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Q8IYB3

- SRRM1_HUMAN

UniProt

Q8IYB3 - SRRM1_HUMAN

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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

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
Complete GO annotation...

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. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

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

BgeeiQ8IYB3.
CleanExiHS_SRRM1.
ExpressionAtlasiQ8IYB3. baseline and differential.
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. 130 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.
GeneTreeiENSGT00730000111080.
HOGENOMiHOG000231139.
HOVERGENiHBG054044.
InParanoidiQ8IYB3.
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

        10         20         30         40         50
MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP
60 70 80 90 100
WITKRVTEIL GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE
110 120 130 140 150
FMGELWPLLL SAQENIAGIP SAFLELKKEE IKQRQIEQEK LASMKKQDED
160 170 180 190 200
KDKRDKEEKE SSREKRERSR SPRRRKSRSP SPRRRSSPVR RERKRSHSRS
210 220 230 240 250
PRHRTKSRSP SPAPEKKEKT PELPEPSVKV KEPSVQEATS TSDILKVPKP
260 270 280 290 300
EPIPEPKEPS PEKNSKKEKE KEKTRPRSRS RSKSRSRTRS RSPSHTRPRR
310 320 330 340 350
RHRSRSRSYS PRRRPSPRRR PSPRRRTPPR RMPPPPRHRR SRSPVRRRRR
360 370 380 390 400
SSASLSGSSS SSSSSRSRSP PKKPPKRTSS PPRKTRRLSP SASPPRRRHR
410 420 430 440 450
PSPPATPPPK TRHSPTPQQS NRTRKSRVSV SPGRTSGKVT KHKGTEKRES
460 470 480 490 500
PSPAPKPRKV ELSESEEDKG GKMAAADSVQ QRRQYRRQNQ QSSSDSGSSS
510 520 530 540 550
SSEDERPKRS HVKNGEVGRR RRHSPSRSAS PSPRKRQKET SPRGRRRRSP
560 570 580 590 600
SPPPTRRRRS PSPAPPPRRR RTPTPPPRRR TPSPPPRRRS PSPRRYSPPI
610 620 630 640 650
QRRYSPSPPP KRRTASPPPP PKRRASPSPP PKRRVSHSPP PKQRSSPVTK
660 670 680 690 700
RRSPSLSSKH RKGSSPSRST REARSPQPNK RHSPSPRPRA PQTSSSPPPV
710 720 730 740 750
RRGASSSPQR RQSPSPSTRP IRRVSRTPEP KKIKKAASPS PQSVRRVSSS
760 770 780 790 800
RSVSGSPEPA AKKPPAPPSP VQSQSPSTNW SPAVPVKKAK SPTPSPSPPR
810 820 830 840 850
NSDQEGGGKK KKKKKDKKHK KDKKHKKHKK HKKEKAVAAA AAAAVTPAAI
860 870 880 890 900
AAATTTLAQE EPVAAPEPKK ETESEAEDNL DDLEKHLREK ALRSMRKAQV

SPQS
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. 130 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.
GeneTreei ENSGT00730000111080.
HOGENOMi HOG000231139.
HOVERGENi HBG054044.
InParanoidi Q8IYB3.
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

Bgeei Q8IYB3.
CleanExi HS_SRRM1.
ExpressionAtlasi Q8IYB3. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 123 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