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Protein

Cytoplasmic polyadenylation element-binding protein 1

Gene

Cpeb1

Organism
Mus musculus (Mouse)
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 3'-UTR of mRNAs. 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. Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation. Induces the assembly of stress granules in the absence of stress (By similarity).By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi514 – 5141Zinc 1By similarity
Metal bindingi517 – 5171Zinc 1By similarity
Metal bindingi526 – 5261Zinc 2By similarity
Metal bindingi531 – 5311Zinc 2By similarity
Metal bindingi536 – 5361Zinc 1By similarity
Metal bindingi539 – 5391Zinc 1By similarity
Metal bindingi544 – 5441Zinc 2By similarity
Metal bindingi552 – 5521Zinc 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • mRNA 3'-UTR AU-rich region binding Source: UniProtKB
  • mRNA binding Source: MGI
  • nucleotide binding Source: InterPro
  • RNA binding Source: MGI
  • translation repressor activity, nucleic acid binding Source: UniProtKB

GO - Biological processi

  • cellular response to amino acid stimulus Source: UniProtKB
  • cellular response to hypoxia Source: UniProtKB
  • cellular response to insulin stimulus Source: UniProtKB
  • mRNA processing Source: UniProtKB-KW
  • negative regulation of cytoplasmic translation Source: UniProtKB
  • regulation of neuronal synaptic plasticity Source: MGI
  • regulation of translation Source: MGI
  • synaptonemal complex assembly Source: MGI
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:
mCPEB
Short name:
mCPEB-1
Gene namesi
Name:Cpeb1
Synonyms:Cpeb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:108442. Cpeb1.

Subcellular locationi

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

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

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB-SubCell
  • meiotic spindle Source: MGI
  • membrane Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • postsynaptic density Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi171 – 1711T → A: Inhibits CPE-containing cytoplasmic polyadenylation and translation activation. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Cytoplasmic polyadenylation element-binding protein 1PRO_0000269252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei171 – 1711Phosphothreonine; by AURKA and CAMK2A4 Publications

Post-translational modificationi

Phosphorylated on serine/threonine residues by AURKA within positions 165 and 196 (By similarity). Phosphorylation and dephosphorylation on Thr-171 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-171 by AURKA in embryonic ovaries at 16.5 dpc (mostly pachytene oocytes) activates CPEB1. Not phosphorylated on Thr-171 in embryonic ovaries between 18.5 dpc (diplotene oocytes) and metaphase I. Dephosphorylation on Thr-171 by PP1 in embryonic ovaries at 18.5 dpc (mostly diplotene oocytes) inactivates CPEB1. In maturing oocytes, re-phosphorylation on Thr-171 by AURKA reactivates CPEB1. Phosphorylation on Thr-171 by CAMK2A in depolarized hippocampal neurons activates CPEB1. Dephosphorylation on Thr-171 (indirectly by PP1) in hippocampal neurons inactivates CPEB1. Phosphorylation on Thr-171 may be promoted by APLP1. Phosphorylation increases binding to RNA.By similarity6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP70166.
PaxDbiP70166.
PRIDEiP70166.

PTM databases

iPTMnetiP70166.
PhosphoSiteiP70166.

Expressioni

Tissue specificityi

Expressed in hippocampus, cerebral cortex and oocytes (at protein level). Expressed in brain, heart, kidney, lung and ovary and testis. Weakly expressed in granular cells of dentate gyrus and the pyramidal cells of CA3 and CA1 of the hippocampus.5 Publications

Developmental stagei

Expressed in embryonic ovaries at 14.5, 16.5 and 18.5 dpc (at protein level).1 Publication

Inductioni

Not induced by kainate.

Gene expression databases

BgeeiP70166.
ExpressionAtlasiP70166. baseline and differential.
GenevisibleiP70166. MM.

Interactioni

Subunit structurei

Interacts with kinesin, dynein, APLP1, APLP2, PAPD4/GLD2 and APP. Both phosphorylated and non phosphorylated forms interact with APLP1.4 Publications

Protein-protein interaction databases

BioGridi198856. 4 interactions.
DIPiDIP-41380N.
MINTiMINT-261117.
STRINGi10090.ENSMUSP00000137079.

Structurei

3D structure databases

ProteinModelPortaliP70166.
SMRiP70166. Positions 293-561.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini310 – 40798RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini429 – 51082RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni329 – 561233Necessary for stress granule assembly and correct localization in dcp1 bodiesBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi177 – 20731Ser-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

eggNOGiENOG410KDT8. Eukaryota.
ENOG410YBXF. LUCA.
GeneTreeiENSGT00390000012886.
HOVERGENiHBG079080.
InParanoidiP70166.
KOiK02602.
OrthoDBiEOG751NG9.
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]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFSLEEAAG RIKDCWDNQE VPALSTCSNA NIFRRINAIL DDSLDFSKVC
60 70 80 90 100
TTPINRGIHD QLPDFQDSEE TVTSRMLFPT SAQESPRGLP DANGLCLGLQ
110 120 130 140 150
SLSLTGWDRP WSTQDSDSSA QSSTQSVLSM LQNPLGNVLG KAPLSFLSLD
160 170 180 190 200
PLGSDLDKFP APSVRGSRLD TRPILDSRSS SPSDSDTSGF SSGSDHLSDL
210 220 230 240 250
ISSLRISPPL PFLSMTGNGP RDPLKMGVGS RMDQEQAALA AVAPSPTSAP
260 270 280 290 300
KRWPGASVWP SWDLLGAPKD PFSIEREARL HRQAAAVNEA TCTWSGQLPP
310 320 330 340 350
RNYKNPIYSC KVFLGGVPWD ITEAGLVNTF RVFGSLSVEW PGKDGKHPRC
360 370 380 390 400
PPKGNMPKGY VYLVFELEKS VRALLQACSH DPLSPDGLSE YYFKMSSRRM
410 420 430 440 450
RCKEVQVIPW VLADSNFVWS PSQRLDPSRT VFVGALHGML NAEALAAILN
460 470 480 490 500
DLFGGVVYAG IDTDKHKYPI GSGRVTFNNQ RSYLKAVTAA FVEIKTTKFT
510 520 530 540 550
KKVQIDPYLE DSLCLICSSQ PGPFFCRDQV CFKYFCRSCW HWRHSMEGLR
560
HHSPLMRNQK N
Length:561
Mass (Da):61,917
Last modified:February 1, 1997 - v1
Checksum:iCB7958885AB13FF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08260 mRNA. Translation: CAA69588.1.
AK077799 mRNA. Translation: BAC37017.1.
CCDSiCCDS40007.1.
RefSeqiNP_001239454.1. NM_001252525.1.
NP_001239455.1. NM_001252526.1.
NP_031781.1. NM_007755.5.
UniGeneiMm.273122.

Genome annotation databases

EnsembliENSMUST00000098331; ENSMUSP00000095936; ENSMUSG00000025586.
GeneIDi12877.
KEGGimmu:12877.
UCSCiuc009ibw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08260 mRNA. Translation: CAA69588.1.
AK077799 mRNA. Translation: BAC37017.1.
CCDSiCCDS40007.1.
RefSeqiNP_001239454.1. NM_001252525.1.
NP_001239455.1. NM_001252526.1.
NP_031781.1. NM_007755.5.
UniGeneiMm.273122.

3D structure databases

ProteinModelPortaliP70166.
SMRiP70166. Positions 293-561.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198856. 4 interactions.
DIPiDIP-41380N.
MINTiMINT-261117.
STRINGi10090.ENSMUSP00000137079.

PTM databases

iPTMnetiP70166.
PhosphoSiteiP70166.

Proteomic databases

MaxQBiP70166.
PaxDbiP70166.
PRIDEiP70166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098331; ENSMUSP00000095936; ENSMUSG00000025586.
GeneIDi12877.
KEGGimmu:12877.
UCSCiuc009ibw.2. mouse.

Organism-specific databases

CTDi64506.
MGIiMGI:108442. Cpeb1.

Phylogenomic databases

eggNOGiENOG410KDT8. Eukaryota.
ENOG410YBXF. LUCA.
GeneTreeiENSGT00390000012886.
HOVERGENiHBG079080.
InParanoidiP70166.
KOiK02602.
OrthoDBiEOG751NG9.
TreeFamiTF317658.

Miscellaneous databases

ChiTaRSiCpeb1. mouse.
NextBioi282476.
PROiP70166.
SOURCEiSearch...

Gene expression databases

BgeeiP70166.
ExpressionAtlasiP70166. baseline and differential.
GenevisibleiP70166. MM.

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]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse cytoplasmic polyadenylation element binding protein: an evolutionarily conserved protein that interacts with the cytoplasmic polyadenylation elements of c-mos mRNA."
    Gebauer F., Richter J.D.
    Proc. Natl. Acad. Sci. U.S.A. 93:14602-14607(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, TISSUE SPECIFICITY.
    Tissue: Ovary.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-561.
    Strain: C57BL/6J.
    Tissue: Thymus.
  3. "CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses."
    Wu L., Wells D., Tay J., Mendis D., Abbott M.-A., Barnitt A., Quinlan E., Heynen A., Fallon J.R., Richter J.D.
    Neuron 21:1129-1139(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "CPEB phosphorylation and cytoplasmic polyadenylation are catalyzed by the kinase IAK1/Eg2 in maturing mouse oocytes."
    Hodgman R., Tay J., Mendez R., Richter J.D.
    Development 128:2815-2822(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
  5. "N-methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and alpha CaMKII mRNA polyadenylation at synapses."
    Huang Y.-S., Jung M.-Y., Sarkissian M., Richter J.D.
    EMBO J. 21:2139-2148(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-171 BY AURKA MUTAGENESIS OF THR-171, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Facilitation of dendritic mRNA transport by CPEB."
    Huang Y.-S., Carson J.H., Barbarese E., Richter J.D.
    Genes Dev. 17:638-653(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DYNEIN AND KINESIN, RNA-BINDING, SUBCELLULAR LOCATION.
  7. "Regulated CPEB phosphorylation during meiotic progression suggests a mechanism for temporal control of maternal mRNA translation."
    Tay J., Hodgman R., Sarkissian M., Richter J.D.
    Genes Dev. 17:1457-1462(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-171 BY AURKA, DEPHOSPHORYLATION AT THR-171 BY PP1, MUTAGENESIS OF THR-171, DEVELOPMENTAL STAGE.
  8. "Two previously undescribed members of the mouse CPEB family of genes and their inducible expression in the principal cell layers of the hippocampus."
    Theis M., Si K., Kandel E.R.
    Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, ABSENCE OF KAINATE INDUCTION.
    Strain: BALB/cJ.
    Tissue: Brain.
  9. "Cytoplasmic polyadenylation element binding protein-dependent protein synthesis is regulated by calcium/calmodulin-dependent protein kinase II."
    Atkins C.M., Nozaki N., Shigeri Y., Soderling T.R.
    J. Neurosci. 24:5193-5201(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-171 BY CAMK2A, MUTAGENESIS OF THR-171, SUBCELLULAR LOCATION.
  10. "Bidirectional regulation of cytoplasmic polyadenylation element-binding protein phosphorylation by Ca2+/calmodulin-dependent protein kinase II and protein phosphatase 1 during hippocampal long-term potentiation."
    Atkins C.M., Davare M.A., Oh M.C., Derkach V., Soderling T.R.
    J. Neurosci. 25:5604-5610(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-171 BY CAMK2A, DEPHOSPHORYLATION AT THR-171.
  11. "Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation."
    Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.
    Mol. Cell. Biol. 25:10930-10939(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APLP1; APLP2 AND APP, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  12. "Translational control by neuroguidin, a eukaryotic initiation factor 4E and CPEB binding protein."
    Jung M.-Y., Lorenz L., Richter J.D.
    Mol. Cell. Biol. 26:4277-4287(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NGDN.
  13. "Disruption of mouse poly(A) polymerase mGLD-2 does not alter polyadenylation status in oocytes and somatic cells."
    Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M., Kashiwabara S., Baba T.
    Biochem. Biophys. Res. Commun. 364:14-19(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAPD4.

Entry informationi

Entry nameiCPEB1_MOUSE
AccessioniPrimary (citable) accession number: P70166
Secondary accession number(s): Q8C5P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 1, 1997
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.