQQLQQQREE GEEEGEEEGE EEEEESSDSS SSSDGEGALR RRSLRSHARR 1400
RRPPPPPPPP PPRAYEPRSE FEQMTILYDI WNSGLDSEDM SYLRLTYERL 1450
LQQTSGADWL NDTHWVHHTI TNLTTPKRKR RPQDGPREHQ TGSARSEGYY 1500
PISKKEKDKY LDVCPVSARQ LEGVDTQGTN RVLSERRSEQ RRLLSAIGTS 1550
AIMDSDLLKL NQLKFRKKKL RFGRSRIHEW GLFAMEPIAA DEMVIEYVGQ 1600
NIRQMVADMR EKRYVQEGIG SSYLFRVDHD TIIDATKCGN LARFINHCCT 1650
PNCYAKVITI ESQKKIVIYS KQPIGVDEEI TYDYKFPLED NKIPCLCGTE 1700
SCRGSLN 1707
Length:1,707
Mass (Da):186,034
Last modified:June 21, 2005 - v3
Checksum:i0084217B0D425050
GO

Sequence cautioni

The sequence AAH35795.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAA20797.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti639 – 6391D → N.
Corresponds to variant rs897985 [ dbSNP | Ensembl ].
VAR_059318

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2487PCSQDTS → ACPVTHV in AAH35795. 1 Publication
Sequence conflicti1240 – 12423TEE → FLG in AAH27450. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002337 mRNA. Translation: BAA20797.2. Different initiation.
AC135048 Genomic DNA. No translation available.
BC027450 mRNA. Translation: AAH27450.1.
BC035795 mRNA. Translation: AAH35795.1. Sequence problems.
CCDSiCCDS32435.1.
RefSeqiNP_055527.1. NM_014712.1.
XP_005255780.1. XM_005255723.1.
XP_006721169.1. XM_006721106.1.
XP_006721170.1. XM_006721107.1.
UniGeneiHs.297483.

Genome annotation databases

EnsembliENST00000262519; ENSP00000262519; ENSG00000099381.
GeneIDi9739.
KEGGihsa:9739.
UCSCiuc002ead.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002337 mRNA. Translation: BAA20797.2 . Different initiation.
AC135048 Genomic DNA. No translation available.
BC027450 mRNA. Translation: AAH27450.1 .
BC035795 mRNA. Translation: AAH35795.1 . Sequence problems.
CCDSi CCDS32435.1.
RefSeqi NP_055527.1. NM_014712.1.
XP_005255780.1. XM_005255723.1.
XP_006721169.1. XM_006721106.1.
XP_006721170.1. XM_006721107.1.
UniGenei Hs.297483.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3S8S X-ray 1.30 A 89-197 [» ]
3UVN X-ray 1.79 B/D 1492-1502 [» ]
4EWR X-ray 1.50 C 1488-1501 [» ]
ProteinModelPortali O15047.
SMRi O15047. Positions 89-195.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115088. 18 interactions.
DIPi DIP-33494N.
IntActi O15047. 13 interactions.
STRINGi 9606.ENSP00000262519.

PTM databases

PhosphoSitei O15047.

Proteomic databases

MaxQBi O15047.
PaxDbi O15047.
PRIDEi O15047.

Protocols and materials databases

DNASUi 9739.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262519 ; ENSP00000262519 ; ENSG00000099381 .
GeneIDi 9739.
KEGGi hsa:9739.
UCSCi uc002ead.1. human.

Organism-specific databases

CTDi 9739.
GeneCardsi GC16P030968.
HGNCi HGNC:29010. SETD1A.
HPAi HPA020646.
MIMi 611052. gene.
neXtProti NX_O15047.
PharmGKBi PA128394556.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
HOGENOMi HOG000154291.
HOVERGENi HBG067119.
InParanoidi O15047.
KOi K11422.
OMAi GYLRLTY.
OrthoDBi EOG7GQXTT.
PhylomeDBi O15047.
TreeFami TF106436.

Enzyme and pathway databases

BRENDAi 2.1.1.43. 2681.

Miscellaneous databases

ChiTaRSi SETD1A. human.
GenomeRNAii 9739.
NextBioi 36651.
PROi O15047.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15047.
Bgeei O15047.
CleanExi HS_SETD1A.
Genevestigatori O15047.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR024657. COMPASS_Set1_N-SET.
IPR012677. Nucleotide-bd_a/b_plait.
IPR003616. Post-SET_dom.
IPR000504. RRM_dom.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF11764. N-SET. 1 hit.
PF00076. RRM_1. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00508. PostSET. 1 hit.
SM00360. RRM. 1 hit.
SM00317. SET. 1 hit.
[Graphical view ]
PROSITEi PS50868. POST_SET. 1 hit.
PS50102. RRM. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] OF 1-248 AND 1239-1707.
    Tissue: Brain and Duodenum.
  4. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
    Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
    Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HCFC1.
  5. "CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex."
    Lee J.-H., Skalnik D.G.
    J. Biol. Chem. 280:41725-41731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SET1 COMPLEX.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex."
    Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.
    J. Biol. Chem. 282:13419-13428(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET1 COMPLEX.
  8. "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes."
    Lee J.H., Skalnik D.G.
    Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH ASH2L; RBBP5; CXXC1; HCFC1; WDR5; WDR82 AND POLR2A.
  9. "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS."
    Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A.
    Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SET1 COMPLEX.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: INTERACTION WITH ZNF335.
  16. "The histone chaperone Spt6 is required for activation-induced cytidine deaminase target determination through H3K4me3 regulation."
    Begum N.A., Stanlie A., Nakata M., Akiyama H., Honjo T.
    J. Biol. Chem. 287:32415-32429(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUPT6H.

Entry informationi

Entry nameiSET1A_HUMAN
AccessioniPrimary (citable) accession number: O15047
Secondary accession number(s): A6NP62, Q6PIF3, Q8TAJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: September 3, 2014
This is version 126 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi