Details for: SRRM1
Associated with
Other Information
Genular Protein ID: 809222640
Symbol: SRRM1_HUMAN
Name: Serine/arginine repetitive matrix protein 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9531537
PubMed ID: 16710414
Title: The DNA sequence and biological annotation of human chromosome 1.
PubMed ID: 16710414
DOI: 10.1038/nature04727
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 10339552
Title: The SRm160/300 splicing coactivator is required for exon-enhancer function.
PubMed ID: 10339552
PubMed ID: 11118221
Title: The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions.
PubMed ID: 11118221
PubMed ID: 10809668
Title: Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions.
PubMed ID: 10809668
PubMed ID: 10668804
Title: The SRm160/300 splicing coactivator subunits.
PubMed ID: 10668804
PubMed ID: 11546874
Title: Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1.
PubMed ID: 11546874
PubMed ID: 12093754
Title: The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling.
PubMed ID: 12093754
DOI: 10.1093/emboj/cdf345
PubMed ID: 11739730
Title: SRm160 splicing coactivator promotes transcript 3'-end cleavage.
PubMed ID: 11739730
PubMed ID: 11991638
Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
PubMed ID: 11991638
PubMed ID: 12944400
Title: An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation.
PubMed ID: 12944400
PubMed ID: 12624182
Title: The spatial targeting and nuclear matrix binding domains of SRm160.
PubMed ID: 12624182
PubMed ID: 15144186
Title: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.
PubMed ID: 15144186
DOI: 10.1021/ac035352d
PubMed ID: 15024032
Title: In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160.
PubMed ID: 15024032
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 17924679
Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.
PubMed ID: 17924679
DOI: 10.1021/pr070152u
PubMed ID: 19367720
Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.
PubMed ID: 19367720
DOI: 10.1021/pr800500r
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 18318008
Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.
PubMed ID: 18318008
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 29973724
Title: Kinase-controlled phase transition of membraneless organelles in mitosis.
PubMed ID: 29973724
PubMed ID: 12600940
Title: Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing.
PubMed ID: 12600940
DOI: 10.1101/gad.1060403
PubMed ID: 33509932
Title: Structure of the activated human minor spliceosome.
PubMed ID: 33509932
Sequence Information:
- Length: 904
- Mass: 102335
- Checksum: 27D4D2A48EDBFED3
- Sequence:
MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP WITKRVTEIL GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE FMGELWPLLL SAQENIAGIP SAFLELKKEE IKQRQIEQEK LASMKKQDED KDKRDKEEKE SSREKRERSR SPRRRKSRSP SPRRRSSPVR RERKRSHSRS PRHRTKSRSP SPAPEKKEKT PELPEPSVKV KEPSVQEATS TSDILKVPKP EPIPEPKEPS PEKNSKKEKE KEKTRPRSRS RSKSRSRTRS RSPSHTRPRR RHRSRSRSYS PRRRPSPRRR PSPRRRTPPR RMPPPPRHRR SRSPVRRRRR SSASLSGSSS SSSSSRSRSP PKKPPKRTSS PPRKTRRLSP SASPPRRRHR PSPPATPPPK TRHSPTPQQS NRTRKSRVSV SPGRTSGKVT KHKGTEKRES PSPAPKPRKV ELSESEEDKG GKMAAADSVQ QRRQYRRQNQ QSSSDSGSSS SSEDERPKRS HVKNGEVGRR RRHSPSRSAS PSPRKRQKET SPRGRRRRSP SPPPTRRRRS PSPAPPPRRR RTPTPPPRRR TPSPPPRRRS PSPRRYSPPI QRRYSPSPPP KRRTASPPPP PKRRASPSPP PKRRVSHSPP PKQRSSPVTK RRSPSLSSKH RKGSSPSRST REARSPQPNK RHSPSPRPRA PQTSSSPPPV RRGASSSPQR RQSPSPSTRP IRRVSRTPEP KKIKKAASPS PQSVRRVSSS RSVSGSPEPA AKKPPAPPSP VQSQSPSTNW SPAVPVKKAK SPTPSPSPPR NSDQEGGGKK KKKKKDKKHK KDKKHKKHKK HKKEKAVAAA AAAAVTPAAI AAATTTLAQE EPVAAPEPKK ETESEAEDNL DDLEKHLREK ALRSMRKAQV SPQS
Genular Protein ID: 1232902720
Symbol: B7Z7U0_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Sequence Information:
- Length: 916
- Mass: 103797
- Checksum: D6E2CA5A76B4B4E3
- Sequence:
MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP WITKRVTEIL GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE FMGELWPLLL SAQENIAGIP SAFLELKKEE IKQRQIEQEK LASMKKQDED KDKRDKEEKE SSREKRERSR SPRRRKSRSP SPRRRSSPVR RERKRSHSRS PRHRTKSRSP SPAPEKKEKT PELPEPSVKV KEPSVQEATS TSDILKVPKP EPIPEPKEPS PEKNSKKEKE KEKTRPRSRS RSKSRSRTRS RSPSHTRPRR RHRSRSRSYS PRRRPSPRRR PSPRRRTPPR RMPPPPRHRR SRSPVRRRRR SSASLSGSSS SSSSSRSRSP PKKPPKRTSS PPRKTRRLSP SASPPRRRHR PSPPATPPPK TRHSPTPQQS NRTRKSRVSV SPGRTSVTKH KGTEKRESPS PAPKPRKVEL SESEEDKGGK MAAADSVQQR RQYRRQDQQS SSDSGSSSSS EDERPKRSHV KNGEVGRRRR HSPSRSASPS PRKRQKETSP RMQMGKRWQS PVTKSGRRRR SPSPPPTRRR RSPSPAPPPR RRRTPTPPPR RRTPSPPPRR RSPSPRRYSP PIQRRYSPSP PPKRRTASPP PPPKRRASPS PPPKRRVSHS PPPKQRSSPV TKRRSPSLSS KHRKGSSPSR STREARSPQP NKRHSPSPRP RAPQTSSSPP PVRRGASSSP QRRQSPSPST RPIRRVSRTP EPKKIKKAAS PSPQSVRRVS SSRSVSGSPE PAAKKPPAPP SPVQSQSPST NWSPAVPVKK AKSPTPSPSP PRNSDQEGGG KKKKKKKDKK HKKDKKHKKH KKHKKEKAVA AAAAAAVTPA AIAAATTTLA QEEPVAAPEP KKETESEAED NLDDLEKHLR EKALRSMRKA QVSPQS
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.