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Protein

Polyadenylate-binding protein 1

Gene

Pabpc1

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

Functioni

Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (By similarity).By similarity

GO - Molecular functioni

  1. mRNA binding Source: Ensembl
  2. nucleotide binding Source: InterPro
  3. poly(A) binding Source: UniProtKB
  4. poly(A) RNA binding Source: MGI
  5. poly(U) RNA binding Source: MGI
  6. protein C-terminus binding Source: MGI

GO - Biological processi

  1. gene silencing by RNA Source: UniProtKB
  2. mRNA processing Source: UniProtKB-KW
  3. negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  5. positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
  6. positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
  7. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Nonsense-mediated mRNA decay

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292503. Translation initiation complex formation.
REACT_298772. Deadenylation of mRNA.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein 1
Short name:
PABP-1
Short name:
Poly(A)-binding protein 1
Gene namesi
Name:Pabpc1
Synonyms:Pabp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1349722. Pabpc1.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Nucleus By similarity

  3. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus (By similarity).By similarity

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: MGI
  2. cytoplasm Source: MGI
  3. cytoplasmic ribonucleoprotein granule Source: MGI
  4. cytoplasmic stress granule Source: UniProtKB
  5. extracellular vesicular exosome Source: MGI
  6. focal adhesion Source: MGI
  7. membrane Source: MGI
  8. nucleus Source: MGI
  9. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636Polyadenylate-binding protein 1PRO_0000081699Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei140 – 1401PhosphotyrosineBy similarity
Modified residuei299 – 2991N6-methyllysineBy similarity
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei361 – 3611N6,N6-dimethyllysineBy similarity
Modified residuei455 – 4551Omega-N-methylated arginine; by CARM1By similarity
Modified residuei460 – 4601Omega-N-methylated arginine; by CARM1By similarity
Modified residuei493 – 4931Dimethylated arginine; alternateBy similarity
Modified residuei493 – 4931Omega-N-methylarginine; alternateBy similarity
Modified residuei506 – 5061Dimethylated arginineBy similarity
Modified residuei512 – 5121N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated by MAPKAPK2.By similarity
Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP29341.
PaxDbiP29341.
PRIDEiP29341.

2D gel databases

REPRODUCTION-2DPAGEP29341.

PTM databases

PhosphoSiteiP29341.

Expressioni

Gene expression databases

BgeeiP29341.
CleanExiMM_PABPC1.
ExpressionAtlasiP29341. baseline and differential.
GenevestigatoriP29341.

Interactioni

Subunit structurei

Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Directly interacts with IGF2BP1. Part of a complex associated with the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR. Interacts with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1 and PAIP2. Interacts with PAIP1 with a 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry. Identified in the spliceosome C complex. Interacts with NFX1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with LARP1 and LARP4B. May interact with SETX (By similarity). The interaction with CSDE1 is direct and RNA-independent (PubMed:15314026). Found in a mRNP complex with YBX2 (PubMed:10076007). Interacts with PAPD4/GLD2 (PubMed:17927953). Interacts with PIWIL1 (PubMed:19020299). Interacts (via the second and third RRM domains and the C-terminus) with PAIP2B (via central acidic portion and C-terminus).By similarity4 Publications

Protein-protein interaction databases

BioGridi202010. 15 interactions.
DIPiDIP-32127N.
IntActiP29341. 14 interactions.
MINTiMINT-4123966.

Structurei

3D structure databases

ProteinModelPortaliP29341.
SMRiP29341. Positions 10-435, 494-636.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 8979RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini99 – 17577RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 26878RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini294 – 37077RRM 4PROSITE-ProRule annotationAdd
BLAST
Domaini542 – 61978PABCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 289124CSDE1-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi495 – 5017Poly-Ala

Domaini

The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact respectively with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.By similarity
The RNA-binding domains RRM2 and RRM3 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively.By similarity

Sequence similaritiesi

Contains 1 PABC domain.PROSITE-ProRule annotation
Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000217922.
HOVERGENiHBG002295.
InParanoidiP29341.
KOiK13126.
OMAiCLEHEIL.
OrthoDBiEOG7RV9FP.
TreeFamiTF300458.

Family and domain databases

Gene3Di1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF63570. SSF63570. 1 hit.
TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
PROSITEiPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR
60 70 80 90 100
SLGYAYVNFQ QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN
110 120 130 140 150
IFIKNLDKSI DNKALYDTFS AFGNILSCKV VCDENGSKGY GFVHFETQEA
160 170 180 190 200
AERAIEKMNG MLLNDRKVFV GRFKSRKERE AELGARAKEF TNVYIKNFGE
210 220 230 240 250
DMDDERLKEL FGKFGPALSV KVMTDESGKS KGFGFVSFER HEDAQKAVDE
260 270 280 290 300
MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
310 320 330 340 350
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV
360 370 380 390 400
TEMNGRIVAT KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY
410 420 430 440 450
QPAPPSGYFM AAIPQTQNRA AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM
460 470 480 490 500
PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ RVANTSTQTM GPRPAAAAAA
510 520 530 540 550
ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ GQEPLTASML
560 570 580 590 600
ASAPPQEQKQ MLGERLFPLI QAMHPSLAGK ITGMLLEIDN SELLHMLESP
610 620 630
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
Length:636
Mass (Da):70,671
Last modified:July 27, 2011 - v2
Checksum:iE5BB6D5BA4F86CB7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761R → Q in CAA46522 (PubMed:1630930).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65553 mRNA. Translation: CAA46522.1.
AK044829 mRNA. Translation: BAC32110.1.
AK133196 mRNA. Translation: BAE21553.1.
AK159703 mRNA. Translation: BAE35302.1.
AK159733 mRNA. Translation: BAE35327.1.
AK160968 mRNA. Translation: BAE36120.1.
AK161123 mRNA. Translation: BAE36203.1.
AK161671 mRNA. Translation: BAE36522.1.
AK168466 mRNA. Translation: BAE40360.1.
CH466541 Genomic DNA. Translation: EDL08818.1.
BC003870 mRNA. Translation: AAH03870.1.
BC011207 mRNA. Translation: AAH11207.1.
BC023145 mRNA. Translation: AAH23145.1.
BC046233 mRNA. Translation: AAH46233.1.
CCDSiCCDS27431.1.
PIRiI48718.
RefSeqiNP_032800.2. NM_008774.3.
UniGeneiMm.371570.

Genome annotation databases

EnsembliENSMUST00000001809; ENSMUSP00000001809; ENSMUSG00000022283.
GeneIDi18458.
KEGGimmu:18458.
UCSCiuc007vmx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65553 mRNA. Translation: CAA46522.1.
AK044829 mRNA. Translation: BAC32110.1.
AK133196 mRNA. Translation: BAE21553.1.
AK159703 mRNA. Translation: BAE35302.1.
AK159733 mRNA. Translation: BAE35327.1.
AK160968 mRNA. Translation: BAE36120.1.
AK161123 mRNA. Translation: BAE36203.1.
AK161671 mRNA. Translation: BAE36522.1.
AK168466 mRNA. Translation: BAE40360.1.
CH466541 Genomic DNA. Translation: EDL08818.1.
BC003870 mRNA. Translation: AAH03870.1.
BC011207 mRNA. Translation: AAH11207.1.
BC023145 mRNA. Translation: AAH23145.1.
BC046233 mRNA. Translation: AAH46233.1.
CCDSiCCDS27431.1.
PIRiI48718.
RefSeqiNP_032800.2. NM_008774.3.
UniGeneiMm.371570.

3D structure databases

ProteinModelPortaliP29341.
SMRiP29341. Positions 10-435, 494-636.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202010. 15 interactions.
DIPiDIP-32127N.
IntActiP29341. 14 interactions.
MINTiMINT-4123966.

PTM databases

PhosphoSiteiP29341.

2D gel databases

REPRODUCTION-2DPAGEP29341.

Proteomic databases

MaxQBiP29341.
PaxDbiP29341.
PRIDEiP29341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001809; ENSMUSP00000001809; ENSMUSG00000022283.
GeneIDi18458.
KEGGimmu:18458.
UCSCiuc007vmx.2. mouse.

Organism-specific databases

CTDi26986.
MGIiMGI:1349722. Pabpc1.

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000217922.
HOVERGENiHBG002295.
InParanoidiP29341.
KOiK13126.
OMAiCLEHEIL.
OrthoDBiEOG7RV9FP.
TreeFamiTF300458.

Enzyme and pathway databases

ReactomeiREACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292503. Translation initiation complex formation.
REACT_298772. Deadenylation of mRNA.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

ChiTaRSiPabpc1. mouse.
NextBioi294152.
PROiP29341.
SOURCEiSearch...

Gene expression databases

BgeeiP29341.
CleanExiMM_PABPC1.
ExpressionAtlasiP29341. baseline and differential.
GenevestigatoriP29341.

Family and domain databases

Gene3Di1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF63570. SSF63570. 1 hit.
TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
PROSITEiPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a mouse testis poly(A) binding protein cDNA."
    Wang M.-Y., Cutler M., Karimpour I., Kleene K.C.
    Nucleic Acids Res. 20:3519-3519(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  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].
    Strain: C57BL/6J.
    Tissue: Embryo, Head, Skin and Testis.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    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].
    Strain: C57BL/6 and Czech II.
    Tissue: Mammary tumor.
  5. "The mouse Y-box protein, MSY2, is associated with a kinase on non-polysomal mouse testicular mRNAs."
    Herbert T.P., Hecht N.B.
    Nucleic Acids Res. 27:1747-1753(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH YBX2.
  6. "UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant."
    Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.
    Genes Dev. 18:2010-2023(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSDE1.
  7. "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.
  8. "Characterization of two cytoplasmic poly(A)-binding proteins, PABPC1 and PABPC2, in mouse spermatogenic cells."
    Kimura M., Ishida K., Kashiwabara S., Baba T.
    Biol. Reprod. 80:545-554(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIWIL1.

Entry informationi

Entry nameiPABP1_MOUSE
AccessioniPrimary (citable) accession number: P29341
Secondary accession number(s): Q99L36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: April 29, 2015
This is version 151 of the entry and version 2 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

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.