Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15047

- SET1A_HUMAN

UniProt

O15047 - SET1A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. 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
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: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-KW
  2. histone methyltransferase complex Source: UniProtKB
  3. nucleus Source: HPA
  4. Set1C/COMPASS complex Source: UniProtKB
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 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

BgeeiO15047.
CleanExiHS_SETD1A.
ExpressionAtlasiO15047. baseline and differential.
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. 23 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 – 1006Combined sources
Helixi107 – 1148Combined sources
Turni115 – 1173Combined sources
Beta strandi120 – 1278Combined sources
Turni129 – 1313Combined sources
Beta strandi134 – 14411Combined sources
Helixi145 – 15511Combined sources
Beta strandi166 – 1694Combined sources
Helixi174 – 18411Combined sources
Turni190 – 1923Combined sources
Helixi1494 – 14974Combined sources

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.
GeneTreeiENSGT00760000119228.
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

        10         20         30         40         50
MDQEGGGDGQ KAPSFQWRNY KLIVDPALDP ALRRPSQKVY RYDGVHFSVN
60 70 80 90 100
DSKYIPVEDL QDPRCHVRSK NRDFSLPVPK FKLDEFYIGQ IPLKEVTFAR
110 120 130 140 150
LNDNVRETFL KDMCRKYGEV EEVEILLHPR TRKHLGLARV LFTSTRGAKE
160 170 180 190 200
TVKNLHLTSV MGNIIHAQLD IKGQQRMKYY ELIVNGSYTP QTVPTGGKAL
210 220 230 240 250
SEKFQGSGAA TETAESRRRS SSDTAAYPAG TTAVGTPGNG TPCSQDTSFS
260 270 280 290 300
SSRQDTPSSF GQFTPQSSQG TPYTSRGSTP YSQDSAYSSS TTSTSFKPRR
310 320 330 340 350
SENSYQDAFS RRHFSASSAS TTASTAIAAT TAATASSSAS SSSLSSSSSS
360 370 380 390 400
SSSSSSSQFR SSDANYPAYY ESWNRYQRHT SYPPRRATRE EPPGAPFAEN
410 420 430 440 450
TAERFPPSYT SYLPPEPSRP TDQDYRPPAS EAPPPEPPEP GGGGGGGGPS
460 470 480 490 500
PEREEVRTSP RPASPARSGS PAPETTNESV PFAQHSSLDS RIEMLLKEQR
510 520 530 540 550
SKFSFLASDT EEEEENSSMV LGARDTGSEV PSGSGHGPCT PPPAPANFED
560 570 580 590 600
VAPTGSGEPG ATRESPKANG QNQASPCSSG DDMEISDDDR GGSPPPAPTP
610 620 630 640 650
PQQPPPPPPP PPPPPPYLAS LPLGYPPHQP AYLLPPRPDG PPPPEYPPPP
660 670 680 690 700
PPPPHIYDFV NSLELMDRLG AQWGGMPMSF QMQTQMLTRL HQLRQGKGLI
710 720 730 740 750
AASAGPPGGA FGEAFLPFPP PQEAAYGLPY ALYAQGQEGR GAYSREAYHL
760 770 780 790 800
PMPMAAEPLP SSSVSGEEAR LPPREEAELA EGKTLPTAGT VGRVLAMLVQ
810 820 830 840 850
EMKSIMQRDL NRKMVENVAF GAFDQWWESK EEKAKPFQNA AKQQAKEEDK
860 870 880 890 900
EKTKLKEPGL LSLVDWAKSG GTTGIEAFAF GSGLRGALRL PSFKVKRKEP
910 920 930 940 950
SEISEASEEK RPRPSTPAEE DEDDPEQEKE AGEPGRPGTK PPKRDEERGK
960 970 980 990 1000
TQGKHRKSFA LDSEGEEASQ ESSSEKDEED DEEDEEDEDR EEAVDTTKKE
1010 1020 1030 1040 1050
TEVSDGEDEE SDSSSKCSLY ADSDGENDST SDSESSSSSS SSSSSSSSSS
1060 1070 1080 1090 1100
SSSSSSSSES SSEDEEEEER PAALPSASPP PREVPVPTPA PVEVPVPERV
1110 1120 1130 1140 1150
AGSPVTPLPE QEASPARPAG PTEESPPSAP LRPPEPPAGP PAPAPRPDER
1160 1170 1180 1190 1200
PSSPIPLLPP PKKRRKTVSF SAIEVVPAPE PPPATPPQAK FPGPASRKAP
1210 1220 1230 1240 1250
RGVERTIRNL PLDHASLVKS WPEEVSRGGR SRAGGRGRLT EEEEAEPGTE
1260 1270 1280 1290 1300
VDLAVLADLA LTPARRGLPA LPAVEDSEAT ETSDEAERPR PLLSHILLEH
1310 1320 1330 1340 1350
NYALAVKPTP PAPALRPPEP VPAPAALFSS PADEVLEAPE VVVAEAEEPK
1360 1370 1380 1390 1400
PQQLQQQREE GEEEGEEEGE EEEEESSDSS SSSDGEGALR RRSLRSHARR
1410 1420 1430 1440 1450
RRPPPPPPPP PPRAYEPRSE FEQMTILYDI WNSGLDSEDM SYLRLTYERL
1460 1470 1480 1490 1500
LQQTSGADWL NDTHWVHHTI TNLTTPKRKR RPQDGPREHQ TGSARSEGYY
1510 1520 1530 1540 1550
PISKKEKDKY LDVCPVSARQ LEGVDTQGTN RVLSERRSEQ RRLLSAIGTS
1560 1570 1580 1590 1600
AIMDSDLLKL NQLKFRKKKL RFGRSRIHEW GLFAMEPIAA DEMVIEYVGQ
1610 1620 1630 1640 1650
NIRQMVADMR EKRYVQEGIG SSYLFRVDHD TIIDATKCGN LARFINHCCT
1660 1670 1680 1690 1700
PNCYAKVITI ESQKKIVIYS KQPIGVDEEI TYDYKFPLED NKIPCLCGTE

SCRGSLN
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. 23 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.
GeneTreei ENSGT00760000119228.
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

Bgeei O15047.
CleanExi HS_SETD1A.
ExpressionAtlasi O15047. baseline and differential.
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: 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 29, 2014
This is version 128 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