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Protein PAT1 homolog 1

 
Known also as: PAT1-like protein 1, Protein PAT1 homolog b

Known abbreviations: PATL1

 

FUNCTION:
 
RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly. In case of infection, required for translation and replication of hepatitis C virus (HCV). 
 
SUBUNIT STRUCTURE:
 
Interacts (via region A) with DDX6/RCK. Interacts (via region H and region C) with LSM1 and LSM4. Interacts (via region N) with DCP1A, DCP2, EDC3, EDC4 and XRN1. Interacts with the CCR4-NOT complex. Interacts with the Lsm-containing SMN-Sm protein complex. 
 
CELLULAR LOCALIZATION:
 
Cytoplasm › P-body 
 
TISSUE SPECIFICITY:
 
Ubiquitous. 
 
DOMAIN:
 
The region A, also named N-term, mediates the interaction with DDX6/RCK and is required for cytoplasmic mRNA processing body assembly. Ref.11 Ref.15
The region C, also named Pat-C, is required for RNA-binding and mediates the binding with the Lsm-containing SMN-Sm protein complex and the decapping machinery. It folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain. Ref.11 Ref.15



This protein can be a part of a given complexes: Activities in which Protein PAT1 homolog 1 is involved: Pathways in which Protein PAT1 homolog 1 is involved:

NCBI GI number(s): 189217919
189217918
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q86TB9 Q86TB9
BRENDA - -
KEGG hsa:219988 hsa:219988
PFAM: PF09770
PF09770
InterPro: IPR019167
IPR019167
CATH: - -
SCOP: - -
Solved crystal structures: 2XEQ
2XER
2XES
[PDB] [details]
[PDB] [details]
[PDB] [details]


Protein sequence:
MFRYESLEDCPLDEDEDAFQGLGEEDEEIDQFNDDTFGSGAVDDDWQEAH
ERLAELEEKLPVAVNEQTGNGERDEMDLLGDHEENLAERLSKMVIENELE
DPAIMRAVQTRPVLQPQPGSLNSSIWDGSEVLRRIRGPLLAQEMPTVSVL
EYALPQRPPQGPEDDRDLSERALPRRSTSPIIGSPPVRAVPIGTPPKQMA
VPSFTQQILCPKPVHVRPPMPPRYPAPYGERMSPNQLCSVPNSSLLGHPF
PPSVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKL
LQGRVGQMLPPAPGFRAFFSAPPSATPPPQQHPPGPGPHLQNLRSQAPMF
RPDTTHLHPQHRRLLHQRQQQNRSQHRNLNGAGDRGSHRSSHQDHLRKDP
YANLMLQREKDWVSKIQMMQLQSTDPYLDDFYYQNYFEKLEKLSAAEEIQ
GDGPKKERTKLITPQVAKLEHAYKPVQFEGSLGKLTVSSVNNPRKMIDAV
VTSRSEDDETKEKQVRDKRRKTLVIIEKTYSLLLDVEDYERRYLLSLEEE
RPALMDDRKHKICSMYDNLRGKLPGQERPSDDHFVQIMCIRKGKRMVARI
LPFLSTEQAADILMTTARNLPFLIKKDAQDEVLPCLLSPFSLLLYHLPSV
SITSLLRQLMNLPQSAATPALSNPHLTAVLQNKFGLSLLLILLSRGEDLQ
SSDPATESTQNNQWTEVMFMATRELLRIPQAALAKPISIPTNLVSLFSRY
VDRQKLNLLETKLQLVQGIR

Protein PAT1 homolog 1 (Homo sapiens) is product of expression of PATL1 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
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 Nat Genet 2004-02-01 (36) 14702039
The human Pat1b protein: a novel mRNA deadenylation factor identified by a new immunoprecipitation technique. Totaro A, Renzi F, La Fata G, Mattioli C, Raabe M, Urlaub H, Achsel T Nucleic Acids Res 2011-02-01 (39) 20852261
Distinct functions of maternal and somatic Pat1 protein paralogs. Marnef A, Maldonado M, Bugaut A, Balasubramanian S, Kress M, Weil D, Standart N RNA 2010-11-01 (16) 20826699
Human Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodies. Ozgur S, Chekulaeva M, Stoecklin G Mol Cell Biol 2010-09-01 (30) 20584987
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem 2009-06-01 (81) 19413330
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
The full-ORF clone resource of the German cDNA Consortium. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I BMC Genomics 2007-01-01 (8) 17974005
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
Human chromosome 11 DNA sequence and analysis including novel gene identification. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y Nature 2006-03-23 (440) 16554811
Identification of PatL1, a human homolog to yeast P body component Pat1. Scheller N, Resa-Infante P, de la Luna S, Galao RP, Albrecht M, Kaestner L, Lipp P, Lengauer T, Meyerhans A, Diez J Biochim Biophys Acta 2007-12-01 (1773) 17936923
Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates. Scheller N, Mina LB, Galao RP, Chari A, Gimenez-Barcons M, Noueiry A, Fischer U, Meyerhans A, Diez J Proc Natl Acad Sci U S A 2009-08-11 (106) 19628699
The C-terminal alpha-alpha superhelix of Pat is required for mRNA decapping in metazoa. Braun JE, Tritschler F, Haas G, Igreja C, Truffault V, Weichenrieder O, Izaurralde E EMBO J 2010-07-21 (29) 20543818



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Last modification of this entry: Sept. 25, 2012.

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