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Q8IYB3 (SRRM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SRRM1
Synonyms:SRM160
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length904 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.9 Ref.12 Ref.14 Ref.31

Subunit structure

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Nucleus matrix. Nucleus speckle Ref.1 Ref.10 Ref.15.

Post-translational modification

Citrullinated by PADI4 By similarity.

Sequence similarities

Belongs to the splicing factor SR family.

Contains 1 PWI domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
RNA-binding
   PTMAcetylation
Citrullination
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

RNA splicing, via transesterification reactions

Traceable author statement Ref.1. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.13. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.13. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IYB3-1)

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.
Isoform 2 (identifier: Q8IYB3-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 904904Serine/arginine repetitive matrix protein 1
PRO_0000076326

Regions

Domain27 – 126100PWI
Region1 – 156156Necessary for mRNA 3'-end cleavage and cytoplasmic accumulation
Region1 – 151151Necessary for DNA and RNA-binding
Region300 – 688389Necessary for speckles and matrix localization
Compositional bias163 – 726564Arg-rich
Compositional bias210 – 417208Pro-rich
Compositional bias278 – 756479Ser-rich
Compositional bias550 – 799250Pro-rich
Compositional bias809 – 83527Lys-rich
Compositional bias836 – 86530Ala-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5 Ref.30
Modified residue71Citrulline By similarity
Modified residue1401N6-acetyllysine Ref.26
Modified residue2201Phosphothreonine Ref.18 Ref.21 Ref.22 Ref.27 Ref.29
Modified residue2271Phosphoserine Ref.27
Modified residue2341Phosphoserine Ref.27
Modified residue2601Phosphoserine Ref.18 Ref.27 Ref.29
Modified residue3891Phosphoserine Ref.5 Ref.27 Ref.29
Modified residue3911Phosphoserine Ref.27 Ref.29
Modified residue3931Phosphoserine Ref.5 Ref.27 Ref.29
Modified residue4021Phosphoserine Ref.16 Ref.18 Ref.27 Ref.29
Modified residue4061Phosphothreonine Ref.16 Ref.18 Ref.27
Modified residue4141Phosphoserine Ref.29
Modified residue4161Phosphothreonine Ref.29
Modified residue4201Phosphoserine Ref.29
Modified residue4291Phosphoserine Ref.22 Ref.27 Ref.29
Modified residue4311Phosphoserine Ref.22 Ref.27 Ref.29
Modified residue4361Phosphoserine Ref.22
Modified residue4501Phosphoserine Ref.18 Ref.20 Ref.27 Ref.29
Modified residue4521Phosphoserine Ref.18 Ref.20 Ref.27 Ref.29
Modified residue4631Phosphoserine Ref.18 Ref.27 Ref.29
Modified residue4651Phosphoserine Ref.18 Ref.27 Ref.29
Modified residue4781Phosphoserine Ref.19 Ref.27
Modified residue5491Phosphoserine Ref.29
Modified residue5511Phosphoserine Ref.29
Modified residue5551Phosphothreonine Ref.29
Modified residue5601Phosphoserine Ref.18 Ref.19 Ref.27
Modified residue5621Phosphoserine Ref.18 Ref.19 Ref.27
Modified residue5721Phosphothreonine Ref.29
Modified residue5741Phosphothreonine Ref.29
Modified residue5811Phosphothreonine Ref.29
Modified residue5831Phosphoserine Ref.29
Modified residue5971Phosphoserine Ref.22 Ref.27 Ref.29
Modified residue6051Phosphoserine Ref.22 Ref.27 Ref.29
Modified residue6071Phosphoserine Ref.22 Ref.27 Ref.29
Modified residue6141Phosphothreonine Ref.18 Ref.19 Ref.27
Modified residue6161Phosphoserine Ref.18 Ref.19 Ref.27 Ref.29
Modified residue6261Phosphoserine Ref.18 Ref.27 Ref.29
Modified residue6281Phosphoserine Ref.18 Ref.27 Ref.29
Modified residue6361Phosphoserine Ref.27 Ref.29
Modified residue6381Phosphoserine Ref.27 Ref.29
Modified residue6461Phosphoserine Ref.29
Modified residue6941Phosphoserine Ref.22
Modified residue6951Phosphoserine By similarity
Modified residue6961Phosphoserine Ref.22 Ref.25 Ref.27 Ref.29
Modified residue7051Phosphoserine Ref.29
Modified residue7071Phosphoserine Ref.29
Modified residue7131Phosphoserine Ref.22
Modified residue7151Phosphoserine Ref.22
Modified residue7381Phosphoserine Ref.25 Ref.27 Ref.29
Modified residue7401Phosphoserine Ref.25 Ref.29
Modified residue7481Phosphoserine Ref.22
Modified residue7521Phosphoserine Ref.22 Ref.27
Modified residue7541Phosphoserine Ref.19 Ref.22 Ref.27 Ref.29
Modified residue7561Phosphoserine Ref.19 Ref.22 Ref.27 Ref.29
Modified residue7691Phosphoserine Ref.22 Ref.25 Ref.27 Ref.29
Modified residue7751Phosphoserine Ref.22 Ref.25
Modified residue7771Phosphoserine Ref.22
Modified residue7811Phosphoserine Ref.22 Ref.25 Ref.27
Modified residue7911Phosphoserine Ref.29
Modified residue7931Phosphothreonine Ref.29
Modified residue7951Phosphoserine Ref.29
Modified residue8721Phosphothreonine Ref.18 Ref.23 Ref.25 Ref.27 Ref.29
Modified residue8741Phosphoserine Ref.18 Ref.23 Ref.25 Ref.27 Ref.29

Natural variations

Alternative sequence305 – 3084RSRS → DKM in isoform 2.
VSP_016522
Alternative sequence4071Missing in isoform 2.
VSP_016523
Natural variant1701R → H. Ref.4
Corresponds to variant rs17857102 [ dbSNP | Ensembl ].
VAR_024065

Experimental info

Mutagenesis201K → A: Strongly reduces DNA and RNA-binding. Ref.31
Mutagenesis221K → A: Strongly reduces DNA and RNA-binding. Ref.31
Mutagenesis231K → A: Strongly reduces DNA and RNA-binding. Ref.31
Sequence conflict2691K → Q Ref.1
Sequence conflict2691K → Q Ref.2
Sequence conflict2751R → Q in AAH36187. Ref.4
Sequence conflict4131H → D Ref.1
Sequence conflict4131H → D Ref.2

Secondary structure

..................... 904
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 27D4D2A48EDBFED3

FASTA904102,335
        10         20         30         40         50         60 
MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP WITKRVTEIL 

        70         80         90        100        110        120 
GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE FMGELWPLLL SAQENIAGIP 

       130        140        150        160        170        180 
SAFLELKKEE IKQRQIEQEK LASMKKQDED KDKRDKEEKE SSREKRERSR SPRRRKSRSP 

       190        200        210        220        230        240 
SPRRRSSPVR RERKRSHSRS PRHRTKSRSP SPAPEKKEKT PELPEPSVKV KEPSVQEATS 

       250        260        270        280        290        300 
TSDILKVPKP EPIPEPKEPS PEKNSKKEKE KEKTRPRSRS RSKSRSRTRS RSPSHTRPRR 

       310        320        330        340        350        360 
RHRSRSRSYS PRRRPSPRRR PSPRRRTPPR RMPPPPRHRR SRSPVRRRRR SSASLSGSSS 

       370        380        390        400        410        420 
SSSSSRSRSP PKKPPKRTSS PPRKTRRLSP SASPPRRRHR PSPPATPPPK TRHSPTPQQS 

       430        440        450        460        470        480 
NRTRKSRVSV SPGRTSGKVT KHKGTEKRES PSPAPKPRKV ELSESEEDKG GKMAAADSVQ 

       490        500        510        520        530        540 
QRRQYRRQNQ QSSSDSGSSS SSEDERPKRS HVKNGEVGRR RRHSPSRSAS PSPRKRQKET 

       550        560        570        580        590        600 
SPRGRRRRSP SPPPTRRRRS PSPAPPPRRR RTPTPPPRRR TPSPPPRRRS PSPRRYSPPI 

       610        620        630        640        650        660 
QRRYSPSPPP KRRTASPPPP PKRRASPSPP PKRRVSHSPP PKQRSSPVTK RRSPSLSSKH 

       670        680        690        700        710        720 
RKGSSPSRST REARSPQPNK RHSPSPRPRA PQTSSSPPPV RRGASSSPQR RQSPSPSTRP 

       730        740        750        760        770        780 
IRRVSRTPEP KKIKKAASPS PQSVRRVSSS RSVSGSPEPA AKKPPAPPSP VQSQSPSTNW 

       790        800        810        820        830        840 
SPAVPVKKAK SPTPSPSPPR NSDQEGGGKK KKKKKDKKHK KDKKHKKHKK HKKEKAVAAA 

       850        860        870        880        890        900 
AAAAVTPAAI AAATTTLAQE EPVAAPEPKK ETESEAEDNL DDLEKHLREK ALRSMRKAQV 


SPQS 

« Hide

Isoform 2 [UniParc].

Checksum: 0211C6D93260EF32
Show »

FASTA902102,126

References

« Hide 'large scale' references
[1]"A coactivator of pre-mRNA splicing."
Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.
Genes Dev. 12:996-1009(1998) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
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]"The SRm160/300 splicing coactivator subunits."
Blencowe B.J., Bauren G., Eldridge A.G., Issner R., Nickerson J.A., Rosonina E., Sharp P.A.
RNA 6:111-120(2000) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_005830.2. NM_005839.3.
UniGeneHs.18192.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MP1NMR-A27-134[»]
ProteinModelPortalQ8IYB3.
SMRQ8IYB3. Positions 27-134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115544. 123 interactions.
IntActQ8IYB3. 18 interactions.
MINTMINT-1683977.
STRING9606.ENSP00000326261.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteQ8IYB3.

Polymorphism databases

DMDM83305833.

Proteomic databases

PaxDbQ8IYB3.
PRIDEQ8IYB3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323848; ENSP00000326261; ENSG00000133226. [Q8IYB3-1]
GeneID10250.
KEGGhsa:10250.
UCSCuc001bjm.3. human. [Q8IYB3-1]

Organism-specific databases

CTD10250.
GeneCardsGC01P024958.
H-InvDBHIX0023530.
HIX0160039.
HGNCHGNC:16638. SRRM1.
HPAHPA049941.
HPA058612.
MIM605975. gene.
neXtProtNX_Q8IYB3.
PharmGKBPA38177.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242213.
HOGENOMHOG000231139.
HOVERGENHBG054044.
KOK13171.
OrthoDBEOG786H40.
PhylomeDBQ8IYB3.
TreeFamTF318972.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ8IYB3.
BgeeQ8IYB3.
CleanExHS_SRRM1.
GenevestigatorQ8IYB3.

Family and domain databases

Gene3D1.20.1390.10. 1 hit.
InterProIPR002483. PWI_dom.
[Graphical view]
PfamPF01480. PWI. 1 hit.
[Graphical view]
SMARTSM00311. PWI. 1 hit.
[Graphical view]
SUPFAMSSF101233. SSF101233. 1 hit.
PROSITEPS51025. PWI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRRM1. human.
EvolutionaryTraceQ8IYB3.
GeneWikiSRRM1.
GenomeRNAi10250.
NextBio38838.
PMAP-CutDBQ8IYB3.
PROQ8IYB3.
SOURCESearch...

Entry information

Entry nameSRRM1_HUMAN
AccessionPrimary (citable) accession number: Q8IYB3
Secondary accession number(s): O60585, Q5VVN4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM