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Protein

Cyclic AMP-responsive element-binding protein 1

Gene

Creb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei314 – 3141Required for binding TORCsBy similarity

GO - Molecular functioni

  1. cAMP response element binding Source: MGI
  2. DNA binding Source: MGI
  3. enzyme binding Source: MGI
  4. RNA polymerase II activating transcription factor binding Source: MGI
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: MGI
  6. RNA polymerase II distal enhancer sequence-specific DNA binding Source: MGI
  7. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
  8. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: MGI
  9. sequence-specific DNA binding Source: MGI
  10. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. axonogenesis Source: MGI
  2. cellular response to growth factor stimulus Source: BHF-UCL
  3. cellular response to zinc ion Source: MGI
  4. circadian rhythm Source: UniProtKB
  5. lactation Source: MGI
  6. lung epithelium development Source: MGI
  7. lung saccule development Source: MGI
  8. mammary gland development Source: MGI
  9. memory Source: MGI
  10. negative regulation of transcription by competitive promoter binding Source: MGI
  11. pituitary gland development Source: MGI
  12. positive regulation of fat cell differentiation Source: UniProtKB
  13. positive regulation of hormone secretion Source: MGI
  14. positive regulation of lipid biosynthetic process Source: UniProtKB
  15. positive regulation of multicellular organism growth Source: MGI
  16. positive regulation of osteoclast differentiation Source: MGI
  17. positive regulation of transcription, DNA-templated Source: UniProtKB
  18. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  19. protein phosphorylation Source: MGI
  20. protein stabilization Source: UniProtKB
  21. regulation of cell size Source: MGI
  22. regulation of transcription, DNA-templated Source: MGI
  23. response to drug Source: MGI
  24. response to glucagon Source: UniProtKB
  25. response to organic substance Source: MGI
  26. secretory granule organization Source: MGI
  27. transcription from RNA polymerase II promoter Source: MGI
  28. Type I pneumocyte differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Biological rhythms, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_277525. CREB phosphorylation.
REACT_278898. NOTCH2 intracellular domain regulates transcription.
REACT_294637. CREB phosphorylation through the activation of CaMKK.
REACT_303391. CREB phosphorylation through the activation of Adenylate Cyclase.
REACT_308448. AKT phosphorylates targets in the nucleus.
REACT_309693. CaMK IV-mediated phosphorylation of CREB.
REACT_309838. CREB phosphorylation through the activation of CaMKII.
REACT_327612. CREB phosphorylation through the activation of Ras.
REACT_328033. Transcriptional activation of mitochondrial biogenesis.
REACT_328674. Constitutive PI3K/AKT Signaling in Cancer.
REACT_336227. PKA-mediated phosphorylation of CREB.
REACT_337888. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_339798. NCAM signaling for neurite out-growth.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic AMP-responsive element-binding protein 1
Short name:
CREB-1
Short name:
cAMP-responsive element-binding protein 1
Gene namesi
Name:Creb1
Synonyms:Creb-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:88494. Creb1.

Subcellular locationi

Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  1. ATF1-ATF4 transcription factor complex Source: MGI
  2. ATF4-CREB1 transcription factor complex Source: ParkinsonsUK-UCL
  3. nuclear chromatin Source: BHF-UCL
  4. nuclear euchromatin Source: MGI
  5. nucleoplasm Source: MGI
  6. nucleus Source: UniProtKB
  7. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi133 – 1331S → A: Loss of phosphorylation by RPS6KA4 and RPS6KA5. 1 Publication
Mutagenesisi137 – 1382IL → AA: Abolishes CREBBP binding. 1 Publication
Mutagenesisi142 – 1421S → A: Attenuates light-induced phase shifts of locomotion and expression of c-Fos and mPer1 in the SCN. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Cyclic AMP-responsive element-binding protein 1PRO_0000076598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei133 – 1331Phosphoserine; by CaMK1, CaMK2, CaMK4, PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5 and SGK1PROSITE-ProRule annotation3 Publications
Modified residuei142 – 1421Phosphoserine; by CaMK2PROSITE-ProRule annotation
Modified residuei271 – 2711Phosphoserine; by HIPK2PROSITE-ProRule annotation
Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki304 – 304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Post-translational modificationi

Phosphorylation of Ser-133 allows CREBBP binding. Stimulated by phosphorylation. Phosphorylated Ser-142 can be detected in the suprachiasmatic nucleus (SCN), the amygdala, the cortex, and the hippocampus but not in the striatum nor in the cerebellum. In the SCN, phosphorylation of Ser-142 and Ser-133 are stimulated by light exposure and submitted to circadian oscillations. In the retina, only phosphorylation of Ser-133 can be detected upon light exposure. Phosphorylation of both Ser-133 and Ser-142 in the SCN regulates the activity of CREB and participates in circadian rhythm generation. Phosphorylated upon calcium influx by CaMK4 and CaMK2 on Ser-133. CaMK4 is much more potent than CAMK2 in activating CREB. Phosphorylated by CaMK2 on Ser-142. Phosphorylation of Ser-142 blocks CREB-mediated transcription even when Ser-133 is phosphorylated. Phosphorylated by CaMK1. Phosphorylation of Ser-271 by HIPK2 in response to genotoxic stress promotes CREB1 activity, facilitating the recruitment of the coactivator CBP (By similarity). Phosphorylated at Ser-133 by RPS6KA3, RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli. CREBL2 positively regulates phosphorylation at Ser-133 thereby stimulating CREB1 transcriptional activity. In liver, phosphorylation is induced by fasting or glucagon in a circadian fashion.By similarity4 Publications
Sumoylated with SUMO1. Sumoylation on Lys-304, but not on Lys-285, is required for nuclear localization of this protein. Sumoylation is enhanced under hypoxia, promoting nuclear localization and stabilization (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ01147.
PRIDEiQ01147.

PTM databases

PhosphoSiteiQ01147.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ01147.
CleanExiMM_CREB1.
ExpressionAtlasiQ01147. baseline and differential.
GenevestigatoriQ01147.

Interactioni

Subunit structurei

Interacts with PPRC1. Binds DNA as a dimer. This dimer is stabilized by magnesium ions. Interacts, through the bZIP domain, with the coactivators TORC1/CRTC1, TORC2/CRTC2 and TORC3/CRTC3. Interacts (phosphorylated form) with TOX3 (By similarity). When phosphorylated on Ser-133, binds CREBBP. Interacts with ARRB1. Binds to HIPK2 (By similarity). Interacts with SGK1 (By similarity). Interacts with CREBL2; regulates CREB1 phosphorylation, stability and transcriptional activity.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CrebbpP454812EBI-2291098,EBI-296306
Crebl2Q32M004EBI-2291098,EBI-5314489
EP300Q094722EBI-2291098,EBI-447295From a different organism.
Ncor1Q609745EBI-2291098,EBI-349004

Protein-protein interaction databases

BioGridi198873. 13 interactions.
IntActiQ01147. 10 interactions.
MINTiMINT-263062.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi286 – 33348Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DH3X-ray3.00A/C285-339[»]
ProteinModelPortaliQ01147.
SMRiQ01147. Positions 116-149, 285-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01147.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 16060KIDPROSITE-ProRule annotationAdd
BLAST
Domaini283 – 34159bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni284 – 30926Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni311 – 33222Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation
Contains 1 KID (kinase-inducible) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG300199.
HOGENOMiHOG000007365.
HOVERGENiHBG011077.
InParanoidiQ01147.
KOiK05870.
OMAiQXISTIA.
OrthoDBiEOG72G18D.
PhylomeDBiQ01147.
TreeFamiTF106464.

Family and domain databases

InterProiIPR004827. bZIP.
IPR003102. Coactivator_CBP_pKID.
IPR029802. CREB1.
IPR001630. Leuzip_CREB.
[Graphical view]
PANTHERiPTHR22952:SF104. PTHR22952:SF104. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
PF02173. pKID. 1 hit.
[Graphical view]
PRINTSiPR00041. LEUZIPPRCREB.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS50953. KID. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: At least 6 isoforms are produced.

Isoform 1 (identifier: Q01147-1) [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
MTMESGADNQ QSGDAAVTEA ENQQMTVQAQ PQIATLAQVS MPAAHATSSA
60 70 80 90 100
PTVTLVQLPN GQTVQVHGVI QAAQPSVIQS PQVQTVQSSC KDLKRLFSGT
110 120 130 140 150
QISTIAESED SQESVDSVTD SQKRREILSR RPSYRKILND LSSDAPGVPR
160 170 180 190 200
IEEEKSEEET SAPAITTVTV PTPIYQTSSG QYIAITQGGA IQLANNGTDG
210 220 230 240 250
VQGLQTLTMT NAAATQPGTT ILQYAQTTDG QQILVPSNQV VVQAASGDVQ
260 270 280 290 300
TYQIRTAPTS TIAPGVVMAS SPALPTQPAE EAARKREVRL MKNREAAREC
310 320 330 340
RRKKKEYVKC LENRVAVLEN QNKTLIEELK ALKDLYCHKS D
Length:341
Mass (Da):36,674
Last modified:May 31, 1994 - v1
Checksum:iCF2958DE9174968A
GO
Isoform 2 (identifier: Q01147-2) [UniParc]FASTAAdd to basket

Also known as: CREB-delta

The sequence of this isoform differs from the canonical sequence as follows:
     88-101: Missing.

Show »
Length:327
Mass (Da):35,122
Checksum:i00D1F26B00D48442
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei88 – 10114Missing in isoform 2. CuratedVSP_000597Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67719
, X67721, X67724, X67725, X67726, X67727, X67728 Genomic DNA. Translation: CAA47953.1.
X67719
, X67721, X67722, X67724, X67725, X67726, X67727, X67728 Genomic DNA. Translation: CAA47954.1.
M95106 mRNA. Translation: AAA37456.1.
CCDSiCCDS15004.1. [Q01147-1]
CCDS15005.1. [Q01147-2]
PIRiS20955.
S42699.
RefSeqiNP_034082.1. NM_009952.2. [Q01147-1]
NP_598589.2. NM_133828.2. [Q01147-2]
XP_006495713.1. XM_006495650.2. [Q01147-1]
XP_006495714.1. XM_006495651.2. [Q01147-2]
UniGeneiMm.422634.

Genome annotation databases

EnsembliENSMUST00000049932; ENSMUSP00000059973; ENSMUSG00000025958. [Q01147-1]
ENSMUST00000087366; ENSMUSP00000084624; ENSMUSG00000025958. [Q01147-2]
ENSMUST00000185594; ENSMUSP00000139995; ENSMUSG00000025958. [Q01147-2]
ENSMUST00000190348; ENSMUSP00000140112; ENSMUSG00000025958. [Q01147-1]
GeneIDi12912.
KEGGimmu:12912.
UCSCiuc007bgr.1. mouse. [Q01147-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67719
, X67721, X67724, X67725, X67726, X67727, X67728 Genomic DNA. Translation: CAA47953.1.
X67719
, X67721, X67722, X67724, X67725, X67726, X67727, X67728 Genomic DNA. Translation: CAA47954.1.
M95106 mRNA. Translation: AAA37456.1.
CCDSiCCDS15004.1. [Q01147-1]
CCDS15005.1. [Q01147-2]
PIRiS20955.
S42699.
RefSeqiNP_034082.1. NM_009952.2. [Q01147-1]
NP_598589.2. NM_133828.2. [Q01147-2]
XP_006495713.1. XM_006495650.2. [Q01147-1]
XP_006495714.1. XM_006495651.2. [Q01147-2]
UniGeneiMm.422634.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DH3X-ray3.00A/C285-339[»]
ProteinModelPortaliQ01147.
SMRiQ01147. Positions 116-149, 285-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198873. 13 interactions.
IntActiQ01147. 10 interactions.
MINTiMINT-263062.

PTM databases

PhosphoSiteiQ01147.

Proteomic databases

PaxDbiQ01147.
PRIDEiQ01147.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049932; ENSMUSP00000059973; ENSMUSG00000025958. [Q01147-1]
ENSMUST00000087366; ENSMUSP00000084624; ENSMUSG00000025958. [Q01147-2]
ENSMUST00000185594; ENSMUSP00000139995; ENSMUSG00000025958. [Q01147-2]
ENSMUST00000190348; ENSMUSP00000140112; ENSMUSG00000025958. [Q01147-1]
GeneIDi12912.
KEGGimmu:12912.
UCSCiuc007bgr.1. mouse. [Q01147-1]

Organism-specific databases

CTDi1385.
MGIiMGI:88494. Creb1.

Phylogenomic databases

eggNOGiNOG300199.
HOGENOMiHOG000007365.
HOVERGENiHBG011077.
InParanoidiQ01147.
KOiK05870.
OMAiQXISTIA.
OrthoDBiEOG72G18D.
PhylomeDBiQ01147.
TreeFamiTF106464.

Enzyme and pathway databases

ReactomeiREACT_277525. CREB phosphorylation.
REACT_278898. NOTCH2 intracellular domain regulates transcription.
REACT_294637. CREB phosphorylation through the activation of CaMKK.
REACT_303391. CREB phosphorylation through the activation of Adenylate Cyclase.
REACT_308448. AKT phosphorylates targets in the nucleus.
REACT_309693. CaMK IV-mediated phosphorylation of CREB.
REACT_309838. CREB phosphorylation through the activation of CaMKII.
REACT_327612. CREB phosphorylation through the activation of Ras.
REACT_328033. Transcriptional activation of mitochondrial biogenesis.
REACT_328674. Constitutive PI3K/AKT Signaling in Cancer.
REACT_336227. PKA-mediated phosphorylation of CREB.
REACT_337888. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_339798. NCAM signaling for neurite out-growth.

Miscellaneous databases

ChiTaRSiCreb1. mouse.
EvolutionaryTraceiQ01147.
NextBioi282540.
PROiQ01147.
SOURCEiSearch...

Gene expression databases

BgeeiQ01147.
CleanExiMM_CREB1.
ExpressionAtlasiQ01147. baseline and differential.
GenevestigatoriQ01147.

Family and domain databases

InterProiIPR004827. bZIP.
IPR003102. Coactivator_CBP_pKID.
IPR029802. CREB1.
IPR001630. Leuzip_CREB.
[Graphical view]
PANTHERiPTHR22952:SF104. PTHR22952:SF104. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
PF02173. pKID. 1 hit.
[Graphical view]
PRINTSiPR00041. LEUZIPPRCREB.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS50953. KID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Multiple mRNA isoforms of the transcription activator protein CREB: generation by alternative splicing and specific expression in primary spermatocytes."
    Ruppert S., Cole T.J., Boshart M., Schmid E., Schuetz G.
    EMBO J. 11:1503-1512(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "The mouse CREB (cAMP responsive element binding protein) gene: structure, promoter analysis, and chromosomal localization."
    Cole T.J., Copeland N.G., Gilbert D.J., Jenkins N.A., Schuetz G., Ruppert R.
    Genomics 13:974-982(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  3. "Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism."
    Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C., Hoeger C., Montminy M.R.
    Mol. Cell. Biol. 16:694-703(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREBBP, PHOSPHORYLATION AT SER-133, MUTAGENESIS OF 137-ILE-LEU-138.
  4. "Phosphorylation of CREB Ser142 regulates light-induced phase shifts of the circadian clock."
    Gau D., Lemberger T., von Gall C., Kretz O., Le Minh N., Gass P., Schmid W., Schibler U., Korf H.W., Schuetz G.
    Neuron 34:245-253(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-133 AND SER-142, MUTAGENESIS OF SER-142, FUNCTION.
  5. "The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling."
    Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M., Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S.
    Nat. Immunol. 9:1028-1036(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-133, MUTAGENESIS OF SER-133.
  6. "Cryptochrome mediates circadian regulation of cAMP signaling and hepatic gluconeogenesis."
    Zhang E.E., Liu Y., Dentin R., Pongsawakul P.Y., Liu A.C., Hirota T., Nusinow D.A., Sun X., Landais S., Kodama Y., Brenner D.A., Montminy M., Kay S.A.
    Nat. Med. 16:1152-1156(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  7. "CREBL2, interacting with CREB, induces adipogenesis in 3T3-L1 adipocytes."
    Ma X., Zhang H., Yuan L., Jing H., Thacker P., Li D.
    Biochem. J. 439:27-38(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION, INTERACTION WITH CREBL2, SUBCELLULAR LOCATION.
  8. "The structure of a CREB bZIP.somatostatin CRE complex reveals the basis for selective dimerization and divalent cation-enhanced DNA binding."
    Schumacher M.A., Goodman R.H., Brennan R.G.
    J. Biol. Chem. 275:35242-35247(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH THE SOMATOSTATIN CAMP RESPONSE ELEMENT (SSCRE).

Entry informationi

Entry nameiCREB1_MOUSE
AccessioniPrimary (citable) accession number: Q01147
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 1994
Last sequence update: May 31, 1994
Last modified: March 31, 2015
This is version 154 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.