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Protein

Transcriptional repressor p66-alpha

Gene

GATAD2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_263923. HDACs deacetylate histones.
REACT_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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:29989. GATAD2A.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • NuRD complex 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.

Polymorphism and mutation databases

BioMutaiGATAD2A.
DMDMi50401012.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Transcriptional repressor p66-alphaPRO_0000083500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491Phosphothreonine6 Publications
Modified residuei100 – 1001Phosphoserine7 Publications
Modified residuei107 – 1071Phosphoserine7 Publications
Modified residuei114 – 1141Phosphoserine3 Publications
Modified residuei189 – 1891Phosphothreonine2 Publications
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

BgeeiQ86YP4.
CleanExiHS_GATAD2A.
ExpressionAtlasiQ86YP4. baseline and differential.
GenevisibleiQ86YP4. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT40Q6A1623EBI-10261080,EBI-10171697

Protein-protein interaction databases

BioGridi120172. 31 interactions.
DIPiDIP-36053N.
IntActiQ86YP4. 18 interactions.
MINTiMINT-1387810.
STRINGi9606.ENSP00000351552.

Structurei

Secondary structure

1
633
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi138 – 16831Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2LNMR-A137-178[»]
ProteinModelPortaliQ86YP4.
SMRiQ86YP4. Positions 137-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili139 – 17436Sequence AnalysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri411 – 46454GATA-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG252421.
GeneTreeiENSGT00390000004097.
HOGENOMiHOG000074070.
HOVERGENiHBG053401.
InParanoidiQ86YP4.
OMAiLVNIPQP.
OrthoDBiEOG783MV0.
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. AlignAdd to basket

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

        10         20         30         40         50
MTEEACRTRS QKRALERDPT EDDVESKKIK MERGLLASDL NTDGDMRVTP
60 70 80 90 100
EPGAGPTQGL LRATEATAMA MGRGEGLVGD GPVDMRTSHS DMKSERRPPS
110 120 130 140 150
PDVIVLSDNE QPSSPRVNGL TTVALKETST EALMKSSPEE RERMIKQLKE
160 170 180 190 200
ELRLEEAKLV LLKKLRQSQI QKEATAQKPT GSVGSTVTTP PPLVRGTQNI
210 220 230 240 250
PAGKPSLQTS SARMPGSVIP PPLVRGGQQA SSKLGPQASS QVVMPPLVRG
260 270 280 290 300
AQQIHSIRQH SSTGPPPLLL APRASVPSVQ IQGQRIIQQG LIRVANVPNT
310 320 330 340 350
SLLVNIPQPT PASLKGTTAT SAQANSTPTS VASVVTSAES PASRQAAAKL
360 370 380 390 400
ALRKQLEKTL LEIPPPKPPA PEMNFLPSAA NNEFIYLVGL EEVVQNLLET
410 420 430 440 450
QGRMSAATVL SREPYMCAQC KTDFTCRWRE EKSGAIMCEN CMTTNQKKAL
460 470 480 490 500
KVEHTSRLKA AFVKALQQEQ EIEQRLLQQG TAPAQAKAEP TAAPHPVLKQ
510 520 530 540 550
VIKPRRKLAF RSGEARDWSN GAVLQASSQL SRGSATTPRG VLHTFSPSPK
560 570 580 590 600
LQNSASATAL VSRTGRHSER TVSAGKGSAT SNWKKTPLST GGTLAFVSPS
610 620 630
LAVHKSSSAV DRQREYLLDM IPPRSIPQSA TWK
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.Curated
The sequence BAA90939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti432 – 4321K → E in BAA90939 (PubMed:14702039).Curated

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. 1 PublicationVSP_053410
Alternative sequencei500 – 52425Missing in isoform 2. 1 PublicationVSP_010929Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001287875.1. NM_001300946.1. [Q86YP4-3]
NP_060130.3. NM_017660.3. [Q86YP4-1]
XP_005260016.1. XM_005259959.2. [Q86YP4-3]
XP_005260017.1. XM_005259960.3. [Q86YP4-3]
XP_005260018.1. XM_005259961.1. [Q86YP4-3]
UniGeneiHs.118964.

Genome annotation databases

EnsembliENST00000358713; 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.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001287875.1. NM_001300946.1. [Q86YP4-3]
NP_060130.3. NM_017660.3. [Q86YP4-1]
XP_005260016.1. XM_005259959.2. [Q86YP4-3]
XP_005260017.1. XM_005259960.3. [Q86YP4-3]
XP_005260018.1. XM_005259961.1. [Q86YP4-3]
UniGeneiHs.118964.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2LNMR-A137-178[»]
ProteinModelPortaliQ86YP4.
SMRiQ86YP4. Positions 137-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120172. 31 interactions.
DIPiDIP-36053N.
IntActiQ86YP4. 18 interactions.
MINTiMINT-1387810.
STRINGi9606.ENSP00000351552.

PTM databases

PhosphoSiteiQ86YP4.

Polymorphism and mutation databases

BioMutaiGATAD2A.
DMDMi50401012.

Proteomic databases

MaxQBiQ86YP4.
PaxDbiQ86YP4.
PRIDEiQ86YP4.

Protocols and materials databases

DNASUi54815.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358713; 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.

Organism-specific databases

CTDi54815.
GeneCardsiGC19P019496.
H-InvDBHIX0014940.
HGNCiHGNC:29989. GATAD2A.
HPAiHPA006759.
HPA024373.
MIMi614997. gene.
neXtProtiNX_Q86YP4.
PharmGKBiPA142671746.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG252421.
GeneTreeiENSGT00390000004097.
HOGENOMiHOG000074070.
HOVERGENiHBG053401.
InParanoidiQ86YP4.
OMAiLVNIPQP.
OrthoDBiEOG783MV0.
PhylomeDBiQ86YP4.
TreeFamiTF321369.

Enzyme and pathway databases

ReactomeiREACT_263923. HDACs deacetylate histones.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiGATAD2A. human.
GenomeRNAii54815.
NextBioi35478060.
PMAP-CutDBQ86YP4.
PROiQ86YP4.
SOURCEiSearch...

Gene expression databases

BgeeiQ86YP4.
CleanExiHS_GATAD2A.
ExpressionAtlasiQ86YP4. baseline and differential.
GenevisibleiQ86YP4. HS.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107 AND THR-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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: June 24, 2015
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.