SRRM1

Protein-coding gene in the species Homo sapiens
SRRM1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1MP1

Identifiers
AliasesSRRM1, 160-KD, POP101, SRM160, serine and arginine repetitive matrix 1
External IDsOMIM: 605975; MGI: 1858303; HomoloGene: 136796; GeneCards: SRRM1; OMA:SRRM1 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for SRRM1
Genomic location for SRRM1
Band1p36.11Start24,631,716 bp[1]
End24,673,267 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for SRRM1
Genomic location for SRRM1
Band4|4 D3Start135,320,484 bp[2]
End135,353,321 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • corpus epididymis

  • sural nerve

  • caput epididymis

  • right uterine tube

  • left ovary

  • buccal mucosa cell

  • right ovary

  • body of uterus

  • tail of epididymis

  • right hemisphere of cerebellum
Top expressed in
  • tail of embryo

  • genital tubercle

  • primitive streak

  • Paneth cell

  • abdominal wall

  • neural layer of retina

  • ciliary body

  • Ileal epithelium

  • zygote

  • cumulus cell
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • protein binding
  • RNA binding
Cellular component
  • nuclear matrix
  • cytosol
  • catalytic step 2 spliceosome
  • spliceosomal complex
  • nucleus
  • nucleoplasm
  • nuclear speck
Biological process
  • RNA splicing, via transesterification reactions
  • mRNA splicing, via spliceosome
  • termination of RNA polymerase II transcription
  • mRNA processing
  • mRNA 3'-end processing
  • mRNA export from nucleus
  • RNA splicing
  • RNA export from nucleus
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10250

51796

Ensembl

ENSG00000133226

ENSMUSG00000028809

UniProt

Q8IYB3

Q52KI8

RefSeq (mRNA)

NM_001303448
NM_001303449
NM_005839

NM_001130477
NM_016799
NM_001369067
NM_001369068
NM_001369069

NM_001369070
NM_001369071
NM_001369072
NM_001369073
NM_001369074

RefSeq (protein)
NP_001290377
NP_001290378
NP_005830
NP_001353494
NP_001353495

NP_001353496
NP_001353497
NP_001353498
NP_001353499
NP_001353500
NP_001353501
NP_001353502
NP_001353504
NP_001353505
NP_001353506
NP_001353507
NP_001353510
NP_001353511
NP_001353513
NP_001353514
NP_001353515
NP_001353516
NP_001353517
NP_001353518
NP_001353519
NP_001353520
NP_001353521
NP_001353522
NP_001353523
NP_001353524
NP_001353525
NP_001353526
NP_001353527
NP_001353528
NP_001353529

NP_001123949
NP_058079
NP_001355996
NP_001355997
NP_001355998

NP_001355999
NP_001356000
NP_001356001
NP_001356002
NP_001356003

Location (UCSC)Chr 1: 24.63 – 24.67 MbChr 4: 135.32 – 135.35 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/arginine repetitive matrix protein 1 is a protein that in humans is encoded by the SRRM1 gene.[5][6]

Interactions

SRRM1 has been shown to interact with CDC5L.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000133226 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028809 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Blencowe BJ, Issner R, Nickerson JA, Sharp PA (May 1998). "A coactivator of pre-mRNA splicing". Genes Dev. 12 (7): 996–1009. doi:10.1101/gad.12.7.996. PMC 316672. PMID 9531537.
  6. ^ "Entrez Gene: SRRM1 serine/arginine repetitive matrix 1".
  7. ^ Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.

Further reading

  • Wang HY, Lin W, Dyck JA, Yeakley JM, Songyang Z, Cantley LC, Fu XD (1998). "SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells". J. Cell Biol. 140 (4): 737–50. doi:10.1083/jcb.140.4.737. PMC 2141757. PMID 9472028.
  • Wilson KF, Fortes P, Singh US, Ohno M, Mattaj IW, Cerione RA (1999). "The nuclear cap-binding complex is a novel target of growth factor receptor-coupled signal transduction". J. Biol. Chem. 274 (7): 4166–73. doi:10.1074/jbc.274.7.4166. PMID 9933612.
  • Eldridge AG, Li Y, Sharp PA, Blencowe BJ (1999). "The SRm160/300 splicing coactivator is required for exon-enhancer function". Proc. Natl. Acad. Sci. U.S.A. 96 (11): 6125–30. Bibcode:1999PNAS...96.6125E. doi:10.1073/pnas.96.11.6125. PMC 26846. PMID 10339552.
  • Blencowe BJ, Baurén G, Eldridge AG, Issner R, Nickerson JA, Rosonina E, Sharp PA (2000). "The SRm160/300 splicing coactivator subunits". RNA. 6 (1): 111–20. doi:10.1017/S1355838200991982. PMC 1369899. PMID 10668804.
  • Le Hir H, Moore MJ, Maquat LE (2000). "Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions". Genes Dev. 14 (9): 1098–108. doi:10.1101/gad.14.9.1098. PMC 316578. PMID 10809668.
  • McGarvey T, Rosonina E, McCracken S, Li Q, Arnaout R, Mientjes E, Nickerson JA, Awrey D, Greenblatt J, Grosveld G, Blencowe BJ (2000). "The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes". J. Cell Biol. 150 (2): 309–20. doi:10.1083/jcb.150.2.309. PMC 2180225. PMID 10908574.
  • Le Hir H, Izaurralde E, Maquat LE, Moore MJ (2000). "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions". EMBO J. 19 (24): 6860–9. doi:10.1093/emboj/19.24.6860. PMC 305905. PMID 11118221.
  • Lykke-Andersen J, Shu MD, Steitz JA (2001). "Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1". Science. 293 (5536): 1836–9. Bibcode:2001Sci...293.1836L. doi:10.1126/science.1062786. PMID 11546874. S2CID 389385.
  • McCracken S, Lambermon M, Blencowe BJ (2002). "SRm160 splicing coactivator promotes transcript 3'-end cleavage". Mol. Cell. Biol. 22 (1): 148–60. doi:10.1128/MCB.22.1.148-160.2002. PMC 134228. PMID 11739730.
  • Szymczyna BR, Pineda-Lucena A, Mills JL, Szyperski T, Arrowsmith CH (2002). "1H, 13C, and 15N resonance assignments and secondary structure of the PWI domain from SRm160 using reduced dimensionality NMR". J. Biomol. NMR. 22 (3): 299–300. doi:10.1023/A:1014904502424. PMID 11991360. S2CID 13594831.
  • Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ (2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA. 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.
  • Lejeune F, Ishigaki Y, Li X, Maquat LE (2002). "The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling". EMBO J. 21 (13): 3536–45. doi:10.1093/emboj/cdf345. PMC 126094. PMID 12093754.
  • Meissner M, Lopato S, Gotzmann J, Sauermann G, Barta A (2003). "Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins". Exp. Cell Res. 283 (2): 184–95. doi:10.1016/S0014-4827(02)00046-0. PMID 12581738.
  • Szymczyna BR, Bowman J, McCracken S, Pineda-Lucena A, Lu Y, Cox B, Lambermon M, Graveley BR, Arrowsmith CH, Blencowe BJ (2003). "Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing". Genes Dev. 17 (4): 461–75. doi:10.1101/gad.1060403. PMC 196000. PMID 12600940.
  • Wagner S, Chiosea S, Nickerson JA (2003). "The spatial targeting and nuclear matrix binding domains of SRm160". Proc. Natl. Acad. Sci. U.S.A. 100 (6): 3269–74. Bibcode:2003PNAS..100.3269W. doi:10.1073/pnas.0438055100. PMC 152281. PMID 12624182.
  • McCracken S, Longman D, Johnstone IL, Cáceres JF, Blencowe BJ (2003). "An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation". J. Biol. Chem. 278 (45): 44153–60. doi:10.1074/jbc.M306856200. PMID 12944400.
  • Wagner S, Chiosea S, Ivshina M, Nickerson JA (2004). "In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160". J. Cell Biol. 164 (6): 843–50. doi:10.1083/jcb.200307002. PMC 2172284. PMID 15024032.
  • Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • v
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  • e
  • 1mp1: Solution structure of the PWI motif from SRm160
    1mp1: Solution structure of the PWI motif from SRm160


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