Q8IYB3 (SRRM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SRRM1
Synonyms:	SRM160

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	904 AA.
Sequence status	Complete.
Protein existence	Evidence 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.29
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.
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 process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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
Cellular_component	catalytic 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
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 904

904

Serine/arginine repetitive matrix protein 1

PRO_0000076326

Regions

Domain

27 – 126

100

PWI

Region

1 – 156

156

Necessary for mRNA 3'-end cleavage and cytoplasmic accumulation

Region

1 – 151

151

Necessary for DNA and RNA-binding

Region

300 – 688

389

Necessary for speckles and matrix localization

Compositional bias

163 – 726

564

Arg-rich

Compositional bias

210 – 417

208

Pro-rich

Compositional bias

278 – 756

479

Ser-rich

Compositional bias

550 – 799

250

Pro-rich

Compositional bias

809 – 835

27

Lys-rich

Compositional bias

836 – 865

30

Ala-rich

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.5

Modified residue

140

1

N6-acetyllysine Ref.25

Modified residue

207

1

Phosphoserine By similarity

Modified residue

209

1

Phosphoserine By similarity

Modified residue

211

1

Phosphoserine By similarity

Modified residue

220

1

Phosphothreonine Ref.18 Ref.21 Ref.22 Ref.26 Ref.28

Modified residue

227

1

Phosphoserine Ref.26

Modified residue

234

1

Phosphoserine Ref.26

Modified residue

260

1

Phosphoserine Ref.18 Ref.26 Ref.28

Modified residue

389

1

Phosphoserine Ref.5 Ref.26 Ref.28

Modified residue

391

1

Phosphoserine Ref.26 Ref.28

Modified residue

393

1

Phosphoserine Ref.5 Ref.26 Ref.28

Modified residue

402

1

Phosphoserine Ref.16 Ref.18 Ref.26 Ref.28

Modified residue

406

1

Phosphothreonine Ref.16 Ref.18 Ref.26

Modified residue

414

1

Phosphoserine Ref.28

Modified residue

416

1

Phosphothreonine Ref.28

Modified residue

420

1

Phosphoserine Ref.28

Modified residue

429

1

Phosphoserine Ref.22 Ref.26 Ref.28

Modified residue

431

1

Phosphoserine Ref.22 Ref.26 Ref.28

Modified residue

436

1

Phosphoserine Ref.22

Modified residue

450

1

Phosphoserine Ref.18 Ref.20 Ref.26 Ref.28

Modified residue

452

1

Phosphoserine Ref.18 Ref.20 Ref.26 Ref.28

Modified residue

463

1

Phosphoserine Ref.18 Ref.26 Ref.28

Modified residue

465

1

Phosphoserine Ref.18 Ref.26 Ref.28

Modified residue

478

1

Phosphoserine Ref.19 Ref.26

Modified residue

549

1

Phosphoserine Ref.28

Modified residue

551

1

Phosphoserine Ref.28

Modified residue

555

1

Phosphothreonine Ref.28

Modified residue

560

1

Phosphoserine Ref.18 Ref.19 Ref.26

Modified residue

562

1

Phosphoserine Ref.18 Ref.19 Ref.26

Modified residue

572

1

Phosphothreonine Ref.28

Modified residue

574

1

Phosphothreonine Ref.28

Modified residue

581

1

Phosphothreonine Ref.26 Ref.28

Modified residue

583

1

Phosphoserine Ref.26 Ref.28

Modified residue

597

1

Phosphoserine Ref.22 Ref.26 Ref.28

Modified residue

605

1

Phosphoserine Ref.22 Ref.26 Ref.28

Modified residue

607

1

Phosphoserine Ref.22 Ref.26 Ref.28

Modified residue

614

1

Phosphothreonine Ref.18 Ref.19 Ref.26

Modified residue

616

1

Phosphoserine Ref.18 Ref.19 Ref.26 Ref.28

Modified residue

626

1

Phosphoserine Ref.18 Ref.26 Ref.28

Modified residue

628

1

Phosphoserine Ref.18 Ref.26 Ref.28

Modified residue

636

1

Phosphoserine Ref.26 Ref.28

Modified residue

638

1

Phosphoserine Ref.26 Ref.28

Modified residue

646

1

Phosphoserine Ref.28

Modified residue

653

1

Phosphoserine By similarity

Modified residue

675

1

Phosphoserine By similarity

Modified residue

683

1

Phosphoserine By similarity

Modified residue

685

1

Phosphoserine By similarity

Modified residue

694

1

Phosphoserine Ref.22

Modified residue

696

1

Phosphoserine Ref.22 Ref.24 Ref.26 Ref.28

Modified residue

705

1

Phosphoserine Ref.28

Modified residue

707

1

Phosphoserine Ref.28

Modified residue

713

1

Phosphoserine Ref.22

Modified residue

715

1

Phosphoserine Ref.22

Modified residue

738

1

Phosphoserine Ref.24 Ref.26 Ref.28

Modified residue

740

1

Phosphoserine Ref.24 Ref.28

Modified residue

743

1

Phosphoserine By similarity

Modified residue

748

1

Phosphoserine Ref.22

Modified residue

752

1

Phosphoserine Ref.22 Ref.26

Modified residue

754

1

Phosphoserine Ref.19 Ref.22 Ref.26 Ref.28

Modified residue

756

1

Phosphoserine Ref.19 Ref.22 Ref.26 Ref.28

Modified residue

769

1

Phosphoserine Ref.22 Ref.24 Ref.26 Ref.28

Modified residue

773

1

Phosphoserine By similarity

Modified residue

775

1

Phosphoserine Ref.22 Ref.24

Modified residue

777

1

Phosphoserine Ref.22

Modified residue

781

1

Phosphoserine Ref.22 Ref.24 Ref.26

Modified residue

791

1

Phosphoserine Ref.28

Modified residue

793

1

Phosphothreonine Ref.28

Modified residue

795

1

Phosphoserine Ref.28

Modified residue

872

1

Phosphothreonine Ref.18 Ref.23 Ref.24 Ref.26 Ref.28

Modified residue

874

1

Phosphoserine Ref.18 Ref.23 Ref.24 Ref.26 Ref.28

Natural variations

Alternative sequence

305 – 308

4

RSRS → DKM in isoform 2.

VSP_016522

Alternative sequence

407

1

Missing in isoform 2.

VSP_016523

Natural variant

170

1

R → H. Ref.4
Corresponds to variant rs17857102 [ dbSNP | Ensembl ].

VAR_024065

Experimental info

Mutagenesis

20

1

K → A: Strongly reduces DNA and RNA-binding. Ref.29

Mutagenesis

22

1

K → A: Strongly reduces DNA and RNA-binding. Ref.29

Mutagenesis

23

1

K → A: Strongly reduces DNA and RNA-binding. Ref.29

Sequence conflict

269

1

K → Q Ref.1

Sequence conflict

269

1

K → Q Ref.2

Sequence conflict

275

1

R → Q in AAH36187. Ref.4

Sequence conflict

413

1

H → D Ref.1

Sequence conflict

413

1

H → D Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

904

Helix Strand Turn

Details...

Helix

33 – 36

4

Turn

40 – 42

3

Helix

46 – 48

3

Helix

49 – 60

12

Helix

66 – 74

9

Beta strand

77 – 79

3

Helix

82 – 89

8

Turn

90 – 92

3

Helix

96 – 112

17

Beta strand

115 – 118

4

Helix

121 – 124

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 27D4D2A48EDBFED3	FASTA	904	102,335
	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
	Isoform 2 [UniParc]. Checksum: 0211C6D93260EF32	FASTA	902	102,126
	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 RHRSDKMYSP RRRPSPRRRP SPRRRTPPRR MPPPPRHRRS RSPVRRRRRS SASLSGSSSS 370 380 390 400 410 420 SSSSRSRSPP KKPPKRTSSP PRKTRRLSPS ASPPRRRHRP SPPATPPKTR HSPTPQQSNR 430 440 450 460 470 480 TRKSRVSVSP GRTSGKVTKH KGTEKRESPS PAPKPRKVEL SESEEDKGGK MAAADSVQQR 490 500 510 520 530 540 RQYRRQNQQS SSDSGSSSSS EDERPKRSHV KNGEVGRRRR HSPSRSASPS PRKRQKETSP 550 560 570 580 590 600 RGRRRRSPSP PPTRRRRSPS PAPPPRRRRT PTPPPRRRTP SPPPRRRSPS PRRYSPPIQR 610 620 630 640 650 660 RYSPSPPPKR RTASPPPPPK RRASPSPPPK RRVSHSPPPK QRSSPVTKRR SPSLSSKHRK 670 680 690 700 710 720 GSSPSRSTRE ARSPQPNKRH SPSPRPRAPQ TSSSPPPVRR GASSSPQRRQ SPSPSTRPIR 730 740 750 760 770 780 RVSRTPEPKK IKKAASPSPQ SVRRVSSSRS VSGSPEPAAK KPPAPPSPVQ SQSPSTNWSP 790 800 810 820 830 840 AVPVKKAKSP TPSPSPPRNS DQEGGGKKKK KKKDKKHKKD KKHKKHKKHK KEKAVAAAAA 850 860 870 880 890 900 AAVTPAAIAA ATTTLAQEEP VAAPEPKKET ESEAEDNLDD LEKHLREKAL RSMRKAQVSP QS

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[24]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"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, MASS SPECTROMETRY.
[26]	"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; THR-581; SER-583; 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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].
[28]	"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, MASS SPECTROMETRY.
[29]	"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.

IPI

IPI00328293.
IPI00647720.

RefSeq

NP_005830.2. NM_005839.3.

UniGene

Hs.18192.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MP1	NMR	-	A	27-134	[»]

ProteinModelPortal

Q8IYB3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IYB3. 10 interactions.

MINT

MINT-1683977.

STRING

9606.ENSP00000326261.

Protein family/group databases

TCDB

3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSite

Q8IYB3.

Polymorphism databases

DMDM

83305833.

Proteomic databases

PaxDb

Q8IYB3.

PRIDE

Q8IYB3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000323848; ENSP00000326261; ENSG00000133226.

GeneID

10250.

KEGG

hsa:10250.

UCSC

uc001bjm.3. human.

Organism-specific databases

CTD

10250.

GeneCards

GC01P024958.

H-InvDB

HIX0023530.
HIX0160039.

HGNC

HGNC:16638. SRRM1.

HPA

HPA049941.

MIM

605975. gene.

neXtProt

NX_Q8IYB3.

PharmGKB

PA38177.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG242213.

HOGENOM

HOG000231139.

HOVERGEN

HBG054044.

KO

K13171.

OrthoDB

EOG4DV5N4.

PhylomeDB

Q8IYB3.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

Q8IYB3.

Bgee

Q8IYB3.

CleanEx

HS_SRRM1.

Genevestigator

Q8IYB3.

GermOnline

ENSG00000133226. Homo sapiens.

Family and domain databases

Gene3D

1.20.1390.10. 1 hit.

InterPro

IPR002483. PWI_dom.
[Graphical view]

Pfam

PF01480. PWI. 1 hit.
[Graphical view]

SMART

SM00311. PWI. 1 hit.
[Graphical view]

SUPFAM

SSF101233. PWI. 1 hit.

PROSITE

PS51025. PWI. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SRRM1. human.

EvolutionaryTrace

Q8IYB3.

GenomeRNAi

10250.

NextBio

38838.

PMAP-CutDB

Q8IYB3.

SOURCE

Search...

Entry information

Entry name

SRRM1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.