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Protein

Serine/arginine repetitive matrix protein 1

Gene

SRRM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • DNA binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16638. SRRM1.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytosol Source: Reactome
  • nuclear matrix Source: UniProtKB-SubCell
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
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.

Polymorphism and mutation databases

BioMutaiSRRM1.
DMDMi83305833.

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-acetylmethionineCombined sources1 Publication
Modified residuei7 – 71CitrullineBy similarity
Modified residuei140 – 1401N6-acetyllysineCombined sources
Modified residuei220 – 2201PhosphothreonineCombined sources
Modified residuei227 – 2271PhosphoserineCombined sources
Modified residuei234 – 2341PhosphoserineCombined sources
Cross-linki249 – 249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei260 – 2601PhosphoserineCombined sources
Modified residuei389 – 3891PhosphoserineCombined sources1 Publication
Modified residuei391 – 3911PhosphoserineCombined sources
Modified residuei393 – 3931PhosphoserineCombined sources1 Publication
Modified residuei402 – 4021PhosphoserineCombined sources
Modified residuei406 – 4061PhosphothreonineCombined sources
Modified residuei414 – 4141PhosphoserineCombined sources
Modified residuei416 – 4161PhosphothreonineCombined sources
Modified residuei420 – 4201PhosphoserineCombined sources
Modified residuei429 – 4291PhosphoserineCombined sources
Modified residuei431 – 4311PhosphoserineCombined sources
Modified residuei436 – 4361PhosphoserineCombined sources
Modified residuei450 – 4501PhosphoserineCombined sources
Modified residuei452 – 4521PhosphoserineCombined sources
Modified residuei463 – 4631PhosphoserineCombined sources
Modified residuei465 – 4651PhosphoserineCombined sources
Modified residuei478 – 4781PhosphoserineCombined sources
Modified residuei524 – 5241PhosphoserineCombined sources
Modified residuei526 – 5261PhosphoserineCombined sources
Modified residuei528 – 5281PhosphoserineCombined sources
Modified residuei530 – 5301PhosphoserineCombined sources
Modified residuei532 – 5321PhosphoserineCombined sources
Modified residuei549 – 5491PhosphoserineCombined sources
Modified residuei551 – 5511PhosphoserineCombined sources
Modified residuei555 – 5551PhosphothreonineCombined sources
Modified residuei560 – 5601PhosphoserineCombined sources
Modified residuei562 – 5621PhosphoserineCombined sources
Modified residuei572 – 5721PhosphothreonineCombined sources
Modified residuei574 – 5741PhosphothreonineCombined sources
Modified residuei581 – 5811PhosphothreonineCombined sources
Modified residuei583 – 5831PhosphoserineCombined sources
Modified residuei596 – 5961PhosphotyrosineCombined sources
Modified residuei597 – 5971PhosphoserineCombined sources
Modified residuei605 – 6051PhosphoserineCombined sources
Modified residuei607 – 6071PhosphoserineCombined sources
Modified residuei614 – 6141PhosphothreonineCombined sources
Modified residuei616 – 6161PhosphoserineCombined sources
Modified residuei626 – 6261PhosphoserineCombined sources
Modified residuei628 – 6281PhosphoserineCombined sources
Modified residuei636 – 6361PhosphoserineCombined sources
Modified residuei638 – 6381PhosphoserineCombined sources
Modified residuei694 – 6941PhosphoserineCombined sources
Modified residuei695 – 6951PhosphoserineBy similarity
Modified residuei696 – 6961PhosphoserineCombined sources
Modified residuei705 – 7051PhosphoserineCombined sources
Modified residuei707 – 7071PhosphoserineCombined sources
Modified residuei713 – 7131PhosphoserineCombined sources
Modified residuei715 – 7151PhosphoserineCombined sources
Modified residuei718 – 7181PhosphothreonineCombined sources
Modified residuei738 – 7381PhosphoserineCombined sources
Modified residuei740 – 7401PhosphoserineCombined sources
Modified residuei748 – 7481PhosphoserineCombined sources
Modified residuei752 – 7521PhosphoserineCombined sources
Modified residuei754 – 7541PhosphoserineCombined sources
Modified residuei756 – 7561PhosphoserineCombined sources
Modified residuei769 – 7691PhosphoserineCombined sources
Modified residuei773 – 7731PhosphoserineCombined sources
Modified residuei775 – 7751PhosphoserineCombined sources
Modified residuei777 – 7771PhosphoserineCombined sources
Modified residuei778 – 7781PhosphothreonineBy similarity
Modified residuei781 – 7811PhosphoserineCombined sources
Modified residuei791 – 7911PhosphoserineCombined sources
Modified residuei793 – 7931PhosphothreonineCombined sources
Modified residuei795 – 7951PhosphoserineCombined sources
Modified residuei797 – 7971PhosphoserineBy similarity
Modified residuei802 – 8021PhosphoserineBy similarity
Modified residuei872 – 8721PhosphothreonineCombined sources
Modified residuei874 – 8741PhosphoserineCombined sources
Modified residuei901 – 9011PhosphoserineCombined sources

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8IYB3.
PaxDbiQ8IYB3.
PRIDEiQ8IYB3.

PTM databases

iPTMnetiQ8IYB3.
PhosphoSiteiQ8IYB3.

Miscellaneous databases

PMAP-CutDBQ8IYB3.

Expressioni

Gene expression databases

BgeeiQ8IYB3.
CleanExiHS_SRRM1.
ExpressionAtlasiQ8IYB3. baseline and differential.
GenevisibleiQ8IYB3. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CLK2P497603EBI-1055880,EBI-750020

Protein-protein interaction databases

BioGridi115544. 147 interactions.
IntActiQ8IYB3. 19 interactions.
MINTiMINT-1683977.
STRINGi9606.ENSP00000326261.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

eggNOGiKOG2146. Eukaryota.
ENOG4111IMU. LUCA.
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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691K → Q (PubMed:9531537).Curated
Sequence conflicti269 – 2691K → Q (Ref. 2) Curated
Sequence conflicti275 – 2751R → Q in AAH36187 (PubMed:15489334).Curated
Sequence conflicti413 – 4131H → D (PubMed:9531537).Curated
Sequence conflicti413 – 4131H → D (Ref. 2) Curated

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:
EMBLi
GenBanki
DDBJi
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_001290377.1. NM_001303448.1.
NP_001290378.1. NM_001303449.1.
NP_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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001290377.1. NM_001303448.1.
NP_001290378.1. NM_001303449.1.
NP_005830.2. NM_005839.3. [Q8IYB3-1]
UniGeneiHs.18192.

3D structure databases

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

Protein-protein interaction databases

BioGridi115544. 147 interactions.
IntActiQ8IYB3. 19 interactions.
MINTiMINT-1683977.
STRINGi9606.ENSP00000326261.

Protein family/group databases

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

PTM databases

iPTMnetiQ8IYB3.
PhosphoSiteiQ8IYB3.

Polymorphism and mutation databases

BioMutaiSRRM1.
DMDMi83305833.

Proteomic databases

MaxQBiQ8IYB3.
PaxDbiQ8IYB3.
PRIDEiQ8IYB3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10250.
GeneCardsiSRRM1.
H-InvDBHIX0023530.
HIX0160039.
HGNCiHGNC:16638. SRRM1.
HPAiHPA049941.
HPA058612.
MIMi605975. gene.
neXtProtiNX_Q8IYB3.
PharmGKBiPA38177.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2146. Eukaryota.
ENOG4111IMU. LUCA.
GeneTreeiENSGT00730000111080.
HOGENOMiHOG000231139.
HOVERGENiHBG054044.
InParanoidiQ8IYB3.
KOiK13171.
OrthoDBiEOG786H40.
PhylomeDBiQ8IYB3.
TreeFamiTF318972.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.

Miscellaneous databases

ChiTaRSiSRRM1. human.
EvolutionaryTraceiQ8IYB3.
GeneWikiiSRRM1.
GenomeRNAii10250.
NextBioi38838.
PMAP-CutDBQ8IYB3.
PROiQ8IYB3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IYB3.
CleanExiHS_SRRM1.
ExpressionAtlasiQ8IYB3. baseline and differential.
GenevisibleiQ8IYB3. HS.

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]
ProtoNetiSearch...

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-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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-234; SER-260; SER-389; SER-402; THR-406; SER-450; SER-524; SER-526; SER-528; SER-530; SER-532; SER-549; SER-551; SER-560; SER-562; TYR-596; SER-597; THR-614; SER-616; SER-638; SER-705; SER-713; THR-718; SER-738; SER-769; SER-773; SER-781; SER-874 AND SER-901, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  32. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "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: January 20, 2016
This is version 136 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.