Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8IYB3

- SRRM1_HUMAN

UniProt

Q8IYB3 - SRRM1_HUMAN

Protein

Serine/arginine repetitive matrix protein 1

Gene

SRRM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Part of pre- and post-splicing multiprotein mRNP complexes. Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates.6 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA 3'-end processing Source: Reactome
    3. mRNA export from nucleus Source: Reactome
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. RNA splicing Source: Reactome
    6. RNA splicing, via transesterification reactions Source: UniProtKB
    7. termination of RNA polymerase II transcription Source: Reactome
    8. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Protein family/group databases

    TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/arginine repetitive matrix protein 1
    Alternative name(s):
    SR-related nuclear matrix protein of 160 kDa
    Short name:
    SRm160
    Ser/Arg-related nuclear matrix protein
    Gene namesi
    Name:SRRM1
    Synonyms:SRM160
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16638. SRRM1.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytosol Source: Reactome
    3. nuclear matrix Source: UniProtKB-SubCell
    4. nuclear speck Source: UniProtKB-SubCell
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201K → A: Strongly reduces DNA and RNA-binding. 1 Publication
    Mutagenesisi22 – 221K → A: Strongly reduces DNA and RNA-binding. 1 Publication
    Mutagenesisi23 – 231K → A: Strongly reduces DNA and RNA-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA38177.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 904904Serine/arginine repetitive matrix protein 1PRO_0000076326Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei7 – 71CitrullineBy similarity
    Modified residuei140 – 1401N6-acetyllysine1 Publication
    Modified residuei220 – 2201Phosphothreonine5 Publications
    Modified residuei227 – 2271Phosphoserine1 Publication
    Modified residuei234 – 2341Phosphoserine1 Publication
    Modified residuei260 – 2601Phosphoserine3 Publications
    Modified residuei389 – 3891Phosphoserine3 Publications
    Modified residuei391 – 3911Phosphoserine2 Publications
    Modified residuei393 – 3931Phosphoserine3 Publications
    Modified residuei402 – 4021Phosphoserine4 Publications
    Modified residuei406 – 4061Phosphothreonine3 Publications
    Modified residuei414 – 4141Phosphoserine1 Publication
    Modified residuei416 – 4161Phosphothreonine1 Publication
    Modified residuei420 – 4201Phosphoserine1 Publication
    Modified residuei429 – 4291Phosphoserine3 Publications
    Modified residuei431 – 4311Phosphoserine3 Publications
    Modified residuei436 – 4361Phosphoserine1 Publication
    Modified residuei450 – 4501Phosphoserine4 Publications
    Modified residuei452 – 4521Phosphoserine4 Publications
    Modified residuei463 – 4631Phosphoserine3 Publications
    Modified residuei465 – 4651Phosphoserine3 Publications
    Modified residuei478 – 4781Phosphoserine2 Publications
    Modified residuei549 – 5491Phosphoserine1 Publication
    Modified residuei551 – 5511Phosphoserine1 Publication
    Modified residuei555 – 5551Phosphothreonine1 Publication
    Modified residuei560 – 5601Phosphoserine3 Publications
    Modified residuei562 – 5621Phosphoserine3 Publications
    Modified residuei572 – 5721Phosphothreonine1 Publication
    Modified residuei574 – 5741Phosphothreonine1 Publication
    Modified residuei581 – 5811Phosphothreonine1 Publication
    Modified residuei583 – 5831Phosphoserine1 Publication
    Modified residuei597 – 5971Phosphoserine3 Publications
    Modified residuei605 – 6051Phosphoserine3 Publications
    Modified residuei607 – 6071Phosphoserine3 Publications
    Modified residuei614 – 6141Phosphothreonine3 Publications
    Modified residuei616 – 6161Phosphoserine4 Publications
    Modified residuei626 – 6261Phosphoserine3 Publications
    Modified residuei628 – 6281Phosphoserine3 Publications
    Modified residuei636 – 6361Phosphoserine2 Publications
    Modified residuei638 – 6381Phosphoserine2 Publications
    Modified residuei646 – 6461Phosphoserine1 Publication
    Modified residuei694 – 6941Phosphoserine1 Publication
    Modified residuei695 – 6951PhosphoserineBy similarity
    Modified residuei696 – 6961Phosphoserine4 Publications
    Modified residuei705 – 7051Phosphoserine1 Publication
    Modified residuei707 – 7071Phosphoserine1 Publication
    Modified residuei713 – 7131Phosphoserine1 Publication
    Modified residuei715 – 7151Phosphoserine1 Publication
    Modified residuei738 – 7381Phosphoserine3 Publications
    Modified residuei740 – 7401Phosphoserine2 Publications
    Modified residuei748 – 7481Phosphoserine1 Publication
    Modified residuei752 – 7521Phosphoserine2 Publications
    Modified residuei754 – 7541Phosphoserine4 Publications
    Modified residuei756 – 7561Phosphoserine4 Publications
    Modified residuei769 – 7691Phosphoserine4 Publications
    Modified residuei775 – 7751Phosphoserine2 Publications
    Modified residuei777 – 7771Phosphoserine1 Publication
    Modified residuei781 – 7811Phosphoserine3 Publications
    Modified residuei791 – 7911Phosphoserine1 Publication
    Modified residuei793 – 7931Phosphothreonine1 Publication
    Modified residuei795 – 7951Phosphoserine1 Publication
    Modified residuei872 – 8721Phosphothreonine5 Publications
    Modified residuei874 – 8741Phosphoserine5 Publications

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiQ8IYB3.
    PaxDbiQ8IYB3.
    PRIDEiQ8IYB3.

    PTM databases

    PhosphoSiteiQ8IYB3.

    Miscellaneous databases

    PMAP-CutDBQ8IYB3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IYB3.
    BgeeiQ8IYB3.
    CleanExiHS_SRRM1.
    GenevestigatoriQ8IYB3.

    Organism-specific databases

    HPAiHPA049941.
    HPA058612.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, PRPF8, NCBP1, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with BAT1, CPSF1, RBM8A, RNPS1, and ALYREF/THOC4. Seems to be a compound of RNA export complexes that are released from speckles in a ATP-dependent manner.8 Publications

    Protein-protein interaction databases

    BioGridi115544. 124 interactions.
    IntActiQ8IYB3. 18 interactions.
    MINTiMINT-1683977.
    STRINGi9606.ENSP00000326261.

    Structurei

    Secondary structure

    1
    904
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 364
    Turni40 – 423
    Helixi46 – 483
    Helixi49 – 6012
    Helixi66 – 749
    Beta strandi77 – 793
    Helixi82 – 898
    Turni90 – 923
    Helixi96 – 11217
    Beta strandi115 – 1184
    Helixi121 – 1244

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MP1NMR-A27-134[»]
    ProteinModelPortaliQ8IYB3.
    SMRiQ8IYB3. Positions 27-134.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IYB3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 126100PWIPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 156156Necessary for mRNA 3'-end cleavage and cytoplasmic accumulationAdd
    BLAST
    Regioni1 – 151151Necessary for DNA and RNA-bindingAdd
    BLAST
    Regioni300 – 688389Necessary for speckles and matrix localizationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi163 – 726564Arg-richAdd
    BLAST
    Compositional biasi210 – 417208Pro-richAdd
    BLAST
    Compositional biasi278 – 756479Ser-richAdd
    BLAST
    Compositional biasi550 – 799250Pro-richAdd
    BLAST
    Compositional biasi809 – 83527Lys-richAdd
    BLAST
    Compositional biasi836 – 86530Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the splicing factor SR family.Curated
    Contains 1 PWI domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG242213.
    HOGENOMiHOG000231139.
    HOVERGENiHBG054044.
    KOiK13171.
    OrthoDBiEOG786H40.
    PhylomeDBiQ8IYB3.
    TreeFamiTF318972.

    Family and domain databases

    Gene3Di1.20.1390.10. 1 hit.
    InterProiIPR002483. PWI_dom.
    [Graphical view]
    PfamiPF01480. PWI. 1 hit.
    [Graphical view]
    SMARTiSM00311. PWI. 1 hit.
    [Graphical view]
    SUPFAMiSSF101233. SSF101233. 1 hit.
    PROSITEiPS51025. PWI. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IYB3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP    50
    WITKRVTEIL GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE 100
    FMGELWPLLL SAQENIAGIP SAFLELKKEE IKQRQIEQEK LASMKKQDED 150
    KDKRDKEEKE SSREKRERSR SPRRRKSRSP SPRRRSSPVR RERKRSHSRS 200
    PRHRTKSRSP SPAPEKKEKT PELPEPSVKV KEPSVQEATS TSDILKVPKP 250
    EPIPEPKEPS PEKNSKKEKE KEKTRPRSRS RSKSRSRTRS RSPSHTRPRR 300
    RHRSRSRSYS PRRRPSPRRR PSPRRRTPPR RMPPPPRHRR SRSPVRRRRR 350
    SSASLSGSSS SSSSSRSRSP PKKPPKRTSS PPRKTRRLSP SASPPRRRHR 400
    PSPPATPPPK TRHSPTPQQS NRTRKSRVSV SPGRTSGKVT KHKGTEKRES 450
    PSPAPKPRKV ELSESEEDKG GKMAAADSVQ QRRQYRRQNQ QSSSDSGSSS 500
    SSEDERPKRS HVKNGEVGRR RRHSPSRSAS PSPRKRQKET SPRGRRRRSP 550
    SPPPTRRRRS PSPAPPPRRR RTPTPPPRRR TPSPPPRRRS PSPRRYSPPI 600
    QRRYSPSPPP KRRTASPPPP PKRRASPSPP PKRRVSHSPP PKQRSSPVTK 650
    RRSPSLSSKH RKGSSPSRST REARSPQPNK RHSPSPRPRA PQTSSSPPPV 700
    RRGASSSPQR RQSPSPSTRP IRRVSRTPEP KKIKKAASPS PQSVRRVSSS 750
    RSVSGSPEPA AKKPPAPPSP VQSQSPSTNW SPAVPVKKAK SPTPSPSPPR 800
    NSDQEGGGKK KKKKKDKKHK KDKKHKKHKK HKKEKAVAAA AAAAVTPAAI 850
    AAATTTLAQE EPVAAPEPKK ETESEAEDNL DDLEKHLREK ALRSMRKAQV 900
    SPQS 904
    Length:904
    Mass (Da):102,335
    Last modified:December 6, 2005 - v2
    Checksum:i27D4D2A48EDBFED3
    GO
    Isoform 2 (identifier: Q8IYB3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         305-308: RSRS → DKM
         407-407: Missing.

    Show »
    Length:902
    Mass (Da):102,126
    Checksum:i0211C6D93260EF32
    GO

    Sequence cautioni

    The sequence AAC09321.1 differs from that shown. Reason: Frameshift at position 791.
    The sequence AAP97290.1 differs from that shown. Reason: Frameshift at position 791.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691K → Q(PubMed:9531537)Curated
    Sequence conflicti269 – 2691K → Q1 PublicationCurated
    Sequence conflicti275 – 2751R → Q in AAH36187. (PubMed:15489334)Curated
    Sequence conflicti413 – 4131H → D(PubMed:9531537)Curated
    Sequence conflicti413 – 4131H → D1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti170 – 1701R → H.1 Publication
    Corresponds to variant rs17857102 [ dbSNP | Ensembl ].
    VAR_024065

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei305 – 3084RSRS → DKM in isoform 2. 2 PublicationsVSP_016522
    Alternative sequencei407 – 4071Missing in isoform 2. 2 PublicationsVSP_016523

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF048977 mRNA. Translation: AAC09321.1. Frameshift.
    AF419855 mRNA. Translation: AAP97290.1. Frameshift.
    AL445648, AL445686 Genomic DNA. Translation: CAH73090.1.
    AL445686, AL445648 Genomic DNA. Translation: CAI14682.1.
    BC036187 mRNA. Translation: AAH36187.1.
    CCDSiCCDS255.1. [Q8IYB3-1]
    RefSeqiNP_005830.2. NM_005839.3. [Q8IYB3-1]
    UniGeneiHs.18192.

    Genome annotation databases

    EnsembliENST00000323848; ENSP00000326261; ENSG00000133226. [Q8IYB3-1]
    GeneIDi10250.
    KEGGihsa:10250.
    UCSCiuc001bjm.3. human. [Q8IYB3-1]

    Polymorphism databases

    DMDMi83305833.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF048977 mRNA. Translation: AAC09321.1 . Frameshift.
    AF419855 mRNA. Translation: AAP97290.1 . Frameshift.
    AL445648 , AL445686 Genomic DNA. Translation: CAH73090.1 .
    AL445686 , AL445648 Genomic DNA. Translation: CAI14682.1 .
    BC036187 mRNA. Translation: AAH36187.1 .
    CCDSi CCDS255.1. [Q8IYB3-1 ]
    RefSeqi NP_005830.2. NM_005839.3. [Q8IYB3-1 ]
    UniGenei Hs.18192.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MP1 NMR - A 27-134 [» ]
    ProteinModelPortali Q8IYB3.
    SMRi Q8IYB3. Positions 27-134.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115544. 124 interactions.
    IntActi Q8IYB3. 18 interactions.
    MINTi MINT-1683977.
    STRINGi 9606.ENSP00000326261.

    Protein family/group databases

    TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    PTM databases

    PhosphoSitei Q8IYB3.

    Polymorphism databases

    DMDMi 83305833.

    Proteomic databases

    MaxQBi Q8IYB3.
    PaxDbi Q8IYB3.
    PRIDEi Q8IYB3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323848 ; ENSP00000326261 ; ENSG00000133226 . [Q8IYB3-1 ]
    GeneIDi 10250.
    KEGGi hsa:10250.
    UCSCi uc001bjm.3. human. [Q8IYB3-1 ]

    Organism-specific databases

    CTDi 10250.
    GeneCardsi GC01P024958.
    H-InvDB HIX0023530.
    HIX0160039.
    HGNCi HGNC:16638. SRRM1.
    HPAi HPA049941.
    HPA058612.
    MIMi 605975. gene.
    neXtProti NX_Q8IYB3.
    PharmGKBi PA38177.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242213.
    HOGENOMi HOG000231139.
    HOVERGENi HBG054044.
    KOi K13171.
    OrthoDBi EOG786H40.
    PhylomeDBi Q8IYB3.
    TreeFami TF318972.

    Enzyme and pathway databases

    Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi SRRM1. human.
    EvolutionaryTracei Q8IYB3.
    GeneWikii SRRM1.
    GenomeRNAii 10250.
    NextBioi 38838.
    PMAP-CutDB Q8IYB3.
    PROi Q8IYB3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IYB3.
    Bgeei Q8IYB3.
    CleanExi HS_SRRM1.
    Genevestigatori Q8IYB3.

    Family and domain databases

    Gene3Di 1.20.1390.10. 1 hit.
    InterProi IPR002483. PWI_dom.
    [Graphical view ]
    Pfami PF01480. PWI. 1 hit.
    [Graphical view ]
    SMARTi SM00311. PWI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101233. SSF101233. 1 hit.
    PROSITEi PS51025. PWI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN MRNA SPLICING, IDENTIFICATION IN A PRE-MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRP70; SNRPA1 AND SRRM2, SUBCELLULAR LOCATION.
    2. "Molecular cloning and characterization of human SRM160 gene."
      Guo J.H., Yu L.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1), VARIANT HIS-170.
      Tissue: Testis.
    5. Cited for: PROTEIN SEQUENCE OF 1-7; 30-36; 43-54; 84-96; 230-246; 387-396; 690-701 AND 870-885, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-389 AND SER-393, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma and Ovarian carcinoma.
    6. "The SRm160/300 splicing coactivator is required for exon-enhancer function."
      Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.
      Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA EXONIC SPLICING ENHANCER (ESE)-DEPENDENT SPLICING, IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH SNRP70; SNRPA1 AND TRA2B.
    7. "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
      Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
      EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RBM8A; RNPS1 AND ALYREF/THOC4.
    8. "Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions."
      Le Hir H., Moore M.J., Maquat L.E.
      Genes Dev. 14:1098-1108(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH PRPF8, ASSOCIATION WITH THE SPLICEOSOME, RNA-BINDING.
    9. Cited for: FUNCTION IN MRNA SPLICING.
    10. "Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1."
      Lykke-Andersen J., Shu M.-D., Steitz J.A.
      Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, SUBCELLULAR LOCATION.
    11. "The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling."
      Lejeune F., Ishigaki Y., Li X., Maquat L.E.
      EMBO J. 21:3536-3545(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE EXON JUNCTION COMPLEX.
    12. "SRm160 splicing coactivator promotes transcript 3'-end cleavage."
      McCracken S., Lambermon M., Blencowe B.J.
      Mol. Cell. Biol. 22:148-160(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA SPLICING AND 3'-END FORMATION, INTERACTION WITH CPSF1.
    13. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    14. "An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation."
      McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.
      J. Biol. Chem. 278:44153-44160(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA 3'-END FORMATION, INTERACTION WITH BAT1; RBM8A; RNPS1 AND ALYREF/THOC4.
    15. "The spatial targeting and nuclear matrix binding domains of SRm160."
      Wagner S., Chiosea S., Nickerson J.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:3269-3274(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402 AND THR-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160."
      Wagner S., Chiosea S., Ivshina M., Nickerson J.A.
      J. Cell Biol. 164:843-850(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ATP-DEPENDENT MOBILITY OF A SRRM1-COMPLEX.
    18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-260; SER-402; THR-406; SER-450; SER-452; SER-463; SER-465; SER-560; SER-562; THR-614; SER-616; SER-626; SER-628; THR-872 AND SER-874, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-560; SER-562; THR-614; SER-616; SER-754 AND SER-756, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-429; SER-431; SER-436; SER-597; SER-605; SER-607; SER-694; SER-696; SER-713; SER-715; SER-748; SER-752; SER-754; SER-756; SER-769; SER-775; SER-777 AND SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-872 AND SER-874, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-738; SER-740; SER-769; SER-775; SER-781; THR-872 AND SER-874, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-227; SER-234; SER-260; SER-389; SER-391; SER-393; SER-402; THR-406; SER-429; SER-431; SER-450; SER-452; SER-463; SER-465; SER-478; SER-560; SER-562; SER-597; SER-605; SER-607; THR-614; SER-616; SER-626; SER-628; SER-636; SER-638; SER-696; SER-738; SER-752; SER-754; SER-756; SER-769; SER-781; THR-872 AND SER-874, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-260; SER-389; SER-391; SER-393; SER-402; SER-414; THR-416; SER-420; SER-429; SER-431; SER-450; SER-452; SER-463; SER-465; SER-549; SER-551; THR-555; THR-572; THR-574; THR-581; SER-583; SER-597; SER-605; SER-607; SER-616; SER-626; SER-628; SER-636; SER-638; SER-646; SER-696; SER-705; SER-707; SER-738; SER-740; SER-754; SER-756; SER-769; SER-791; THR-793; SER-795; THR-872 AND SER-874, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing."
      Szymczyna B.R., Bowman J., McCracken S., Pineda-Lucena A., Lu Y., Cox B., Lambermon M., Graveley B.R., Arrowsmith C.H., Blencowe B.J.
      Genes Dev. 17:461-475(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 27-134, FUNCTION IN MRNA 3'-END FORMATION, MUTAGENESIS OF LYS-20; LYS-22 AND LYS-23, DNA-BINDING, RNA-BINDING.

    Entry informationi

    Entry nameiSRRM1_HUMAN
    AccessioniPrimary (citable) accession number: Q8IYB3
    Secondary accession number(s): O60585, Q5VVN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3