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Q86YP4

- P66A_HUMAN

UniProt

Q86YP4 - P66A_HUMAN

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Protein
Transcriptional repressor p66-alpha
Gene
GATAD2A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri411 – 46454GATA-type
Add
BLAST

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein binding, bridging Source: UniProtKB
  3. sequence-specific DNA binding Source: InterPro
  4. sequence-specific DNA binding transcription factor activity Source: InterPro
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA methylation Source: UniProtKB
  2. anterior neuropore closure Source: Ensembl
  3. blood vessel development Source: Ensembl
  4. embryonic body morphogenesis Source: Ensembl
  5. in utero embryonic development Source: Ensembl
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
  7. neural fold formation Source: Ensembl
  8. programmed cell death Source: Ensembl
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_953. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional repressor p66-alpha
Short name:
Hp66alpha
Alternative name(s):
GATA zinc finger domain-containing protein 2A
Gene namesi
Name:GATAD2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:29989. GATAD2A.

Subcellular locationi

Nucleus speckle
Note: Speckled nuclear localization requires both CR1 and CR2 regions.2 Publications

GO - Cellular componenti

  1. NuRD complex Source: UniProtKB
  2. nuclear speck Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi149 – 1491K → R: Disruption of MBD2-binding, loss of enhancement of MBD2-mediated repression and loss of speckled nuclear localization. 1 Publication

Organism-specific databases

PharmGKBiPA142671746.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Transcriptional repressor p66-alpha
PRO_0000083500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491Phosphothreonine5 Publications
Modified residuei100 – 1001Phosphoserine6 Publications
Modified residuei107 – 1071Phosphoserine6 Publications
Modified residuei114 – 1141Phosphoserine3 Publications
Modified residuei189 – 1891Phosphothreonine1 Publication
Modified residuei340 – 3401Phosphoserine1 Publication
Modified residuei343 – 3431Phosphoserine1 Publication
Modified residuei546 – 5461Phosphoserine2 Publications
Modified residuei548 – 5481Phosphoserine2 Publications
Modified residuei598 – 5981Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ86YP4.
PaxDbiQ86YP4.
PRIDEiQ86YP4.

PTM databases

PhosphoSiteiQ86YP4.

Miscellaneous databases

PMAP-CutDBQ86YP4.

Expressioni

Tissue specificityi

Ubiquitous, both in fetal and adult tissues.1 Publication

Gene expression databases

ArrayExpressiQ86YP4.
BgeeiQ86YP4.
CleanExiHS_GATAD2A.
GenevestigatoriQ86YP4.

Organism-specific databases

HPAiHPA006759.
HPA024373.

Interactioni

Subunit structurei

Binds MBD2 and MBD3. Interaction with MBD2 is required for the enhancement of MBD2-mediated repression and for targeting to the chromatin. Component of the MeCP1 histone deacetylase complex. Interacts with histone tails, including that of histones H2A, H2B, H3 and H4. This interaction is reduced by histone acetylation.3 Publications

Protein-protein interaction databases

BioGridi120172. 22 interactions.
IntActiQ86YP4. 15 interactions.
MINTiMINT-1387810.
STRINGi9606.ENSP00000351552.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi138 – 16831

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2LNMR-A137-178[»]
ProteinModelPortaliQ86YP4.
SMRiQ86YP4. Positions 137-178.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 17835CR1; MBD2-binding
Add
BLAST
Regioni340 – 480141CR2; histone tail-binding
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili139 – 17436 Reviewed prediction
Add
BLAST

Domaini

Both CR1 and CR2 regions are required for speckled nuclear localization.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG252421.
HOGENOMiHOG000074070.
HOVERGENiHBG053401.
OMAiLVNIPQP.
PhylomeDBiQ86YP4.
TreeFamiTF321369.

Family and domain databases

Gene3Di3.30.50.10. 1 hit.
InterProiIPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PROSITEiPS00344. GATA_ZN_FINGER_1. 1 hit.
PS50114. GATA_ZN_FINGER_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86YP4-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MTEEACRTRS QKRALERDPT EDDVESKKIK MERGLLASDL NTDGDMRVTP    50
EPGAGPTQGL LRATEATAMA MGRGEGLVGD GPVDMRTSHS DMKSERRPPS 100
PDVIVLSDNE QPSSPRVNGL TTVALKETST EALMKSSPEE RERMIKQLKE 150
ELRLEEAKLV LLKKLRQSQI QKEATAQKPT GSVGSTVTTP PPLVRGTQNI 200
PAGKPSLQTS SARMPGSVIP PPLVRGGQQA SSKLGPQASS QVVMPPLVRG 250
AQQIHSIRQH SSTGPPPLLL APRASVPSVQ IQGQRIIQQG LIRVANVPNT 300
SLLVNIPQPT PASLKGTTAT SAQANSTPTS VASVVTSAES PASRQAAAKL 350
ALRKQLEKTL LEIPPPKPPA PEMNFLPSAA NNEFIYLVGL EEVVQNLLET 400
QGRMSAATVL SREPYMCAQC KTDFTCRWRE EKSGAIMCEN CMTTNQKKAL 450
KVEHTSRLKA AFVKALQQEQ EIEQRLLQQG TAPAQAKAEP TAAPHPVLKQ 500
VIKPRRKLAF RSGEARDWSN GAVLQASSQL SRGSATTPRG VLHTFSPSPK 550
LQNSASATAL VSRTGRHSER TVSAGKGSAT SNWKKTPLST GGTLAFVSPS 600
LAVHKSSSAV DRQREYLLDM IPPRSIPQSA TWK 633
Length:633
Mass (Da):68,063
Last modified:June 1, 2003 - v1
Checksum:i64F0066B4BEFCB39
GO
Isoform 2 (identifier: Q86YP4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     500-524: Missing.

Note: No experimental confirmation available.

Show »
Length:608
Mass (Da):65,225
Checksum:i751DB0FC42DA3BC8
GO
Isoform 3 (identifier: Q86YP4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     401-401: Q → QA

Note: No experimental confirmation available.

Show »
Length:634
Mass (Da):68,134
Checksum:i4C5D2B9CD5FE719E
GO

Sequence cautioni

The sequence AAH11684.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA90939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171R → Q.
Corresponds to variant rs10426883 [ dbSNP | Ensembl ].
VAR_059308
Natural varianti296 – 2961N → S.
Corresponds to variant rs2288851 [ dbSNP | Ensembl ].
VAR_059309

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei401 – 4011Q → QA in isoform 3.
VSP_053410
Alternative sequencei500 – 52425Missing in isoform 2.
VSP_010929Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti432 – 4321K → E in BAA90939. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY186731 mRNA. Translation: AAO31797.1.
AC003030 Genomic DNA. No translation available.
AC011448 Genomic DNA. No translation available.
AC092067 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84819.1.
BC011684 mRNA. Translation: AAH11684.1. Different initiation.
BC012902 mRNA. Translation: AAH12902.2.
AK000092 mRNA. Translation: BAA90939.1. Different initiation.
AL390164 mRNA. Translation: CAB99095.1.
CCDSiCCDS12402.2. [Q86YP4-1]
PIRiT51878.
RefSeqiNP_060130.3. NM_017660.3. [Q86YP4-1]
XP_005260015.1. XM_005259958.1. [Q86YP4-3]
XP_005260016.1. XM_005259959.2. [Q86YP4-3]
XP_005260017.1. XM_005259960.2. [Q86YP4-3]
XP_005260018.1. XM_005259961.1. [Q86YP4-3]
UniGeneiHs.118964.

Genome annotation databases

EnsembliENST00000252577; ENSP00000252577; ENSG00000167491. [Q86YP4-2]
ENST00000358713; ENSP00000351552; ENSG00000167491. [Q86YP4-1]
ENST00000360315; ENSP00000353463; ENSG00000167491. [Q86YP4-1]
ENST00000404158; ENSP00000384899; ENSG00000167491. [Q86YP4-3]
GeneIDi54815.
KEGGihsa:54815.
UCSCiuc010xqt.2. human. [Q86YP4-1]
uc010xqv.3. human.

Polymorphism databases

DMDMi50401012.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY186731 mRNA. Translation: AAO31797.1 .
AC003030 Genomic DNA. No translation available.
AC011448 Genomic DNA. No translation available.
AC092067 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84819.1 .
BC011684 mRNA. Translation: AAH11684.1 . Different initiation.
BC012902 mRNA. Translation: AAH12902.2 .
AK000092 mRNA. Translation: BAA90939.1 . Different initiation.
AL390164 mRNA. Translation: CAB99095.1 .
CCDSi CCDS12402.2. [Q86YP4-1 ]
PIRi T51878.
RefSeqi NP_060130.3. NM_017660.3. [Q86YP4-1 ]
XP_005260015.1. XM_005259958.1. [Q86YP4-3 ]
XP_005260016.1. XM_005259959.2. [Q86YP4-3 ]
XP_005260017.1. XM_005259960.2. [Q86YP4-3 ]
XP_005260018.1. XM_005259961.1. [Q86YP4-3 ]
UniGenei Hs.118964.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2L2L NMR - A 137-178 [» ]
ProteinModelPortali Q86YP4.
SMRi Q86YP4. Positions 137-178.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120172. 22 interactions.
IntActi Q86YP4. 15 interactions.
MINTi MINT-1387810.
STRINGi 9606.ENSP00000351552.

PTM databases

PhosphoSitei Q86YP4.

Polymorphism databases

DMDMi 50401012.

Proteomic databases

MaxQBi Q86YP4.
PaxDbi Q86YP4.
PRIDEi Q86YP4.

Protocols and materials databases

DNASUi 54815.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252577 ; ENSP00000252577 ; ENSG00000167491 . [Q86YP4-2 ]
ENST00000358713 ; ENSP00000351552 ; ENSG00000167491 . [Q86YP4-1 ]
ENST00000360315 ; ENSP00000353463 ; ENSG00000167491 . [Q86YP4-1 ]
ENST00000404158 ; ENSP00000384899 ; ENSG00000167491 . [Q86YP4-3 ]
GeneIDi 54815.
KEGGi hsa:54815.
UCSCi uc010xqt.2. human. [Q86YP4-1 ]
uc010xqv.3. human.

Organism-specific databases

CTDi 54815.
GeneCardsi GC19P019496.
H-InvDB HIX0014940.
HGNCi HGNC:29989. GATAD2A.
HPAi HPA006759.
HPA024373.
MIMi 614997. gene.
neXtProti NX_Q86YP4.
PharmGKBi PA142671746.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG252421.
HOGENOMi HOG000074070.
HOVERGENi HBG053401.
OMAi LVNIPQP.
PhylomeDBi Q86YP4.
TreeFami TF321369.

Enzyme and pathway databases

Reactomei REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

GenomeRNAii 54815.
NextBioi 35478060.
PMAP-CutDB Q86YP4.
PROi Q86YP4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q86YP4.
Bgeei Q86YP4.
CleanExi HS_GATAD2A.
Genevestigatori Q86YP4.

Family and domain databases

Gene3Di 3.30.50.10. 1 hit.
InterProi IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
PROSITEi PS00344. GATA_ZN_FINGER_1. 1 hit.
PS50114. GATA_ZN_FINGER_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3."
    Brackertz M., Boeke J., Zhang R., Renkawitz R.
    J. Biol. Chem. 277:40958-40966(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MBD2 AND MBD3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 3).
    Tissue: Ovary and Skin.
  5. "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] OF 417-633 (ISOFORM 1).
    Tissue: Colon.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-633 (ISOFORM 2).
    Tissue: Brain.
  7. "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.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-107 AND SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone interaction."
    Brackertz M., Gong Z., Leers J., Renkawitz R.
    Nucleic Acids Res. 34:397-406(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MBD2 AND HISTONE TAILS, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-149.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107; SER-114; SER-546; SER-548 AND SER-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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].
  14. "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 THR-49; SER-100; SER-107; SER-114; THR-189 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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 THR-49; SER-100; SER-107; SER-546 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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 THR-49; SER-100; SER-107 AND SER-343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2-NuRD complex."
    Gnanapragasam M.N., Scarsdale J.N., Amaya M.L., Webb H.D., Desai M.A., Walavalkar N.M., Wang S.Z., Zu Zhu S., Ginder G.D., Williams D.C. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 108:7487-7492(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 137-178 IN COMPLEX WITH MBD2, SUBUNIT, INTERACTION WITH MBD2.

Entry informationi

Entry nameiP66A_HUMAN
AccessioniPrimary (citable) accession number: Q86YP4
Secondary accession number(s): B5MC40
, Q7L3J2, Q96F28, Q9NPU2, Q9NXS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 114 of the entry and version 1 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 19
    Human chromosome 19: 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

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