Skip Header

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

Cytoplasmic polyadenylation element-binding protein 1

Gene

CPEB1

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

Functioni

Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses (By similarity). Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity). Induces the assembly of stress granules in the absence of stress.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi515 – 5151Zinc 11 Publication
Metal bindingi518 – 5181Zinc 11 Publication
Metal bindingi527 – 5271Zinc 21 Publication
Metal bindingi532 – 5321Zinc 21 Publication
Metal bindingi537 – 5371Zinc 11 Publication
Metal bindingi540 – 5401Zinc 11 Publication
Metal bindingi545 – 5451Zinc 21 Publication
Metal bindingi553 – 5531Zinc 21 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

mRNA processing, Translation regulation

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic polyadenylation element-binding protein 1
Short name:
CPE-BP1
Short name:
CPE-binding protein 1
Short name:
h-CPEB
Short name:
hCPEB-1
Gene namesi
Name:CPEB1
Synonyms:CPEB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:21744. CPEB1.

Subcellular locationi

  • CytoplasmP-body
  • Cytoplasmic granule
  • Cell junctionsynapse
  • Membrane
  • Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity
  • Cell projectiondendrite By similarity

  • Note: Also found in stress granules. Recruited to stress granules (SGs) upon arsenite treatment. In dendrites (By similarity). Localizes in synaptosomes at dendritic synapses of neurons (By similarity). Strongly enriched in postsynaptic density (PSD) fractions (By similarity). Transported into dendrites in a microtubule-dependent fashion and colocalizes in mRNA-containing particles with TACC3, dynein and kinesin (By similarity). Membrane-associated (By similarity). Colocalizes at excitatory synapses with members of the polyadenylation and translation complex factors (CPSF, APLP1, TACC3, AURKA, SYP, etc.) including CPE-containing RNAs (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi172 – 1721T → A: Does not affect its localization. 1 Publication
Mutagenesisi172 – 1721T → D: Does not affect its localization. 1 Publication
Mutagenesisi314 – 3141F → A: Abolishes stress granule assembly and correct localization in dcp1 bodies. 1 Publication
Mutagenesisi545 – 5451H → A: Abolishes stress granule assembly and correct localization in dcp1 bodies. 1 Publication

Organism-specific databases

PharmGKBiPA134929879.

Polymorphism and mutation databases

BioMutaiCPEB1.
DMDMi74762720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 566566Cytoplasmic polyadenylation element-binding protein 1PRO_0000269251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei172 – 1721Phosphothreonine; by AURKA and CAMK2ABy similarity

Post-translational modificationi

Phosphorylated on serine/threonine residues by AURKA within positions 166 and 197. Phosphorylation and dephosphorylation on Thr-172 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-172 by AURKA and CAMK2A activates CPEB1. Phosphorylation on Thr-172 may be promoted by APLP1. Phosphorylation increases binding to RNA (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BZB8.
MaxQBiQ9BZB8.
PaxDbiQ9BZB8.
PRIDEiQ9BZB8.

PTM databases

iPTMnetiQ9BZB8.
PhosphoSiteiQ9BZB8.

Expressioni

Tissue specificityi

Isoform 1 is expressed in immature oocytes, ovary, brain and heart. Isoform 2 is expressed in brain and heart. Isoform 3 and isoform 4 are expressed in brain. Expressed in breast tumors and several tumor cell lines.3 Publications

Gene expression databases

BgeeiQ9BZB8.
CleanExiHS_CPEB1.
ExpressionAtlasiQ9BZB8. baseline and differential.
GenevisibleiQ9BZB8. HS.

Organism-specific databases

HPAiCAB033351.
HPA061586.

Interactioni

Subunit structurei

Interacts with kinesin, dynein, APLP1, APLP2, PAPD4/GLD2 and APP. Both phosphorylated and non phosphorylated forms interact with APLP1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi122202. 11 interactions.
IntActiQ9BZB8. 3 interactions.
STRINGi9606.ENSP00000457881.

Structurei

Secondary structure

1
566
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi294 – 2963Combined sources
Beta strandi309 – 3168Combined sources
Helixi324 – 3318Combined sources
Helixi332 – 3343Combined sources
Beta strandi337 – 3404Combined sources
Turni342 – 3454Combined sources
Beta strandi361 – 3666Combined sources
Helixi370 – 3767Combined sources
Beta strandi379 – 3846Combined sources
Beta strandi387 – 3893Combined sources
Beta strandi391 – 3944Combined sources
Beta strandi399 – 4013Combined sources
Beta strandi406 – 4127Combined sources
Helixi413 – 4153Combined sources
Beta strandi417 – 4204Combined sources
Beta strandi431 – 4366Combined sources
Helixi443 – 45311Combined sources
Beta strandi458 – 4625Combined sources
Beta strandi466 – 4705Combined sources
Beta strandi472 – 4776Combined sources
Beta strandi479 – 4813Combined sources
Helixi482 – 4909Combined sources
Beta strandi492 – 4965Combined sources
Beta strandi501 – 5077Combined sources
Turni508 – 5103Combined sources
Turni516 – 5183Combined sources
Beta strandi524 – 5274Combined sources
Turni530 – 5323Combined sources
Beta strandi534 – 5363Combined sources
Helixi538 – 5458Combined sources
Helixi548 – 5503Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M13NMR-A504-566[»]
2MKENMR-A506-566[»]
2MKHNMR-A294-509[»]
2MKKNMR-A294-510[»]
2N1ONMR-B206-213[»]
ProteinModelPortaliQ9BZB8.
SMRiQ9BZB8. Positions 294-566.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini311 – 40898RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini430 – 51182RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni330 – 566237Necessary for stress granule assembly and correct localization in dcp1 bodiesAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi178 – 21740Ser-richAdd
BLAST

Domaini

The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA.By similarity

Sequence similaritiesi

Belongs to the RRM CPEB family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410ITXD. Eukaryota.
ENOG410YBXF. LUCA.
GeneTreeiENSGT00390000012886.
HOGENOMiHOG000290661.
HOVERGENiHBG079080.
InParanoidiQ9BZB8.
KOiK02602.
PhylomeDBiQ9BZB8.
TreeFamiTF317658.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR032292. CEBP1_N.
IPR032296. CEBP_ZZ.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF16368. CEBP1_N. 1 hit.
PF16366. CEBP_ZZ. 1 hit.
PF16367. RRM_7. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZB8-1) [UniParc]FASTAAdd to basket

Also known as: hCPEB long, hCPEBg

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
MALSLEEEAG RIKDCWDNQE APALSTCSNA NIFRRINAIL DNSLDFSRVC
60 70 80 90 100
TTPINRGIHD HLPDFQDSEE TVTSRMLFPT SAQESSRGLP DANDLCLGLQ
110 120 130 140 150
SLSLTGWDRP WSTQDSDSSA QSSTHSVLSM LHNPLGNVLG KPPLSFLPLD
160 170 180 190 200
PLGSDLVDKF PAPSVRGSRL DTRPILDSRS SSPSDSDTSG FSSGSDHLSD
210 220 230 240 250
LISSLRISPP LPFLSLSGGG PRDPLKMGVG SRMDQEQAAL AAVTPSPTSA
260 270 280 290 300
SKRWPGASVW PSWDLLEAPK DPFSIEREAR LHRQAAAVNE ATCTWSGQLP
310 320 330 340 350
PRNYKNPIYS CKVFLGGVPW DITEAGLVNT FRVFGSLSVE WPGKDGKHPR
360 370 380 390 400
CPPKGNMPKG YVYLVFELEK SVRSLLQACS HDPLSPDGLS EYYFKMSSRR
410 420 430 440 450
MRCKEVQVIP WVLADSNFVR SPSQRLDPSR TVFVGALHGM LNAEALAAIL
460 470 480 490 500
NDLFGGVVYA GIDTDKHKYP IGSGRVTFNN QRSYLKAVSA AFVEIKTTKF
510 520 530 540 550
TKKVQIDPYL EDSLCHICSS QPGPFFCRDQ VCFKYFCRSC WHWRHSMEGL
560
RHHSPLMRNQ KNRDSS
Length:566
Mass (Da):62,595
Last modified:June 1, 2001 - v1
Checksum:i9E41E5B0EC69DA87
GO
Isoform 2 (identifier: Q9BZB8-2) [UniParc]FASTAAdd to basket

Also known as: hCPEB short, hCPEBs

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.

Show »
Length:491
Mass (Da):54,162
Checksum:i561A40FEBD482262
GO
Isoform 3 (identifier: Q9BZB8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MALSL → MAFPL
     354-358: Missing.

Show »
Length:561
Mass (Da):62,111
Checksum:iDCE6E16D700DD14E
GO
Isoform 4 (identifier: Q9BZB8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.
     354-358: Missing.

Show »
Length:486
Mass (Da):53,635
Checksum:i19FA96CE00D0B9FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti446 – 4461L → Q in BAB14496 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7575Missing in isoform 2 and isoform 4. 3 PublicationsVSP_022027Add
BLAST
Alternative sequencei1 – 55MALSL → MAFPL in isoform 3. 1 PublicationVSP_022028
Alternative sequencei354 – 3585Missing in isoform 3 and isoform 4. 2 PublicationsVSP_022029

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329402 mRNA. Translation: AAK01239.1.
AF329403 mRNA. Translation: AAK01240.1.
AK023265 mRNA. Translation: BAB14496.1.
AK300105 mRNA. Translation: BAH13212.1.
CH471188 Genomic DNA. Translation: EAW62449.1.
BC035348 mRNA. Translation: AAH35348.1.
BC050629 mRNA. Translation: AAH50629.1.
CCDSiCCDS42072.2. [Q9BZB8-2]
CCDS45329.2. [Q9BZB8-3]
CCDS45330.2. [Q9BZB8-4]
RefSeqiNP_001073001.1. NM_001079533.1. [Q9BZB8-2]
NP_001073002.1. NM_001079534.1. [Q9BZB8-4]
NP_001073003.1. NM_001079535.1. [Q9BZB8-4]
NP_001275748.1. NM_001288819.1. [Q9BZB8-4]
NP_085097.3. NM_030594.4. [Q9BZB8-3]
UniGeneiHs.459132.
Hs.547988.

Genome annotation databases

EnsembliENST00000611163; ENSP00000483857; ENSG00000214575. [Q9BZB8-4]
ENST00000615198; ENSP00000477715; ENSG00000214575. [Q9BZB8-3]
ENST00000616775; ENSP00000482116; ENSG00000277445. [Q9BZB8-2]
ENST00000617462; ENSP00000477557; ENSG00000214575. [Q9BZB8-4]
ENST00000617522; ENSP00000481009; ENSG00000214575. [Q9BZB8-4]
ENST00000618449; ENSP00000483590; ENSG00000214575. [Q9BZB8-2]
ENST00000619696; ENSP00000482965; ENSG00000277445. [Q9BZB8-4]
ENST00000620182; ENSP00000484549; ENSG00000214575. [Q9BZB8-4]
ENST00000620212; ENSP00000478558; ENSG00000277445. [Q9BZB8-4]
ENST00000631674; ENSP00000488352; ENSG00000277445. [Q9BZB8-4]
ENST00000632526; ENSP00000487757; ENSG00000277445. [Q9BZB8-4]
GeneIDi64506.
KEGGihsa:64506.
UCSCiuc002biq.4. human. [Q9BZB8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329402 mRNA. Translation: AAK01239.1.
AF329403 mRNA. Translation: AAK01240.1.
AK023265 mRNA. Translation: BAB14496.1.
AK300105 mRNA. Translation: BAH13212.1.
CH471188 Genomic DNA. Translation: EAW62449.1.
BC035348 mRNA. Translation: AAH35348.1.
BC050629 mRNA. Translation: AAH50629.1.
CCDSiCCDS42072.2. [Q9BZB8-2]
CCDS45329.2. [Q9BZB8-3]
CCDS45330.2. [Q9BZB8-4]
RefSeqiNP_001073001.1. NM_001079533.1. [Q9BZB8-2]
NP_001073002.1. NM_001079534.1. [Q9BZB8-4]
NP_001073003.1. NM_001079535.1. [Q9BZB8-4]
NP_001275748.1. NM_001288819.1. [Q9BZB8-4]
NP_085097.3. NM_030594.4. [Q9BZB8-3]
UniGeneiHs.459132.
Hs.547988.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M13NMR-A504-566[»]
2MKENMR-A506-566[»]
2MKHNMR-A294-509[»]
2MKKNMR-A294-510[»]
2N1ONMR-B206-213[»]
ProteinModelPortaliQ9BZB8.
SMRiQ9BZB8. Positions 294-566.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122202. 11 interactions.
IntActiQ9BZB8. 3 interactions.
STRINGi9606.ENSP00000457881.

PTM databases

iPTMnetiQ9BZB8.
PhosphoSiteiQ9BZB8.

Polymorphism and mutation databases

BioMutaiCPEB1.
DMDMi74762720.

Proteomic databases

EPDiQ9BZB8.
MaxQBiQ9BZB8.
PaxDbiQ9BZB8.
PRIDEiQ9BZB8.

Protocols and materials databases

DNASUi64506.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000611163; ENSP00000483857; ENSG00000214575. [Q9BZB8-4]
ENST00000615198; ENSP00000477715; ENSG00000214575. [Q9BZB8-3]
ENST00000616775; ENSP00000482116; ENSG00000277445. [Q9BZB8-2]
ENST00000617462; ENSP00000477557; ENSG00000214575. [Q9BZB8-4]
ENST00000617522; ENSP00000481009; ENSG00000214575. [Q9BZB8-4]
ENST00000618449; ENSP00000483590; ENSG00000214575. [Q9BZB8-2]
ENST00000619696; ENSP00000482965; ENSG00000277445. [Q9BZB8-4]
ENST00000620182; ENSP00000484549; ENSG00000214575. [Q9BZB8-4]
ENST00000620212; ENSP00000478558; ENSG00000277445. [Q9BZB8-4]
ENST00000631674; ENSP00000488352; ENSG00000277445. [Q9BZB8-4]
ENST00000632526; ENSP00000487757; ENSG00000277445. [Q9BZB8-4]
GeneIDi64506.
KEGGihsa:64506.
UCSCiuc002biq.4. human. [Q9BZB8-1]

Organism-specific databases

CTDi64506.
GeneCardsiCPEB1.
HGNCiHGNC:21744. CPEB1.
HPAiCAB033351.
HPA061586.
MIMi607342. gene.
neXtProtiNX_Q9BZB8.
PharmGKBiPA134929879.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITXD. Eukaryota.
ENOG410YBXF. LUCA.
GeneTreeiENSGT00390000012886.
HOGENOMiHOG000290661.
HOVERGENiHBG079080.
InParanoidiQ9BZB8.
KOiK02602.
PhylomeDBiQ9BZB8.
TreeFamiTF317658.

Miscellaneous databases

GeneWikiiCPEB1.
GenomeRNAii64506.
PROiQ9BZB8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BZB8.
CleanExiHS_CPEB1.
ExpressionAtlasiQ9BZB8. baseline and differential.
GenevisibleiQ9BZB8. HS.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR032292. CEBP1_N.
IPR032296. CEBP_ZZ.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF16368. CEBP1_N. 1 hit.
PF16366. CEBP_ZZ. 1 hit.
PF16367. RRM_7. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of the gene encoding human cytoplasmic polyadenylation element binding protein."
    Welk J.F., Charlesworth A., Smith G.D., MacNicol A.M.
    Gene 263:113-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), RNA-BINDING, TISSUE SPECIFICITY.
    Tissue: Brain and Ovary.
  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 4).
    Tissue: Pericardium and Teratocarcinoma.
  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 3 AND 4).
    Tissue: Brain and Melanoma.
  5. "Over-expression of Aurora-A targets cytoplasmic polyadenylation element binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1."
    Sasayama T., Marumoto T., Kunitoku N., Zhang D., Tamaki N., Kohmura E., Saya H., Hirota T.
    Genes Cells 10:627-638(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules."
    Wilczynska A., Aigueperse C., Kress M., Dautry F., Weil D.
    J. Cell Sci. 118:981-992(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING, MUTAGENESIS OF THR-172; PHE-314 AND HIS-545, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "The C-Terminal region of cytoplasmic polyadenylation element binding protein is a ZZ domain with potential for protein-protein interactions."
    Merkel D.J., Wells S.B., Hilburn B.C., Elazzouzi F., Perez-Alvarado G.C., Lee B.M.
    J. Mol. Biol. 425:2015-2026(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 504-566 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiCPEB1_HUMAN
AccessioniPrimary (citable) accession number: Q9BZB8
Secondary accession number(s): B7Z6C6
, Q86W46, Q8IV41, Q9BZB7, Q9H8V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
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 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.