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Protein

Protein ecdysoneless homolog

Gene

ECD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulator of p53/TP53 stability and function. Inhibits MDM2-mediated degradation of p53/TP53 possibly by cooperating in part with TXNIP (PubMed:16849563, PubMed:23880345). May be involved transcriptional regulation. In vitro has intrinsic transactivation activity enhanced by EP300. May be a transcriptional activator required for the expression of glycolytic genes (PubMed:19919181, PubMed:9928932). Involved in regulation of cell cycle progression. Proposed to disrupt Rb-E2F binding leading to transcriptional activation of E2F proteins (PubMed:19640839). The cell cycle -regulating function may depend on its RUVBL1-mediated association with the R2TP complex (PubMed:26711270). May play a role in regulation of pre-mRNA splicing (PubMed:24722212).2 Publications5 Publications

GO - Molecular functioni

  • histone acetyltransferase binding Source: UniProtKB
  • transcription coactivator activity Source: ProtInc

GO - Biological processi

  • cell proliferation Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  • regulation of glycolytic process Source: ProtInc
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ecdysoneless homologBy similarity
Alternative name(s):
Human suppressor of GCR two1 Publication
Short name:
hSGT11 Publication
Gene namesi
Name:ECD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:17029. ECD.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi481 – 4811I → A: Decreases transactivation activity. 1 Publication
Mutagenesisi484 – 4841D → F: Decreases transactivation activity. 1 Publication
Mutagenesisi489 – 4891L → A: Decreases transactivation activity. 1 Publication
Mutagenesisi503 – 5031S → A: Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-505, A-518, A-572, A-579 and A-584. 1 Publication
Mutagenesisi505 – 5051S → A: Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-518, A-572, A-579 and A-584. 1 Publication
Mutagenesisi510 – 5101D → R: Increases transactivation activity. 1 Publication
Mutagenesisi512 – 5121D → R: Increases transactivation activity. 1 Publication
Mutagenesisi518 – 5181S → A: Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-505, A-572, A-579 and A-584. 1 Publication
Mutagenesisi520 – 5201D → P: Increases transactivation activity. 1 Publication
Mutagenesisi572 – 5721S → A: Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-505, A-518, A-579 and A-584. 1 Publication
Mutagenesisi579 – 5791S → A: Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-505, A-518, A-572 and A-584. 1 Publication
Mutagenesisi584 – 5841S → A: Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-505, A-518, A-572 and A-579. 1 Publication

Organism-specific databases

PharmGKBiPA143485450.

Polymorphism and mutation databases

BioMutaiECD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 644644Protein ecdysoneless homologPRO_0000220844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei503 – 5031PhosphoserineCombined sources
Modified residuei505 – 5051PhosphoserineCombined sources
Modified residuei518 – 5181PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated predominantly by CK2 on two serine-containing clusters; involved in cell cycle regulation activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO95905.
MaxQBiO95905.
PaxDbiO95905.
PeptideAtlasiO95905.
PRIDEiO95905.

PTM databases

iPTMnetiO95905.
PhosphoSiteiO95905.

Expressioni

Tissue specificityi

Highly expressed in muscle and heart. Over-expressed in pancreatic and breast cancers.2 Publications

Gene expression databases

BgeeiO95905.
CleanExiHS_ECD.
ExpressionAtlasiO95905. baseline and differential.
GenevisibleiO95905. HS.

Organism-specific databases

HPAiHPA006465.

Interactioni

Subunit structurei

Interacts with TP53, MDM2, TXNIP (PubMed:16849563, PubMed:23880345). Interacts (phosphorylated) with PIH1D1. Interacts with RUVBL1 mediating the PIH1D1-independent association with the R2TP complex (PubMed:24656813, PubMed:26711270). Interacts with RB1, RBL1 and RBL2; ECD competes with E2F1 for binding to hypophospshorylated RB1 (PubMed:19640839). Interacts with EP300 (PubMed:19919181).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIH1D1Q9NWS03EBI-2557598,EBI-357318

GO - Molecular functioni

  • histone acetyltransferase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116450. 48 interactions.
IntActiO95905. 23 interactions.
MINTiMINT-265905.
STRINGi9606.ENSP00000401566.

Structurei

3D structure databases

ProteinModelPortaliO95905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni439 – 644206Transcription activation1 PublicationAdd
BLAST
Regioni481 – 49717Involved in nuclear export1 PublicationAdd
BLAST
Regioni502 – 53231Acidic region required for transactivation activity1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the ECD family.Curated

Phylogenomic databases

eggNOGiKOG2406. Eukaryota.
ENOG410XR07. LUCA.
GeneTreeiENSGT00390000015361.
HOGENOMiHOG000029899.
HOVERGENiHBG023145.
InParanoidiO95905.
OMAiIVYIVKQ.
OrthoDBiEOG7M3J13.
PhylomeDBiO95905.
TreeFamiTF324229.

Family and domain databases

InterProiIPR010770. Ecd.
[Graphical view]
PANTHERiPTHR13060. PTHR13060. 1 hit.
PfamiPF07093. SGT1. 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: O95905-1) [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
MEETMKLATM EDTVEYCLFL IPDESRDSDK HKEILQKYIE RIITRFAPML
60 70 80 90 100
VPYIWQNQPF NLKYKPGKGG VPAHMFGVTK FGDNIEDEWF IVYVIKQITK
110 120 130 140 150
EFPELVARIE DNDGEFLLIE AADFLPKWLD PENSTNRVFF CHGELCIIPA
160 170 180 190 200
PRKSGAESWL PTTPPTIPQA LNIITAHSEK ILASESIRAA VNRRIRGYPE
210 220 230 240 250
KIQASLHRAH CFLPAGIVAV LKQRPRLVAA AVQAFYLRDP IDLRACRVFK
260 270 280 290 300
TFLPETRIMT SVTFTKCLYA QLVQQRFVPD RRSGYRLPPP SDPQYRAHEL
310 320 330 340 350
GMKLAHGFEI LCSKCSPHFS DCKKSLVTAS PLWASFLESL KKNDYFKGLI
360 370 380 390 400
EGSAQYRERL EMAENYFQLS VDWPESSLAM SPGEEILTLL QTIPFDIEDL
410 420 430 440 450
KKEAANLPPE DDDQWLDLSP DQLDQLLQEA VGKKESESVS KEEKEQNYDL
460 470 480 490 500
TEVSESMKAF ISKVSTHKGA ELPREPSEAP ITFDADSFLN YFDKILGPRP
510 520 530 540 550
NESDSDDLDD EDFECLDSDD DLDFETHEPG EEASLKGTLD NLKSYMAQMD
560 570 580 590 600
QELAHTCISK SFTTRNQVEP VSQTTDNNSD EEDSGTGESV MAPVDVDLNL
610 620 630 640
VSNILESYSS QAGLAGPASN LLQSMGVQLP DNTDHRPTSK PTKN
Length:644
Mass (Da):72,758
Last modified:May 1, 1999 - v1
Checksum:iF9B0D2BBFDB38CAF
GO
Isoform 2 (identifier: O95905-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     262-304: Missing.

Note: No experimental confirmation available.
Show »
Length:601
Mass (Da):67,712
Checksum:i4F0AC1D928853E85
GO
Isoform 3 (identifier: O95905-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-375: E → ERLEVQWRDPGLLQAPPPGFTPFICLSLLSTWDN

Note: No experimental confirmation available.
Show »
Length:677
Mass (Da):76,508
Checksum:i4628E86C662AE075
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281S → P in AK225519 (PubMed:14702039).Curated
Sequence conflicti319 – 3191F → S in AK225519 (PubMed:14702039).Curated
Sequence conflicti333 – 3331W → R in AK225519 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451R → Q.
Corresponds to variant rs3812619 [ dbSNP | Ensembl ].
VAR_051970
Natural varianti281 – 2811R → G Could be a rare polymorphism. 1 Publication
VAR_012191
Natural varianti452 – 4521E → Q.
Corresponds to variant rs3736518 [ dbSNP | Ensembl ].
VAR_051971
Natural varianti501 – 5011N → S.
Corresponds to variant rs36152134 [ dbSNP | Ensembl ].
VAR_051972
Natural varianti634 – 6341D → G.
Corresponds to variant rs2271904 [ dbSNP | Ensembl ].
VAR_051973

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei262 – 30443Missing in isoform 2. 1 PublicationVSP_045670Add
BLAST
Alternative sequencei375 – 3751E → ERLEVQWRDPGLLQAPPPGF TPFICLSLLSTWDN in isoform 3. 1 PublicationVSP_045671

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88208 mRNA. Translation: BAA75199.1.
AK315711 mRNA. No translation available.
AK225519 mRNA. No translation available.
AC016394 Genomic DNA. No translation available.
BC000721 mRNA. Translation: AAH00721.1.
CCDSiCCDS44433.1. [O95905-2]
CCDS44434.1. [O95905-3]
CCDS7321.1. [O95905-1]
RefSeqiNP_001129224.1. NM_001135752.1. [O95905-3]
NP_001129225.1. NM_001135753.1. [O95905-2]
NP_009196.1. NM_007265.2. [O95905-1]
UniGeneiHs.631822.

Genome annotation databases

EnsembliENST00000372979; ENSP00000362070; ENSG00000122882. [O95905-1]
ENST00000430082; ENSP00000401566; ENSG00000122882. [O95905-3]
ENST00000454759; ENSP00000395786; ENSG00000122882. [O95905-2]
GeneIDi11319.
KEGGihsa:11319.
UCSCiuc001jtn.4. human. [O95905-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88208 mRNA. Translation: BAA75199.1.
AK315711 mRNA. No translation available.
AK225519 mRNA. No translation available.
AC016394 Genomic DNA. No translation available.
BC000721 mRNA. Translation: AAH00721.1.
CCDSiCCDS44433.1. [O95905-2]
CCDS44434.1. [O95905-3]
CCDS7321.1. [O95905-1]
RefSeqiNP_001129224.1. NM_001135752.1. [O95905-3]
NP_001129225.1. NM_001135753.1. [O95905-2]
NP_009196.1. NM_007265.2. [O95905-1]
UniGeneiHs.631822.

3D structure databases

ProteinModelPortaliO95905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116450. 48 interactions.
IntActiO95905. 23 interactions.
MINTiMINT-265905.
STRINGi9606.ENSP00000401566.

PTM databases

iPTMnetiO95905.
PhosphoSiteiO95905.

Polymorphism and mutation databases

BioMutaiECD.

Proteomic databases

EPDiO95905.
MaxQBiO95905.
PaxDbiO95905.
PeptideAtlasiO95905.
PRIDEiO95905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372979; ENSP00000362070; ENSG00000122882. [O95905-1]
ENST00000430082; ENSP00000401566; ENSG00000122882. [O95905-3]
ENST00000454759; ENSP00000395786; ENSG00000122882. [O95905-2]
GeneIDi11319.
KEGGihsa:11319.
UCSCiuc001jtn.4. human. [O95905-1]

Organism-specific databases

CTDi11319.
GeneCardsiECD.
HGNCiHGNC:17029. ECD.
HPAiHPA006465.
MIMi616464. gene.
neXtProtiNX_O95905.
PharmGKBiPA143485450.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2406. Eukaryota.
ENOG410XR07. LUCA.
GeneTreeiENSGT00390000015361.
HOGENOMiHOG000029899.
HOVERGENiHBG023145.
InParanoidiO95905.
OMAiIVYIVKQ.
OrthoDBiEOG7M3J13.
PhylomeDBiO95905.
TreeFamiTF324229.

Miscellaneous databases

ChiTaRSiECD. human.
GeneWikiiECD_(gene).
GenomeRNAii11319.
NextBioi43003.
PROiO95905.
SOURCEiSearch...

Gene expression databases

BgeeiO95905.
CleanExiHS_ECD.
ExpressionAtlasiO95905. baseline and differential.
GenevisibleiO95905. HS.

Family and domain databases

InterProiIPR010770. Ecd.
[Graphical view]
PANTHERiPTHR13060. PTHR13060. 1 hit.
PfamiPF07093. SGT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human gene, hSGT1, can substitute for GCR2, which encodes a general regulatory factor of glycolytic gene expression in Saccharomyces cerevisiae."
    Sato T., Jigami Y., Suzuki T., Uemura H.
    Mol. Gen. Genet. 260:535-540(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Brain.
  2. "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] (ISOFORM 3).
    Tissue: Testis.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Signet-ring cell carcinoma.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Placenta.
  6. "The human orthologue of Drosophila ecdysoneless protein interacts with p53 and regulates its function."
    Zhang Y., Chen J., Gurumurthy C.B., Kim J., Bhat I., Gao Q., Dimri G., Lee S.W., Band H., Band V.
    Cancer Res. 66:7167-7175(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53 AND MDM2, SUBCELLULAR LOCATION.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503; SER-505 AND SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: FUNCTION, INTERACTION WITH RB1; RBL1 AND RBL2.
  10. "Biochemical characterization of human Ecdysoneless reveals a role in transcriptional regulation."
    Kim J.H., Gurumurthy C.B., Band H., Band V.
    Biol. Chem. 391:9-19(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EP300, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-481; ASP-484; LEU-489; ASP-510; ASP-512 AND ASP-520.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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].
  13. "Overexpression of a novel cell cycle regulator ecdysoneless in breast cancer: a marker of poor prognosis in HER2/neu-overexpressing breast cancer patients."
    Zhao X., Mirza S., Alshareeda A., Zhang Y., Gurumurthy C.B., Bele A., Kim J.H., Mohibi S., Goswami M., Lele S.M., West W., Qiu F., Ellis I.O., Rakha E.A., Green A.R., Band H., Band V.
    Breast Cancer Res. Treat. 134:171-180(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "Overexpression of ecdysoneless in pancreatic cancer and its role in oncogenesis by regulating glycolysis."
    Dey P., Rachagani S., Chakraborty S., Singh P.K., Zhao X., Gurumurthy C.B., Anderson J.M., Lele S., Hollingsworth M.A., Band V., Batra S.K.
    Clin. Cancer Res. 18:6188-6198(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  15. "TXNIP interacts with hEcd to increase p53 stability and activity."
    Suh H.W., Yun S., Song H., Jung H., Park Y.J., Kim T.D., Yoon S.R., Choi I.
    Biochem. Biophys. Res. Commun. 438:264-269(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TXNIP.
  16. "Phosphorylation-dependent PIH1D1 interactions define substrate specificity of the R2TP cochaperone complex."
    Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M., O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.
    Cell Rep. 7:19-26(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIH1D1.
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Unexpected role of the steroid-deficiency protein ecdysoneless in pre-mRNA splicing."
    Claudius A.K., Romani P., Lamkemeyer T., Jindra M., Uhlirova M.
    PLoS Genet. 10:E1004287-E1004287(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "A novel interaction of ecdysoneless (ECD) protein with R2TP complex component RUVBL1 is required for the functional role of ECD in cell cycle progression."
    Mir R.A., Bele A., Mirza S., Srivastava S., Olou A.A., Ammons S.A., Kim J.H., Gurumurthy C.B., Qiu F., Band H., Band V.
    Mol. Cell. Biol. 36:886-899(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH RUVBL1, ASSOCIATION WITH THE R2TP COMPLEX, MUTAGENESIS OF SER-503; SER-505; SER-518; SER-572; SER-579 AND SER-584.
  20. Cited for: VARIANT GLY-281.

Entry informationi

Entry nameiECD_HUMAN
AccessioniPrimary (citable) accession number: O95905
Secondary accession number(s): C9JX46, E9PAW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.