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Accession Number: | Q13838 |
Protein Name: | Spliceosome RNA helicase BAT1 aka DEAD box protein UAP56 |
Length: | 428 |
Molecular Weight: | 48991.00 |
Species: | Homo sapiens (Human) [9606] |
Location1 / Topology2 / Orientation3: | Nucleus1 |
Substrate | messenger RNA |
Cross database links:
RefSeq: | NP_004631.1 NP_542165.1 |
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Entrez Gene ID: | 7919 |
Pfam: | PF00270 PF00271 |
OMIM: |
142560 gene |
KEGG: | hsa:7919 |
Gene Ontology
GO:0016607
C:nuclear speck
GO:0005681
C:spliceosomal complex
GO:0000346
C:transcription export complex
GO:0005524
F:ATP binding
GO:0043008
F:ATP-dependent protein binding
GO:0004004
F:ATP-dependent RNA helicase activity
GO:0042802
F:identical protein binding
GO:0030621
F:U4 snRNA binding
GO:0017070
F:U6 snRNA binding
GO:0046784
P:intronless viral mRNA export from host nucleus
GO:0010501
P:RNA secondary structure unwinding
GO:0000245
P:spliceosome assembly
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References (20)[1] “The BAT1 gene in the MHC encodes an evolutionarily conserved putative nuclear RNA helicase of the DEAD family.” Peelman L.et.al. 7601445 [2] “Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity.” Shiina T.et.al. 16702430 [3] “The DNA sequence and analysis of human chromosome 6.” Mungall A.J.et.al. 14574404 [4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [5] “U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction.” Fleckner J.et.al. 9242493 [6] “Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly.” Luo M.-J.et.al. 11675789 [7] “An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation.” McCracken S.et.al. 12944400 [8] “Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region.” Lehner B.et.al. 14667819 [9] “Linking transcriptional elongation and messenger RNA export to metastatic breast cancers.” Guo S.et.al. 15833825 [10] “Recruitment of the human TREX complex to mRNA during splicing.” Masuda S.et.al. 15998806 [11] “Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically links RNA polymerase II and RNA processing factors.” Li Y.et.al. 15870275 [12] “Human mRNA export machinery recruited to the 5' end of mRNA.” Cheng H.et.al. 17190602 [13] “Biochemical characterization of the ATPase and helicase activity of UAP56, an essential pre-mRNA splicing and mRNA export factor.” Shen J.et.al. 17562711 [14] “Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication.” Boyne J.R.et.al. 18974867 [15] “A quantitative atlas of mitotic phosphorylation.” Dephoure N.et.al. 18669648 [16] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.” Gauci S.et.al. 19413330 | |
Structure: | |
External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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1: MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI 61: VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVSVLVMC 121: HTRELAFQIS KEYERFSKYM PNVKVAVFFG GLSIKKDEEV LKKNCPHIVV GTPGRILALA 181: RNKSLNLKHI KHFILDECDK MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR 241: KFMQDPMEIF VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC 301: IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG MDIERVNIAF 361: NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL NDVQDRFEVN ISELPDEIDI 421: SSYIEQTR