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O15047

- SET1A_HUMAN

UniProt

O15047 - SET1A_HUMAN

Protein

Histone-lysine N-methyltransferase SETD1A

Gene

SETD1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (21 Jun 2005)
      Previous versions | rss
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    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. histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. protein binding Source: UniProtKB
    4. RNA binding Source: UniProtKB-KW

    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

    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:KIAA0339Imported, KMT2F, SET1, SET1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:29010. SETD1A.

    Subcellular locationi

    Nucleus speckle 1 Publication. Chromosome 1 Publication
    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.

    GO - Cellular componenti

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

    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 SETD1APRO_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

    1
    1707
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini84 – 17289RRMPROSITE-ProRule annotationAdd
    BLAST
    Domaini1568 – 1685118SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1691 – 170717Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1415 – 145036Interaction with CFP1Add
    BLAST
    Regioni1450 – 153788Interaction with ASH2L, RBBP5 and WDR5Add
    BLAST

    Motif

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

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti242 – 2487PCSQDTS → ACPVTHV in AAH35795. (PubMed:15489334)Curated
    Sequence conflicti1240 – 12423TEE → FLG in AAH27450. (PubMed:15489334)Curated

    Natural variant

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

    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

    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: BrainImported.
    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: BrainImported and DuodenumImported.
    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: October 1, 2014
    This is version 127 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